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SCRB2_RAT
ID   SCRB2_RAT               Reviewed;         478 AA.
AC   P27615;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Lysosome membrane protein 2;
DE   AltName: Full=85 kDa lysosomal membrane sialoglycoprotein;
DE            Short=LGP85;
DE   AltName: Full=CD36 antigen-like 2;
DE   AltName: Full=Lysosome membrane protein II;
DE            Short=LIMP II;
DE   AltName: Full=Scavenger receptor class B member 2;
DE   AltName: CD_antigen=CD36;
GN   Name=Scarb2; Synonyms=Cd36l2, Limpii;
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], PROTEIN SEQUENCE OF 2-13 AND 41-63, AND
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Liver;
RX   PubMed=1715871; DOI=10.1016/s0021-9258(18)55375-8;
RA   Vega M.A., Segui-Real B., Alcalde Garcia J., Cales C., Rodriquez F.,
RA   Vanderkerckhove J., Sandoval I.V.;
RT   "Cloning, sequencing, and expression of a cDNA encoding rat LIMP II, a
RT   novel 74-kDa lysosomal membrane protein related to the surface adhesion
RT   protein CD36.";
RL   J. Biol. Chem. 266:16818-16824(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Liver;
RX   PubMed=1859403; DOI=10.1016/0006-291x(91)90127-s;
RA   Fujita H., Ezaki J., Noguchi Y., Kono A., Himeno M., Kato K.;
RT   "Isolation and sequencing of a cDNA clone encoding 85kDa sialoglycoprotein
RT   in rat liver lysosomal membranes.";
RL   Biochem. Biophys. Res. Commun. 178:444-452(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
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   PROTEIN SEQUENCE OF 32-48; 116-121; 135-161; 228-234; 263-294; 331-348;
RP   361-378; 382-402 AND 460-472, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RA   Lubec G., Kang S.U., Lubec S.;
RL   Submitted (SEP-2007) to UniProtKB.
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-122 AND ASN-412, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=24090084; DOI=10.1021/pr400783j;
RA   Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA   Graham M.E., Packer N.H., Cordwell S.J.;
RT   "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT   heterogeneity.";
RL   J. Proteome Res. 12:5791-5800(2013).
CC   -!- FUNCTION: Acts as a lysosomal receptor for glucosylceramidase (GBA)
CC       targeting. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with GBA. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:1715871,
CC       ECO:0000269|PubMed:1859403}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:1715871, ECO:0000269|PubMed:1859403}.
CC   -!- PTM: Acylated by palmitic acid group(s).
CC   -!- SIMILARITY: Belongs to the CD36 family. {ECO:0000305}.
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DR   EMBL; M68965; AAA41531.1; -; mRNA.
DR   EMBL; D10587; BAA01444.1; -; mRNA.
DR   EMBL; BC061853; AAH61853.1; -; mRNA.
DR   PIR; JH0241; JH0241.
DR   RefSeq; NP_446453.1; NM_054001.2.
DR   AlphaFoldDB; P27615; -.
DR   SMR; P27615; -.
DR   IntAct; P27615; 3.
DR   STRING; 10116.ENSRNOP00000003052; -.
DR   GlyGen; P27615; 11 sites, 6 N-linked glycans (2 sites).
DR   iPTMnet; P27615; -.
DR   SwissPalm; P27615; -.
DR   jPOST; P27615; -.
DR   PaxDb; P27615; -.
DR   PRIDE; P27615; -.
DR   Ensembl; ENSRNOT00000103647; ENSRNOP00000097524; ENSRNOG00000002225.
DR   GeneID; 117106; -.
DR   KEGG; rno:117106; -.
DR   UCSC; RGD:621882; rat.
DR   CTD; 950; -.
DR   RGD; 621882; Scarb2.
DR   eggNOG; KOG3776; Eukaryota.
DR   GeneTree; ENSGT00940000153372; -.
