SCRB2_MOUSE
ID SCRB2_MOUSE Reviewed; 478 AA.
AC O35114; Q3UNF8;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Lysosome membrane protein 2;
DE AltName: Full=85 kDa lysosomal membrane sialoglycoprotein;
DE Short=LGP85;
DE AltName: Full=Lysosome membrane protein II;
DE Short=LIMP II;
DE AltName: Full=Scavenger receptor class B member 2;
GN Name=Scarb2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=9399579; DOI=10.1093/oxfordjournals.jbchem.a021820;
RA Tabuchi N., Akasaki K., Sasaki T., Kanda N., Tsuji H.;
RT "Identification and characterization of a major lysosomal membrane
RT glycoprotein, LGP85/LIMP II in mouse liver.";
RL J. Biochem. 122:756-763(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver, and Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 276-294 AND 361-378, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP FUNCTION, AND INTERACTION WITH GBA.
RX PubMed=18022370; DOI=10.1016/j.cell.2007.10.018;
RA Reczek D., Schwake M., Schroder J., Hughes H., Blanz J., Jin X.,
RA Brondyk W., Van Patten S., Edmunds T., Saftig P.;
RT "LIMP-2 is a receptor for lysosomal mannose-6-phosphate-independent
RT targeting of beta-glucocerebrosidase.";
RL Cell 131:770-783(2007).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-105.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION, INTERACTION WITH GBA, SUBCELLULAR LOCATION, REGION, AND
RP MUTAGENESIS OF ASN-45; ASN-68; ASN-105; ASN-122; LEU-155; ILE-156; MET-159;
RP LEU-160; ALA-162; TYR-163; LYS-166; ILE-184; LEU-187; PHE-191; ASN-206;
RP ASN-224; ASN-249; ASN-304; ASN-325; ASP-400; ASN-412 AND ASN-430.
RX PubMed=24162852; DOI=10.1038/nature12684;
RA Neculai D., Schwake M., Ravichandran M., Zunke F., Collins R.F., Peters J.,
RA Neculai M., Plumb J., Loppnau P., Pizarro J.C., Seitova A., Trimble W.S.,
RA Saftig P., Grinstein S., Dhe-Paganon S.;
RT "Structure of LIMP-2 provides functional insights with implications for SR-
RT BI and CD36.";
RL Nature 504:172-176(2013).
CC -!- FUNCTION: Acts as a lysosomal receptor for glucosylceramidase (GBA)
CC targeting. {ECO:0000269|PubMed:18022370, ECO:0000269|PubMed:24162852}.
CC -!- SUBUNIT: Interacts with GBA. {ECO:0000269|PubMed:18022370,
CC ECO:0000269|PubMed:24162852}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:24162852,
CC ECO:0000269|PubMed:9399579}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:24162852, ECO:0000269|PubMed:9399579}.
CC -!- TISSUE SPECIFICITY: Detected in the extracts of brain, heart, lung,
CC liver and kidney.
CC -!- PTM: Acylated by palmitic acid group(s). {ECO:0000250}.
CC -!- PTM: Heavily glycosylated. {ECO:0000269|PubMed:19349973}.
CC -!- SIMILARITY: Belongs to the CD36 family. {ECO:0000305}.
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DR EMBL; AB008553; BAA23372.1; -; mRNA.
DR EMBL; AK011123; BAB27416.1; -; mRNA.
DR EMBL; AK083038; BAC38740.1; -; mRNA.
DR EMBL; AK144235; BAE25789.1; -; mRNA.
DR EMBL; BC029073; AAH29073.1; -; mRNA.
DR CCDS; CCDS19431.1; -.
DR PIR; JC5670; JC5670.
DR RefSeq; NP_031670.1; NM_007644.4.
DR AlphaFoldDB; O35114; -.
DR SMR; O35114; -.
DR IntAct; O35114; 2.
DR STRING; 10090.ENSMUSP00000031377; -.
DR TCDB; 9.B.39.1.9; the long chain fatty acid translocase (lcfat) family.
DR GlyConnect; 2497; 9 N-Linked glycans (2 sites).
DR GlyGen; O35114; 11 sites, 8 N-linked glycans (2 sites).
DR iPTMnet; O35114; -.
DR PhosphoSitePlus; O35114; -.
