SCRB2_HUMAN
ID SCRB2_HUMAN Reviewed; 478 AA.
AC Q14108; B4DKD8; E7EM68; Q53Y63;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 201.
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, LIMP2, LIMPII;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1374238; DOI=10.1016/0006-291x(92)90632-u;
RA Fujita H., Takata Y., Kono A., Tanaka Y., Takahashi T., Himeno M., Kato K.;
RT "Isolation and sequencing of a cDNA clone encoding the 85 kDa human
RT lysosomal sialoglycoprotein (hLGP85) in human metastatic pancreas islet
RT tumor cells.";
RL Biochem. Biophys. Res. Commun. 184:604-611(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7539776; DOI=10.1016/0888-7543(95)80114-2;
RA Calvo D., Dopazo J., Vega M.A.;
RT "The CD36, CLA-1 (CD36L1), and LIMPII (CD36L2) gene family: cellular
RT distribution, chromosomal location, and genetic evolution.";
RL Genomics 25:100-106(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cerebellum, and Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 [8]
RP MUTAGENESIS OF LEU-475; ILE-476; ARG-477 AND THR-478, AND SUBCELLULAR
RP LOCATION.
RX PubMed=7509809; DOI=10.1016/s0021-9258(17)37418-5;
RA Sandoval I.V., Arredondo J.J., Alcalde J., Gonzalez Noriega A.,
RA Vandekerckhove J., Jimenez M.A., Rico M.;
RT "The residues Leu(Ile)475-Ile(Leu, Val, Ala)476, contained in the extended
RT carboxyl cytoplasmic tail, are critical for targeting of the resident
RT lysosomal membrane protein LIMP II to lysosomes.";
RL J. Biol. Chem. 269:6622-6631(1994).
RN [9]
RP MASS SPECTROMETRY.
RC TISSUE=Mammary cancer;
RX PubMed=11840567;
RX DOI=10.1002/1615-9861(200202)2:2<212::aid-prot212>3.0.co;2-h;
RA Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A.,
RA Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J.,
RA Zvelebil M.J.;
RT "Cluster analysis of an extensive human breast cancer cell line protein
RT expression map database.";
RL Proteomics 2:212-223(2002).
RN [10]
RP GLYCOSYLATION AT ASN-249 AND ASN-412.
RX PubMed=12754519; DOI=10.1038/nbt827;
RA Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT "Identification and quantification of N-linked glycoproteins using
RT hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL Nat. Biotechnol. 21:660-666(2003).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, REGION, 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 [12]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Placenta;
RX PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x;
RA Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., Schaefer H.,
RA Elsaesser H.-P., Mann M., Hasilik A.;
RT "Integral and associated lysosomal membrane proteins.";
RL Traffic 8:1676-1686(2007).
RN [13]
RP INVOLVEMENT IN EPM4.
RX PubMed=18308289; DOI=10.1016/j.ajhg.2007.12.019;
RA Berkovic S.F., Dibbens L.M., Oshlack A., Silver J.D., Katerelos M.,
RA Vears D.F., Luellmann-Rauch R., Blanz J., Zhang K.W., Stankovich J.,
RA Kalnins R.M., Dowling J.P., Andermann E., Andermann F., Faldini E.,
RA D'Hooge R., Vadlamudi L., Macdonell R.A., Hodgson B.L., Bayly M.A.,
RA Savige J., Mulley J.C., Smyth G.K., Power D.A., Saftig P., Bahlo M.;
RT "Array-based gene discovery with three unrelated subjects shows
RT SCARB2/LIMP-2 deficiency causes myoclonus epilepsy and
RT glomerulosclerosis.";
RL Am. J. Hum. Genet. 82:673-684(2008).
RN [14]
RP INVOLVEMENT IN EPM4.
RX PubMed=18424452; DOI=10.1093/hmg/ddn124;
RA Balreira A., Gaspar P., Caiola D., Chaves J., Beirao I., Lima J.L.,
RA Azevedo J.E., Miranda M.C.;
RT "A nonsense mutation in the LIMP-2 gene associated with progressive
RT myoclonic epilepsy and nephrotic syndrome.";
RL Hum. Mol. Genet. 17:2238-2243(2008).
