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MFS4B_RAT
ID   MFS4B_RAT               Reviewed;         484 AA.
AC   Q80T22; Q4KMB5;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Sodium-dependent glucose transporter 1 {ECO:0000303|PubMed:12590146};
DE            Short=rNaGLT1;
DE   AltName: Full=Major facilitator superfamily domain-containing protein 4B;
GN   Name=Mfsd4b {ECO:0000312|RGD:631438}; Synonyms=Naglt1;
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, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=Wistar; TISSUE=Kidney;
RX   PubMed=12590146; DOI=10.1074/jbc.m212240200;
RA   Horiba N., Masuda S., Takeuchi A., Takeuchi D., Okuda M., Inui K.;
RT   "Cloning and characterization of a novel Na+-dependent glucose transporter
RT   (NaGLT1) in rat kidney.";
RL   J. Biol. Chem. 278:14669-14676(2003).
RN   [2]
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [4]
RP   INDUCTION, TISSUE SPECIFICITY, AND FUNCTION.
RX   PubMed=26423860; DOI=10.1152/ajprenal.00392.2015;
RA   Nawata C.M., Dantzler W.H., Pannabecker T.L.;
RT   "Alternative channels for urea in the inner medulla of the rat kidney.";
RL   Am. J. Physiol. 309:F916-F924(2015).
CC   -!- FUNCTION: May function as a sodium-dependent glucose transporter
CC       (PubMed:12590146). Potential channels for urea in the inner medulla of
CC       kidney (PubMed:26423860). {ECO:0000269|PubMed:12590146,
CC       ECO:0000269|PubMed:26423860}.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000269|PubMed:12590146}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:12590146}.
CC   -!- TISSUE SPECIFICITY: Expressed in brain, liver, lung, and kidney. In
CC       kidney expressed in cortex and inner medulla, in ascending thin limbs
CC       (ATLs) and lower descending thin limbs (DTLs). Primarily expressed in
CC       the proximal tubules of the kidney. {ECO:0000269|PubMed:12590146,
CC       ECO:0000269|PubMed:26423860}.
CC   -!- INDUCTION: After water restriction, up-regulated in inner medulla
CC       ascending thin limbs (ATLs) and lower descending thin limbs.
CC       {ECO:0000269|PubMed:26423860}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC       {ECO:0000305}.
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DR   EMBL; AB089802; BAC57446.1; -; mRNA.
DR   EMBL; BC098651; AAH98651.1; -; mRNA.
DR   RefSeq; NP_788269.1; NM_176080.2.
DR   AlphaFoldDB; Q80T22; -.
DR   SMR; Q80T22; -.
DR   STRING; 10116.ENSRNOP00000054044; -.
DR   TCDB; 2.A.1.7.4; the major facilitator superfamily (mfs).
DR   iPTMnet; Q80T22; -.
DR   PhosphoSitePlus; Q80T22; -.
DR   PaxDb; Q80T22; -.
DR   PRIDE; Q80T22; -.
DR   GeneID; 337920; -.
DR   KEGG; rno:337920; -.
DR   UCSC; RGD:631438; rat.
DR   CTD; 337920; -.
DR   RGD; 631438; Naglt1.
DR   eggNOG; ENOG502R5UW; Eukaryota.
DR   InParanoid; Q80T22; -.
DR   OrthoDB; 1122917at2759; -.
DR   PhylomeDB; Q80T22; -.
DR   TreeFam; TF314613; -.
DR   PRO; PR:Q80T22; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005355; F:glucose transmembrane transporter activity; IDA:RGD.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1250.20; -; 2.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Ion transport; Membrane; Phosphoprotein; Reference proteome;
KW   Sodium; Sodium transport; Sugar transport; Symport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..484
FT                   /note="Sodium-dependent glucose transporter 1"
FT                   /id="PRO_0000294514"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        106..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        135..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        168..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        227..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        274..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        317..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        340..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        366..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        401..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        428..448
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         6
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   CONFLICT        3
FT                   /note="F -> S (in Ref. 2; AAH98651)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        166
FT                   /note="I -> M (in Ref. 2; AAH98651)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   484 AA;  51775 MW;  FDDA74A332A16FC1 CRC64;
     MEFRGSGATA VEQHLLQSET PGKNGLQATS SDQVGRTLRW FTTVVLNAAF LGMGVSAAVL
     GPTFPDLARN VNRNISSLSE IFVGRALGYL GGSVVGGVLF DCMNHFLLLG LSHLLTAAGL
     YLTPFCKTAA LLTAMMSITG VSFGVLDTGG NVLILDLWGD KGAPHIQALH FSFALGAFLA
     PLLAKLAWGT TASAQNHTEP QLDRSALNRS FEAASDSVLA VPDDMNLLWA YASIGTYVLV
     LSVFLFAPFF KKRSKQKKSA ASAQGARRAK YHRALLCLLF LFFFFYVGAE VTYGSYVFSF
     ATTHVGMEES EAAGLNSIFW GTFAACRGLA IFFATLLQPG TMMVLCNIGS LASSFFLVLF
     DKSPLCLWIA SSVYGASMAA TFPSGISWIE QYTTLTGKSA AFILVGAALG LMATPALSGI
     LQGHYPDLPV ILYMCLGSAV LTTVLFPVMY KVATLPLDRK QEKSINSEGQ KILLSSSRLI
     KEAK
 
 
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