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SC5A4_PIG
ID   SC5A4_PIG               Reviewed;         660 AA.
AC   P31636;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Solute carrier family 5 member 4 {ECO:0000305};
DE   AltName: Full=Low affinity sodium-glucose cotransporter {ECO:0000303|PubMed:8077195};
GN   Name=SLC5A4; Synonyms=SAAT1, SGLT3;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Kidney;
RX   PubMed=8420925; DOI=10.1016/s0021-9258(18)53880-1;
RA   Kong C.-T., Yet S.-F., Lever J.E.;
RT   "Cloning and expression of a mammalian Na+/amino acid cotransporter with
RT   sequence similarity to Na+/glucose cotransporters.";
RL   J. Biol. Chem. 268:1509-1512(1993).
RN   [2]
RP   FUNCTION, AND ACTIVITY REGULATION.
RX   PubMed=8077195; DOI=10.1016/s0021-9258(17)31672-1;
RA   McKenzie B., Panayotova-Heiermann M., Loo D.D.F., Lever J.E., Wright E.M.;
RT   "SAAT1 is a low affinity Na+/glucose cotransporter and not an amino acid
RT   transporter. A reinterpretation.";
RL   J. Biol. Chem. 269:22488-22491(1994).
RN   [3]
RP   FUNCTION.
RC   TISSUE=Small intestine;
RX   PubMed=13130073; DOI=10.1073/pnas.1733027100;
RA   Diez-Sampedro A., Hirayama B.A., Osswald C., Gorboulev V., Baumgarten K.,
RA   Volk C., Wright E.M., Koepsell H.;
RT   "A glucose sensor hiding in a family of transporters.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:11753-11758(2003).
CC   -!- FUNCTION: Has electrogenic activity in response to glucose, and may
CC       function as a glucose sensor (PubMed:8077195). Also has low-affinity
CC       sodium/glucose cotransporter activity; sugar transport activity is
CC       tightly coupled to ion transport at neutral pH but is reduced under
CC       more acidic conditions (PubMed:8077195, PubMed:13130073).
CC       {ECO:0000269|PubMed:13130073, ECO:0000269|PubMed:8077195}.
CC   -!- ACTIVITY REGULATION: Inhibited by phlorizin.
CC       {ECO:0000269|PubMed:8077195}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:8077195,
CC       ECO:0000305|PubMed:8420925}; Multi-pass membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Kidney, intestine, liver, skeletal muscle and
CC       spleen. {ECO:0000269|PubMed:8420925}.
CC   -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21)
CC       family. {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to be a sodium/neutral amino acid
CC       cotransporter (system a neutral amino acid transporter) responsible for
CC       the sodium-dependent intake of neutral amino acids such as alanine,
CC       glycine, serine, cysteine, and proline. {ECO:0000305|PubMed:8420925}.
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DR   EMBL; L02900; AAC37325.1; -; mRNA.
DR   PIR; A44432; A44432.
DR   RefSeq; NP_999347.1; NM_214182.1.
DR   AlphaFoldDB; P31636; -.
DR   SMR; P31636; -.
DR   STRING; 9823.ENSSSCP00000010710; -.
DR   TCDB; 2.A.21.3.4; the solute:sodium symporter (sss) family.
DR   PaxDb; P31636; -.
DR   PeptideAtlas; P31636; -.
DR   PRIDE; P31636; -.
DR   Ensembl; ENSSSCT00005065693; ENSSSCP00005040644; ENSSSCG00005040678.
DR   Ensembl; ENSSSCT00055022062; ENSSSCP00055017465; ENSSSCG00055011006.
DR   GeneID; 397376; -.
DR   KEGG; ssc:397376; -.
DR   CTD; 6527; -.
DR   eggNOG; KOG2349; Eukaryota.
DR   InParanoid; P31636; -.
DR   OrthoDB; 243316at2759; -.
DR   PRO; PR:P31636; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005412; F:glucose:sodium symporter activity; IBA:GO_Central.
DR   GO; GO:0006814; P:sodium ion transport; IBA:GO_Central.
DR   Gene3D; 1.20.1730.10; -; 1.
DR   InterPro; IPR038377; Na/Glc_symporter_sf.
DR   InterPro; IPR001734; Na/solute_symporter.
DR   InterPro; IPR018212; Na/solute_symporter_CS.
DR   Pfam; PF00474; SSF; 1.
DR   TIGRFAMs; TIGR00813; sss; 1.
DR   PROSITE; PS00456; NA_SOLUT_SYMP_1; 1.
DR   PROSITE; PS00457; NA_SOLUT_SYMP_2; 1.
DR   PROSITE; PS50283; NA_SOLUT_SYMP_3; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; Ion transport; Membrane; Reference proteome;
KW   Sodium; Sodium transport; Sugar transport; Symport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..660
FT                   /note="Solute carrier family 5 member 4"
FT                   /id="PRO_0000105378"
FT   TOPO_DOM        1..28
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        29..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        48..64
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        65..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        86..105
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        106..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        127..171
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        172..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        192..208
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        209..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        230..270
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        271..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        292..314
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        315..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        335..423
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        424..443
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        444..455
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        456..476
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        477..526
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        527..547
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        548..638
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        639..659
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        248
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   660 AA;  72745 MW;  38616367F8F18F1A CRC64;
     MASTLSPSTV TKTPGPPEIS ERIQNAADIS VIVIYFVVVM AVGLWAMLRT NRGTVGGFFL
     AGRDVTWWPM GASLFASNIG SGHFVGLAGT GAASGIAIAA FEWNALLLLL VLGWFFVPIY
     IKAGVMTMPE YLRKRFGGKR LQIYLSILSL FICVALRISS DIFSGAIFIK LALGLDLYLA
     IFSLLAITAI YTITGGLASV IYTDTLQTII MLIGSFILMG FAFVEVGGYE SFTEKYMNAI
     PTIVEGDNLT ISPKCYTPQG DSFHIFRDAV TGDIPWPGMI FGMTVVAAWY WCTDQVIVQR
     CLSGKDMSHV KAACIMCGYL KLLPMFLMVM PGMISRILYT EKVACVVPSE CVKHCGTEVG
     CSNYAYPLLV MELMPSGLRG LMLSVMLASL MSSLTSIFNS ASTLFTMDLY TKIRKQASEK
     ELLIAGRLFI ILLIVISIVW VPLVQVAQNG QLFHYIESIS SYLGPPIAAV FLLAIFCKRV
     NEQGAFWGLI IGFVMGLIRM IAEFVYGTGS CLAASNCPQI ICGVHYLYFA LILFFVSILV
     VLAISLLTKP IPDVHLYRLC WALRNSTEER IDLDAEEKRH EEAHDGVDED NPEETRGCLR
     KAYDLFCGLQ RKGPKLSKEE EEAQKRKLTD TSEKPLWKTI VNINAILLLA VAVFVHGYFA
 
 
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