RN [15]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-45; ASN-68; ASN-105; ASN-206;
RP ASN-249; ASN-304 AND ASN-325.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [16]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HOST ENTEROVIRUS 71
RP CAPSID PROTEIN VP1 AND VP2 (MICROBIAL INFECTION).
RX PubMed=19543282; DOI=10.1038/nm.1992;
RA Yamayoshi S., Yamashita Y., Li J., Hanagata N., Minowa T., Takemura T.,
RA Koike S.;
RT "Scavenger receptor B2 is a cellular receptor for enterovirus 71.";
RL Nat. Med. 15:798-801(2009).
RN [17]
RP INVOLVEMENT IN EPM4.
RX PubMed=21670406; DOI=10.1001/archneurol.2011.120;
RA Dibbens L.M., Karakis I., Bayly M.A., Costello D.J., Cole A.J.,
RA Berkovic S.F.;
RT "Mutation of SCARB2 in a patient with progressive myoclonus epilepsy and
RT demyelinating peripheral neuropathy.";
RL Arch. Neurol. 68:812-813(2011).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP INVOLVEMENT IN GAUCHER DISEASE AS MODIFIER GENE, AND VARIANT GLY-471.
RX PubMed=21796727; DOI=10.1002/humu.21566;
RA Velayati A., DePaolo J., Gupta N., Choi J.H., Moaven N., Westbroek W.,
RA Goker-Alpan O., Goldin E., Stubblefield B.K., Kolodny E., Tayebi N.,
RA Sidransky E.;
RT "A mutation in SCARB2 is a modifier in Gaucher disease.";
RL Hum. Mutat. 32:1232-1238(2011).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [22] {ECO:0007744|PDB:6I2K}
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HOST ENTEROVIRUS 71
RP CAPSID PROTEIN VP1 AND VP2 (MICROBIAL INFECTION).
RX PubMed=30531980; DOI=10.1038/s41564-018-0319-z;
RA Zhou D., Zhao Y., Kotecha A., Fry E.E., Kelly J.T., Wang X., Rao Z.,
RA Rowlands D.J., Ren J., Stuart D.I.;
RT "Unexpected mode of engagement between enterovirus 71 and its receptor
RT SCARB2.";
RL Nat. Microbiol. 4:414-419(2019).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 35-430, DISULFIDE BOND,
RP GLYCOSYLATION AT ASN-45; ASN-68; ASN-206; ASN-224; ASN-249; ASN-304;
RP ASN-325 AND ASN-412, AND INTERACTION WITH GBA.
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).
RN [24]
RP VARIANT EPM4 ASN-363.
RX PubMed=19454373; DOI=10.1016/j.ymgme.2009.04.011;
RA Dardis A., Filocamo M., Grossi S., Ciana G., Franceschetti S.,
RA Dominissini S., Rubboli G., Di Rocco M., Bembi B.;
RT "Biochemical and molecular findings in a patient with myoclonic epilepsy
RT due to a mistarget of the beta-glucosidase enzyme.";
RL Mol. Genet. Metab. 97:309-311(2009).
CC -!- FUNCTION: Acts as a lysosomal receptor for glucosylceramidase (GBA)
CC targeting. {ECO:0000269|PubMed:18022370}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for enterovirus 71.
CC {ECO:0000269|PubMed:19543282, ECO:0000269|PubMed:30531980}.
CC -!- SUBUNIT: Interacts with GBA. {ECO:0000269|PubMed:18022370,
CC ECO:0000269|PubMed:24162852}.
CC -!- SUBUNIT: (Microbial infection) Interacts with enterovirus 71 capsid
CC proteins VP1 and VP2. {ECO:0000269|PubMed:19543282,
CC ECO:0000269|PubMed:30531980}.
