VATH_PIG
ID VATH_PIG Reviewed; 483 AA.
AC Q9TVC1; Q9XSM4; Q9XSM5;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=V-type proton ATPase subunit H;
DE Short=V-ATPase subunit H;
DE AltName: Full=V-ATPase 50/57 kDa subunits;
DE AltName: Full=Vacuolar proton pump subunit H;
DE AltName: Full=Vacuolar proton pump subunit SFD;
GN Name=ATP6V1H;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS ALPHA AND BETA).
RC STRAIN=German Landrace; TISSUE=Liver;
RX PubMed=10051322; DOI=10.1007/s003359900984;
RA Hui D., Deppe A., Wen G., Leeb T., Masabanda J., Robic A.,
RA Baumgartner B.G., Fries R., Brenig B.;
RT "Molecular cloning and chromosomal assignment of the porcine 54 kDa and 56
RT kDa vacuolar H(+)-ATPase subunit gene (V-ATPase).";
RL Mamm. Genome 10:266-270(1999).
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 H is
CC essential for V-ATPase activity, but not for the assembly of the
CC complex (By similarity). Involved in the endocytosis mediated by
CC clathrin-coated pits, required for the formation of endosomes (By
CC similarity). {ECO:0000250|UniProtKB:O46563,
CC ECO:0000250|UniProtKB:P41807, ECO:0000250|UniProtKB:Q9UI12}.
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). Interacts with AP2M1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9UI12}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC membrane {ECO:0000250|UniProtKB:O46563}; Peripheral membrane protein
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Alpha; Synonyms=57 kDa;
CC IsoId=Q9TVC1-1; Sequence=Displayed;
CC Name=Beta; Synonyms=50 kDa;
CC IsoId=Q9TVC1-2; Sequence=VSP_000443;
CC -!- SIMILARITY: Belongs to the V-ATPase H 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; AJ223744; CAB39537.1; -; Genomic_DNA.
DR EMBL; AJ223745; CAB39537.1; JOINED; Genomic_DNA.
DR EMBL; AJ223746; CAB39537.1; JOINED; Genomic_DNA.
DR EMBL; AJ223747; CAB39537.1; JOINED; Genomic_DNA.
DR EMBL; AJ223748; CAB39537.1; JOINED; Genomic_DNA.
DR EMBL; AJ223749; CAB39537.1; JOINED; Genomic_DNA.
DR EMBL; AJ223750; CAB39537.1; JOINED; Genomic_DNA.
DR EMBL; AJ223751; CAB39537.1; JOINED; Genomic_DNA.
DR EMBL; AJ223752; CAB39537.1; JOINED; Genomic_DNA.
DR EMBL; AJ223753; CAB39537.1; JOINED; Genomic_DNA.
DR EMBL; AJ223754; CAB39537.1; JOINED; Genomic_DNA.
DR EMBL; AJ223755; CAB39537.1; JOINED; Genomic_DNA.
DR EMBL; AJ223756; CAB39537.1; JOINED; Genomic_DNA.
DR EMBL; AJ223757; CAB39532.1; -; mRNA.
DR EMBL; AJ223758; CAB39533.1; -; mRNA.
DR RefSeq; NP_999405.1; NM_214240.1.
DR RefSeq; XP_013848694.1; XM_013993240.1.
DR AlphaFoldDB; Q9TVC1; -.
DR SMR; Q9TVC1; -.
DR STRING; 9823.ENSSSCP00000006676; -.
DR PaxDb; Q9TVC1; -.
DR PeptideAtlas; Q9TVC1; -.
DR PRIDE; Q9TVC1; -.
DR GeneID; 397472; -.
DR KEGG; ssc:397472; -.
DR CTD; 51606; -.
DR eggNOG; KOG2759; Eukaryota.
DR InParanoid; Q9TVC1; -.
DR OrthoDB; 751335at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0030665; C:clathrin-coated 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:InterPro.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 1.25.40.150; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR004908; ATPase_V1-cplx_hsu.
DR InterPro; IPR011987; ATPase_V1-cplx_hsu_C.
DR InterPro; IPR038497; ATPase_V1-cplx_hsu_C_sf.
DR PANTHER; PTHR10698; PTHR10698; 1.
DR Pfam; PF11698; V-ATPase_H_C; 1.
DR Pfam; PF03224; V-ATPase_H_N; 1.
DR PIRSF; PIRSF032184; ATPase_V1_H; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasmic vesicle; Hydrogen ion transport;
KW Ion transport; Membrane; Phosphoprotein; Reference proteome; Transport.
FT CHAIN 1..483
FT /note="V-type proton ATPase subunit H"
FT /id="PRO_0000124195"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UI12"
FT VAR_SEQ 176..193
FT /note="Missing (in isoform Beta)"
FT /evidence="ECO:0000303|PubMed:10051322"
FT /id="VSP_000443"
FT VARIANT 173
FT /note="A -> S"
FT CONFLICT 408
FT /note="A -> R (in Ref. 1; CAB39532)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 483 AA; 55850 MW; CB72E44A3FADD290 CRC64;
MTKMDIRGAV DAAVPTNIIA AKAAEVRANK VNWQSYLQGQ MISSEDCEFI QRFEMKRSPE
EKQEMLQTEG SQCAKTFINL MTHISKEQTV QYILTMVDDT LQENHQRVSI FFDYAKRSKN
TAWSYFLPML NRQDLFTVHM AARIIAKLAA WGKELMEGSD LNYYFNWIKT QLASQKLRGS
GVAVETGTVS SSDSSQYVQC VAGCLQLMLR VNEYRFAWVE ADGVNCIMGV LSNKCGFQLQ
YQMIFSIWLL AFSPQMCEHL RRYNIIPVLS DILQESVKEK VTRIILAAFR NFLEKSTERE
TRQEYALALI QCKVLKQLEN LEQQKYDDED ISEDIKFLLE KLGESVQDLS SFDEYSSELK
SGRLEWSPVH KSEKFWRENA VRLNEKNYEL LKILTKLLEV SDDPQVLAVA AHDVGEYVRH
YPRGKRVIEQ LGGKQLVMNH MHHEDQQVRY NALLAVQKLM VHNWEYLGKQ LQSEQPQTAA
ARS
