VMAT2_MOUSE
ID VMAT2_MOUSE Reviewed; 517 AA.
AC Q8BRU6; Q8CC55;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 154.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Gilsbach R., Bonisch H., Bruess M.;
RT "Molecular cloning and pharmacological characterization of the mouse
RT vesicular monoamine transporter 2 (mVMAT2).";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Aorta, Diencephalon, and Vein;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP INTERACTION WITH SLC6A3.
RX PubMed=19357284; DOI=10.1523/jneurosci.4559-08.2009;
RA Egana L.A., Cuevas R.A., Baust T.B., Parra L.A., Leak R.K., Hochendoner S.,
RA Pena K., Quiroz M., Hong W.C., Dorostkar M.M., Janz R., Sitte H.H.,
RA Torres G.E.;
RT "Physical and functional interaction between the dopamine transporter and
RT the synaptic vesicle protein synaptogyrin-3.";
RL J. Neurosci. 29:4592-4604(2009).
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 exocytosis
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SLC6A3. {ECO:0000269|PubMed:19357284}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Vesicular
CC transporter family. {ECO:0000305}.
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DR EMBL; AJ555564; CAD88262.1; -; mRNA.
DR EMBL; AK033871; BAC28501.1; -; mRNA.
DR EMBL; AK041274; BAC30887.1; -; mRNA.
DR CCDS; CCDS29935.1; -.
DR RefSeq; NP_766111.1; NM_172523.3.
DR AlphaFoldDB; Q8BRU6; -.
DR SMR; Q8BRU6; -.
DR MINT; Q8BRU6; -.
DR STRING; 10090.ENSMUSP00000026084; -.
DR BindingDB; Q8BRU6; -.
DR ChEMBL; CHEMBL4295886; -.
DR DrugBank; DB01126; Dutasteride.
DR GlyGen; Q8BRU6; 5 sites.
DR iPTMnet; Q8BRU6; -.
DR PhosphoSitePlus; Q8BRU6; -.
DR EPD; Q8BRU6; -.
DR MaxQB; Q8BRU6; -.
DR PaxDb; Q8BRU6; -.
DR PRIDE; Q8BRU6; -.
DR ProteomicsDB; 297607; -.
DR Antibodypedia; 2802; 394 antibodies from 38 providers.
DR DNASU; 214084; -.
DR Ensembl; ENSMUST00000026084; ENSMUSP00000026084; ENSMUSG00000025094.
DR GeneID; 214084; -.
DR KEGG; mmu:214084; -.
DR UCSC; uc008ibi.2; mouse.
DR CTD; 6571; -.
DR MGI; MGI:106677; Slc18a2.
DR VEuPathDB; HostDB:ENSMUSG00000025094; -.
DR eggNOG; KOG3764; Eukaryota.
DR GeneTree; ENSGT00940000157593; -.
DR HOGENOM; CLU_001265_10_9_1; -.
DR InParanoid; Q8BRU6; -.
DR OMA; IVAPLWG; -.
DR OrthoDB; 956763at2759; -.
DR PhylomeDB; Q8BRU6; -.
DR TreeFam; TF313494; -.
DR Reactome; R-MMU-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-MMU-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-MMU-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-MMU-442660; Na+/Cl- dependent neurotransmitter transporters.
DR BioGRID-ORCS; 214084; 3 hits in 75 CRISPR screens.
DR PRO; PR:Q8BRU6; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8BRU6; protein.
DR Bgee; ENSMUSG00000025094; Expressed in ventral tegmental area and 163 other tissues.
DR Genevisible; Q8BRU6; MM.
DR GO; GO:0043679; C:axon terminus; ISO:MGI.
DR GO; GO:0044297; C:cell body; ISO:MGI.
DR GO; GO:0042995; C:cell projection; ISO:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031045; C:dense core granule; ISO:MGI.
DR GO; GO:0098691; C:dopaminergic synapse; IMP:SynGO.
DR GO; GO:0099066; C:integral component of neuronal dense core vesicle membrane; ISO:MGI.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0098992; C:neuronal dense core vesicle; ISO:MGI.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0043195; C:terminal bouton; ISO:MGI.
DR GO; GO:0005275; F:amine transmembrane transporter activity; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR GO; GO:1901363; F:heterocyclic compound binding; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0015842; P:aminergic neurotransmitter loading into synaptic vesicle; ISO:MGI.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISO:MGI.
DR GO; GO:0042593; P:glucose homeostasis; ISO:MGI.
DR GO; GO:0030073; P:insulin secretion; ISO:MGI.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0015844; P:monoamine transport; ISO:MGI.
DR GO; GO:0051589; P:negative regulation of neurotransmitter transport; ISO:MGI.
DR GO; GO:0098700; P:neurotransmitter loading into synaptic vesicle; IMP:SynGO.
DR GO; GO:0006836; P:neurotransmitter transport; ISO:MGI.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:0001975; P:response to amphetamine; IMP:MGI.
DR GO; GO:0009636; P:response to toxic substance; IMP:MGI.
DR GO; GO:0051610; P:serotonin uptake; ISO:MGI.
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..517
FT /note="Synaptic vesicular amine transporter"
FT /id="PRO_0000127515"
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 REGION 100..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 120..327
FT /evidence="ECO:0000250"
FT CONFLICT 150
FT /note="P -> T (in Ref. 2; BAC28501)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 517 AA; 55754 MW; 97B40B65DE3DDBEE CRC64;
MALSDLVLLR WLRDSRHSRK LILFIVFLAL LLDNMLLTVV VPIIPSYLYS IKHEKNTTEI
QTARPALTAS TSESFHSIFS YYNNSTVFTG NATGGLPGGE SPKATTTQHT VTNTTVPPDC
PSEDKDLLNE NVQVGLLFAS KATVQLLTNP FIGLLTNRIG YPIPMFAGFC IMFISTVMFA
FSSSYAFLLI ARSLQGIGSS CSSVAGMGML ASVYTDDEER GNAMGIALGG LAMGVLVGPP
FGSVLYEFVG KTAPFLVLAA LVLLDGAIQL FVLQPSRVQP ESQKGTPLTT LLKDPYILIA
AGSICFANMG IAMLEPALPI WMMETMCSRK WQLGVAFLPA SISYLIGTNI FGILAHKMGR
WLCALLGMIV VGISILCIPF AKNIYGLIAP NFGVGFAIGM VDSSMMPIMG YLVDLRHVSV
YGSVYAIADV AFCMGYAIGP SAGGAIAKAI GFPWLMTIIG IIDIVFAPLC FFLRSPPAKE
EKMAILMDHN CPIKTKMYTQ NNVQPYPVGD DEESESD
