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S6A13_BOVIN
ID   S6A13_BOVIN             Reviewed;         602 AA.
AC   A5PJX7;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Sodium- and chloride-dependent GABA transporter 2;
DE            Short=GAT-2;
DE   AltName: Full=Solute carrier family 6 member 13;
GN   Name=SLC6A13;
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 [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal medulla;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Mediates sodium- and chloride-dependent transport of gamma-
CC       aminobutyric acid (GABA) (By similarity). Can also mediate transport of
CC       beta-alanine, taurine and hypotaurine (By similarity).
CC       {ECO:0000250|UniProtKB:P31649}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-aminobutanoate(out) + chloride(out) + 2 Na(+)(out) = 4-
CC         aminobutanoate(in) + chloride(in) + 2 Na(+)(in);
CC         Xref=Rhea:RHEA:70687, ChEBI:CHEBI:17996, ChEBI:CHEBI:29101,
CC         ChEBI:CHEBI:59888; Evidence={ECO:0000250|UniProtKB:P31649};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70688;
CC         Evidence={ECO:0000250|UniProtKB:P31649};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chloride(out) + 2 Na(+)(out) + taurine(out) = chloride(in) + 2
CC         Na(+)(in) + taurine(in); Xref=Rhea:RHEA:71223, ChEBI:CHEBI:17996,
CC         ChEBI:CHEBI:29101, ChEBI:CHEBI:507393;
CC         Evidence={ECO:0000250|UniProtKB:P31649};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71224;
CC         Evidence={ECO:0000250|UniProtKB:P31649};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-alanine(out) + chloride(out) + 2 Na(+)(out) = beta-
CC         alanine(in) + chloride(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71247,
CC         ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:57966;
CC         Evidence={ECO:0000250|UniProtKB:P31649};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71248;
CC         Evidence={ECO:0000250|UniProtKB:P31649};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chloride(out) + hypotaurine(out) + 2 Na(+)(out) = chloride(in)
CC         + hypotaurine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71243,
CC         ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:57853;
CC         Evidence={ECO:0000250|UniProtKB:P31649};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71244;
CC         Evidence={ECO:0000250|UniProtKB:P31649};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P31649};
CC       Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane
CC       {ECO:0000250|UniProtKB:P31649}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) (TC
CC       2.A.22) family. SLC6A13 subfamily. {ECO:0000305}.
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DR   EMBL; BC142276; AAI42277.1; -; mRNA.
DR   RefSeq; NP_001092497.1; NM_001099027.1.
DR   AlphaFoldDB; A5PJX7; -.
DR   SMR; A5PJX7; -.
DR   STRING; 9913.ENSBTAP00000019308; -.
DR   PaxDb; A5PJX7; -.
DR   Ensembl; ENSBTAT00000019308; ENSBTAP00000019308; ENSBTAG00000014525.
DR   GeneID; 523784; -.
DR   KEGG; bta:523784; -.
DR   CTD; 6540; -.
DR   VEuPathDB; HostDB:ENSBTAG00000014525; -.
DR   VGNC; VGNC:34916; SLC6A13.
DR   eggNOG; KOG3660; Eukaryota.
DR   GeneTree; ENSGT00940000157478; -.
DR   HOGENOM; CLU_006855_9_5_1; -.
DR   InParanoid; A5PJX7; -.
DR   OMA; TIWFVSR; -.
DR   OrthoDB; 250396at2759; -.
DR   TreeFam; TF343812; -.
DR   Reactome; R-BTA-442660; Na+/Cl- dependent neurotransmitter transporters.
DR   Reactome; R-BTA-888593; Reuptake of GABA.
DR   Proteomes; UP000009136; Chromosome 5.
DR   Bgee; ENSBTAG00000014525; Expressed in midbrain and 20 other tissues.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0005332; F:gamma-aminobutyric acid:sodium symporter activity; IBA:GO_Central.
DR   GO; GO:0089718; P:amino acid import across plasma membrane; IEA:Ensembl.
DR   GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
DR   GO; GO:0010940; P:positive regulation of necrotic cell death; IEA:Ensembl.
DR   GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR   InterPro; IPR000175; Na/ntran_symport.
DR   InterPro; IPR002981; Na/ntran_symport_GABA_GAT2.
DR   InterPro; IPR037272; SNS_sf.
DR   PANTHER; PTHR11616; PTHR11616; 1.
DR   Pfam; PF00209; SNF; 1.
DR   PRINTS; PR01196; GAT2TRNSPORT.
DR   PRINTS; PR00176; NANEUSMPORT.
DR   SUPFAM; SSF161070; SSF161070; 1.
DR   PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1.
DR   PROSITE; PS00754; NA_NEUROTRAN_SYMP_2; 1.
DR   PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Membrane;
KW   Neurotransmitter transport; Phosphoprotein; Reference proteome; Symport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..602
FT                   /note="Sodium- and chloride-dependent GABA transporter 2"
FT                   /id="PRO_0000351503"
FT   TOPO_DOM        1..40
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        41..61
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        68..88
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        121..141
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        142..206
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        207..227
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        233..253
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        282..302
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        319..339
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        366..386
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        418..438
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        453..473
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        490..510
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        528..548
FT                   /note="Helical; Name=12"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        549..602
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         587
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P31649"
FT   MOD_RES         591
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P31649"
FT   CARBOHYD        169
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        173
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        269
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        153..162
FT                   /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
SQ   SEQUENCE   602 AA;  67788 MW;  8B378732075B9F07 CRC64;
     MDSRVSGTTS NGETKPVCPG LEKAAEDGAL QREQWSNKME FLLSVAGEII GLGNVWRFPY
     LCYKNGGGAF FIPYLIFLFT CGIPVFLLET ALGQYTSQGG ITAWRKICPI FEGIGYASQM
     IVTLLNIYYI IVLAWALFYL FSSFTIDLPW GSCRHDWNTE RCVEFQRTNG SLNATAENAT
     SPVIEFWERR VLKISEGIQH LGALRWELAL CLLLAWVVCY FCIWKGVKST GKVVYFTATF
     PYLMLVVLLI RGVTLPGAAQ GIQFYLYPNL TRLWDPQVWM DAGTQIFFSF AICLGCLTAL
     GSYNKYHNNC YRDSIALCFL NSGTSFVAGF AIFSILGFMS QEQGVPISEV AESGPGLAFI
     AYPRAVVMLP FSPLWACCFF FMVVLLGLDS QFVCVESLVT ALVDMYPRVF RKKNRREVLI
     LGVSVTSFLV GLVMLTEGGM YVFQLFDYYA ASGMCLLFVA IFESFCVAWA YGAGRFYDNI
     EDMIGYRPWP LIKYCWLFLT PAVCTATFLF SLIKYTPLTY NKKYKYPWWG DALGWLLALS
     SMVCIPAWSC YKLSTLKGSF RERVRQLLCP AKDLPQGHRE GPSAPATPRT SLLILTELEP
     HH
 
 
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