VMAT1_MOUSE
ID VMAT1_MOUSE Reviewed; 521 AA.
AC Q8R090;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Chromaffin granule amine transporter;
DE AltName: Full=Solute carrier family 18 member 1;
DE AltName: Full=Vesicular amine transporter 1;
DE Short=VAT1;
GN Name=Slc18a1; Synonyms=Vmat1;
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 [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=21712771;
RA Ashe K.M., Chiu W.L., Khalifa A.M., Nicolas A.N., Brown B.L.,
RA De Martino R.R., Alexander C.P., Waggener C.T., Fischer-Stenger K.,
RA Stewart J.K.;
RT "Vesicular monoamine transporter-1 (VMAT-1) mRNA and immunoreactive
RT proteins in mouse brain.";
RL Neuroendocrinol. Lett. 32:253-258(2011).
RN [3]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=23201251; DOI=10.1016/j.neuroscience.2012.11.023;
RA Multani P.K., Hodge R., Estevez M.A., Abel T., Kung H., Alter M.,
RA Brookshire B., Lucki I., Nall A.H., Talbot K., Doyle G.A., Lohoff F.W.;
RT "VMAT1 deletion causes neuronal loss in the hippocampus and neurocognitive
RT deficits in spatial discrimination.";
RL Neuroscience 232:32-44(2013).
CC -!- FUNCTION: Involved in the transport of biogenic monoamines, such as
CC serotonin, from the cytoplasm into the secretory vesicles of
CC neuroendocrine and endocrine cells. {ECO:0000269|PubMed:21712771}.
CC -!- ACTIVITY REGULATION: Inhibited by reserpine, and the proton ionophore
CC carbonyl cyanide-p-trifluoromethoxyphenylhydrazone (FCCP).
CC {ECO:0000269|PubMed:21712771}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000305|PubMed:21712771}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle
CC membrane {ECO:0000305|PubMed:23201251}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Detected in adrenal medulla, and brain (at protein
CC level). In brain, specifically found in the medulla oblongata, pons,
CC prefrontal cortex, striatum, dentate gyrus and hippocampus (at protein
CC level). {ECO:0000269|PubMed:21712771, ECO:0000269|PubMed:23201251}.
CC -!- DISRUPTION PHENOTYPE: Increased apoptosis and reduced neurogenesis in
CC the hippocampus. Spatial memory formation is mildly impaired.
CC {ECO:0000269|PubMed:23201251}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Vesicular
CC transporter family. {ECO:0000305}.
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DR EMBL; BC027192; AAH27192.1; -; mRNA.
DR EMBL; BC031146; AAH31146.1; -; mRNA.
DR CCDS; CCDS22344.1; -.
DR RefSeq; NP_694694.1; NM_153054.2.
DR RefSeq; XP_006509597.1; XM_006509534.3.
DR AlphaFoldDB; Q8R090; -.
DR SMR; Q8R090; -.
DR STRING; 10090.ENSMUSP00000046924; -.
DR GlyGen; Q8R090; 3 sites.
DR iPTMnet; Q8R090; -.
DR PhosphoSitePlus; Q8R090; -.
DR SwissPalm; Q8R090; -.
DR PaxDb; Q8R090; -.
DR PRIDE; Q8R090; -.
DR ProteomicsDB; 299954; -.
DR Antibodypedia; 1514; 177 antibodies from 32 providers.
DR DNASU; 110877; -.
DR Ensembl; ENSMUST00000037478; ENSMUSP00000046924; ENSMUSG00000036330.
DR GeneID; 110877; -.
DR KEGG; mmu:110877; -.
DR UCSC; uc009lwt.1; mouse.
DR CTD; 6570; -.
DR MGI; MGI:106684; Slc18a1.
DR VEuPathDB; HostDB:ENSMUSG00000036330; -.
DR eggNOG; KOG3764; Eukaryota.
DR GeneTree; ENSGT00940000159352; -.
DR HOGENOM; CLU_001265_10_9_1; -.
DR InParanoid; Q8R090; -.
DR OMA; FGWCVDR; -.
DR OrthoDB; 956763at2759; -.
DR PhylomeDB; Q8R090; -.
DR TreeFam; TF313494; -.
DR Reactome; R-MMU-442660; Na+/Cl- dependent neurotransmitter transporters.
DR BioGRID-ORCS; 110877; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Slc18a1; mouse.
DR PRO; PR:Q8R090; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8R090; protein.
DR Bgee; ENSMUSG00000036330; Expressed in right kidney and 89 other tissues.
DR ExpressionAtlas; Q8R090; baseline and differential.
DR Genevisible; Q8R090; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0030672; C:synaptic vesicle membrane; IBA:GO_Central.
DR GO; GO:0043195; C:terminal bouton; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0005335; F:serotonin:sodium symporter activity; ISO:MGI.
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:0015842; P:aminergic neurotransmitter loading into synaptic vesicle; IBA:GO_Central.
DR GO; GO:0051612; P:negative regulation of serotonin uptake; ISO:MGI.
DR GO; GO:0033603; P:positive regulation of dopamine secretion; ISO: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; Glycoprotein; Membrane; Neurotransmitter transport;
KW Reference proteome; Synapse; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..521
FT /note="Chromaffin granule amine transporter"
FT /id="PRO_0000127511"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..135
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..164
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..194
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..253
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..296
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..332
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 358..362
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 384..394
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 416..419
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 441..445
FT /note="Lumenal, vesicle"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..467
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 468..521
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 521 AA; 56033 MW; 2258D64F5F3D15DB CRC64;
MFQVVLGAPQ RLLKEGRQSR KLVLVVVFVA LLLDNMLLTV VVPIVPTFLY ATEFKDINSS
LLRGPSVSSQ QALTSPAFST TFSFFDNTTM TVEEHVPFRV AWINGTIPPP VTEAGSVPKN
NCLQGIEFLE EENVRIGILF ASKALMQLLV NPFVGPLTNR IGYHIPMFVG FMIMFLSTLM
FAFSGTYALL FVARTLQGIG SSFSSVAGLG MLASVYTDNY ERGRAMGIAL GGLALGLLVG
APFGSVMYEF VGKSSPFLIL AFLALLDGAL QFCILWPSKV SPESAMGTPL LTLLKDPYIL
VAAGSICLAN MGVAILEPTL PIWMMQTMCS PEWQLGLAFL PASVAYLIGT NLFGVLANKM
GRWLCSLVGM VAVGISLLCV PLAHNIFGLI GPNAGLGFAI GMVDSSLMPI MGYLVDLRHT
SVYGSVYAIA DVAFCVGFAI GPSTGGVIVP VIGFPWLMVI IGTINIIYAP LCCFLQNPPA
KEEELAILNQ ECPTETQMYT IQRPTKEFPL GENSDDPGSE E
