P-POD: Princeton Protein Orthology Database: GO3/Nens112

This family has 83 members: 4 Arabidopsis thaliana, 7 Caenorhabditis elegans, 16 Danio rerio, 3 Dictyostelium discoideum, 5 Drosophila melanogaster, 1 Escherichia coli, 8 Gallus gallus, 11 Homo sapiens, 11 Mus musculus, 11 Rattus norvegicus, 4 Saccharomyces cerevisiae, 2 Schizosaccharomyces pombe.

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GO3/Nens112
83 members.
OrganismProtein (Synonyms)DescriptionAmiGO
A. thalianaNCBI:NP_191999.1 · TAIR:locus:2134623 (A_TM018A10.4 · T18A10_20 · T18A10.20 · ATECA2 · A_TM018A10_4 · AT4G00900 · ECA2)ER-TYPE CA2+-ATPASE 2 · ARABIDOPSIS THALIANA ER-TYPE CA2+-ATPASE 2⌘
A. thalianaNCBI:NP_563860.1 · TAIR:locus:2201916 (T27I1_16 · T27I1.16 · ATECA3 · AT1G10130 · ECA3)ENDOPLASMIC RETICULUM-TYPE CALCIUM-TRANSPORTING ATPASE 3 · ARABIDOPSIS THALIANA ER-TYPE CA2+-ATPASE 3⌘
A. thalianaNCBI:NP_172259.1 · TAIR:locus:2026580 (F24B9_9 · F24B9.9 · ATECA1 · ECA1 · ACA3 · AT1G07810)ER-TYPE CA2+-ATPASE · ARABIDOPSIS THALIANA ER-TYPE CA2+-ATPASE 1 · ER-TYPE CA2+-ATPASE 1⌘
A. thalianaNCBI:NP_172246.3 · TAIR:locus:2026555 (F24B9_24 · F24B9.24 · AT1G07670)⌘
C. elegansWB:WBGene00015660 (C09H5.2 · catp-3) · UniProtKB:O16331⌘
C. elegansWB:WBGene00015338 (C02E7.1 · catp-2) · UniProtKB:O16436⌘
C. elegansWB:WBGene00007248 (catp-4 · C01G12.8) · UniProtKB:O45240⌘
C. elegansWB:WBGene00001137 (B0365.3 · eat-6) · UniProtKB:P90735⌘
C. elegansWB:WBGene00004063 (ZK256.1 · pmr-1) · UniProtKB:Q6LA80⌘
C. elegansWB:WBGene00013672 (Y105E8A.12 · catp-1) · UniProtKB:Q8WQB1⌘
C. elegansWB:WBGene00004736 (K11D9.2 · sca-1) · UniProtKB:Q9XTG6⌘
D. rerioENSEMBL:ENSDARP00000046561
D. rerioUniProtKB:A0JMP4 · ZFIN:ZDB-GENE-041229-2 (atp2a1l)ATPase, Ca++ transporting, cardiac muscle, fast twitch 1 like⌘
D. rerioENSEMBL:ENSDARG00000060978 · UniProtKB:A2BIP1
D. rerioENSEMBL:ENSDARG00000060197 · UniProtKB:Q1LYL7
D. rerioUniProtKB:Q5U3A4 · ZFIN:ZDB-GENE-020905-1 (atp2a1)ATPase, Ca++ transporting, cardiac muscle, fast twitch 1⌘
D. rerioUniProtKB:Q6ZM60 · ZFIN:ZDB-GENE-030131-867 (atp2a2b)ATPase, Ca++ transporting, cardiac muscle, slow twitch 2b⌘
D. rerioUniProtKB:Q8JIV1 · ZFIN:ZDB-GENE-020501-1 (atp1a1a.5)ATPase, Na+/K+ transporting, alpha 1a.5 polypeptide⌘
D. rerioUniProtKB:Q9DEU1 · ZFIN:ZDB-GENE-001212-5 (atp1a1b)ATPase, Na+/K+ transporting, alpha 1b polypeptide⌘
D. rerioUniProtKB:Q9DEU2 · ZFIN:ZDB-GENE-001212-8 (atp1a3b)ATPase, Na+/K+ transporting, alpha 3b polypeptide⌘
D. rerioUniProtKB:Q9DEY3 · ZFIN:ZDB-GENE-001212-3 (atp1a1a.3)ATPase, Na+/K+ transporting, alpha 1a.3 polypeptide⌘
D. rerioUniProtKB:Q9DGL5 · ZFIN:ZDB-GENE-001212-6 (atp1a2a)ATPase, Na+/K+ transporting, alpha 2a polypeptide⌘
D. rerioUniProtKB:A9C3Q4 · ZFIN:ZDB-GENE-040426-702 (atp2a2a)ATPase, Ca++ transporting, cardiac muscle, slow twitch 2a⌘