CC -!- INTERACTION:
CC Q14108; Q8N6F1-2: CLDN19; NbExp=3; IntAct=EBI-1564650, EBI-12256978;
CC Q14108; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-1564650, EBI-781551;
CC Q14108; O60883: GPR37L1; NbExp=3; IntAct=EBI-1564650, EBI-2927498;
CC Q14108; Q8TED1: GPX8; NbExp=3; IntAct=EBI-1564650, EBI-11721746;
CC Q14108; P31937: HIBADH; NbExp=3; IntAct=EBI-1564650, EBI-11427100;
CC Q14108; Q86VI4: LAPTM4B; NbExp=3; IntAct=EBI-1564650, EBI-3267258;
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:17897319,
CC ECO:0000269|PubMed:18022370, ECO:0000269|PubMed:7509809}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:17897319,
CC ECO:0000269|PubMed:18022370, ECO:0000269|PubMed:7509809}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q14108-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14108-2; Sequence=VSP_044826;
CC -!- MASS SPECTROMETRY: Mass=54158.97; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:11840567};
CC -!- DISEASE: Epilepsy, progressive myoclonic 4, with or without renal
CC failure (EPM4) [MIM:254900]: A form of progressive myoclonic epilepsy,
CC a clinically and genetically heterogeneous group of disorders defined
CC by the combination of action and reflex myoclonus, other types of
CC epileptic seizures, and progressive neurodegeneration and
CC neurocognitive impairment. EPM4 is an autosomal recessive form
CC associated with renal failure in some cases. Cognitive function is
CC preserved. {ECO:0000269|PubMed:18308289, ECO:0000269|PubMed:18424452,
CC ECO:0000269|PubMed:19454373, ECO:0000269|PubMed:21670406}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Note=Genetic variants in SCARB2 can act as modifier of the
CC phenotypic expression and severity of Gaucher disease.
CC {ECO:0000269|PubMed:21796727}.
CC -!- SIMILARITY: Belongs to the CD36 family. {ECO:0000305}.
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DR EMBL; D12676; BAA02177.1; -; mRNA.
DR EMBL; BT006939; AAP35585.1; -; mRNA.
DR EMBL; AK296519; BAG59150.1; -; mRNA.
DR EMBL; AK313016; BAG35851.1; -; mRNA.
DR EMBL; AC034139; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC110795; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471057; EAX05779.1; -; Genomic_DNA.
DR EMBL; BC021892; AAH21892.1; -; mRNA.
DR CCDS; CCDS3577.1; -. [Q14108-1]
DR CCDS; CCDS56335.1; -. [Q14108-2]
DR PIR; A56525; A56525.
DR RefSeq; NP_001191184.1; NM_001204255.1. [Q14108-2]
DR RefSeq; NP_005497.1; NM_005506.3. [Q14108-1]
DR PDB; 4F7B; X-ray; 3.00 A; A/B/C/D/E/F=35-430.
DR PDB; 4Q4B; X-ray; 2.82 A; A=28-431.
DR PDB; 4Q4F; X-ray; 2.80 A; A=28-432.
DR PDB; 4TVZ; X-ray; 3.01 A; A/B=37-430.
DR PDB; 4TW0; X-ray; 3.65 A; A/B/C/D=37-429.
DR PDB; 4TW2; X-ray; 2.89 A; A/B=37-430.
DR PDB; 5UPH; X-ray; 3.00 A; A/B=28-431.
DR PDB; 5XBM; X-ray; 3.50 A; C/F=37-430.
DR PDB; 6I2K; EM; 3.40 A; E=28-432.
DR PDBsum; 4F7B; -.
DR PDBsum; 4Q4B; -.
DR PDBsum; 4Q4F; -.
DR PDBsum; 4TVZ; -.
DR PDBsum; 4TW0; -.
DR PDBsum; 4TW2; -.
DR PDBsum; 5UPH; -.
DR PDBsum; 5XBM; -.
DR PDBsum; 6I2K; -.
DR AlphaFoldDB; Q14108; -.