DR   HOGENOM; CLU_019853_3_0_1; -.
DR   InParanoid; P27615; -.
DR   OMA; DVFGMRP; -.
DR   OrthoDB; 1106566at2759; -.
DR   PhylomeDB; P27615; -.
DR   TreeFam; TF317925; -.
DR   Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR   PRO; PR:P27615; -.
DR   Proteomes; UP000002494; Chromosome 14.
DR   Bgee; ENSRNOG00000002225; Expressed in lung and 19 other tissues.
DR   Genevisible; P27615; RN.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0030666; C:endocytic vesicle membrane; ISO:RGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043202; C:lysosomal lumen; ISO:RGD.
DR   GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0038024; F:cargo receptor activity; ISO:RGD.
DR   GO; GO:0051087; F:chaperone binding; ISO:RGD.
DR   GO; GO:0015485; F:cholesterol binding; ISO:RGD.
DR   GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR   GO; GO:0031210; F:phosphatidylcholine binding; ISO:RGD.
DR   GO; GO:0001786; F:phosphatidylserine binding; ISO:RGD.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR   GO; GO:0005044; F:scavenger receptor activity; ISO:RGD.
DR   GO; GO:0015917; P:aminophospholipid transport; ISO:RGD.
DR   GO; GO:0010467; P:gene expression; ISO:RGD.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0006622; P:protein targeting to lysosome; ISO:RGD.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; ISO:RGD.
DR   GO; GO:0043471; P:regulation of cellular carbohydrate catabolic process; ISO:RGD.
DR   GO; GO:1905123; P:regulation of glucosylceramidase activity; ISO:RGD.
DR   GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
DR   InterPro; IPR002159; CD36_fam.
DR   InterPro; IPR005429; LimpII.
DR   PANTHER; PTHR11923; PTHR11923; 1.
DR   Pfam; PF01130; CD36; 1.
DR   PRINTS; PR01609; CD36FAMILY.
DR   PRINTS; PR01611; LIMPII.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Lipoprotein;
KW   Lysosome; Membrane; Palmitate; Receptor; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1715871"
FT   CHAIN           2..478
FT                   /note="Lysosome membrane protein 2"
FT                   /id="PRO_0000144157"
FT   TOPO_DOM        2..4
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        5..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        28..433
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        434..459
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        460..478
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          155..191
FT                   /note="Important for interaction with GBA"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        45
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        68
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        122
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0007744|PubMed:24090084"
FT   CARBOHYD        206
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        224
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        249
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        304
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        325
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        412
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0007744|PubMed:24090084"
FT   CARBOHYD        430
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        274..329
FT                   /evidence="ECO:0000250"
FT   DISULFID        312..318
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   478 AA;  54091 MW;  3EA6E653C38E3002 CRC64;
     MARCCFYTAG TLSLLLLVTS VTLLVARVFQ KAVDQTIEKN MVLQNGTKVF DSWEKPPLPV
     YIQFYFFNVT NPEEILQGEI PLLEEVGPYT YRELRNKANV QFGENGTTIS AVTNKAYIFE
     RNQSVGDPTV DLIRTINIPL LTVVEMAQQP FLREIIEAML KAYQQTLFVT HTVHELLWGY
     KDEVLSLVHI FRPDVSPNFG LFYERNGTND GEYVFLTGED NYLNFTKIVE WNGKTSLDWW
     TTDTCNMING TDGDSFHPLI SKDETLYIFP SDFCRSVYIT FSSFENVEGL PAFRYKVPAE
     ILANSSENAG FCIPEGNCMD AGVLNVSICK NGAPIIMSFP HFYQADEKFV SAIKGMRPNK
     EEHESFVDIN PLTGIILRGA KRFQINTYVK KLDDFVETGN IRTMVFPVMY LNESVLIDKE
     TASQLKSVIN TTLIVTNIPY IIMALGVFFG LIFTWLACRG QGSTDEGTAD ERAPLIRT
 
 
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