D. rerioUniProtKB:Q9DEU0 · ZFIN:ZDB-GENE-001212-4 (atp1a1a.4)ATPase, Na+/K+ transporting, alpha 1a.4 polypeptide⌘
D. rerioUniProtKB:Q9DEY2 · ZFIN:ZDB-GENE-001212-7 (atp1a3a)ATPase, Na+/K+ transporting, alpha 3a polypeptide⌘
D. rerioUniProtKB:Q9DGL4 · ZFIN:ZDB-GENE-001212-2 (atp1a1a.2)ATPase, Na+/K+ transporting, alpha 1a.2 polypeptide⌘
D. rerioUniProtKB:Q9DGL6 · ZFIN:ZDB-GENE-001212-1 (atp1a1)ATPase, Na+/K+ transporting, alpha 1 polypeptide⌘
D. discoideumNCBI:EAL73415.2 · dictyBase:DDB_G0267924 (DDB_G0267924)sodium/potassium-transporting ATPase alpha chain 2, Na+/K+ ATPase, P-type ATPase, transmembrane protein⌘
D. discoideumNCBI:EAL72994.1 · dictyBase:DDB_G0268810 (DDB_G0268810)magnesium-translocating P-type ATPase, transmembrane protein⌘
D. discoideumUniProtKB:Q76P11 · dictyBase:DDB_G0277269 (ionA)P-type ATPase, ATPase, P-type cation exchange, alpha subunit, putative sodium/potassium-transporting ATPase⌘
D. melanogasterUniProtKB:P22700 · FB:FBgn0004551 (l(2)k09025 · Kumbhakarna · CG3725 · Ca-p · Ca[2+]ATPase · Ca-P60 · Ca-P60A · Kum · SERCA · CA-P60A · CaP60A · l(2)k08308ab · Ca-ATPase · dSERCA)sarco/endoplasmic reticulum-type Ca-2+-ATPase. · calcium ATPase · Ca[2+] ATPase · Calcium ATPase at 60A · organellar-type Ca-ATPase⌘
D. melanogasterUniProtKB:P13607 · FB:FBgn0002921 (ATPa · Na[+]K[+]ATPase · NaK · l(3)01453 · Na-p · dnATPase · Na[+]/K[+]ATPase · Na[+],K[+]-ATPase · ATPBagr · Da-47 · l(3)j3B7 · Na/K-ATPase · ATPalpha · CG5670 · l(3)j6A4 · Na+-K+-ATPase · l(3)ry136 · l(3)01164 · l(3)04492 · JY · Na,K-ATPase · l(3)rM454 · l(3)j3B2 · Atpalpha · Na[+]/K[+]-ATPase)Na[+],K[+]-ATPase alpha subunit · Na+,K+ ATPase alpha-subunit · alpha-subunit of ATPase · Na,K-ATPase alpha subunit · Na pump alpha subunit · Atp a · Na[+], K[+] -ATPase · Na/K-ATPase alpha-subunit · Na,K ATPase alpha subunit · (Na[+],K[+])ATPase alpha subunit · Na,K-ATPase alpha-subunit · Na[+],K[+] ATPase alpha subunit · Na[+],K[+]-ATPase alpha-subunit · sodium/potassium transporting ATPase alpha · (Na[+] + K[+])-ATPase alpha-subunit · ATPase alpha subunit · NaK ATPase · Na[+]-K[+] ATPase · Na,K ATPase · ATPase alpha · Na[+]/K[+] ATPase · Na+/K+ ATPase alpha subunit · Na[+]-K[+]-ATPase alpha[[5]]-subunit⌘
D. melanogasterUniProtKB:Q7KTU2 · FB:FBgn0052451 (SPoCK · CG32451 · anon-WO0118547.249 · CG7651 · SPoCk · CG14449)Secretory Pathway Calcium atpase⌘
D. melanogasterFB:FBgn0040037 (JYalpha · JYAlpha · CG17923) · UniProtKB:Q9U458⌘
D. melanogasterFB:FBgn0034732 (CG3701) · UniProtKB:Q9W248⌘
E. coliUniProtKB:P0ABB8 · ECOLI:MGTA-MONOMER (corB · b4242 · mtg · ECK4237 · mgtA · mgt · atmA · MgtA)magnesium transporter⌘
G. gallusNCBI:XP_426010 · ENTREZ:428450
G. gallusNCBI:XP_415130 · ENTREZ:396446
G. gallusENTREZ:396530 · UniProtKB:P09572 (P09572 · IPI00819216 · ATP1A1 · AT1A1_CHICK)Sodium/potassium-transporting ATPase subunit alpha-1⌘
