VMAT2_RAT
ID VMAT2_RAT Reviewed; 515 AA.
AC Q01827; Q9QVP1;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2003, sequence version 2.
DT 25-MAY-2022, entry version 155.
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=Svat, Vmat2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1505023; DOI=10.1016/0092-8674(92)90425-c;
RA Liu Y., Peter D., Roghani A., Schuldiner S., Prive G.G., Eisenberg D.,
RA Brecha N., Edwards R.H.;
RT "A cDNA that suppresses MPP+ toxicity encodes a vesicular amine
RT transporter.";
RL Cell 70:539-551(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1438304; DOI=10.1073/pnas.89.22.10993;
RA Erickson J.D., Eiden L.E., Hoffman B.J.;
RT "Expression cloning of a reserpine-sensitive vesicular monoamine
RT transporter.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:10993-10997(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Gastric corpus;
RX PubMed=8745292; DOI=10.1113/jphysiol.1996.sp021140;
RA Dimaline R., Struthers J.;
RT "Expression and regulation of a vesicular monoamine transporter in rat
RT stomach: a putative histamine transporter.";
RL J. Physiol. (Lond.) 490:249-256(1996).
RN [4]
RP PHOSPHORYLATION AT SER-512 AND SER-514.
RX PubMed=9045708; DOI=10.1074/jbc.272.10.6752;
RA Krantz D.E., Peter D., Lui Y., Edwards R.H.;
RT "Phosphorylation of a vesicular monoamine transporter by casein kinase
RT II.";
RL J. Biol. Chem. 272:6752-6759(1997).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512 AND SER-514, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- TISSUE SPECIFICITY: Brainstem and stomach.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Vesicular
CC transporter family. {ECO:0000305}.
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DR EMBL; M97381; AAA42190.1; -; mRNA.
DR EMBL; L00603; AAA41627.1; -; mRNA.
DR PIR; A46374; A46374.
DR RefSeq; NP_037163.1; NM_013031.1.
DR RefSeq; XP_006231726.1; XM_006231664.3.
DR RefSeq; XP_017444313.1; XM_017588824.1.
DR AlphaFoldDB; Q01827; -.
DR SMR; Q01827; -.
DR BioGRID; 247580; 2.
DR CORUM; Q01827; -.
DR STRING; 10116.ENSRNOP00000011983; -.
DR BindingDB; Q01827; -.
DR ChEMBL; CHEMBL4828; -.
DR DrugCentral; Q01827; -.
DR GuidetoPHARMACOLOGY; 1012; -.
DR GlyGen; Q01827; 5 sites.
DR iPTMnet; Q01827; -.
DR PhosphoSitePlus; Q01827; -.
DR PaxDb; Q01827; -.
DR PRIDE; Q01827; -.
DR ABCD; Q01827; 1 sequenced antibody.
DR GeneID; 25549; -.
DR KEGG; rno:25549; -.
DR CTD; 6571; -.
DR RGD; 3694; Slc18a2.
DR eggNOG; KOG3764; Eukaryota.
DR InParanoid; Q01827; -.
DR OrthoDB; 956763at2759; -.
DR PhylomeDB; Q01827; -.
DR TreeFam; TF313494; -.
DR Reactome; R-RNO-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-RNO-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-RNO-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-RNO-442660; Na+/Cl- dependent neurotransmitter transporters.
DR PRO; PR:Q01827; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0043679; C:axon terminus; IDA:RGD.
DR GO; GO:0044297; C:cell body; IDA:RGD.
DR GO; GO:0042995; C:cell projection; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0031045; C:dense core granule; IDA:RGD.
DR GO; GO:0098691; C:dopaminergic synapse; IDA:SynGO.
DR GO; GO:0099066; C:integral component of neuronal dense core vesicle membrane; IDA:SynGO.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0098992; C:neuronal dense core vesicle; IDA:SynGO.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:RGD.
DR GO; GO:0043195; C:terminal bouton; IDA:RGD.
DR GO; GO:0005275; F:amine transmembrane transporter activity; IDA:RGD.
