P-POD: Princeton Protein Orthology Database: GO3/Jaccard615

This family has 37 members: 7 Arabidopsis thaliana, 4 Caenorhabditis elegans, 3 Danio rerio, 2 Dictyostelium discoideum, 7 Drosophila melanogaster, 2 Gallus gallus, 2 Homo sapiens, 2 Mus musculus, 2 Rattus norvegicus, 3 Saccharomyces cerevisiae, 3 Schizosaccharomyces pombe.

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GO3/Jaccard615
37 members.
OrganismProtein (Synonyms)DescriptionAmiGO
A. thalianaNCBI:NP_564098.2 · TAIR:locus:2035401 (AVA-2PE · AT1G19910 · F6F9_3 · F6F9.3 · ATVHA-C2 · AVA-P2)VACUOLAR-TYPE H+ ATPASE C2 · VACUOLAR H+-PUMPING ATPASE 16 KDA PROTEOLIPID⌘
A. thalianaNCBI:NP_177693.1 · TAIR:locus:2005649 (F10A5.17 · F10A5_17 · AT1G75630 · AVA-P4)VACUOLAR H+-PUMPING ATPASE 16 KD PROTEOLIPID⌘
A. thalianaNCBI:NP_180132.1 · TAIR:locus:2050286 (AT2G25610 · F3N11_6 · F3N11.6)⌘
A. thalianaNCBI:NP_195198.1 · TAIR:locus:2139634 (VHA-C1 · AT4G34720 · T4L20.300 · ATVHA-C1 · AVA-P1)VACUOLAR H+-PUMPING ATPASE C1 · VACUOLAR H+-PUMPING ATPASE 16 KDA PROTEOLIPID⌘
A. thalianaNCBI:NP_195603.1 · TAIR:locus:2120237 (F19H22.20 · AT4G38920 · AVA-P3 · ATVHA-C3)VACUOLAR-TYPE H(+)-ATPASE C3⌘
A. thalianaNCBI:NP_001119099.1 · TAIR:locus:2131337 (L23H3.10 · AT4G32530 · L23H3_10)⌘
A. thalianaNCBI:NP_179244.1 · TAIR:locus:2045101 (AT2G16510 · F1P15_11 · F1P15.11)⌘
C. elegansWB:WBGene00006910 (R10E11.8 · vha-1) · UniProtKB:Q21898 (VATL1_CAEEL · R10E11.8 · vha-1)V-type proton ATPase 16 kDa proteolipid subunit 1⌘⌘
C. elegansWB:WBGene00006912 (Y38F2AL.4 · vha-3) · UniProtKB:P34546 (vha-2 · Y38F2AL.4 · R10E11.2 · VATL2_CAEEL · vha-3)V-type proton ATPase 16 kDa proteolipid subunit 2/3⌘⌘
C. elegansWB:WBGene00006911 (vha-2 · R10E11.2) · UniProtKB:P34546 (vha-2 · Y38F2AL.4 · R10E11.2 · VATL2_CAEEL · vha-3)V-type proton ATPase 16 kDa proteolipid subunit 2/3⌘⌘
C. elegansWB:WBGene00006913 (vha-4 · T01H3.1) · UniProtKB:Q22087⌘
D. rerioUniProtKB:Q6PD81 · ZFIN:ZDB-GENE-030131-443 (atp6v0b)ATPase, H+ transporting, V0 subunit B⌘
D. rerioUniProtKB:Q8JGS3 · ZFIN:ZDB-GENE-020419-23 (atp6v0c)ATPase, H+ transporting, lysosomal, V0 subunit c⌘
D. rerioZFIN:ZDB-GENE-030131-4127 (zgc:77708) · UniProtKB:Q6P041⌘
D. discoideumUniProtKB:P54642 · dictyBase:DDB_G0274381 (vatP)Vacuolar ATP synthase proteolipid subunit, vacuolar ATPase proteolipid subunit⌘
D. discoideumUniProtKB:Q86AS7 · dictyBase:DDB_G0274141 (DDB_G0274141)Vacuolar ATP synthase 21 kDa proteolipid subunit⌘
D. melanogasterUniProtKB:P23380 · FB:FBgn0004145 (vha16-1 · BcDNA:SD02875 · ductin · EP2372 · vha16 · V-ATPase · CG3161 · Ductin · Vha1 · DucC · Vha16 · Vhac)Ductin subunit C · Vacuolar H[+] ATPase 16kD subunit · c subunit · Vacuolar H[+]-ATPase c subunit · ductin, vacuolar H(+)-ATPase subunit C proteolipid⌘