G. gallusENTREZ:396468 · UniProtKB:P24797 (ATP1A2 · AT1A2_CHICK · IPI00583240 · P24797)Sodium/potassium-transporting ATPase subunit alpha-2⌘
G. gallusENTREZ:396467 · UniProtKB:P24798 (P24798 · AT1A3_CHICK · IPI00587236 · ATP1A3)Sodium/potassium-transporting ATPase subunit alpha-3⌘
G. gallusENTREZ:396528 · UniProtKB:P13585 (IPI00578635 · ATP2A1 · AT2A1_CHICK · P13585)Sarcoplasmic/endoplasmic reticulum calcium ATPase 1⌘
G. gallusENTREZ:395707 · UniProtKB:Q9YGL9 (IPI00599579 · ATP2A3 · Q9YGL9 · IPI00582754 · AT2A3_CHICK)Sarcoplasmic/endoplasmic reticulum calcium ATPase 3⌘
G. gallusUniProtKB:Q5ZIK7 (RCJMB04_25f22 · IPI00594501 · Q5ZIK7) · ENTREZ:419743⌘
H. sapiensENSEMBL:ENSG00000075673 · UniProtKB:P54707 (P54707 · AT12A_HUMAN · ATP12A · IPI00008161 · ATP1AL1 · IPI00872242)Potassium-transporting ATPase alpha chain 2⌘
H. sapiensENSEMBL:ENSG00000163399 · UniProtKB:P05023 (IPI00414005 · AT1A1_HUMAN · IPI00006482 · ATP1A1 · P05023)Sodium/potassium-transporting ATPase subunit alpha-1⌘
H. sapiensENSEMBL:ENSG00000018625 · UniProtKB:P50993 (ATP1A2 · AT1A2_HUMAN · IPI00003021 · KIAA0778 · P50993)Sodium/potassium-transporting ATPase subunit alpha-2⌘
H. sapiensENSEMBL:ENSG00000105409 · UniProtKB:P13637 (IPI00302840 · AT1A3_HUMAN · P13637 · ATP1A3)Sodium/potassium-transporting ATPase subunit alpha-3⌘
H. sapiensENSEMBL:ENSG00000132681 · UniProtKB:Q13733 (AT1A4_HUMAN · ATP1A4 · Q13733 · IPI00375339 · IPI00252122 · ATP1AL2)Sodium/potassium-transporting ATPase subunit alpha-4⌘
H. sapiensENSEMBL:ENSG00000196296 · UniProtKB:O14983 (O14983 · AT2A1_HUMAN · IPI00024804 · ATP2A1 · IPI00396118)Sarcoplasmic/endoplasmic reticulum calcium ATPase 1⌘
H. sapiensENSEMBL:ENSG00000174437 · UniProtKB:P16615 (ATP2A2 · IPI00219078 · P16615 · IPI00177817 · ATP2B · AT2A2_HUMAN)Sarcoplasmic/endoplasmic reticulum calcium ATPase 2⌘
H. sapiensENSEMBL:ENSG00000074370 · UniProtKB:Q93084 (AT2A3_HUMAN · IPI00004092 · ATP2A3 · IPI00218442 · IPI00218440 · IPI00303760 · Q93084 · IPI00748794 · IPI00478023)Sarcoplasmic/endoplasmic reticulum calcium ATPase 3⌘
H. sapiensENSEMBL:ENSG00000017260 · UniProtKB:P98194 (ATP2C1 · HUSSY-28 · IPI00413116 · IPI00220473 · IPI00745171 · IPI00607568 · IPI00607812 · IPI00419957 · KIAA1347 · PMR1L · P98194 · AT2C1_HUMAN)Calcium-transporting ATPase type 2C member 1⌘
H. sapiensENSEMBL:ENSG00000064270 · UniProtKB:O75185 (AT2C2_HUMAN · KIAA0703 · ATP2C2 · O75185 · IPI00915432 · IPI00006653 · SPCA2)Calcium-transporting ATPase type 2C member 2⌘
H. sapiensENSEMBL:ENSG00000105675 · UniProtKB:P20648 (IPI00218919 · P20648 · ATP4A · ATP4A_HUMAN)Potassium-transporting ATPase alpha chain 1⌘
M. musculusUniProtKB:Q9Z1W8 · MGI:MGI:1926943 (Atp1al1 · Atp12a · HKalpha2 · cHKA)ATPase H+K+-transporting, alpha 2 · ATPase, H+/K+ transporting, nongastric, alpha polypeptide⌘
M. musculusUniProtKB:Q8VDN2 · MGI:MGI:88105 (Atpa-1 · Atp1a1)ATPase, Na+/K+ transporting, alpha 1 polypeptide⌘
