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SC6A8_MOUSE
ID   SC6A8_MOUSE             Reviewed;         640 AA.
AC   Q8VBW1; A2ALM4; Q80YC9; Q8K4R3; Q8R1L0;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Sodium- and chloride-dependent creatine transporter 1;
DE            Short=CT1;
DE            Short=Creatine transporter 1;
DE   AltName: Full=Solute carrier family 6 member 8;
GN   Name=Slc6a8; Synonyms=Crt;
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] (ISOFORM 2).
RX   PubMed=12439290; DOI=10.1097/01.wcb.0000033966.83623.7d;
RA   Ohtsuki S., Tachikawa M., Takanaga H., Shimizu H., Watanabe M., Hosoya K.,
RA   Terasaki T.;
RT   "The blood-brain barrier creatine transporter is a major pathway for
RT   supplying creatine to the brain.";
RL   J. Cereb. Blood Flow Metab. 22:1327-1335(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 1).
RA   Liu Q.-R., Li Q.-F.;
RT   "Cloning and expression of mouse creatine transporter gene.";
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 58-640 (ISOFORMS 2 AND 3).
RC   STRAIN=FVB/N; TISSUE=Embryo, and 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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-625 AND SER-628, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Required for the uptake of creatine. Plays an important role
CC       in supplying creatine to the brain via the blood-brain barrier.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8VBW1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8VBW1-2; Sequence=VSP_012133;
CC       Name=3;
CC         IsoId=Q8VBW1-3; Sequence=VSP_012132;
CC   -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) (TC
CC       2.A.22) family. SLC6A8 subfamily. {ECO:0000305}.
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DR   EMBL; AB077327; BAC11857.1; -; mRNA.
DR   EMBL; AF459435; AAL66354.1; -; mRNA.
DR   EMBL; AF459436; AAL66355.1; -; Genomic_DNA.
DR   EMBL; AL805924; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC024444; AAH24444.1; -; mRNA.
DR   EMBL; BC049801; AAH49801.1; -; mRNA.
DR   CCDS; CCDS30208.1; -. [Q8VBW1-1]
DR   CCDS; CCDS53098.1; -. [Q8VBW1-2]
DR   RefSeq; NP_001136281.1; NM_001142809.1. [Q8VBW1-2]
DR   RefSeq; NP_001136282.1; NM_001142810.1. [Q8VBW1-3]
DR   RefSeq; NP_598748.1; NM_133987.2. [Q8VBW1-1]
DR   AlphaFoldDB; Q8VBW1; -.
DR   SMR; Q8VBW1; -.
DR   BioGRID; 221964; 6.
DR   IntAct; Q8VBW1; 6.
DR   STRING; 10090.ENSMUSP00000033752; -.
DR   GlyGen; Q8VBW1; 3 sites.
DR   iPTMnet; Q8VBW1; -.
DR   PhosphoSitePlus; Q8VBW1; -.
DR   jPOST; Q8VBW1; -.
DR   MaxQB; Q8VBW1; -.
DR   PaxDb; Q8VBW1; -.
DR   PRIDE; Q8VBW1; -.
DR   ProteomicsDB; 255475; -. [Q8VBW1-1]
DR   ProteomicsDB; 255476; -. [Q8VBW1-2]
DR   ProteomicsDB; 255477; -. [Q8VBW1-3]
DR   DNASU; 102857; -.
DR   Ensembl; ENSMUST00000033752; ENSMUSP00000033752; ENSMUSG00000019558. [Q8VBW1-1]
DR   Ensembl; ENSMUST00000114465; ENSMUSP00000110109; ENSMUSG00000019558. [Q8VBW1-2]
DR   Ensembl; ENSMUST00000114467; ENSMUSP00000110111; ENSMUSG00000019558. [Q8VBW1-2]
DR   GeneID; 102857; -.
DR   KEGG; mmu:102857; -.
DR   UCSC; uc009tmf.2; mouse. [Q8VBW1-1]
DR   UCSC; uc009tmg.2; mouse. [Q8VBW1-3]
DR   CTD; 6535; -.
DR   MGI; MGI:2147834; Slc6a8.
DR   VEuPathDB; HostDB:ENSMUSG00000019558; -.
DR   eggNOG; KOG3660; Eukaryota.
DR   GeneTree; ENSGT00940000155869; -.