DR GO; GO:0019899; F:enzyme binding; IPI:RGD.
DR GO; GO:0031072; F:heat shock protein binding; IPI:RGD.
DR GO; GO:1901363; F:heterocyclic compound binding; IPI:RGD.
DR GO; GO:0005335; F:serotonin:sodium symporter activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0007568; P:aging; IDA:RGD.
DR GO; GO:0015842; P:aminergic neurotransmitter loading into synaptic vesicle; IMP:RGD.
DR GO; GO:0071242; P:cellular response to ammonium ion; IEP:RGD.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IMP:RGD.
DR GO; GO:0032456; P:endocytic recycling; IEP:RGD.
DR GO; GO:0042593; P:glucose homeostasis; IDA:RGD.
DR GO; GO:0030073; P:insulin secretion; IDA:RGD.
DR GO; GO:0007626; P:locomotory behavior; ISO:RGD.
DR GO; GO:0015844; P:monoamine transport; IDA:RGD.
DR GO; GO:0051589; P:negative regulation of neurotransmitter transport; IMP:RGD.
DR GO; GO:0098700; P:neurotransmitter loading into synaptic vesicle; ISO:RGD.
DR GO; GO:0006836; P:neurotransmitter transport; IDA:RGD.
DR GO; GO:0009791; P:post-embryonic development; ISO:RGD.
DR GO; GO:0001975; P:response to amphetamine; IEP:RGD.
DR GO; GO:0042220; P:response to cocaine; IEP:RGD.
DR GO; GO:0051412; P:response to corticosterone; IEP:RGD.
DR GO; GO:0009635; P:response to herbicide; IEP:RGD.
DR GO; GO:0010038; P:response to metal ion; IEP:RGD.
DR GO; GO:0042594; P:response to starvation; IEP:RGD.
DR GO; GO:0009636; P:response to toxic substance; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0010043; P:response to zinc ion; IEP:RGD.
DR GO; GO:0051610; P:serotonin uptake; IMP:RGD.
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; Disulfide bond; Glycoprotein; Membrane;
KW Neurotransmitter transport; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..515
FT /note="Synaptic vesicular amine transporter"
FT /id="PRO_0000127516"
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..130
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..190
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..220
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..249
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..292
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..329
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 354..358
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 380..390
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 412..415
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 437..441
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 442..463
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 464..515
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 512
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:9045708,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 514
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:9045708,
FT ECO:0007744|PubMed:22673903"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 118..325
FT /evidence="ECO:0000250"
FT CONFLICT 220..221
FT /note="KP -> NA (in Ref. 2; AAA41627)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="G -> F (in Ref. 1; AAA42190)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="R -> T (in Ref. 2; AAA41627)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 515 AA; 55690 MW; 627A904C1D35D552 CRC64;
MALSDLVLLR WLRDSRHSRK LILFIVFLAL LLDNMLLTVV VPIIPSYLYS IKHEKNSTEI
QTTRPELVVS TSESIFSYYN NSTVLITGNA TGTLPGGQSH KATSTQHTVA NTTVPSDCPS
EDRDLLNENV QVGLLFASKA TVQLLTNPFI GLLTNRIGYP IPMFAGFCIM FISTVMFAFS
SSYAFLLIAR SLQGIGSSCS SVAGMGMLAS VYTDDEERGK PMGIALGGLA MGVLVGPPFG
SVLYEFVGKT APFLVLAALV LLDGAIQLFV LQPSRVQPES QKGTPLTTLL KDPYILIAAG
SICFANMGIA MLEPALPIWM METMCSRKWQ LGVAFLPASI SYLIGTNIFG ILAHKMGRWL
CALLGMVIVG ISILCIPFAK NIYGLIAPNF GVGFAIGMVD SSMMPIMGYL VDLRHVSVYG
SVYAIADVAF CMGYAIGPSA GGAIAKAIGF PWLMTIIGII DIAFAPLCFF LRSPPAKEEK
MAILMDHNCP IKRKMYTQNN VQSYPIGDDE ESESD