M. musculusUniProtKB:Q6PIE5 · MGI:MGI:88106 (Atp1a2 · Atpa-3)ATPase, Na+/K+ transporting, alpha 2 polypeptide⌘
M. musculusUniProtKB:Q6PIC6 · MGI:MGI:88107 (Atp1a3 · Atpa-2)ATPase, Na+/K+ transporting, alpha 3 polypeptide⌘
M. musculusUniProtKB:Q9WV27 · MGI:MGI:1351335 (Atp1a4)ATPase, Na+/K+ transporting, alpha 4 polypeptide⌘
M. musculusUniProtKB:Q8R429 · MGI:MGI:105058 (SERCA1 · Atp2a1)ATPase, Ca++ transporting, cardiac muscle, fast twitch 1⌘
M. musculusUniProtKB:O55143 · MGI:MGI:88110 (D5Wsu150e · Atp2a2 · SERCA2)sarco/endoplasmic reticulum Ca2+-ATPase 2 · ATPase, Ca++ transporting, cardiac muscle, slow twitch 2⌘
M. musculusUniProtKB:Q64518 · MGI:MGI:1194503 (Serca3 · Atp2a3)ATPase, Ca++ transporting, ubiquitous⌘
M. musculusUniProtKB:Q80XR2 · MGI:MGI:1889008 (SPCA · PMR1 · Atp2c1 · ATP2C1A)ATPase, Ca++-sequestering⌘
M. musculusUniProtKB:A7L9Z8 · MGI:MGI:1916297 (Atp2c2)ATPase, Ca++ transporting, type 2C, member 2⌘
M. musculusUniProtKB:Q64436 · MGI:MGI:88113 (Atp4a)ATPase, H+/K+ exchanging, gastric, alpha polypeptide · H+K+-transporting alpha 1⌘
R. norvegicusRGD:620569 (Atp12a) · UniProtKB:P54708 (Atp1al1 · AT12A_RAT · Atp12a · P54708 · IPI00188119 · IPI00231462)ATPase, H+/K+ transporting, nongastric, alpha polypeptide · Potassium-transporting ATPase alpha chain 2⌘⌘
R. norvegicusRGD:2167 (Atp1a1) · UniProtKB:P06685 (IPI00326305 · AT1A1_RAT · Atp1a1 · P06685)ATPase, Na+/K+ transporting, alpha 1 polypeptide · Sodium/potassium-transporting ATPase subunit alpha-1⌘⌘
R. norvegicusUniProtKB:P06686 · RGD:2168 (Atp1a2)ATPase, Na+/K+ transporting, alpha 2 polypeptide⌘
R. norvegicusUniProtKB:P06687 · RGD:2169 (Atp1a3)ATPase, Na+/K+ transporting, alpha 3 polypeptide⌘
R. norvegicusUniProtKB:Q64541 · RGD:61952 (Atp1a4)ATPase, Na+/K+ transporting, alpha 4 polypeptide⌘
R. norvegicusUniProtKB:Q64578 · RGD:621293 (Atp2a1)ATPase, Ca++ transporting, cardiac muscle, fast twitch 1⌘
R. norvegicusRGD:2174 (Atp2a2) · UniProtKB:P11507 (P11507 · IPI00190020 · IPI00231369 · AT2A2_RAT · Atp2a2)ATPase, Ca++ transporting, cardiac muscle, slow twitch 2 · Sarcoplasmic/endoplasmic reticulum calcium ATPase 2⌘⌘
R. norvegicusRGD:2175 (Atp2a3) · UniProtKB:P18596 (P18596 · IPI00192914 · Atp2a3 · AT2A3_RAT)ATPase, Ca++ transporting, ubiquitous · Sarcoplasmic/endoplasmic reticulum calcium ATPase 3⌘⌘
R. norvegicusRGD:621311 (Atp2c1) · UniProtKB:Q64566 (IPI00231405 · AT2C1_RAT · Q64566 · IPI00213585 · Atp2c1)ATPase, Ca++ transporting, type 2C, member 1 · Calcium-transporting ATPase type 2C member 1⌘⌘
R. norvegicusUniProtKB:Q8R4C1 · RGD:620647 (Atp2c2)ATPase, Ca++ transporting, type 2C, member 2⌘
R. norvegicusRGD:2177 (Atp4a) · UniProtKB:P09626 (Hka · ATP4A_RAT · Atp4a · IPI00365705 · P09626)ATPase, H+/K+ exchanging, alpha polypeptide · Potassium-transporting ATPase alpha chain 1⌘⌘