D. melanogasterFB:FBgn0034169 (CG9013) · UniProtKB:A1ZAL7⌘
D. melanogasterFB:FBgn0028667 (V-ATPase · CG7547 · CG32090 · Vha16-3 · vha16-3) · UniProtKB:Q8IQG3⌘
D. melanogasterFB:FBgn0028662 (V-ATPase · CG7007 · vhaPPA1-1 · VhaPPA1-1) · UniProtKB:Q9VFE3⌘
D. melanogasterFB:FBgn0038276 (CG7026) · UniProtKB:Q9VFE5⌘
D. melanogasterFB:FBgn0032294 (CG6737) · UniProtKB:Q9VKQ8⌘
D. melanogasterFB:FBgn0028668 (V-ATPase · CG7547 · Vha16-2 · CG32089 · vha16-2) · UniProtKB:Q9VTI6⌘
G. gallusNCBI:XP_001232268 · ENTREZ:770475
G. gallusNCBI:XP_422414 · ENTREZ:424575
H. sapiensENSEMBL:ENSG00000185883 · UniProtKB:P27449 (P27449 · VATL_HUMAN · ATP6C · IPI00018855 · ATP6L · ATPL · ATP6V0C)V-type proton ATPase 16 kDa proteolipid subunit⌘
H. sapiensENSEMBL:ENSG00000117410 · UniProtKB:Q99437 (VATO_HUMAN · Q99437 · IPI00015261 · ATP6V0B · ATP6F)V-type proton ATPase 21 kDa proteolipid subunit⌘
M. musculusUniProtKB:P63082 · MGI:MGI:88116 (PL16 · Atpl-rs1 · Vma3 · Atp6l · Atp6c · Atpl · Atp6v0c · Atp6c2 · proteolipid)H(+)-ATPase (mvp) · lysosomal 16kDa · ATPase, H+ transporting, lysosomal V0 subunit C⌘
M. musculusUniProtKB:Q91V37 · MGI:MGI:1890510 (VMA16 · Atp6f · Atp6v0b)ATPase, H+ transporting, lysosomal V0 subunit B⌘
R. norvegicusNCBI:XP_216510 · RGD:1308303 (Atp6v0b)ATPase, H+ transporting, lysosomal 21kDa, V0 subunit b⌘
R. norvegicusUniProtKB:P63081 · RGD:621394 (Atp6v0c)ATPase, H+ transporting, lysosomal 16kDa, V0 subunit c⌘
S. cerevisiaeUniProtKB:P25515 · SGD:S000000753 (CLS7 · VMA3 · GEF2 · YEL027W · CUP5)Proteolipid subunit of the vacuolar H(+)-ATPase V0 sector (subunit c⌘
S. cerevisiaeUniProtKB:P32842 · SGD:S000006155 (TFP3 · YPL234C · VMA11 · CLS9)Vacuolar ATPase V0 domain subunit c', involved in proton transport activity⌘
S. cerevisiaeUniProtKB:P23968 · SGD:S000001068 (VMA16 · PPA1 · YHR026W)Subunit c'' of the vacuolar ATPase, which functions in acidification of the vacuole⌘
S. pombeUniProtKB:Q9URZ8 · GeneDB_Spombe:SPAC732.01 (SPAC732.01 · vma11)V-type ATPase proteolipid subunit⌘
S. pombeUniProtKB:P50515 · GeneDB_Spombe:SPAC1B3.14 (SPAC1B3.14 · vma3)V-type ATPase subunit c⌘
S. pombeUniProtKB:O14046 · GeneDB_Spombe:SPAC2C4.13 (SPAC2C4.13 · vma16)V-type ATPase subunit c''⌘
ProteinPublicationCurator Notes
UniProtKB:P25515 · SGD:S000000753PMID:15958496 Tyagi W, et al. Cloning and regulation of a stress-regulated Pennisetum glaucum vacuolar ATPase c gene and characterization of its promoter that is expressed in shoot hairs and floral organs. Plant Cell Physiol. 2005 Aug;46(8):1411-22.The P. glaucum protein PgVHA-c1 does not complement a homologous mutation in S. cerevisiae.
