VMAT2_BOVIN
ID VMAT2_BOVIN Reviewed; 517 AA.
AC Q27963; Q28211;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Synaptic vesicular amine transporter;
DE AltName: Full=Monoamine transporter;
DE AltName: Full=Solute carrier family 18 member 2;
DE AltName: Full=Vesicular amine transporter 2;
DE Short=VAT2;
GN Name=SLC18A2; Synonyms=VMAT2;
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=8307150; DOI=10.1016/0014-5793(94)80108-8;
RA Howell M.L., Shirvan A., Stern-Bach Y., Steiner-Mordach S., Dean G.E.,
RA Schuldiner S.;
RT "Cloning and functional expression of a tetrabenazine sensitive vesicular
RT monoamine transporter from bovine chromaffin granules.";
RL FEBS Lett. 338:16-22(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Adrenal medulla;
RX PubMed=7902299; DOI=10.1016/0014-5793(93)80432-t;
RA Krejci E., Gasnier B., Botton D., Isambert M.-F., Sagne C., Gagnon J.,
RA Massoulie J., Henry J.-P.;
RT "Expression and regulation of the bovine vesicular monoamine transporter
RT gene.";
RL FEBS Lett. 335:27-32(1993).
RN [3]
RP PROTEIN SEQUENCE OF 3-30 AND 294-302.
RX PubMed=1357668; DOI=10.1073/pnas.89.20.9730;
RA Stern-Bach Y., Keen J.N., Bejerano M., Steiner-Mordoch S., Wallach M.,
RA Findlay J.B.C., Schuldiner S.;
RT "Homology of a vesicular amine transporter to a gene conferring resistance
RT to 1-methyl-4-phenylpyridinium.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:9730-9733(1992).
CC -!- FUNCTION: Involved in the ATP-dependent vesicular transport of biogenic
CC amine neurotransmitters. Pumps cytosolic monoamines including dopamine,
CC norepinephrine, serotonin, and histamine into synaptic vesicles.
CC Requisite for vesicular amine storage prior to secretion via
CC exocytosis.
CC -!- SUBUNIT: Interacts with SLC6A3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Multi-pass membrane
CC protein.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Vesicular
CC transporter family. {ECO:0000305}.
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DR EMBL; U02876; AAA18333.1; -; mRNA.
DR EMBL; X76380; CAA53970.1; -; mRNA.
DR PIR; S41081; S41081.
DR RefSeq; NP_777078.1; NM_174653.2.
DR AlphaFoldDB; Q27963; -.
DR SMR; Q27963; -.
DR STRING; 9913.ENSBTAP00000006221; -.
DR BindingDB; Q27963; -.
DR ChEMBL; CHEMBL4271; -.
DR DrugCentral; Q27963; -.
DR PaxDb; Q27963; -.
DR PRIDE; Q27963; -.
DR GeneID; 282471; -.
DR KEGG; bta:282471; -.
DR CTD; 6571; -.
DR eggNOG; KOG3764; Eukaryota.
DR InParanoid; Q27963; -.
DR OrthoDB; 956763at2759; -.
DR PRO; PR:Q27963; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0042583; C:chromaffin granule; IDA:AgBase.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0097159; F:organic cyclic compound binding; IDA:AgBase.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
DR GO; GO:0035864; P:response to potassium ion; IDA:AgBase.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR004734; Multidrug-R.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00880; 2_A_01_02; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Membrane; Neurotransmitter transport; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..517
FT /note="Synaptic vesicular amine transporter"
FT /id="PRO_0000127513"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..132
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..192
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..251
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 275..294
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..331
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..360
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 382..392
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 414..417
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 439..443
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 444..465
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 466..517
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 514
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:Q01827"
FT MOD_RES 516
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:Q01827"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 120..327
FT /evidence="ECO:0000250"
FT CONFLICT 63
FT /note="A -> T (in Ref. 2; CAA53970)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="T -> S (in Ref. 2; CAA53970)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="Y -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="A -> K (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="L -> SF (in Ref. 2; CAA53970)"
FT /evidence="ECO:0000305"
FT CONFLICT 474..476
FT /note="RSP -> SKS (in Ref. 2; CAA53970)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 517 AA; 55756 MW; 8FD24BDBBF4D85E9 CRC64;
MALSELALLR RLQESRHSRK LILFIVFLAL LLDNMLLTVV VPIIPSYLYS IEHEKDALEI
QTAKPGLTAS APGSFQNIFS YYDNSTMVTG NSTDHLQGAL VHEATTQHMA TNSSSASSDC
PSEDKDLLNE NVQVGLLFAS KATVQLLTNP FIGLLTNRIG YPIPMFTGFC IMFISTVMFA
FSRTYAFLLI ARSLQGIGSS CSSVAGMGML ASVYTDDEER GNAMGIALGG LAMGVLVGPP
FGSVLYEFVG KTAPFLVLAA LVLLDGAIQL FVLQPSRVQP ESQKGTPLTT LLRDPYILIA
AGSICFANMG IAMLEPALPI WMMETMCSHK WQLGVAFLPA SVSYLIGTNV FGILAHKMGR
WLCALLGMII VGMSILCIPL AKNIYGLIAP NFGVGFAIGM VDSSMMPIMG YLVDLRHVSV
YGSVYAIADV AFCMGYAIGP SAGGAIAKAI GFPWLMTIIG IIDILFAPLC FFLRSPPAKE
EKMAILMDHN CPIKTKMYTQ NSSQSHPIGE DEESESD