DR SMR; Q14108; -.
DR BioGRID; 107388; 191.
DR ELM; Q14108; -.
DR IntAct; Q14108; 156.
DR MINT; Q14108; -.
DR STRING; 9606.ENSP00000264896; -.
DR TCDB; 9.B.39.1.13; the long chain fatty acid translocase (lcfat) family.
DR GlyConnect; 1479; 41 N-Linked glycans (7 sites).
DR GlyGen; Q14108; 11 sites, 45 N-linked glycans (8 sites), 1 O-linked glycan (1 site).
DR iPTMnet; Q14108; -.
DR PhosphoSitePlus; Q14108; -.
DR SwissPalm; Q14108; -.
DR BioMuta; SCARB2; -.
DR DMDM; 2498525; -.
DR CPTAC; CPTAC-127; -.
DR CPTAC; CPTAC-128; -.
DR EPD; Q14108; -.
DR jPOST; Q14108; -.
DR MassIVE; Q14108; -.
DR MaxQB; Q14108; -.
DR PaxDb; Q14108; -.
DR PeptideAtlas; Q14108; -.
DR PRIDE; Q14108; -.
DR ProteomicsDB; 16872; -.
DR ProteomicsDB; 59816; -. [Q14108-1]
DR ABCD; Q14108; 1 sequenced antibody.
DR Antibodypedia; 3014; 427 antibodies from 38 providers.
DR DNASU; 950; -.
DR Ensembl; ENST00000264896.8; ENSP00000264896.2; ENSG00000138760.11. [Q14108-1]
DR Ensembl; ENST00000452464.6; ENSP00000399154.2; ENSG00000138760.11. [Q14108-2]
DR GeneID; 950; -.
DR KEGG; hsa:950; -.
DR MANE-Select; ENST00000264896.8; ENSP00000264896.2; NM_005506.4; NP_005497.1.
DR UCSC; uc003hju.3; human. [Q14108-1]
DR CTD; 950; -.
DR DisGeNET; 950; -.
DR GeneCards; SCARB2; -.
DR GeneReviews; SCARB2; -.
DR HGNC; HGNC:1665; SCARB2.
DR HPA; ENSG00000138760; Low tissue specificity.
DR MalaCards; SCARB2; -.
DR MIM; 254900; phenotype.
DR MIM; 602257; gene.
DR neXtProt; NX_Q14108; -.
DR OpenTargets; ENSG00000138760; -.
DR Orphanet; 163696; Action myoclonus-renal failure syndrome.
DR Orphanet; 77259; Gaucher disease type 1.
DR Orphanet; 308; Progressive myoclonic epilepsy type 1.
DR PharmGKB; PA35038; -.
DR VEuPathDB; HostDB:ENSG00000138760; -.
DR eggNOG; KOG3776; Eukaryota.
DR GeneTree; ENSGT00940000153372; -.
DR HOGENOM; CLU_019853_3_0_1; -.
DR InParanoid; Q14108; -.
DR OMA; FLVMYIN; -.
DR PhylomeDB; Q14108; -.
DR TreeFam; TF317925; -.
DR PathwayCommons; Q14108; -.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR SignaLink; Q14108; -.
DR BioGRID-ORCS; 950; 16 hits in 1081 CRISPR screens.
DR ChiTaRS; SCARB2; human.
DR GeneWiki; SCARB2; -.
DR GenomeRNAi; 950; -.
DR Pharos; Q14108; Tbio.
DR PRO; PR:Q14108; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q14108; protein.
DR Bgee; ENSG00000138760; Expressed in inferior vagus X ganglion and 212 other tissues.
DR ExpressionAtlas; Q14108; baseline and differential.
DR Genevisible; Q14108; HS.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030666; C:endocytic vesicle membrane; ISS:ARUK-UCL.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:ARUK-UCL.
DR GO; GO:0010008; C:endosome membrane; TAS:ARUK-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; TAS:ARUK-UCL.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; TAS:ParkinsonsUK-UCL.
