ID IGLL1_HUMAN Reviewed; 213 AA. AC P15814; Q0P681; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 16-JAN-2019, entry version 175. DE RecName: Full=Immunoglobulin lambda-like polypeptide 1; DE AltName: Full=CD179 antigen-like family member B; DE AltName: Full=Ig lambda-5; DE AltName: Full=Immunoglobulin omega polypeptide; DE AltName: Full=Immunoglobulin-related protein 14.1; DE AltName: CD_antigen=CD179b; DE Flags: Precursor; GN Name=IGLL1; Synonyms=IGL1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=2501791; DOI=10.1073/pnas.86.14.5552; RA Hollis G.F., Evans R.J., Stafford-Hollis J.M., Korsmeyer S.J., RA McKearn J.P.; RT "Immunoglobulin lambda light-chain-related genes 14.1 and 16.1 are RT expressed in pre-B cells and may encode the human immunoglobulin omega RT light-chain protein."; RL Proc. Natl. Acad. Sci. U.S.A. 86:5552-5556(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Lymphoid tissue; RX PubMed=1703205; DOI=10.1084/jem.173.2.305; RA Evans R.J., Hollis G.F.; RT "Genomic structure of the human Ig lambda 1 gene suggests that it may RT be expressed as an Ig lambda 14.1-like protein or as a canonical B RT cell Ig lambda light chain: implications for Ig lambda gene RT evolution."; RL J. Exp. Med. 173:305-311(1991). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J., RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., RA Khan A.S., Lane L., Tilahun Y., Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Testis; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-193, AND TISSUE SPECIFICITY. RX PubMed=2128466; DOI=10.1093/intimm/2.3.201; RA Schiff C., Bensmana M., Guglielmi P., Milili M., Lefranc M.-P., RA Fougereau M.; RT "The immunoglobulin lambda-like gene cluster (14.1, 16.1 and F lambda RT 1) contains gene(s) selectively expressed in pre-B cells and is the RT human counterpart of the mouse lambda 5 gene."; RL Int. Immunol. 2:201-207(1990). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 95-213. RX PubMed=3003227; DOI=10.1084/jem.163.2.425; RA Chang H., Dmitrovsky E., Hieter P.A., Mitchell K., Leder P., RA Turoczi L., Kirsch I.R., Hollis G.F.; RT "Identification of three new Ig lambda-like genes in man."; RL J. Exp. Med. 163:425-435(1986). RN [7] RP FUNCTION, SUBCELLULAR LOCATION, AND VARIANT AGM2 LEU-142. RX PubMed=9419212; DOI=10.1084/jem.187.1.71; RA Minegishi Y., Coustan-Smith E., Wang Y.H., Cooper M.D., Campana D., RA Conley M.E.; RT "Mutations in the human lambda5/14.1 gene result in B cell deficiency RT and agammaglobulinemia."; RL J. Exp. Med. 187:71-77(1998). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 93-209 IN COMPLEX WITH RP VPREB1, SUBUNIT, AND DISULFIDE BOND. RX PubMed=17431183; DOI=10.1126/science.1139412; RA Bankovich A.J., Raunser S., Juo Z.S., Walz T., Davis M.M., RA Garcia K.C.; RT "Structural insight into pre-B cell receptor function."; RL Science 316:291-294(2007). CC -!- FUNCTION: Critical for B-cell development. CC {ECO:0000269|PubMed:9419212}. CC -!- SUBUNIT: Associates non-covalently with VPREB1. CC {ECO:0000269|PubMed:17431183}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9419212}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P15814-1; Sequence=Displayed; CC Name=2; CC IsoId=P15814-2; Sequence=VSP_042748; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Expressed only in pre-B-cells and a special B- CC cell line (which is surface Ig negative). CC {ECO:0000269|PubMed:2128466}. CC -!