S. cerevisiaeUniProtKB:P13586 · SGD:S000003135 (YGL167C · LDB1 · BSD1 · PMR1 · SSC1)High affinity Ca2+/Mn2+ P-type ATPase required for Ca2+ and Mn2+ transport into Golgi⌘
S. cerevisiaeUniProtKB:P13587 · SGD:S000002447 (HOR6 · PMR2 · YDR040C · ENA1)P-type ATPase sodium pump, involved in Na+ and Li+ efflux to allow salt tolerance⌘
S. cerevisiaeUniProtKB:Q01896 · SGD:S000002446 (YDR039C · ENA2)P-type ATPase sodium pump, involved in Na+ efflux to allow salt tolerance⌘
S. cerevisiaeUniProtKB:Q12691 · SGD:S000002445 (YDR038C · ENA5)Protein with similarity to P-type ATPase sodium pumps, member of the Na+ efflux ATPase family⌘
S. pombeUniProtKB:O59868 · GeneDB_Spombe:SPBC31E1.02c (SPBC31E1.02c · pmr1)P-type ATPase, calcium transporting Pmr1⌘
S. pombeUniProtKB:P22189 · GeneDB_Spombe:SPBC839.06 (SPBC839.06 · cta3)P-type ATPase, calcium transporting Cta3⌘
ProteinPublicationCurator Notes
UniProtKB:P13587 · SGD:S000002447PMID:9430707 Bañuelos MA, et al. P-type ATPases mediate sodium and potassium effluxes in Schwanniomyces occidentalis. J Biol Chem. 1998 Jan 16;273(3):1640-6.The S. occidentalis protein ENA1 complements a homologous mutation in S. cerevisiae.
UniProtKB:P13587 · SGD:S000002447PMID:14991656 Nakayama H, et al. Yeast plasma membrane Ena1p ATPase alters alkali-cation homeostasis and confers increased salt tolerance in tobacco cultured cells. Biotechnol Bioeng. 2004 Mar 30;85(7):776-89.The S. cerevisiae protein ENA1 was expressed in N. tabacum, but complementation was not directly tested. This paper describes functional expression of yeast ENA1 in tobacco.
UniProtKB:Q01896 · SGD:S000002446PMID:15702539 Kinclová-Zimmermannová O, et al. Rice Na+/H+-antiporter Nhx1 partially complements the alkali-metal-cation sensitivity of yeast strains lacking three sodium transporters. Folia Microbiol (Praha). 2004;49(5):519-25.The O. sativa protein NHX1 was expressed in S. cerevisiae, but complementation was not directly tested. This paper shows that rice NHX1 partially restores growth to a yeast ena1 ena2 nha1 nhx1 mutant grown in high salt.
UniProtKB:P13587 · SGD:S000002447PMID:15702539 Kinclová-Zimmermannová O, et al. Rice Na+/H+-antiporter Nhx1 partially complements the alkali-metal-cation sensitivity of yeast strains lacking three sodium transporters. Folia Microbiol (Praha). 2004;49(5):519-25.The O. sativa protein NHX1 was expressed in S. cerevisiae, but complementation was not directly tested. This paper shows that rice NHX1 partially restores growth to a yeast ena1 ena2 nha1 nhx1 mutant grown in high salt.
UniProtKB:P13587 · SGD:S000002447PMID:15907686 Brini F, et al. Cloning and characterization of a wheat vacuolar cation/proton antiporter and pyrophosphatase proton pump. Plant Physiol Biochem. 2005 Apr;43(4):347-54.The T. aestivum protein TVP1 complements a homologous mutation in S. cerevisiae.
