ID Q9GJT3_SAGOE Unreviewed; 336 AA. AC Q9GJT3; DT 01-MAR-2001, integrated into UniProtKB/TrEMBL. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 111. DE SubName: Full=CDw150 {ECO:0000313|EMBL:AAG02017.1}; DE SubName: Full=Signaling lymphocytic activation molecule 1 {ECO:0000313|EMBL:AAG18445.1}; GN Name=CDw150 {ECO:0000313|EMBL:AAG18445.1}; OS Saguinus oedipus (Cotton-top tamarin). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae; OC Callitrichinae; Saguinus. OX NCBI_TaxID=9490 {ECO:0000313|EMBL:AAG18445.1}; RN [1] {ECO:0000313|EMBL:AAG02017.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Lymphoblastoid {ECO:0000313|EMBL:AAG02017.1}; RX PubMed=10972291; DOI=10.1038/35022579; RA Tatsuo H., Ono N., Tanaka K., Yanagi Y.; RT "SLAM (CDw150) is a cellular receptor for measles virus."; RL Nature 406:893-897(2000). RN [2] {ECO:0000313|EMBL:AAG18445.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=11145884; DOI=10.1006/viro.2000.0711; RA Hsu E.C., Iorio C., Sarangi F., Khine A.A., Richardson C.D.; RT "CDw150(SLAM) is a receptor for a lymphotropic strain of measles virus and RT may account for the immunosuppressive properties of this virus."; RL Virology 279:9-21(2001). RN [3] {ECO:0007829|PDB:3ALW, ECO:0007829|PDB:3ALX} RP X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 26-140, AND DISULFIDE BONDS. RX PubMed=21217702; DOI=10.1038/nsmb.1969; RA Hashiguchi T., Ose T., Kubota M., Maita N., Kamishikiryo J., Maenaka K., RA Yanagi Y.; RT "Structure of the measles virus hemagglutinin bound to its cellular RT receptor SLAM."; RL Nat. Struct. Mol. Biol. 18:135-141(2011). 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; AF257239; AAG02017.1; -; mRNA. DR EMBL; AF302038; AAG18445.1; -; mRNA. DR PDB; 3ALW; X-ray; 3.55 A; A=24-140. DR PDB; 3ALX; X-ray; 3.15 A; A/B/C/D=24-140. DR PDB; 3ALZ; X-ray; 4.51 A; B=1-140. DR PDBsum; 3ALW; -. DR PDBsum; 3ALX; -. DR PDBsum; 3ALZ; -. DR AlphaFoldDB; Q9GJT3; -. DR SMR; Q9GJT3; -. DR DIP; DIP-59071N; -. DR IntAct; Q9GJT3; 1. DR EvolutionaryTrace; Q9GJT3; -. DR GO; GO:0009986; C:cell surface; IEA:InterPro. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro. DR GO; GO:0046649; P:lymphocyte activation; IEA:InterPro. DR Gene3D; 2.60.40.10; Immunoglobulins; 2. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR010407; Sig_lymph_act_molc_N. DR PANTHER; PTHR12080; SIGNALING LYMPHOCYTIC ACTIVATION MOLECULE; 1. DR PANTHER; PTHR12080:SF49; SIGNALING LYMPHOCYTIC ACTIVATION MOLECULE; 1. DR Pfam; PF06214; SLAM; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:3ALW, ECO:0007829|PDB:3ALX}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1..24 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 25..336 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5007716823" FT TRANSMEM 240..261 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 144..223 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT DISULFID 32..132 FT /evidence="ECO:0007829|PDB:3ALW, ECO:0007829|PDB:3ALX" SQ SEQUENCE 336 AA; 37717 MW; 5D5B4ED7FDAEA764 CRC64; MDPKGLFSLT FVLFLSLAFE PSYGTGGRMM NCPKIVQQLG SDVLLPLTHE RINTSMNKSI HIVVTMAKSL ENSVENKIVS LDPSEAGPPR YLKDRYRFYL ENLSLAIRES TKKDEGWYFM TLEKNISVQR FCLHLKLYEQ VSTPEIKVLN KTQENGTCTL ILGCIVKKGD HVAYSWSEKA GTHPLSPANS SHLLSLTLGP QHAKNIYVCT VSNPISNSSQ DFIPWLRCRQ EPSETNIWPV YAWLSLAGVI IILIVIAIML LRRRGKTDHY QTTTEKKNLT IYAQVQKPGP LQKKLDSFPA QDPCTTIYVA ATEPVPEPVQ ETNSITVYAS VTLPES //