DR GO; GO:0043202; C:lysosomal lumen; ISS:BHF-UCL.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:ARUK-UCL.
DR GO; GO:0038024; F:cargo receptor activity; IMP:ARUK-UCL.
DR GO; GO:0051087; F:chaperone binding; IEA:Ensembl.
DR GO; GO:0015485; F:cholesterol binding; ISS:ARUK-UCL.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0031210; F:phosphatidylcholine binding; ISS:ARUK-UCL.
DR GO; GO:0001786; F:phosphatidylserine binding; ISS:ARUK-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:ARUK-UCL.
DR GO; GO:0005044; F:scavenger receptor activity; ISS:ARUK-UCL.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ARUK-UCL.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0015917; P:aminophospholipid transport; ISS:ARUK-UCL.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:ARUK-UCL.
DR GO; GO:0006622; P:protein targeting to lysosome; IMP:BHF-UCL.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISS:ARUK-UCL.
DR GO; GO:0043471; P:regulation of cellular carbohydrate catabolic process; IMP:ARUK-UCL.
DR GO; GO:1904978; P:regulation of endosome organization; TAS:ParkinsonsUK-UCL.
DR GO; GO:1905123; P:regulation of glucosylceramidase activity; IBA:GO_Central.
DR GO; GO:1905671; P:regulation of lysosome organization; TAS:ParkinsonsUK-UCL.
DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
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 3D-structure; Alternative splicing; Disease variant; Disulfide bond;
KW Epilepsy; Glycoprotein; Host cell receptor for virus entry;
KW Host-virus interaction; Lysosome; Membrane; Neurodegeneration; Receptor;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..478
FT /note="Lysosome membrane protein 2"
FT /id="PRO_0000144155"
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:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:24162852"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:24162852"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:24162852"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24162852"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519,
FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:24162852"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:24162852"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:24162852"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519,
FT ECO:0000269|PubMed:24162852"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 274..329
FT /evidence="ECO:0000269|PubMed:24162852"
FT DISULFID 312..318
FT /evidence="ECO:0000269|PubMed:24162852"
FT VAR_SEQ 93..235
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044826"
FT VARIANT 363
FT /note="H -> N (in EPM4; no renal failure;
FT dbSNP:rs758857853)"
FT /evidence="ECO:0000269|PubMed:19454373"
FT /id="VAR_066744"
FT VARIANT 471
FT /note="E -> G (may act as a modifier of Gaucher disease;
FT dbSNP:rs755903502)"
FT /evidence="ECO:0000269|PubMed:21796727"
FT /id="VAR_066745"
FT MUTAGEN 475
FT /note="L->A,G,D,V: Prevents the targeting of the protein to
FT lysosomes."
FT /evidence="ECO:0000269|PubMed:7509809"
FT MUTAGEN 475
FT /note="L->I: Some loss in the efficiency of targeting of
FT the protein to lysosomes."
FT /evidence="ECO:0000269|PubMed:7509809"
FT MUTAGEN 476
FT /note="I->A,V: Does not prevent the targeting of the
FT protein to lysosomes completely."
FT /evidence="ECO:0000269|PubMed:7509809"
FT MUTAGEN 476
FT /note="I->D,E,G: Prevents the targeting of the protein to
FT lysosomes."
FT /evidence="ECO:0000269|PubMed:7509809"
FT MUTAGEN 476
FT /note="I->L: Normal targeting of the protein to lysosomes."
FT /evidence="ECO:0000269|PubMed:7509809"
FT MUTAGEN 477
FT /note="R->A,E,G,K,Q: Normal targeting of the protein to
FT lysosomes."
FT /evidence="ECO:0000269|PubMed:7509809"
FT MUTAGEN 478
FT /note="T->G,I,S,V: Normal targeting of the protein to
FT lysosomes."