UniProtKB:Q01896 · SGD:S000002446PMID:16232587 Watanabe Y, et al. Characterization of the Na+-ATPase gene (ZENA1) from the salt-tolerant yeast Zygosaccharomyces rouxii. J Biosci Bioeng. 1999;88(2):136-42.The Z. rouxii protein ZENA1 complements a homologous mutation in S. cerevisiae. This paper shows that ZENA1 can restore growth to a yeast ena1 ena2 mutant grown in high salt.
UniProtKB:P13587 · SGD:S000002447PMID:16232587 Watanabe Y, et al. Characterization of the Na+-ATPase gene (ZENA1) from the salt-tolerant yeast Zygosaccharomyces rouxii. J Biosci Bioeng. 1999;88(2):136-42.The Z. rouxii protein ZENA1 complements a homologous mutation in S. cerevisiae. This paper shows that ZENA1 can restore growth to a yeast ena1 ena2 mutant grown in high salt.
UniProtKB:P13586 · SGD:S000003135PMID:16088881 Soriani FM, et al. A PMR1-like calcium ATPase of Aspergillus fumigatus: cloning, identification and functional expression in S. cerevisiae. Yeast. 2005 Jul 30;22(10):813-24.The A. fumigatus protein Afpmr1 complements a homologous mutation in S. cerevisiae. This paper shows that A. fumigatus Afpmr1 complements a yeast pmr1 pmc1 cnb1 triple mutant, indicating that it encodes a Ca(2+) ATPase. A. fumigatus Afpmr1 contains all the conserved subdomains found in P-type ATPases such as yeast Pmr1p, and therefore it appears to be a PMR1-like calcium ATPase.
UniProtKB:P13586 · SGD:S000003135PMID:9238019 Liang F, et al. ECA1 complements yeast mutants defective in Ca2+ pumps and encodes an endoplasmic reticulum-type Ca2+-ATPase in Arabidopsis thaliana. Proc Natl Acad Sci U S A. 1997 Aug 5;94(16):8579-84.The A. thaliana protein AT1G07810.1 complements a homologous mutation in S. cerevisiae. This paper shows that A. thaliana AT1G07810.1 complements a yeast pmr1 mutant, indicating that it functions as a Ca(2+) pump, and also suppresses a triple mutant (pmr1 pmc1 cnb 1) deficient in Golgi and vacuolar Ca(2+) pumps and calcineurin B.
UniProtKB:P13586 · SGD:S000003135PMID:9808725 Liang F, et al. A high-affinity Ca2+ pump, ECA1, from the endoplasmic reticulum is inhibited by cyclopiazonic acid but not by thapsigargin. Plant Physiol. 1998 Nov;118(3):817-25.The A. thaliana protein AT1G07810.1 complements a homologous mutation in S. cerevisiae. This paper shows A. thaliana ECA1 (AT1G07810.1) is a Ca2+-ATPase homolog that complements a yeast pmc1 pmr1 cnb1 triple mutant, deficient in Ca(2+) pumps, indicating that ECA1 encodes a functional Ca2+-ATPase. The triple mutant includes cnb1 which encodes the protein phosphatase calcineurin B, but the triple mutant was used to test for Ca2+-pump activity, not protein phosphatase activity.
UniProtKB:P13586 · SGD:S000003135PMID:11115896 Geisler M, et al. The ACA4 gene of Arabidopsis encodes a vacuolar membrane calcium pump that improves salt tolerance in yeast. Plant Physiol. 2000 Dec;124(4):1814-27.The A. thaliana protein AT2G41560.1 complements a homologous mutation in S. cerevisiae. This paper shows that AT2G41560.1 (ACA4) functions as a Ca2+ Pump, but only an N-terminally modified form of ACA4 rescues a yeast pmr1 pmc1 cnb1 triple mutant. The truncation of the N-terminal region seems to transfer ACA4 into an activated state.
UniProtKB:P13586 · SGD:S000003135PMID:15197266 Schiøtt M, et al. A plant plasma membrane Ca2+ pump is required for normal pollen tube growth and fertilization. Proc Natl Acad Sci U S A. 2004 Jun 22;101(25):9502-7.The A. thaliana protein AT3G21180.1 complements a homologous mutation in S. cerevisiae. An N-terminally modified form of AT3G21180.1 (ACA9) complements a yeast mutant devoid of Ca2+-ATPases (i.e. pmr1 pmc1 cnb1), demonstrating the Ca2+-ATPase activity of AT3G21180.1.