DR SwissPalm; O35114; -.
DR EPD; O35114; -.
DR jPOST; O35114; -.
DR MaxQB; O35114; -.
DR PaxDb; O35114; -.
DR PeptideAtlas; O35114; -.
DR PRIDE; O35114; -.
DR ProteomicsDB; 256714; -.
DR Antibodypedia; 3014; 427 antibodies from 38 providers.
DR DNASU; 12492; -.
DR Ensembl; ENSMUST00000031377; ENSMUSP00000031377; ENSMUSG00000029426.
DR GeneID; 12492; -.
DR KEGG; mmu:12492; -.
DR UCSC; uc008ydm.1; mouse.
DR CTD; 950; -.
DR MGI; MGI:1196458; Scarb2.
DR VEuPathDB; HostDB:ENSMUSG00000029426; -.
DR eggNOG; KOG3776; Eukaryota.
DR GeneTree; ENSGT00940000153372; -.
DR HOGENOM; CLU_019853_3_0_1; -.
DR InParanoid; O35114; -.
DR OMA; DVFGMRP; -.
DR OrthoDB; 1106566at2759; -.
DR PhylomeDB; O35114; -.
DR TreeFam; TF317925; -.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 12492; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Scarb2; mouse.
DR PRO; PR:O35114; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; O35114; protein.
DR Bgee; ENSMUSG00000029426; Expressed in urinary bladder urothelium and 255 other tissues.
DR Genevisible; O35114; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030666; C:endocytic vesicle membrane; IDA:ARUK-UCL.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043202; C:lysosomal lumen; IDA:BHF-UCL.
DR GO; GO:0005765; C:lysosomal membrane; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0038024; F:cargo receptor activity; IMP:ARUK-UCL.
DR GO; GO:0051087; F:chaperone binding; IPI:UniProtKB.
DR GO; GO:0015485; F:cholesterol binding; IDA:ARUK-UCL.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0031210; F:phosphatidylcholine binding; IDA:ARUK-UCL.
DR GO; GO:0001786; F:phosphatidylserine binding; IDA:ARUK-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:ARUK-UCL.
DR GO; GO:0005044; F:scavenger receptor activity; IDA:ARUK-UCL.
DR GO; GO:0015917; P:aminophospholipid transport; IDA:ARUK-UCL.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:0006622; P:protein targeting to lysosome; IMP:BHF-UCL.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IDA:ARUK-UCL.
DR GO; GO:0043471; P:regulation of cellular carbohydrate catabolic process; IMP:ARUK-UCL.
DR GO; GO:1905123; P:regulation of glucosylceramidase activity; IMP:ParkinsonsUK-UCL.
DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
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 CHAIN 1..478
FT /note="Lysosome membrane protein 2"
FT /id="PRO_0000144156"
FT TOPO_DOM 1..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 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:0000269|PubMed:19349973"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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:0000255"
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"
FT MUTAGEN 45
FT /note="N->Q: Loss of glycosylation site. No effect on
FT normal location in lysosomes."
FT /evidence="ECO:0000269|PubMed:24162852"
FT MUTAGEN 68
FT /note="N->Q: Loss of glycosylation site. Causes retention
FT in the endoplasmic reticulum and abolishes normal location
FT in lysosomes."
FT /evidence="ECO:0000269|PubMed:24162852"
FT MUTAGEN 105
FT /note="N->Q: Loss of glycosylation site. No effect on
FT normal location in lysosomes."
FT /evidence="ECO:0000269|PubMed:24162852"
FT MUTAGEN 122
FT /note="N->Q: Loss of glycosylation site. No effect on
FT normal location in lysosomes."
FT /evidence="ECO:0000269|PubMed:24162852"
FT MUTAGEN 155
FT /note="L->D: Abolishes interaction with GBA. No effect on
FT normal location in lysosomes."
FT /evidence="ECO:0000269|PubMed:24162852"
FT MUTAGEN 156
FT /note="I->D: Abolishes interaction with GBA. No effect on
FT normal location in lysosomes."
FT /evidence="ECO:0000269|PubMed:24162852"
FT MUTAGEN 159
FT /note="M->D: Abolishes interaction with GBA. No effect on
FT normal location in lysosomes."
