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 27-MAR-2024, entry version 210. 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 GBA1. 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 GBA1. 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 (GBA1) 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 GBA1. {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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EMDB; EMD-0332; -. DR SMR; Q14108; -. DR BioGRID; 107388; 201. DR ELM; Q14108; -. DR IntAct; Q14108; 157. 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 GlyCosmos; Q14108; 10 sites, 43 glycans. 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; 9606-ENSP00000264896; -. DR PeptideAtlas; Q14108; -. DR ProteomicsDB; 16872; -. DR ProteomicsDB; 59816; -. [Q14108-1] DR Pumba; Q14108; -. DR ABCD; Q14108; 1 sequenced antibody. DR Antibodypedia; 3014; 474 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 AGR; HGNC:1665; -. 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; ARIVEWN; -. DR OrthoDB; 315994at2759; -. 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 1161 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 214 other cell types or tissues. DR ExpressionAtlas; Q14108; baseline and differential. 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: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: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:0051087; F:protein-folding chaperone binding; IEA:Ensembl. 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:0099638; P:endosome to plasma membrane protein transport; 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:0043470; P:regulation of carbohydrate catabolic process; IMP:ARUK-UCL. DR GO; GO:1904978; P:regulation of endosome organization; TAS:ParkinsonsUK-UCL. DR GO; GO:2000752; P:regulation of glucosylceramide catabolic process; TAS:ARUK-UCL. 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:SF92; LYSOSOME MEMBRANE PROTEIN 2; 1. DR PANTHER; PTHR11923; SCAVENGER RECEPTOR CLASS B TYPE-1 SR-B1; 1. DR Pfam; PF01130; CD36; 1. DR PRINTS; PR01609; CD36FAMILY. DR PRINTS; PR01611; LIMPII. DR Genevisible; Q14108; HS. 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 GBA1" 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 //