UniProtKB:P13586 · SGD:S000003135PMID:15623514 Ramos-Castañeda J, et al. Deficiency of ATP2C1, a Golgi ion pump, induces secretory pathway defects in endoplasmic reticulum (ER)-associated degradation and sensitivity to ER stress. J Biol Chem. 2005 Mar 11;280(10):9467-73.The R. norvegicus protein ATP2C1 complements a homologous mutation in S. cerevisiae. The authors only used a yeast pmr1 mutant.
UniProtKB:P13587 · SGD:S000002447PMID:16303259 Velkova K, et al. The Debaryomyces hansenii NHA1 gene encodes a plasma membrane alkali-metal-cation antiporter with broad substrate specificity. Gene. 2006 Mar 15;369:27-34.The D. hansenii protein DhNHA1 was expressed in S. cerevisiae, but complementation was not directly tested. This paper shows functional expression of D. hansenii DhNHA1 in an S. cerevisiae ena1 nha1 double mutant.
UniProtKB:P13587 · SGD:S000002447PMID:17311588 Montiel V, et al. Intracellular Na and K distribution in Debaryomyces hansenii. Cloning and expression in Saccharomyces cerevisiae of DhNHX1. FEMS Yeast Res. 2007 Jan;7(1):102-9.The D. hansenii protein DhNHX1 was expressed in S. cerevisiae, but complementation was not directly tested. This paper shows functional expression of DhNHX1 in a yeast ena1-4 nhx1 nha1 mutant.
UniProtKB:P13586 · SGD:S000003135PMID:11741891 Ton VK, et al. Functional expression in yeast of the human secretory pathway Ca(2+), Mn(2+)-ATPase defective in Hailey-Hailey disease. J Biol Chem. 2002 Feb 22;277(8):6422-7.The H. sapiens protein P98194 complements a homologous mutation in S. cerevisiae. Human ATP2C1/hSPCA1 complements the yeast triple mutant (pmr1 pmc1 cnb1) deficient in the Golgi and vacuolar Ca(2+) pumps. In this study, ATP2C1/hSPCA1 also transports Ca2+ and Mn2+ with a high affinity similar to yeast PMR1 which was also re-introduced into the triple mutant in a separate complementation experiment. Human ATP2C1/hSPCA1 appears to be the functional homolog of yeast PMR1.
UniProtKB:P13586 · SGD:S000003135PMID:15610533 Ton VK, et al. Expression of Hailey-Hailey disease mutations in yeast. J Invest Dermatol. 2004 Dec;123(6):1192-4.The H. sapiens protein P98194 complements a homologous mutation in S. cerevisiae. This paper shows that human ATP2C1 complements a yeast pmr1 pmc1 cnb1 triple mutant lacking endogenouse calcium pumps, however, human ATP2C1 shows greater homology to yeast PMR1.
UniProtKB:P13586 · SGD:S000003135PMID:15811312 Kellermayer R. Hailey-Hailey disease as an orthodisease of PMR1 deficiency in Saccharomyces cerevisiae. FEBS Lett. 2005 Apr 11;579(10):2021-5.The H. sapiens protein P98194 complements a homologous mutation in S. cerevisiae. Human ATP2C1 complements a yeast pmr1 mutant.
UniProtKB:P13586 · SGD:S000003135PMID:10948258 Chung WS, et al. Identification of a calmodulin-regulated soybean Ca(2+)-ATPase (SCA1) that is located in the plasma membrane. Plant Cell. 2000 Aug;12(8):1393-407.The G. max protein SCA1 complements a homologous mutation in S. cerevisiae. This papers shows that soybean SCA1 (Q9FVE8_SOYBN) encodes a Ca(2+)-ATPase and complements complements a yeast pmc1 pmr1 cnb1 triple mutant, deficient in Ca(2+) pumps, indicating that ECA1 encodes a functional Ca2+-ATPase. The triple mutant includes cnb1 which encodes the protein phosphatase calcineurin B, but the triple mutant was used to test for Ca2+-pump activity, not protein phosphatase activity.
UniProtKB:P13586 · SGD:S000003135PMID:10027971 Degand I, et al. Rabbit sarcoplasmic reticulum Ca(2+)-ATPase replaces yeast PMC1 and PMR1 Ca(2+)-ATPases for cell viability and calcineurin-dependent regulation of calcium tolerance. Mol Microbiol. 1999 Jan;31(2):545-56.The O. cuniculus protein SERCA1a complements a homologous mutation in S. cerevisiae. This paper shows that the rabbit SERCA1a Ca(2+)-ATPase complements yeast pmr1 pmc1 cnb1 and pmr1 pmc1 vcx1 triple mutants.