- DISEASE: Agammaglobulinemia 2, autosomal recessive (AGM2) CC [MIM:613500]: A primary immunodeficiency characterized by CC profoundly low or absent serum antibodies and low or absent CC circulating B cells due to an early block of B-cell development. CC Affected individuals develop severe infections in the first years CC of life. {ECO:0000269|PubMed:9419212}. Note=The disease is caused CC by mutations affecting the gene represented in this entry. CC -!- WEB RESOURCE: Name=IGLL1base; Note=IGLL1 mutation db; CC URL="http://structure.bmc.lu.se/idbase/IGLL1base/"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=IGLL1; CC URL="https://en.wikipedia.org/wiki/IGLL1"; 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; M27749; AAA36100.1; -; mRNA. DR EMBL; M34513; AAA36096.1; -; Genomic_DNA. DR EMBL; M34511; AAA36096.1; JOINED; Genomic_DNA. DR EMBL; M34512; AAA36096.1; JOINED; Genomic_DNA. DR EMBL; AP000345; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC030239; AAH30239.2; -; mRNA. DR EMBL; BC012293; AAH12293.1; -; mRNA. DR EMBL; X03528; CAA27229.1; -; Genomic_DNA. DR EMBL; X03530; CAA27231.1; -; Genomic_DNA. DR CCDS; CCDS13809.1; -. [P15814-1] DR CCDS; CCDS13810.1; -. [P15814-2] DR PIR; A33911; A33911. DR RefSeq; NP_064455.1; NM_020070.3. [P15814-1] DR RefSeq; NP_690594.1; NM_152855.2. [P15814-2] DR UniGene; Hs.348935; -. DR PDB; 2H32; X-ray; 2.70 A; B=93-213. DR PDB; 2H3N; X-ray; 2.30 A; B/D=94-209. DR PDB; 2LKQ; NMR; -; A=59-82. DR PDBsum; 2H32; -. DR PDBsum; 2H3N; -. DR PDBsum; 2LKQ; -. DR ProteinModelPortal; P15814; -. DR SMR; P15814; -. DR BioGrid; 109759; 3. DR CORUM; P15814; -. DR IntAct; P15814; 6. DR MINT; P15814; -. DR STRING; 9606.ENSP00000329312; -. DR iPTMnet; P15814; -. DR PhosphoSitePlus; P15814; -. DR BioMuta; IGLL1; -. DR DMDM; 123944; -. DR jPOST; P15814; -. DR MaxQB; P15814; -. DR PaxDb; P15814; -. DR PeptideAtlas; P15814; -. DR PRIDE; P15814; -. DR ProteomicsDB; 53223; -. DR ProteomicsDB; 53224; -. [P15814-2] DR DNASU; 3543; -. DR Ensembl; ENST00000249053; ENSP00000249053; ENSG00000128322. [P15814-2] DR Ensembl; ENST00000330377; ENSP00000329312; ENSG00000128322. [P15814-1] DR GeneID; 3543; -. DR KEGG; hsa:3543; -. DR UCSC; uc002zxd.4; human. [P15814-1] DR CTD; 3543; -. DR DisGeNET; 3543; -. DR EuPathDB; HostDB:ENSG00000128322.6; -. DR GeneCards; IGLL1; -. DR HGNC; HGNC:5870; IGLL1. DR HPA; HPA051134; -. DR HPA; HPA071406; -. DR MalaCards; IGLL1; -. DR MIM; 146770; gene. DR MIM; 613500; phenotype. DR neXtProt; NX_P15814; -. DR OpenTargets; ENSG00000128322; -. DR Orphanet; 33110; Autosomal agammaglobulinemia. DR PharmGKB; PA29756; -. DR eggNOG; ENOG410J0XA; Eukaryota. DR eggNOG; ENOG410YZ00; LUCA. DR GeneTree; ENSGT00940000153307; -. DR HOGENOM; HOG000119396; -. DR HOVERGEN; HBG108319; -. DR InParanoid; P15814; -. DR KO; K06554; -. DR OMA; WKVDGIP; -. DR OrthoDB; 1568661at2759; -. DR PhylomeDB; P15814; -. DR TreeFam; TF335549; -. DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall. DR EvolutionaryTrace; P15814; -. DR GeneWiki; IGLL1; -. DR