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S45A1_RAT
ID   S45A1_RAT               Reviewed;         751 AA.
AC   Q8K4S3;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Proton-associated sugar transporter A {ECO:0000303|PubMed:12417639};
DE            Short=PAST-A {ECO:0000303|PubMed:12417639};
DE   AltName: Full=Solute carrier family 45 member 1;
GN   Name=Slc45a1 {ECO:0000312|RGD:708502}; Synonyms=Dnb5;
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, TISSUE SPECIFICITY, TRANSPORTER
RP   ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC   TISSUE=Brain;
RX   PubMed=12417639; DOI=10.1523/jneurosci.22-21-09160.2002;
RA   Shimokawa N., Okada J., Haglund K., Dikic I., Koibuchi N., Miura M.;
RT   "Past-A, a novel proton-associated sugar transporter, regulates glucose
RT   homeostasis in the brain.";
RL   J. Neurosci. 22:9160-9165(2002).
CC   -!- FUNCTION: Proton-associated glucose transporter in the brain.
CC       {ECO:0000269|PubMed:12417639}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-galactose(in) + H(+)(in) = D-galactose(out) + H(+)(out);
CC         Xref=Rhea:RHEA:29019, ChEBI:CHEBI:4139, ChEBI:CHEBI:15378;
CC         Evidence={ECO:0000269|PubMed:12417639};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glucose(out) + H(+)(out) = D-glucose(in) + H(+)(in);
CC         Xref=Rhea:RHEA:69556, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378;
CC         Evidence={ECO:0000269|PubMed:12417639};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.5. {ECO:0000269|PubMed:12417639};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12417639}; Multi-
CC       pass membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in brain.
CC       {ECO:0000269|PubMed:12417639}.
CC   -!- SIMILARITY: Belongs to the glycoside-pentoside-hexuronide (GPH) cation
CC       symporter transporter (TC 2.A.2) family. {ECO:0000305}.
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DR   EMBL; AB075229; BAB97313.1; -; mRNA.
DR   AlphaFoldDB; Q8K4S3; -.
DR   STRING; 10116.ENSRNOP00000024581; -.
DR   TCDB; 2.A.2.4.4; the glycoside-pentoside-hexuronide (gph):cation symporter family.
DR   PaxDb; Q8K4S3; -.
DR   PRIDE; Q8K4S3; -.
DR   UCSC; RGD:708502; rat.
DR   RGD; 708502; Slc45a1.
DR   eggNOG; KOG0637; Eukaryota.
DR   InParanoid; Q8K4S3; -.
DR   PhylomeDB; Q8K4S3; -.
DR   PRO; PR:Q8K4S3; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0015517; F:galactose:proton symporter activity; IDA:UniProtKB.
DR   GO; GO:0005355; F:glucose transmembrane transporter activity; IMP:RGD.
DR   GO; GO:0005356; F:glucose:proton symporter activity; IDA:UniProtKB.
DR   GO; GO:0008506; F:sucrose:proton symporter activity; IBA:GO_Central.
DR   GO; GO:0015757; P:galactose transmembrane transport; IDA:UniProtKB.
DR   GO; GO:1904659; P:glucose transmembrane transport; IMP:UniProtKB.
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   Membrane; Phosphoprotein; Reference proteome; Sugar transport; Symport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..751
FT                   /note="Proton-associated sugar transporter A"
FT                   /id="PRO_0000122516"
FT   TRANSMEM        93..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        123..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        155..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        191..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        233..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        268..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        536..556
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        576..596
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        606..626
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        630..650
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        688..708
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        710..730
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         500
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BIV7"
SQ   SEQUENCE   751 AA;  81752 MW;  5C33E1C2E4A1B2EC CRC64;
     MIPPAGSTPP GEALIPSVAP QDFWRSPISG YSGSVTRHIS HRANNFKRHP KRRKYIRPSP
     PPPPNTPCPI ELVDFEDLHP QRSFWELLFN GCILFGIEFS YAMETAYVTP VLLQMGLPDQ
     LYSLVWFISP ILGFLLQPLL GAWSDRCTSR FGRRRPFILV LAIGALLGLS LLLNGRDIGM
     ALADTATNHK WGILLTVCGV VLMDFSADSA DNPSHAYMMD VCGPVDQDRG LNIHALMAGL
     GGGFGYVVGG IHWDKTSFGR ALGGQLRVIY IFTAITLSVT TVFTLVSIPE RPLRPLGEKR
     TAMKSPSLPL PPSPPVLLEE GAGDTLPSTT ATSLYASFSS PISPPSPLTP KYGSFISRDS
     SLTGINEFAS SFGTSNIDSV LIDCFTAGHD NYLALPSSVP RQAISVSFPR APDGFYCQER
     GLERREGPLT LGLDGDVLRV GSLDTSKPRA SGILKRPQTL ALPDVAGGNG PETSRRRNVT
     FSQQVANILL NGVKYESELT GSSEQSEQPL SLRRLCSTIY NMPRPVRNLC VNHFLGWLSF
     EGMLLFYTDF MGEVVFQGDP KAPHASEAYQ KYNSGVTMGC WGMCIYAFSA AFYSAILEKL
     EECLSVRTLY FIAYLLFGLG TGLATLSRNL YVVLSLCTHY GILFSTLCTL PYSLLCDYYQ
     SKKFAGSSAD GTRRGMGVDI SLLSCQYFLA QILVSLVLGP LTSAVGSANG VMYFASLVSF
     LGCLYSSLCV TYEIPSADAA DEERQPLLLN V
 
 
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