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S52A2_RAT
ID   S52A2_RAT               Reviewed;         450 AA.
AC   B5MEV3; A3KN99;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Solute carrier family 52, riboflavin transporter, member 2;
DE   AltName: Full=Porcine endogenous retrovirus A receptor 2;
DE   AltName: Full=Protein GPR172B;
DE   AltName: Full=Riboflavin transporter 1;
DE            Short=rRFT1;
GN   Name=Slc52a2; Synonyms=Gpr172a, Gpr172b, Rft1;
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   TISSUE=Kidney;
RX   PubMed=18632736; DOI=10.1152/ajpcell.00019.2008;
RA   Yonezawa A., Masuda S., Katsura T., Inui K.;
RT   "Identification and functional characterization of a novel human and rat
RT   riboflavin transporter, RFT1.";
RL   Am. J. Physiol. 295:C632-C641(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
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   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=19122205; DOI=10.1093/jb/mvn181;
RA   Yamamoto S., Inoue K., Ohta K.Y., Fukatsu R., Maeda J.Y., Yoshida Y.,
RA   Yuasa H.;
RT   "Identification and functional characterization of rat riboflavin
RT   transporter 2.";
RL   J. Biochem. 145:437-443(2009).
CC   -!- FUNCTION: Plasma membrane transporter mediating the uptake by cells of
CC       the water soluble vitamin B2/riboflavin that plays a key role in
CC       biochemical oxidation-reduction reactions of the carbohydrate, lipid,
CC       and amino acid metabolism. May also act as a receptor for 4-
CC       hydroxybutyrate. {ECO:0000250|UniProtKB:Q9HAB3}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=riboflavin(in) = riboflavin(out); Xref=Rhea:RHEA:35015,
CC         ChEBI:CHEBI:57986; Evidence={ECO:0000250|UniProtKB:Q9HAB3};
CC   -!- ACTIVITY REGULATION: Riboflavin transport is Na(+)-independent but
CC       moderately pH-sensitive (By similarity). Activity is strongly inhibited
CC       by riboflavin analogs, such as lumiflavin (By similarity). Weakly
CC       inhibited by flavin adenine dinucleotide (FAD) and flavin
CC       mononucleotide (FMN) (By similarity). {ECO:0000250|UniProtKB:Q9HAB3}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18632736,
CC       ECO:0000269|PubMed:19122205}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in the placenta and small
CC       intestine, moderately in the kidney, colon, lung, prostate, uterus, and
CC       thymus, and weakly in all other tissues. {ECO:0000269|PubMed:18632736}.
CC   -!- SIMILARITY: Belongs to the riboflavin transporter family.
CC       {ECO:0000305}.
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DR   EMBL; AB362535; BAG71130.1; -; mRNA.
DR   EMBL; BC133726; AAI33727.1; -; mRNA.
DR   EMBL; CH473950; EDM15963.1; -; Genomic_DNA.
DR   RefSeq; NP_001103140.1; NM_001109670.1.
DR   RefSeq; XP_006241888.1; XM_006241826.3.
DR   AlphaFoldDB; B5MEV3; -.
DR   STRING; 10116.ENSRNOP00000046721; -.
DR   GlyGen; B5MEV3; 1 site.
DR   PhosphoSitePlus; B5MEV3; -.
DR   PaxDb; B5MEV3; -.
DR   Ensembl; ENSRNOT00000047380; ENSRNOP00000046721; ENSRNOG00000032561.
DR   GeneID; 362942; -.
DR   KEGG; rno:362942; -.
DR   UCSC; RGD:1560410; rat.
DR   CTD; 79581; -.
DR   RGD; 1560410; Slc52a2.
DR   eggNOG; KOG4255; Eukaryota.
DR   GeneTree; ENSGT00390000003774; -.
DR   HOGENOM; CLU_034789_1_0_1; -.
DR   InParanoid; B5MEV3; -.
DR   OMA; WCGISIQ; -.
DR   OrthoDB; 757564at2759; -.
DR   PhylomeDB; B5MEV3; -.
DR   TreeFam; TF314820; -.
DR   Reactome; R-RNO-196843; Vitamin B2 (riboflavin) metabolism.
DR   PRO; PR:B5MEV3; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Proteomes; UP000234681; Chromosome 7.
DR   Bgee; ENSRNOG00000032561; Expressed in jejunum and 18 other tissues.
DR   Genevisible; B5MEV3; RN.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0062124; F:4-hydroxybutyrate receptor activity; ISS:UniProtKB.
DR   GO; GO:0032217; F:riboflavin transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0032218; P:riboflavin transport; IDA:UniProtKB.
DR   InterPro; IPR009357; Riboflavin_transptr.
DR   PANTHER; PTHR12929; PTHR12929; 1.
DR   Pfam; PF06237; DUF1011; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; Membrane; Receptor; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..450
FT                   /note="Solute carrier family 52, riboflavin transporter,
FT                   member 2"
FT                   /id="PRO_0000399789"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        47..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        147..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        201..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        282..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        317..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        344..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        371..391
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        409..429
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          230..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        178
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        426
FT                   /note="I -> V (in Ref. 1; BAG71130)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   450 AA;  46956 MW;  1D4ABA0DC5C5B955 CRC64;
     MAAPPLGRLV LTHLLVALFG MGSWIAVNGI WVELPVVVKE LPEGWSLPSY LSVLVALGNL
     GLLLVTLWRR LAPGKSERIP IQVVQGLSIV GTGLLAPLWS NMALVAGQLH SVAFLTLAFV
     LALSCCASNV TFLPFLSHLP PPFLRSFFLG QGLSALLPCV LALAQGVGRL ECLHVPANGT
     TGPPIKVSPI NFPERFSAGT FFWVLTALLG TSAAAFQGLL LLLPSPPPEA TMGTGLRVET
     PGTEEEEEEE EASPLQEPPG QVASIVSSPD PKAHRLFSSR SACLLGLLAI TNALTNGVLP
     AVQSFSCLPY GRLAYHLAVV LGSSANPLAC FLAMAVLCRS LAGLYGLCLL GMFFGTYLMT
     LAVLSPCPPL VGTSAGVVLV VLSWVLCAGV FSYIKVATSS MLHSGGRPAL LAAGVAIQVG
     SLLGAIAMFP PTSVYPVFRS GEDCVDQCGP
 
 
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