VATH_BOVIN
ID VATH_BOVIN Reviewed; 483 AA.
AC O46563; A0A3Q1M3I3; F1MZL6; O46562; Q3ZBD5;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 3.
DT 03-AUG-2022, entry version 131.
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 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] (ISOFORMS ALPHA AND BETA).
RX PubMed=9488725; DOI=10.1074/jbc.273.10.5878;
RA Zhou Z., Peng S.-B., Crider B.P., Slaughter C., Xie X.-S., Stone D.K.;
RT "Molecular characterization of the 50- and 57-kDa subunits of the bovine
RT vacuolar proton pump.";
RL J. Biol. Chem. 273:5878-5884(1998).
RN [2] {ECO:0000312|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000312|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA).
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0007829|PDB:6XBW, ECO:0007829|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: 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 (PubMed:32764564). 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 (PubMed:32764564). Subunit H
CC is 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:P41807,
CC ECO:0000250|UniProtKB:Q9UI12, 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 AP2M1
CC (By similarity). {ECO:0000250|UniProtKB:Q9UI12,
CC ECO:0000269|PubMed:32764564}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC membrane {ECO:0000269|PubMed:32764564}; Peripheral membrane protein
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Alpha; Synonyms=57 kDa;
CC IsoId=O46563-1; Sequence=Displayed;
CC Name=Beta; Synonyms=50 kDa;
CC IsoId=O46563-2; Sequence=VSP_000442;
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level).
CC {ECO:0000269|PubMed:32764564}.
CC -!- SIMILARITY: Belongs to the V-ATPase H subunit family. {ECO:0000305}.
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DR EMBL; AF041338; AAC02987.1; -; mRNA.
DR EMBL; AF041337; AAC02986.1; -; mRNA.
DR EMBL; BC103432; AAI03433.1; -; mRNA.
DR RefSeq; NP_777129.2; NM_174704.3.
DR PDB; 6XBW; EM; 3.37 A; P=1-465.
DR PDB; 6XBY; EM; 3.79 A; P=1-465.
DR PDB; 7KHR; EM; 3.62 A; P=1-483.
DR PDBsum; 6XBW; -.
DR PDBsum; 6XBY; -.
DR PDBsum; 7KHR; -.
DR AlphaFoldDB; O46563; -.
DR SMR; O46563; -.
DR CORUM; O46563; -.
DR STRING; 9913.ENSBTAP00000004480; -.
DR PaxDb; O46563; -.
DR PRIDE; O46563; -.
DR Ensembl; ENSBTAT00000004482; ENSBTAP00000004482; ENSBTAG00000003450. [O46563-2]
DR Ensembl; ENSBTAT00000073116; ENSBTAP00000064695; ENSBTAG00000003450. [O46563-1]
DR GeneID; 282657; -.
DR KEGG; bta:282657; -.
DR CTD; 51606; -.
DR VEuPathDB; HostDB:ENSBTAG00000003450; -.
DR eggNOG; KOG2759; Eukaryota.
DR GeneTree; ENSGT00390000003289; -.
DR HOGENOM; CLU_025709_2_0_1; -.
DR InParanoid; O46563; -.
DR OMA; KDQNVRY; -.
DR OrthoDB; 751335at2759; -.
DR Reactome; R-BTA-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-BTA-9639288; Amino acids regulate mTORC1.
DR Proteomes; UP000009136; Chromosome 14.
DR Bgee; ENSBTAG00000003450; Expressed in Ammon's horn and 101 other tissues.
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; 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; 1.25.10.10; -; 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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasmic vesicle;
KW Hydrogen ion transport; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; Transport.
FT CHAIN 1..483
FT /note="V-type proton ATPase subunit H"
FT /id="PRO_0000124192"
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:9488725, ECO:0000303|Ref.3"
FT /id="VSP_000442"
FT CONFLICT 73
FT /note="C -> R (in Ref. 1; AAC02987/AAC02986)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="A -> T (in Ref. 1; AAC02987/AAC02986)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="A -> P (in Ref. 1; AAC02987/AAC02986)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="A -> V (in Ref. 3; AAI03433)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="E -> G (in Ref. 3; AAI03433)"
FT /evidence="ECO:0000305"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 87..100
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 121..129
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 135..149
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 158..172
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 198..208
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 212..222
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 225..231
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 239..249
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 254..260
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 265..273
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 281..294
FT /evidence="ECO:0007829|PDB:6XBW"
FT TURN 300..302
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 303..306
FT /evidence="ECO:0007829|PDB:6XBW"
FT TURN 307..311
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 315..323
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 329..347
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 353..361
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 368..371
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 373..378
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 382..385
FT /evidence="ECO:0007829|PDB:6XBW"
FT TURN 386..391
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 392..400
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 406..420
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 424..431
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 433..440
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 446..459
FT /evidence="ECO:0007829|PDB:6XBW"
SQ SEQUENCE 483 AA; 55824 MW; 4A63D92ADF408A62 CRC64;
MTKMDIRGAV DAAVPTNIIA AKAAEVRANK VNWQSYLQGQ MISSEDCEFI QRFEMKRSPE
EKQEMLQTEG SQCAKTFINL MTHISKEQTV QYILTLVDDT LQENHQRVSI FFDYAKRSKN
TAWSYFLPML NRQDLFTVHM AARIIAKLAA WGKELMEGSD LNYYFNWIKT QLSSQKLRGS
GVTAETGTVS SSDSSQYVQC VAGCLQLMLR VNEYRFAWVE ADGVNCIMGV LSNKCGFQLQ
YQMIFSVWLL AFSPQMCEHL RRYNIIPVLS DILQESVKEK VTRIILAAFR NFLEKSVERE
TRQEYALAMI QCKVLKQLEN LEQQKYDDED ISEDIKFLLE KLGESVQDLS SFDEYSSELK
SGRLEWSPVH KSEKFWRENA ARLNEKNYEL LKILTKLLEV SDDPQVLAVA AHDVGEYVRH
YPRGKRVIEQ LGGKQLVMNH MHHEDQQVRY NALLAVQKLM VHNWEYLGKQ LQSEQPQTAA
ARS
