VATL_BOVIN
ID VATL_BOVIN Reviewed; 155 AA.
AC P23956; Q3SZY0;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=V-type proton ATPase 16 kDa proteolipid subunit c {ECO:0000305};
DE Short=V-ATPase 16 kDa proteolipid subunit c {ECO:0000305};
DE AltName: Full=Vacuolar proton pump 16 kDa proteolipid subunit c {ECO:0000305};
GN Name=ATP6V0C; Synonyms=ATP6C, ATP6L;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2456571; DOI=10.1073/pnas.85.15.5521;
RA Mandel M., Moriyama Y., Hulmes J.D., Pan Y.-C.E., Nelson H., Nelson N.;
RT "cDNA sequence encoding the 16-kDa proteolipid of chromaffin granules
RT implies gene duplication in the evolution of H+-ATPases.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:5521-5524(1988).
RN [2]
RP SEQUENCE REVISION.
RA Nelson N.;
RL Submitted (JUN-1988) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 7-26.
RC TISSUE=Brain;
RX PubMed=2527163; DOI=10.1016/0014-5793(89)80917-2;
RA Dermietzel R., Voelker M., Hwang T.K., Berzborn R.J., Meyer H.E.;
RT "A 16 kDa protein co-isolating with gap junctions from brain tissue
RT belonging to the class of proteolipids of the vacuolar H+-ATPases.";
RL FEBS Lett. 253:1-5(1989).
RN [5] {ECO:0007744|PDB:6XBW, ECO:0007744|PDB:6XBY}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.37 ANGSTROMS), FUNCTION, IDENTIFICATION
RP IN THE V-ATPASE COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=32764564; DOI=10.1038/s41467-020-17762-9;
RA Wang R., Long T., Hassan A., Wang J., Sun Y., Xie X.S., Li X.;
RT "Cryo-EM structures of intact V-ATPase from bovine brain.";
RL Nat. Commun. 11:3921-3921(2020).
CC -!- FUNCTION: Proton-conducting pore forming of the V0 complex of
CC vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a
CC peripheral complex (V1) that hydrolyzes ATP and a membrane integral
CC complex (V0) that translocates protons (PubMed:32764564). V-ATPase is
CC responsible for acidifying and maintaining the pH of intracellular
CC compartments and in some cell types, is targeted to the plasma
CC membrane, where it is responsible for acidifying the extracellular
CC environment (PubMed:32764564). {ECO:0000269|PubMed:32764564}.
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 (PubMed:32764564). The V1 complex consists of three
CC catalytic AB heterodimers that form a heterohexamer, three peripheral
CC stalks each consisting of EG heterodimers, one central rotor including
CC subunits D and F, and the regulatory subunits C and H
CC (PubMed:32764564). The proton translocation complex V0 consists of the
CC proton transport subunit a, a ring of proteolipid subunits c9c'',
CC rotary subunit d, subunits e and f, and the accessory subunits
CC ATP6AP1/Ac45 and ATP6AP2/PRR (PubMed:32764564). Interacts with the V0
CC complex V-ATPase subunit a4 ATP6V0A4 (By similarity). Interacts with
CC LASS2 (By similarity). Interacts with RNF182; this interaction leads to
CC ubiquitination and degradation via the proteasome pathway (By
CC similarity). {ECO:0000250|UniProtKB:P27449,
CC ECO:0000250|UniProtKB:P63082, ECO:0000269|PubMed:32764564}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC membrane {ECO:0000269|PubMed:32764564}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle
CC membrane {ECO:0000250|UniProtKB:P63081}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level).
CC {ECO:0000269|PubMed:32764564}.
CC -!- PTM: Ubiquitinated by RNF182, leading to its degradation via the
CC ubiquitin-proteasome pathway. {ECO:0000250|UniProtKB:P27449}.
CC -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC {ECO:0000305}.
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DR EMBL; J03835; AAA30397.1; -; mRNA.
DR EMBL; BC102659; AAI02660.1; -; mRNA.
DR PIR; A31320; PXBOV6.
DR RefSeq; NP_001017954.1; NM_001017954.1.
DR PDB; 6XBW; EM; 3.37 A; c/g/k/l/m/n/o/p/q=1-155.
DR PDB; 6XBY; EM; 3.79 A; c/g/k/l/m/n/o/p/q=1-155.
DR PDB; 7KHR; EM; 3.62 A; c/g/k/l/m/n/o/p/q=1-155.
DR PDBsum; 6XBW; -.
DR PDBsum; 6XBY; -.
DR PDBsum; 7KHR; -.
DR AlphaFoldDB; P23956; -.
DR SMR; P23956; -.
DR CORUM; P23956; -.
DR IntAct; P23956; 1.
DR MINT; P23956; -.
DR PaxDb; P23956; -.
DR PRIDE; P23956; -.
DR GeneID; 550622; -.
DR KEGG; bta:550622; -.
DR CTD; 527; -.
DR eggNOG; KOG0232; Eukaryota.
DR HOGENOM; CLU_085752_1_2_1; -.
DR InParanoid; P23956; -.
DR OrthoDB; 1534092at2759; -.
DR TreeFam; TF300025; -.
DR Proteomes; UP000009136; Unplaced.
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:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IDA:UniProtKB.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0045851; P:pH reduction; IC:UniProtKB.
DR GO; GO:1902600; P:proton transmembrane transport; IC:UniProtKB.
DR Gene3D; 1.20.120.610; -; 1.
DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR InterPro; IPR000245; ATPase_proteolipid_csu.
DR InterPro; IPR011555; ATPase_proteolipid_su_C_euk.
DR InterPro; IPR035921; F/V-ATP_Csub_sf.
DR Pfam; PF00137; ATP-synt_C; 2.
DR PRINTS; PR00122; VACATPASE.
DR SUPFAM; SSF81333; SSF81333; 2.
DR TIGRFAMs; TIGR01100; V_ATP_synt_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasmic vesicle; Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW Synapse; Transmembrane; Transmembrane helix; Transport; Ubl conjugation.
FT CHAIN 1..155
FT /note="V-type proton ATPase 16 kDa proteolipid subunit c"
FT /id="PRO_0000071742"
FT TOPO_DOM 1..10
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..55
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..92
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..155
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT SITE 139
FT /note="Essential for proton translocation"
FT /evidence="ECO:0000305|PubMed:32764564"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 12..45
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 57..78
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 86..120
FT /evidence="ECO:0007829|PDB:6XBW"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 127..154
FT /evidence="ECO:0007829|PDB:6XBW"
SQ SEQUENCE 155 AA; 15720 MW; 326B20B5F7D7D607 CRC64;
MSEAKNGPEY ASFFAVMGAS AAMVFSALGA AYGTAKSGTG IAAMSVMRPE MIMKSIIPVV
MAGIIAIYGL VVAVLIANSL NDGISLYRSF LQLGAGLSVG LSGLAAGFAI GIVGDAGVRG
TAQQPRLFVG MILILIFAEV LGLYGLIVAL ILSTK
