ID   VATC1_PONAB             Reviewed;         382 AA.
AC   Q5RDQ7; Q5R4F1; Q5R4Z5;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=V-type proton ATPase subunit C 1;
DE            Short=V-ATPase subunit C 1;
DE   AltName: Full=Vacuolar proton pump subunit C 1;
GN   Name=ATP6V1C1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-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 the accessory subunits ATP6AP1/Ac45 and ATP6AP2/PRR (By
CC       similarity). {ECO:0000250|UniProtKB:P21283}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC       vesicle membrane {ECO:0000250|UniProtKB:Q5FVI6}; Peripheral membrane
CC       protein {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle
CC       membrane {ECO:0000250|UniProtKB:Q5FVI6}; Peripheral membrane protein
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the V-ATPase C subunit family. {ECO:0000305}.
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DR   EMBL; CR857846; CAH90100.1; -; mRNA.
DR   EMBL; CR861092; CAH93171.1; -; mRNA.
DR   EMBL; CR861298; CAH93365.1; -; mRNA.
DR   RefSeq; NP_001125006.1; NM_001131534.1.
DR   AlphaFoldDB; Q5RDQ7; -.
DR   SMR; Q5RDQ7; -.
DR   STRING; 9601.ENSPPYP00000021093; -.
DR   Ensembl; ENSPPYT00000021936; ENSPPYP00000021093; ENSPPYG00000018803.
DR   GeneID; 100171885; -.
DR   KEGG; pon:100171885; -.
DR   CTD; 528; -.
DR   eggNOG; KOG2909; Eukaryota.
DR   GeneTree; ENSGT00390000004263; -.
DR   InParanoid; Q5RDQ7; -.
DR   OrthoDB; 1016088at2759; -.
DR   Proteomes; UP000001595; Chromosome 8.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; ISS:UniProtKB.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:Ensembl.
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; Cytoplasmic vesicle; Hydrogen ion transport; Ion transport;
KW   Membrane; Reference proteome; Synapse; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P21283"
FT   CHAIN           2..382
FT                   /note="V-type proton ATPase subunit C 1"
FT                   /id="PRO_0000307373"
FT   MOD_RES         2
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P21283"
FT   CONFLICT        207
FT                   /note="M -> R (in Ref. 1; CAH93365)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        312
FT                   /note="L -> S (in Ref. 1; CAH93171)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   382 AA;  43942 MW;  5626E2AB2BD66BA7 CRC64;
     MTEFWLISAP GEKTCQQTWE KLHAATSKNN NLAVTSKFNI PDLKVGTLDV LVGLSDELAK
     LDAFVEGVVK KVAQYMADVL EDSKDKVQEN LLANGVDLVT YITRFQWDMA KYPIKQSLKN
     ISEIIAKGVT QIDNDLKSRA SAYNNLKGNL QNLERKNAGS LLTRSLAEIV KKDDFVLDSE
     YLVTLLVVVP KLNHNDWIKQ YETLAEMVVP RSSNVLSEDQ DSYLCNVTLF RKAVDDFRHK
     ARENKFIVRD FQYNEEEMKA DKEEMNRLST DKKKQFGPLV RWLKVNFSEA FIAWIHVKAL
     RVFVESVLRY GLPVNFQAML LQPNKKTLKK LREVLHELYK HLDSSAAAII DAPMDIPGLN
     LSQQEYYPYV YYKIDCNLLE FK