ID   VTC1A_DANRE             Reviewed;         383 AA.
AC   Q7T385;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=V-type proton ATPase subunit C 1-A;
DE            Short=V-ATPase subunit C 1-A;
DE   AltName: Full=Vacuolar proton pump subunit C 1-A;
GN   Name=atp6v1c1a; Synonyms=atp6v1c1; ORFNames=zgc:64034;
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 MRNA].
RC   TISSUE=Kidney;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUN-2003) 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; BC053214; AAH53214.1; -; mRNA.
DR   RefSeq; NP_958479.1; NM_201322.1.
DR   AlphaFoldDB; Q7T385; -.
DR   SMR; Q7T385; -.
DR   STRING; 7955.ENSDARP00000029343; -.
DR   PaxDb; Q7T385; -.
DR   PRIDE; Q7T385; -.
DR   Ensembl; ENSDART00000032275; ENSDARP00000029343; ENSDARG00000023967.
DR   Ensembl; ENSDART00000191807; ENSDARP00000147247; ENSDARG00000023967.
DR   GeneID; 368907; -.
DR   KEGG; dre:368907; -.
DR   CTD; 368907; -.
DR   ZFIN; ZDB-GENE-030616-612; atp6v1c1a.
DR   eggNOG; KOG2909; Eukaryota.
DR   GeneTree; ENSGT00390000004263; -.
DR   HOGENOM; CLU_017554_3_0_1; -.
DR   InParanoid; Q7T385; -.
DR   OMA; YLDWQKT; -.
DR   OrthoDB; 1016088at2759; -.
DR   PhylomeDB; Q7T385; -.
DR   TreeFam; TF314912; -.
DR   Reactome; R-DRE-1222556; ROS and RNS production in phagocytes.
DR   Reactome; R-DRE-77387; Insulin receptor recycling.
DR   Reactome; R-DRE-917977; Transferrin endocytosis and recycling.
DR   Reactome; R-DRE-9639288; Amino acids regulate mTORC1.
DR   Reactome; R-DRE-983712; Ion channel transport.
DR   PRO; PR:Q7T385; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 16.
DR   Bgee; ENSDARG00000023967; Expressed in brain and 28 other tissues.
DR   ExpressionAtlas; Q7T385; baseline and differential.
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..383
FT                   /note="V-type proton ATPase subunit C 1-A"
FT                   /id="PRO_0000285666"
FT   MOD_RES         2
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   383 AA;  44315 MW;  A2B0EF6CC2A4F203 CRC64;
     MTEFWLISAP GEKTCQQTWD KLMTATTRTN NLSTNNKFNI PDLKVGTLDV LVGLSDELAK
     LDAFVESVVK KVAQYMADVL EDSRDKVQEN LLANGVDLVT YVTRFQWDMA KYPIKQSLKN
     ISEIISKQVS QIDNDLKARA SAYNNLKGNL QNLERKNAGS LLTRSLADIV KKDDFVLDSE
     YLITLLVVVP KTNYTDWQRT YETLAEMVVP RSTNLLFEDH DSGLFTVTLF RKAIDDFRHK
     ARENKFTVRD FQYNEEEMKA DKEEMTRLST DKKKQFGPLV RWLKVNFSEA FIAWVHIKAL
     RVFVESVLRY GLPVNFQAML LQPNKKNMKK LREVLYDLYK HLDSSAAAII DQSAMDIPGL
     NLSQQEYYPY VYYKIDCNLL DFK