UniProtKB:P23968 · SGD:S000001068PMID:15958496 Tyagi W, et al. Cloning and regulation of a stress-regulated Pennisetum glaucum vacuolar ATPase c gene and characterization of its promoter that is expressed in shoot hairs and floral organs. Plant Cell Physiol. 2005 Aug;46(8):1411-22.The P. glaucum protein PgVHA-c1 does not complement a homologous mutation in S. cerevisiae.
UniProtKB:P32842 · SGD:S000006155PMID:15958496 Tyagi W, et al. Cloning and regulation of a stress-regulated Pennisetum glaucum vacuolar ATPase c gene and characterization of its promoter that is expressed in shoot hairs and floral organs. Plant Cell Physiol. 2005 Aug;46(8):1411-22.The P. glaucum protein PgVHA-c1 does not complement a homologous mutation in S. cerevisiae.
UniProtKB:P25515 · SGD:S000000753PMID:10464277 Harrison MA, et al. Helical interactions and membrane disposition of the 16-kDa proteolipid subunit of the vacuolar H(+)-ATPase analyzed by cysteine replacement mutagenesis. J Biol Chem. 1999 Sep 3;274(36):25461-70.The N. norvegicus protein 16 kDa proteolipid complements a homologous mutation in S. cerevisiae.
UniProtKB:P25515 · SGD:S000000753PMID:11733003 Ikeda M, et al. Expression of V-ATPase proteolipid subunit of Acetabularia acetabulum in a VMA3-deficient strain of Saccharomyces cerevisiae and its complementation study. Eur J Biochem. 2001 Dec;268(23):6097-104.The A. acetabulum protein AACEVAPD2 was expressed in S. cerevisiae, but complementation was not directly tested. This paper shows the heterologous expression of A. acetabulum AACEVAPD2 in a yeast cup5 null mutant in order to demonstrate that it encodes a functional proteolipid subunit of the V-ATPase complex.
UniProtKB:P25515 · SGD:S000000753PMID:11733003 Ikeda M, et al. Expression of V-ATPase proteolipid subunit of Acetabularia acetabulum in a VMA3-deficient strain of Saccharomyces cerevisiae and its complementation study. Eur J Biochem. 2001 Dec;268(23):6097-104.The A. acetabulum protein AACEVAPD4 was expressed in S. cerevisiae, but complementation was not directly tested. This paper shows the heterologous expression of A. acetabulum AACEVAPD4 in a yeast cup5 null mutant in order to demonstrate that it encodes a functional proteolipid subunit of the V-ATPase complex.
UniProtKB:P25515 · SGD:S000000753PMID:11733003 Ikeda M, et al. Expression of V-ATPase proteolipid subunit of Acetabularia acetabulum in a VMA3-deficient strain of Saccharomyces cerevisiae and its complementation study. Eur J Biochem. 2001 Dec;268(23):6097-104.The A. acetabulum protein AACEVAPD5 was expressed in S. cerevisiae, but complementation was not directly tested. This paper shows the heterologous expression of A. acetabulum AACEVAPD5 in a yeast cup5 null mutant in order to demonstrate that it encodes a functional proteolipid subunit of the V-ATPase complex.
UniProtKB:P25515 · SGD:S000000753PMID:11733003 Ikeda M, et al. Expression of V-ATPase proteolipid subunit of Acetabularia acetabulum in a VMA3-deficient strain of Saccharomyces cerevisiae and its complementation study. Eur J Biochem. 2001 Dec;268(23):6097-104.The A. acetabulum protein AACEVAPD6 was expressed in S. cerevisiae, but complementation was not directly tested. This paper shows the heterologous expression of A. acetabulum AACEVAPD6 in a yeast cup5 null mutant in order to demonstrate that it encodes a functional proteolipid subunit of the V-ATPase complex.
UniProtKB:P25515 · SGD:S000000753PMID:12379795 Ikeda M, et al. Functional expression of Acetabularia acetabulum vacuolar H(+)-pyrophosphatase in a yeast VMA3-deficient strain. J Exp Bot. 2002 Nov;53(378):2273-5.The A. acetabulum protein AcVP complements a homologous mutation in S. cerevisiae.
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
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