VTC1B_DANRE
ID VTC1B_DANRE Reviewed; 381 AA.
AC Q5XIY6; Q801V4;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=V-type proton ATPase subunit C 1-B;
DE Short=V-ATPase subunit C 1-B;
DE AltName: Full=Vacuolar proton pump subunit C 1-B;
GN Name=atp6v1c1b; Synonyms=atp6v1c1l; ORFNames=si:ch211-215i13.2, zgc:92684;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase),
CC a multisubunit enzyme composed of a peripheral complex (V1) that
CC hydrolyzes ATP and a membrane integral complex (V0) that translocates
CC protons (By similarity). V-ATPase is responsible for acidifying and
CC maintaining the pH of intracellular compartments and in some cell
CC types, is targeted to the plasma membrane, where it is responsible for
CC acidifying the extracellular environment (By similarity). Subunit C is
CC necessary for the assembly of the catalytic sector of the enzyme and is
CC likely to have a specific function in its catalytic activity (By
CC similarity). {ECO:0000250|UniProtKB:P21282,
CC ECO:0000250|UniProtKB:P21283, ECO:0000250|UniProtKB:P31412}.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme made up of two
CC complexes: the ATP-hydrolytic V1 complex and the proton translocation
CC V0 complex (By similarity). The V1 complex consists of three catalytic
CC AB heterodimers that form a heterohexamer, three peripheral stalks each
CC consisting of EG heterodimers, one central rotor including subunits D
CC and F, and the regulatory subunits C and H (By similarity). The proton
CC translocation complex V0 consists of the proton transport subunit a, a
CC ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f,
CC and two accessory subunits (By similarity).
CC {ECO:0000250|UniProtKB:P21283}.
CC -!- SIMILARITY: Belongs to the V-ATPase C subunit family. {ECO:0000305}.
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DR EMBL; AL807244; CAD87802.2; -; Genomic_DNA.
DR EMBL; BC083532; AAH83532.1; -; mRNA.
DR RefSeq; NP_001005772.2; NM_001005772.2.
DR AlphaFoldDB; Q5XIY6; -.
DR SMR; Q5XIY6; -.
DR STRING; 7955.ENSDARP00000052090; -.
DR PaxDb; Q5XIY6; -.
DR Ensembl; ENSDART00000052091; ENSDARP00000052090; ENSDARG00000035880.
DR Ensembl; ENSDART00000180493; ENSDARP00000147230; ENSDARG00000112507.
DR GeneID; 449655; -.
DR KEGG; dre:449655; -.
DR CTD; 449655; -.
DR ZFIN; ZDB-GENE-041010-104; atp6v1c1b.
DR eggNOG; KOG2909; Eukaryota.
DR GeneTree; ENSGT00390000004263; -.
DR HOGENOM; CLU_017554_3_0_1; -.
DR InParanoid; Q5XIY6; -.
DR OMA; GEYWLIS; -.
DR OrthoDB; 1016088at2759; -.
DR PhylomeDB; Q5XIY6; -.
DR TreeFam; TF314912; -.
DR PRO; PR:Q5XIY6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 19.
DR Bgee; ENSDARG00000035880; Expressed in pharyngeal gill and 28 other tissues.
DR GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; IBA:GO_Central.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
DR CDD; cd14785; V-ATPase_C; 1.
DR InterPro; IPR004907; ATPase_V1-cplx_csu.
DR InterPro; IPR036132; Vac_ATP_synth_c_sf.
DR PANTHER; PTHR10137; PTHR10137; 1.
DR Pfam; PF03223; V-ATPase_C; 1.
DR SUPFAM; SSF118203; SSF118203; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Hydrogen ion transport; Ion transport; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..381
FT /note="V-type proton ATPase subunit C 1-B"
FT /id="PRO_0000285667"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 381 AA; 43943 MW; 2EA98A20FB1E5A1F CRC64;
MTEFWLISAP GDKTCQQTWD KMNMATAESN NLSTNNKFNI PELKVGTLDV LVGLSDELAK
LDTFVESVVK KIAQYMTDVL EDSRDKVQEN LLANGVDLVT YITRFQWDMA KYPIKQSLKS
ISEIMSKQVT QIDNDLKARA SAYNSLKGSL QSLERKNVGS LLTRSLADIV KKEDFVLDSE
YLTTLLVIVS KTNYPEWQKT YETLSEMVVP RSTKLLFEDQ ESGLFSVTLF TKAIDDFKQQ
ARENKFMVRD FLYNEEEMKA DKEEMTRLST DKKKQFGPLV RWLKVNFSET FIAWIHIKAL
RVFTESVLRY GLPVNFQAML LQPNKKNVKK LREVLKDLYK HLDSSAAVID GSVDIPGLNL
SQQEYYPYVY YKIDVNLLEL K