FT /evidence="ECO:0000269|PubMed:24162852"
FT MUTAGEN 160
FT /note="L->D: Abolishes interaction with GBA. No effect on
FT normal location in lysosomes."
FT /evidence="ECO:0000269|PubMed:24162852"
FT MUTAGEN 162
FT /note="A->D: Abolishes interaction with GBA. No effect on
FT normal location in lysosomes."
FT /evidence="ECO:0000269|PubMed:24162852"
FT MUTAGEN 163
FT /note="Y->D: Abolishes interaction with GBA. No effect on
FT normal location in lysosomes."
FT /evidence="ECO:0000269|PubMed:24162852"
FT MUTAGEN 166
FT /note="K->D: Abolishes interaction with GBA. No effect on
FT normal location in lysosomes."
FT /evidence="ECO:0000269|PubMed:24162852"
FT MUTAGEN 184
FT /note="I->D: Abolishes interaction with GBA. No effect on
FT normal location in lysosomes."
FT /evidence="ECO:0000269|PubMed:24162852"
FT MUTAGEN 187
FT /note="L->D: Abolishes interaction with GBA. No effect on
FT normal location in lysosomes."
FT /evidence="ECO:0000269|PubMed:24162852"
FT MUTAGEN 191
FT /note="F->D: Abolishes interaction with GBA. No effect on
FT normal location in lysosomes."
FT /evidence="ECO:0000269|PubMed:24162852"
FT MUTAGEN 206
FT /note="N->Q: Loss of glycosylation site. No effect on
FT normal location in lysosomes."
FT /evidence="ECO:0000269|PubMed:24162852"
FT MUTAGEN 224
FT /note="N->Q: Loss of glycosylation site. No effect on
FT normal location in lysosomes."
FT /evidence="ECO:0000269|PubMed:24162852"
FT MUTAGEN 249
FT /note="N->Q: Loss of glycosylation site. No effect on
FT normal location in lysosomes."
FT /evidence="ECO:0000269|PubMed:24162852"
FT MUTAGEN 304
FT /note="N->Q: Loss of glycosylation site. No effect on
FT normal location in lysosomes."
FT /evidence="ECO:0000269|PubMed:24162852"
FT MUTAGEN 325
FT /note="N->Q: Loss of glycosylation site. Causes retention
FT in the endoplasmic reticulum and abolishes normal location
FT in lysosomes."
FT /evidence="ECO:0000269|PubMed:24162852"
FT MUTAGEN 400
FT /note="D->K: Slightly increased GBA binding. No effect on
FT normal location in lysosomes."
FT /evidence="ECO:0000269|PubMed:24162852"
FT MUTAGEN 412
FT /note="N->Q: Loss of glycosylation site. No effect on
FT normal location in lysosomes."
FT /evidence="ECO:0000269|PubMed:24162852"
FT MUTAGEN 430
FT /note="N->Q: Loss of glycosylation site. No effect on
FT normal location in lysosomes."
FT /evidence="ECO:0000269|PubMed:24162852"
SQ SEQUENCE 478 AA; 54044 MW; 55724B77855470DF CRC64;
MGRCCFYTAG TLSLLLLVTS VTLLVARVFQ KAVDQTIEKN MVLQNGTKVF NSWEKPPLPV
YIQFYFFNVT NPEEILQGEI PLLEEVGPYT YRELRNKANI QFGENGTTIS AVTNKAYVFE
RNQSVGDPNV DLIRTINIPL LTVVDLAQLT LLRELIEAML KAYQQKLFVI HTVHELLWGY
KDEILSLVHI FKPDVSPNFG LFYERNGTND GEYVFLTGED NYLNFSKIVE WNGKTSLDWW
TTDTCNMING TDGDSFHPLI SKDEVLYLFP SDLCRSVHIT FSSFENVEGL PAFRYKVPAE
ILANTSENAG FCIPEGNCMD SGVLNISICK NGAPIIMSFP HFYQADEKFV SAIKGMHPNK
EEHESFVDIN PLTGIILRGA KRFQINTYVR KLDDFVETGD IRTMVFPVMY LNESVLIDKE
TANQLKSVIN TTLVVTNIPY IIMALGVFFG LVFTWLACRG QGSMDEGTAD ERAPLIRT
