ID Q8N355_HUMAN Unreviewed; 234 AA. AC Q8N355; DT 01-OCT-2002, integrated into UniProtKB/TrEMBL. DT 01-OCT-2002, sequence version 1. DT 27-MAR-2024, entry version 150. DE SubName: Full=IGL@ protein {ECO:0000313|EMBL:AAH28090.1}; GN Name=IGL@ {ECO:0000313|EMBL:AAH28090.1}; 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 {ECO:0000313|EMBL:AAH28090.1}; RN [1] {ECO:0000313|EMBL:AAH28090.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain {ECO:0000313|EMBL:AAH28090.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M., RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.; 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 [2] {ECO:0007829|PDB:2DD8} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 20-234, AND DISULFIDE BONDS. RX PubMed=16597622; DOI=10.1074/jbc.m600697200; RA Prabakaran P., Gan J., Feng Y., Zhu Z., Choudhry V., Xiao X., Ji X., RA Dimitrov D.S.; RT "Structure of severe acute respiratory syndrome coronavirus receptor- RT binding domain complexed with neutralizing antibody."; RL J. Biol. Chem. 281:15829-15836(2006). RN [3] {ECO:0007829|PDB:5UGY} RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 22-231, AND DISULFIDE BONDS. RX PubMed=21825125; DOI=10.1073/pnas.1111497108; RA Whittle J.R., Zhang R., Khurana S., King L.R., Manischewitz J., Golding H., RA Dormitzer P.R., Haynes B.F., Walter E.B., Moody M.A., Kepler T.B., RA Liao H.X., Harrison S.C.; RT "Broadly neutralizing human antibody that recognizes the receptor-binding RT pocket of influenza virus hemagglutinin."; RL Proc. Natl. Acad. Sci. U.S.A. 108:14216-14221(2011). RN [4] {ECO:0007829|PDB:4FQQ} RP X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) OF 20-234, AND DISULFIDE BONDS. RX PubMed=23115339; DOI=10.1073/pnas.1217207109; RA Mouquet H., Scharf L., Euler Z., Liu Y., Eden C., Scheid J.F., RA Halper-Stromberg A., Gnanapragasam P.N., Spencer D.I., Seaman M.S., RA Schuitemaker H., Feizi T., Nussenzweig M.C., Bjorkman P.J.; RT "Complex-type N-glycan recognition by potent broadly neutralizing HIV RT antibodies."; RL Proc. Natl. Acad. Sci. U.S.A. 109:E3268-E3277(2012). RN [5] {ECO:0007829|PDB:4HK0, ECO:0007829|PDB:4HK3} RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 22-234, AND DISULFIDE BONDS. RX PubMed=23175789; DOI=10.1073/pnas.1218256109; RA Schmidt A.G., Xu H., Khan A.R., O'Donnell T., Khurana S., King L.R., RA Manischewitz J., Golding H., Suphaphiphat P., Carfi A., Settembre E.C., RA Dormitzer P.R., Kepler T.B., Zhang R., Moody M.A., Haynes B.F., Liao H.X., RA Shaw D.E., Harrison S.C.; RT "Preconfiguration of the antigen-binding site during affinity maturation of RT a broadly neutralizing influenza virus antibody."; RL Proc. Natl. Acad. Sci. U.S.A. 110:264-269(2013). RN [6] {ECO:0007829|PDB:6DC3} RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 22-234, AND DISULFIDE BONDS. RX PubMed=31306469; DOI=10.1371/journal.ppat.1007944; RA Jones H.G., Battles M.B., Lin C.C., Bianchi S., Corti D., McLellan J.S.; RT "Alternative conformations of a major antigenic site on RSV F."; RL PLoS Pathog. 