FT /evidence="ECO:0000269|PubMed:7509809"
FT CONFLICT 351
FT /note="S -> P (in Ref. 4; BAG59150)"
FT /evidence="ECO:0000305"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:4F7B"
FT HELIX 48..54
FT /evidence="ECO:0007829|PDB:4Q4F"
FT STRAND 60..70
FT /evidence="ECO:0007829|PDB:4Q4F"
FT HELIX 72..76
FT /evidence="ECO:0007829|PDB:4Q4F"
FT STRAND 82..103
FT /evidence="ECO:0007829|PDB:4Q4F"
FT TURN 104..107
FT /evidence="ECO:0007829|PDB:4Q4F"
FT STRAND 108..119
FT /evidence="ECO:0007829|PDB:4Q4F"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:4Q4F"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:4Q4F"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:4Q4F"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:4Q4F"
FT HELIX 138..148
FT /evidence="ECO:0007829|PDB:4Q4F"
FT HELIX 153..162
FT /evidence="ECO:0007829|PDB:4Q4F"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:4Q4F"
FT HELIX 173..178
FT /evidence="ECO:0007829|PDB:4Q4F"
FT HELIX 183..191
FT /evidence="ECO:0007829|PDB:4Q4F"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:4Q4F"
FT TURN 201..204
FT /evidence="ECO:0007829|PDB:4Q4F"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:4Q4F"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:4Q4F"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:4Q4F"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:4Q4F"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:4Q4F"
FT TURN 243..246
FT /evidence="ECO:0007829|PDB:4Q4F"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:6I2K"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:4Q4F"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:4Q4F"
FT STRAND 277..287
FT /evidence="ECO:0007829|PDB:4Q4F"
FT STRAND 290..296
FT /evidence="ECO:0007829|PDB:4Q4F"
FT HELIX 299..302
FT /evidence="ECO:0007829|PDB:4Q4F"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:4TW2"
FT HELIX 307..311
FT /evidence="ECO:0007829|PDB:4Q4F"
FT TURN 313..316
FT /evidence="ECO:0007829|PDB:4Q4F"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:4Q4F"
FT TURN 327..332
FT /evidence="ECO:0007829|PDB:4Q4F"
FT STRAND 335..338
FT /evidence="ECO:0007829|PDB:4Q4F"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:4Q4F"
FT HELIX 347..352
FT /evidence="ECO:0007829|PDB:4Q4F"
FT HELIX 360..363
FT /evidence="ECO:0007829|PDB:4Q4F"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:4Q4F"
FT TURN 371..374
FT /evidence="ECO:0007829|PDB:4Q4F"
FT STRAND 375..389
FT /evidence="ECO:0007829|PDB:4Q4F"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:4Q4F"
FT STRAND 404..416
FT /evidence="ECO:0007829|PDB:4Q4F"
FT HELIX 419..428
FT /evidence="ECO:0007829|PDB:4Q4F"
SQ SEQUENCE 478 AA; 54290 MW; FDCF27F3BA337B2C CRC64;
MGRCCFYTAG TLSLLLLVTS VTLLVARVFQ KAVDQSIEKK IVLRNGTEAF DSWEKPPLPV
YTQFYFFNVT NPEEILRGET PRVEEVGPYT YRELRNKANI QFGDNGTTIS AVSNKAYVFE
RDQSVGDPKI DLIRTLNIPV LTVIEWSQVH FLREIIEAML KAYQQKLFVT HTVDELLWGY
KDEILSLIHV FRPDISPYFG LFYEKNGTND GDYVFLTGED SYLNFTKIVE WNGKTSLDWW
ITDKCNMING TDGDSFHPLI TKDEVLYVFP SDFCRSVYIT FSDYESVQGL PAFRYKVPAE
ILANTSDNAG FCIPEGNCLG SGVLNVSICK NGAPIIMSFP HFYQADERFV SAIEGMHPNQ
EDHETFVDIN PLTGIILKAA KRFQINIYVK KLDDFVETGD IRTMVFPVMY LNESVHIDKE
TASRLKSMIN TTLIITNIPY IIMALGVFFG LVFTWLACKG QGSMDEGTAD ERAPLIRT