DR   InParanoid; Q8VBW1; -.
DR   OMA; CVEIFRQ; -.
DR   OrthoDB; 250396at2759; -.
DR   PhylomeDB; Q8VBW1; -.
DR   TreeFam; TF343812; -.
DR   Reactome; R-MMU-71288; Creatine metabolism.
DR   BioGRID-ORCS; 102857; 2 hits in 74 CRISPR screens.
DR   ChiTaRS; Slc6a8; mouse.
DR   PRO; PR:Q8VBW1; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; Q8VBW1; protein.
DR   Bgee; ENSMUSG00000019558; Expressed in small intestine Peyer's patch and 255 other tissues.
DR   ExpressionAtlas; Q8VBW1; baseline and differential.
DR   Genevisible; Q8VBW1; MM.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:MGI.
DR   GO; GO:0015220; F:choline transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0005308; F:creatine transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0005309; F:creatine:sodium symporter activity; ISO:MGI.
DR   GO; GO:0015881; P:creatine transmembrane transport; ISS:UniProtKB.
DR   GO; GO:1990403; P:embryonic brain development; IEA:Ensembl.
DR   GO; GO:0006836; P:neurotransmitter transport; IEA:InterPro.
DR   GO; GO:0071705; P:nitrogen compound transport; ISO:MGI.
DR   GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR   InterPro; IPR000175; Na/ntran_symport.
DR   InterPro; IPR002984; Na/ntran_symport_creatine.
DR   InterPro; IPR037272; SNS_sf.
DR   PANTHER; PTHR11616; PTHR11616; 1.
DR   Pfam; PF00209; SNF; 1.
DR   PRINTS; PR01199; CRTTRANSPORT.
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   1: Evidence at protein level;
KW   Alternative splicing; Glycoprotein; Ion transport; Membrane;
KW   Phosphoprotein; Reference proteome; Sodium; Sodium transport; Symport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..640
FT                   /note="Sodium- and chloride-dependent creatine transporter
FT                   1"
FT                   /id="PRO_0000214775"
FT   TOPO_DOM        1..60
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        82..87
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        109..138
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        160..230
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        231..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        252..269
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        270..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        291..304
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        305..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        326..341
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        342..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        363..394
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        395..415
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        416..444
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        445..470
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        471..484
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        485..505
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        506..525
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        526..546
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        547..565
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        566..586
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        587..640
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         622
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P48029"
FT   MOD_RES         625
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         628
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CARBOHYD        192
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        197
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        553
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         462..469
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_012132"
FT   VAR_SEQ         465..469
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12439290,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_012133"
SQ   SEQUENCE   640 AA;  70999 MW;  67D3AAAC591EEA0B CRC64;
     MAKKSAENGI YSVSGDEKKG PLIVSGPDGA PAKGDGPAGL GAPGGRLAVP PRETWTRQMD
     FIMSCVGFAV GLGNVWRFPY LCYKNGGGVF LIPYVLIALV GGIPIFFLEI SLGQFMKAGS
     INVWNICPLF KGLGYASMVI VFYCNTYYIM VLAWGFYYLV KSFTTTLPWA TCGHTWNTPD
     CVEIFRHEDC ANASLANLTC DQLADRRSPV IEFWENKVLR LSTGLEVPGA LNWEVTLCLL
     ACWVLVYFCV WKGVKSTGKI VYFTATFPYV VLVVLLVRGV LLPGALDGII YYLKPDWSKL
     GSPQVWIDAG TQIFFSYAIG LGALTALGSY NRFNNNCYKD AIILALINSG TSFFAGFVVF
     SILGFMATEQ GVHISKVAES GPGLAFIAYP RAVTLMPVAP LWAALFFFML LLLGLDSQFV
     GVEGFITGLL DLLPASYYFR FQREISVALC CALCFVIDLS MVTDVSGGKG GMYVFQLFDY
     YSASGTTLLW QAFWECVVVA WVYGADRFMD DIACMIGYRP CPWMKWCWSF FTPLVCMGIF
     IFNIVYYEPL VYNNTYVYPW WGEAMGWAFA LSSMLCVPLH LLGCLLRAKG TMAERWQHLT
     QPIWGLHHLE YRAQDADVRG LTTLTPVSES SKVVVVESVM
 
 
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