VMAT1_RAT
ID VMAT1_RAT Reviewed; 521 AA.
AC Q01818;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 143.
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=Cgat, Vmat1;
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], FUNCTION, ACTIVITY REGULATION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
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).
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:1505023}.
CC -!- ACTIVITY REGULATION: Strongly inhibited by reserpine. Also inhibited
CC weakly by tetrabenazine. {ECO:0000269|PubMed:1505023}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000305|PubMed:1505023}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle
CC membrane {ECO:0000250|UniProtKB:Q8R090}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Adrenal gland. {ECO:0000269|PubMed:1505023}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Vesicular
CC transporter family. {ECO:0000305}.
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DR EMBL; M97380; AAA40921.1; -; mRNA.
DR PIR; A43319; A43319.
DR RefSeq; NP_037284.2; NM_013152.2.
DR AlphaFoldDB; Q01818; -.
DR SMR; Q01818; -.
DR CORUM; Q01818; -.
DR STRING; 10116.ENSRNOP00000016193; -.
DR TCDB; 2.A.1.2.11; the major facilitator superfamily (mfs).
DR GlyGen; Q01818; 3 sites.
DR PhosphoSitePlus; Q01818; -.
DR jPOST; Q01818; -.
DR PaxDb; Q01818; -.
DR GeneID; 25693; -.
DR KEGG; rno:25693; -.
DR UCSC; RGD:3693; rat.
DR CTD; 6570; -.
DR RGD; 3693; Slc18a1.
DR eggNOG; KOG3764; Eukaryota.
DR InParanoid; Q01818; -.
DR OrthoDB; 956763at2759; -.
DR PhylomeDB; Q01818; -.
DR Reactome; R-RNO-442660; Na+/Cl- dependent neurotransmitter transporters.
DR PRO; PR:Q01818; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045202; C:synapse; ISO:RGD.
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; IPI:RGD.
DR GO; GO:0005335; F:serotonin:sodium symporter activity; IDA:RGD.
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:0071285; P:cellular response to lithium ion; IEP:RGD.
DR GO; GO:0051612; P:negative regulation of serotonin uptake; IMP:RGD.
DR GO; GO:0033603; P:positive regulation of dopamine secretion; IMP:RGD.
DR GO; GO:0051610; P:serotonin uptake; IDA: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 2: Evidence at transcript 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_0000127512"
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; 55935 MW; DCDC0D0AF0EC15D4 CRC64;
MLQVVLGAPQ RLLKEGRQSR KLVLVVVFVA LLLDNMLLTV VVPIVPTFLY ATEFKDSNSS
LHRGPSVSSQ QALTSPAFST IFSFFDNTTT TVEEHVPFRV TWTNGTIPPP VTEASSVPKN
NCLQGIEFLE EENVRIGILF ASKALMQLLV NPFVGPLTNR IGYHIPMFVG FMIMFLSTLM
FAFSGTYALL FVARTLQGIG SSFSSVAGLG MLASVYTDNY ERGRAMGIAL GGLALGLLVG
APFGSVMYEF VGKSSPFLIL AFLALLDGAL QLCILWPSKV SPESAMGTSL LTLLKDPYIL
VAAGSICLAN MGVAILEPTL PIWMMQTMCS PEWQLGLAFL PASVAYLIGT NLFGVLANKM
GRWLCSLVGM VAVGISLLCV PLAHNIFGLI GPNAGLGFAI GMVDSSLMPI MGYLVDLRHT
SVYGSVYAIA DVAFCVGFAI GPSTGGVIVQ VIGFPWLMVI IGTINIIYAP LCCFLQNPPA
KEEKRAILSQ ECPTETQMYT FQKPTKAFPL GENSDDPSSG E