UniProtKB:P13586 · SGD:S000003135PMID:11382780 Furuya T, et al. TcSCA complements yeast mutants defective in Ca2+ pumps and encodes a Ca2+-ATPase that localizes to the endoplasmic reticulum of Trypanosoma cruzi. J Biol Chem. 2001 Aug 31;276(35):32437-45.The T. cruzi protein TcSCA complements a homologous mutation in S. cerevisiae. This paper shows that T. cruzi TcSCA contains several sequence motifs found in Ca2+-ATPases and that it complements a yeast triple mutant (pmr1 pmc1 cnb 1) deficient in the Ca(2+) pumps, indicating that TsSCA encodes a functional Ca2+-ATPase.
UniProtKB:P13587 · SGD:S000002447PMID:9238019 Liang F, et al. ECA1 complements yeast mutants defective in Ca2+ pumps and encodes an endoplasmic reticulum-type Ca2+-ATPase in Arabidopsis thaliana. Proc Natl Acad Sci U S A. 1997 Aug 5;94(16):8579-84.The A. thaliana protein AT1G07810.1 does not complement a homologous mutation in S. cerevisiae. This paper shows that A. thaliana AT1G07810.1 does not complement a yeast ena1 (alias pmr2) null mutant and does not function as a Na+ and Li+ efflux pump.
DescriptionSuffix
Sequences in this family.fasta
mafft aligned Fasta file.afasta
phyml newick file.newick
Notung rooted & rearranged newick file.newick.rooting.0.rearrange.0
Notung Homolog Table.newick.rooting.0.rearrange.0.homologs.csv
OMIM (7)
ENSEMBL:ENSG00000018625 · UniProtKB:P50993#104290 ALTERNATING HEMIPLEGIA OF CHILDHOOD
ENSEMBL:ENSG00000105409 · UniProtKB:P13637#602481 MIGRAINE, FAMILIAL HEMIPLEGIC, 2; FHM2;;MHP2MIGRAINE, FAMILIAL BASILAR, INCLUDED
ENSEMBL:ENSG00000196296 · UniProtKB:O14983#128235 DYSTONIA 12; DYT12;;DYSTONIA-PARKINSONISM, RAPID-ONSET; RDP
ENSEMBL:ENSG00000174437 · UniProtKB:P16615#601003 BRODY MYOPATHY
ENSEMBL:ENSG00000017260 · UniProtKB:P98194#124200 DARIER-WHITE DISEASE; DAR;;KERATOSIS FOLLICULARIS;;DARIER DISEASE; DDDARIER DISEASE, ACRAL HEMORRHAGIC TYPE, INCLUDED;;DARIER DISEASE, SEGMENTAL, INCLUDED
#101900 ACROKERATOSIS VERRUCIFORMIS; AKV;;HOPF DISEASE
UniProtKB:P13586 · SGD:S000003135#169600 BENIGN CHRONIC PEMPHIGUS; BCPM;;PEMPHIGUS, BENIGN FAMILIAL;;HAILEY-HAILEY DISEASE; HHD
SGD Disease Papers (7)
UniProtKB:P13586 · SGD:S000003135PMID:15811312 Kellermayer R (2005) Hailey-Hailey disease as an orthodisease of PMR1 deficiency in Saccharomyces cerevisiae. FEBS Lett 579(10):2021-5
PMID:15623514 Ramos-Castaneda J, et al. (2005) Deficiency of ATP2C1, a Golgi ion pump, induces secretory pathway defects in endoplasmic reticulum (ER)-associated degradation and sensitivity to ER stress. J Biol Chem 280(10):9467-73
PMID:15610534 Szigeti R and Kellermayer R (2004) Hailey-Hailey disease and calcium: lessons from yeast. J Invest Dermatol 123(6):1195-6
PMID:15610533 Ton VK and Rao R (2004) Expression of Hailey-Hailey disease mutations in yeast. J Invest Dermatol 123(6):1192-4
PMID:11741891 Ton VK, et al. (2002) Functional expression in yeast of the human secretory pathway Ca(2+), Mn(2+)-ATPase defective in Hailey-Hailey disease. J Biol Chem 277(8):6422-7
PMID:10767338 Sudbrak R, et al. (2000) Hailey-Hailey disease is caused by mutations in ATP2C1 encoding a novel Ca(2+) pump. Hum Mol Genet 9(7):1131-40
PMID:10615129 Hu Z, et al. (2000) Mutations in ATP2C1, encoding a calcium pump, cause Hailey-Hailey disease. Nat Genet 24(1):61-5
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