VPP2_BOVIN
ID VPP2_BOVIN Reviewed; 854 AA.
AC O97681;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=V-type proton ATPase 116 kDa subunit a 2;
DE Short=V-ATPase 116 kDa subunit a 2;
DE AltName: Full=Vacuolar proton translocating ATPase 116 kDa subunit a isoform 2;
GN Name=ATP6V0A2; Synonyms=ATP6N1B;
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=9891027; DOI=10.1074/jbc.274.4.2549;
RA Peng S.-B., Li X., Crider B.P., Zhou Z., Andersen P., Tsai S.J., Xie X.-S.,
RA Stone D.K.;
RT "Identification and reconstitution of an isoform of the 116-kDa subunit of
RT the vacuolar proton translocating ATPase.";
RL J. Biol. Chem. 274:2549-2555(1999).
CC -!- FUNCTION: Subunit of the V0 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). Essential
CC component of the endosomal pH-sensing machinery (By similarity). May
CC play a role in maintaining the Golgi functions, such as glycosylation
CC maturation, by controlling the Golgi pH (By similarity). In aerobic
CC conditions, involved in intracellular iron homeostasis, thus triggering
CC the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to
CC HIF1A hydroxylation and subsequent proteasomal degradation (By
CC similarity). {ECO:0000250|UniProtKB:Q29466,
CC ECO:0000250|UniProtKB:Q9Y487}.
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). Directly interacts with PSCD2 through its N-terminal
CC cytosolic tail in an intra-endosomal acidification-dependent manner (By
CC similarity). Disruption of this interaction results in the inhibition
CC of endocytosis (By similarity). Interacts with SPAAR (By similarity).
CC {ECO:0000250|UniProtKB:Q29466, ECO:0000250|UniProtKB:Q9Y487}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Endosome membrane {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in lung, kidney and spleen.
CC -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC {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; AF105016; AAD12058.1; -; mRNA.
DR RefSeq; NP_788810.1; NM_176637.2.
DR AlphaFoldDB; O97681; -.
DR SMR; O97681; -.
DR STRING; 9913.ENSBTAP00000009563; -.
DR PaxDb; O97681; -.
DR PRIDE; O97681; -.
DR Ensembl; ENSBTAT00000009563; ENSBTAP00000009563; ENSBTAG00000007272.
DR GeneID; 338038; -.
DR KEGG; bta:338038; -.
DR CTD; 23545; -.
DR VEuPathDB; HostDB:ENSBTAG00000007272; -.
DR VGNC; VGNC:26308; ATP6V0A2.
DR eggNOG; KOG2189; Eukaryota.
DR GeneTree; ENSGT00950000182881; -.
DR HOGENOM; CLU_005230_0_0_1; -.
DR InParanoid; O97681; -.
DR OMA; MIFFKWL; -.
DR OrthoDB; 181796at2759; -.
DR TreeFam; TF300346; -.
DR Reactome; R-BTA-1222556; ROS and RNS production in phagocytes.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000007272; Expressed in conceptus and 107 other tissues.
DR GO; GO:0001669; C:acrosomal vesicle; ISS:AgBase.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IBA:GO_Central.
DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR GO; GO:0051117; F:ATPase binding; IBA:GO_Central.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0006879; P:cellular iron ion homeostasis; ISS:UniProtKB.
DR GO; GO:0036295; P:cellular response to increased oxygen levels; ISS:UniProtKB.
DR GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
DR InterPro; IPR002490; V-ATPase_116kDa_su.
DR InterPro; IPR026028; V-type_ATPase_116kDa_su_euka.
DR PANTHER; PTHR11629; PTHR11629; 1.
DR Pfam; PF01496; V_ATPase_I; 1.
DR PIRSF; PIRSF001293; ATP6V0A1; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Endosome; Hydrogen ion transport; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..854
FT /note="V-type proton ATPase 116 kDa subunit a 2"
FT /id="PRO_0000119215"
FT TOPO_DOM 1..393
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 413..414
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..431
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 432..445
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..475
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 476..549
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 550..569
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 570..587
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 588..608
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 609..651
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 652..671
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 672..739
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 740..764
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 765..785
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 786..824
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 825..854
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 695
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y487"
FT MOD_RES 700
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15920"
SQ SEQUENCE 854 AA; 98010 MW; 8BD9A128465CCED5 CRC64;
MGSLFRSETM CLAQLFLQSG TAYECLSVLG EKGLVEFRDL NQNVSSFQRK FVGEVKRCEE
LERILAYLVQ EINRADIPLP EGDTSPPAPP LKQVLEMQEQ LQKLEVELRE VTKNKEKLRK
NLLELIEYTH MLRVTKTFVK RNVEFEPTYE EFPPLENESL LDYSCMQRLG AKLGFVSGLI
NQGKVEAFEK MLWRVCKGYT IVTYAELDEP LEDPETGEVI KWYVFLISFW GEQIGHKVKK
ICDCYHCHVY PYPNTAEERR EIQEGLNTRI QDLYTVLHKT EDYLRQVLCK AAESVYSRVI
QVKKMKAIYH MLNMCSFDVT NKCLIAEVWC PEADLHELRR ALEEGSRESG GTIPSFMNTI
PTKETPPTLI RTNKFTEGFQ NIVDAYGVGS YQEVNPALFT IITFPFLFAV MFGDFGHGFV
MFLFALLLVL NENHPRLNQS QEIMRMFFNG RYILLLMGLF SVYTGLIYND CFSKSVNLFG
SRWNVSAMYS SSHSPEEQRK MVLWNDSIVR HHSVLQLDPS VPGVFRGPYP FGIDPIWNLA
TNRLTFLNSF KMKMSVILGI THMTFGVILG IFNHLHFRKK FNICLVSIPE LLFMLCIFGY
LIFMIIYKWL VYSAETSRTA PSILIEFISM FLFLASDTGG LYPGQEHVQR LLLLITVLSV
PVLFLGKPLF LLWLHRGRSC FGVGRSGYTL VRKDSEEEVS LLGGQDIEEG NNQMEDGCRE
VTCEEFDFGE ILMTQIIHSI EYCLGCISNT ASYLRLWALS LAHAQLSEVL WAMLMHVGLR
VDTAYGVLVL LPVIAFFAVL TIFILLIMEG LSAFLHAIRL HWVEFQNKFY VGAGTKFVPF
SFRLLSSKFS DDLA
