ID   VATC1_XENLA             Reviewed;         382 AA.
AC   Q5XH14;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 67.
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   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Xenopus Gene Collection (XGC) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC084262; AAH84262.1; -; mRNA.
DR   RefSeq; NP_001088261.1; NM_001094792.1.
DR   RefSeq; XP_018122121.1; XM_018266632.1.
DR   AlphaFoldDB; Q5XH14; -.
DR   SMR; Q5XH14; -.
DR   DNASU; 495092; -.
DR   GeneID; 495092; -.
DR   KEGG; xla:495092; -.
DR   CTD; 495092; -.
DR   Xenbase; XB-GENE-948415; atp6v1c1.L.
DR   OMA; YLDWQKT; -.
DR   OrthoDB; 1016088at2759; -.
DR   Proteomes; UP000186698; Chromosome 6L.
DR   Bgee; 495092; Expressed in brain and 19 other tissues.
DR   GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
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..382
FT                   /note="V-type proton ATPase subunit C 1"
FT                   /id="PRO_0000285668"
FT   MOD_RES         2
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   382 AA;  43995 MW;  F88093438A6E2168 CRC64;
     MTEFWLISAP GEKTCQQTWE KLMAATTKNN NLSTNAKFNI PDLKVGTLDV LVGLSDELAK
     LDAFVEGAVK KVAQYMADVL EDSRDKVQEN LLANGVDLVT YITRFQWDMA KYPIKQSLKN
     ISEIIAKGVT QIDNDLKARA SAYNNLKGNL QNLERKNAGS LITRSLAEIV KKDDFVLDSE
     YLITLLVVVP KNNYTDWMKE YETLSEMVVP RSSNVLSEDQ DSYLCNVTLF RKAVDDFRHK
     ARENKFVVRD FQYNEEEMKA DKEEMNRLST DKKKQFGPLV RWLKVNFSEA FIAWIHVKAL
     RVFVESVLRY GLPVNFQAML LQPNKKTMKK LREVLNDLYK HLDSSAASII DAPMDIPGLN
     LSQQEYYPYV YYKIDCNLLE FK