15:e1007944-e1007944(2019). RN [7] {ECO:0007829|PDB:6UDJ, ECO:0007829|PDB:6UDK} RP STRUCTURE BY ELECTRON MICROSCOPY (2.50 ANGSTROMS) OF 20-234, AND DISULFIDE RP BONDS. RX PubMed=32004464; DOI=10.1016/j.cell.2020.01.010; RA Schommers P., Gruell H., Abernathy M.E., Tran M.K., Dingens A.S., RA Gristick H.B., Barnes C.O., Schoofs T., Schlotz M., Vanshylla K., Kreer C., RA Weiland D., Holtick U., Scheid C., Valter M.M., van Gils M.J., RA Sanders R.W., Vehreschild J.J., Cornely O.A., Lehmann C., Fatkenheuer G., RA Seaman M.S., Bloom J.D., Bjorkman P.J., Klein F.; RT "Restriction of HIV-1 Escape by a Highly Broad and Potent Neutralizing RT Antibody."; RL Cell 180:471-489.e22(2020). RN [8] {ECO:0007829|PDB:6VPY} RP X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS) OF 20-234, AND DISULFIDE BONDS. RX PubMed=32765530; DOI=10.3389/fimmu.2020.01529; RA Zhou J.O., Zaidi H.A., Ton T., Fera D.; RT "The Effects of Framework Mutations at the Variable Domain Interface on RT Antibody Affinity Maturation in an HIV-1 Broadly Neutralizing Antibody RT Lineage."; RL Front. Immunol. 11:1529-1529(2020). CC -!- INTERACTION: CC Q8N355; O43765: SGTA; NbExp=4; IntAct=EBI-748681, EBI-347996; CC Q8N355; Q9UMX0: UBQLN1; NbExp=4; IntAct=EBI-748681, EBI-741480; CC Q8N355; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-748681, EBI-10173939; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}. 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; BC028090; AAH28090.1; -; mRNA. DR PIR; S09713; S09713. DR PIR; S12441; S12441. DR PIR; S30527; S30527. DR PDB; 2DD8; X-ray; 2.30 A; L=20-234. DR PDB; 4FQQ; X-ray; 2.42 A; A/C/E/L=20-234. DR PDB; 4HK0; X-ray; 2.50 A; B/D=22-234. DR PDB; 4HK3; X-ray; 3.00 A; N=22-234. DR PDB; 5UGY; X-ray; 2.80 A; L/M/N=22-231. DR PDB; 6DC3; X-ray; 3.50 A; L=22-234. DR PDB; 6UDJ; EM; 2.50 A; B/L/R=20-234. DR PDB; 6UDK; EM; 3.90 A; B/I/P=20-234. DR PDB; 6VPY; X-ray; 2.36 A; B/L=20-234. DR PDBsum; 4FQQ; -. DR PDBsum; 4HK0; -. DR PDBsum; 4HK3; -. DR PDBsum; 6UDJ; -. DR PDBsum; 6UDK; -. DR AlphaFoldDB; Q8N355; -. DR SMR; Q8N355; -. DR IntAct; Q8N355; 5. DR MaxQB; Q8N355; -. DR ChiTaRS; IGL; human. DR CDD; cd07699; IgC1_L; 1. DR CDD; cd04984; IgV_L_lambda; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 2. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR013106; Ig_V-set. DR PANTHER; PTHR19944:SF98; IG-LIKE DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR19944; MHC CLASS II-RELATED; 1. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF07686; V-set; 1. DR SMART; SM00409; IG; 2. DR SMART; SM00407; IGc1; 1. DR SMART; SM00406; IGv; 1. DR SUPFAM; SSF48726; Immunoglobulin; 2. DR PROSITE; PS50835; IG_LIKE; 2. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:2DD8, ECO:0007829|PDB:4FQQ}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..16 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 17..234 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004314219" FT DOMAIN 20..108 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT DOMAIN 135..229 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT DISULFID 41..106 FT /evidence="ECO:0007829|PDB:2DD8, ECO:0007829|PDB:4FQQ" FT DISULFID 156..215 FT /evidence="ECO:0007829|PDB:2DD8, ECO:0007829|PDB:4FQQ" SQ SEQUENCE 234 AA; 24793 MW; CC848CAEBA4A9D63 CRC64; MAWTVLLLGL LSHCTGSVTS YVLTQPPSVS VAPGQTARIT CGGNNIGSKS VHWYQQKPGQ APVLVVYDDS DRPSGIPERF SGSNSGNTAT LTISRVDAGD EADYYCQLWD SSSDHPVVFG GGTKLTVLGQ PKAAPSVTLF PPSSEELQAN KATLVCLISD FYPGAVTVAW KADSSPVKAG VETTTPSKQS NNKYAASSYL SLTPEQWKSH RSYSCQVTHE GSTVEKTVAP TECS //