GenomeRNAi; 3543; -. DR PRO; PR:P15814; -. DR Proteomes; UP000005640; Chromosome 22. DR Bgee; ENSG00000128322; Expressed in 61 organ(s), highest expression level in bone marrow. DR CleanEx; HS_IGLL1; -. DR ExpressionAtlas; P15814; baseline and differential. DR Genevisible; P15814; HS. DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0042571; C:immunoglobulin complex, circulating; IBA:GO_Central. DR GO; GO:0016020; C:membrane; NAS:UniProtKB. DR GO; GO:0003823; F:antigen binding; IBA:GO_Central. DR GO; GO:0034987; F:immunoglobulin receptor binding; IBA:GO_Central. DR GO; GO:0050853; P:B cell receptor signaling pathway; IBA:GO_Central. DR GO; GO:0006958; P:complement activation, classical pathway; IBA:GO_Central. DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central. DR GO; GO:0006955; P:immune response; NAS:UniProtKB. DR GO; GO:0045087; P:innate immune response; IBA:GO_Central. DR GO; GO:0050900; P:leukocyte migration; TAS:Reactome. DR GO; GO:0006911; P:phagocytosis, engulfment; IBA:GO_Central. DR GO; GO:0006910; P:phagocytosis, recognition; IBA:GO_Central. DR GO; GO:0050871; P:positive regulation of B cell activation; IBA:GO_Central. DR Gene3D; 2.60.40.10; -; 1. 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 Pfam; PF07654; C1-set; 1. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Complete proteome; KW Disease mutation; Disulfide bond; Immunoglobulin domain; Polymorphism; KW Reference proteome; Secreted; Signal. FT SIGNAL 1 37 {ECO:0000255}. FT CHAIN 38 213 Immunoglobulin lambda-like polypeptide 1. FT /FTId=PRO_0000014777. FT DOMAIN 114 208 Ig-like C1-type. FT REGION 97 108 J region (By similarity to lambda light- FT chain). FT REGION 109 213 C region (By similarity to lambda light- FT chain). FT DISULFID 135 194 {ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:17431183}. FT DISULFID 212 212 Interchain (with a heavy chain). FT {ECO:0000255|PROSITE-ProRule:PRU00114}. FT VAR_SEQ 70 213 FLLQRGSWTGPRCWPRGFQSKHNSVTHVFGSGTQLTVLSQP FT KATPSVTLFPPSSEELQANKATLVCLMNDFYPGILTVTWKA FT DGTPITQGVEMTTPSKQSNNKYAASSYLSLTPEQWRSRRSY FT SCQVMHEGSTVEKTVAPAECS -> SAQGHPLGHSVPAVL FT (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_042748. FT VARIANT 142 142 P -> L (in AGM2; dbSNP:rs1064422). FT {ECO:0000269|PubMed:9419212}. FT /FTId=VAR_034869. FT VARIANT 189 189 R -> H (in dbSNP:rs8138122). FT /FTId=VAR_059392. FT TURN 61 65 {ECO:0000244|PDB:2LKQ}. FT HELIX 66 70 {ECO:0000244|PDB:2LKQ}. FT HELIX 72 75 {ECO:0000244|PDB:2LKQ}. FT STRAND 102 108 {ECO:0000244|PDB:2H3N}. FT STRAND 115 119 {ECO:0000244|PDB:2H3N}. FT HELIX 123 126 {ECO:0000244|PDB:2H3N}. FT TURN 127 129 {ECO:0000244|PDB:2H3N}. FT STRAND 131 143 {ECO:0000244|PDB:2H3N}. FT STRAND 146 151 {ECO:0000244|PDB:2H3N}. FT STRAND 158 162 {ECO:0000244|PDB:2H3N}. FT STRAND 173 181 {ECO:0000244|PDB:2H3N}. FT HELIX 183 188 {ECO:0000244|PDB:2H3N}. FT STRAND 192 198 {ECO:0000244|PDB:2H3N}. FT STRAND 201 207 {ECO:0000244|PDB:2H3N}. SQ SEQUENCE 213 AA; 22963 MW; 9133A7742B943C79 CRC64; MRPGTGQGGL EAPGEPGPNL RQRWPLLLLG LAVVTHGLLR PTAASQSRAL GPGAPGGSSR SSLRSRWGRF LLQRGSWTGP RCWPRGFQSK HNSVTHVFGS GTQLTVLSQP KATPSVTLFP PSSEELQANK ATLVCLMNDF YPGILTVTWK ADGTPITQGV EMTTPSKQSN NKYAASSYLS LTPEQWRSRR SYSCQVMHEG STVEKTVAPA ECS //