IGLL1_HUMAN
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 03-AUG-2022, entry version 195.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 be
RT expressed as an Ig lambda 14.1-like protein or as a canonical B cell Ig
RT lambda light chain: implications for Ig lambda gene 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., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., 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., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., 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., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA 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 project:
RT 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 1)
RT contains gene(s) selectively expressed in pre-B cells and is the human
RT 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., Turoczi L.,
RA 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 and
RT agammaglobulinemia.";
RL J. Exp. Med. 187:71-77(1998).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 93-209 IN COMPLEX WITH VPREB1,
RP 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., 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 (PubMed:17431183).
CC Interacts with SYNV1/HRD1 (via N-terminus); this interaction leads to
CC increased IGLL1 ubiquitination and degradation in pre-B cells, possibly
CC through a lysosomal, not proteasomal, pathway (By similarity).
CC {ECO:0000250|UniProtKB:P20764, ECO:0000269|PubMed:17431183}.
CC -!- INTERACTION:
CC P15814; B3EWG5: FAM25C; NbExp=3; IntAct=EBI-1222221, EBI-14240149;
CC P15814; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-1222221, EBI-947187;
CC P15814; Q2GHU2: ECH_0166; Xeno; NbExp=2; IntAct=EBI-1222221, EBI-26585631;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P20764}. Secreted {ECO:0000269|PubMed:9419212}.
CC Note=In pre-B cells, localizes predominantly to the endoplasmic
CC reticulum. {ECO:0000250|UniProtKB:P20764}.
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 -!- TISSUE SPECIFICITY: Expressed only in pre-B-cells and a special B-cell
CC line (which is surface Ig negative). {ECO:0000269|PubMed:2128466}.
CC -!- DISEASE: Agammaglobulinemia 2, autosomal recessive (AGM2) [MIM:613500]:
CC A primary immunodeficiency characterized by profoundly low or absent
CC serum antibodies and low or absent circulating B cells due to an early
CC block of B-cell development. Affected individuals develop severe
CC infections in the first years of life. {ECO:0000269|PubMed:9419212}.
CC Note=The disease is caused by variants affecting the gene represented
CC 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";
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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 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 AlphaFoldDB; P15814; -.
DR BMRB; P15814; -.
DR SMR; P15814; -.
DR BioGRID; 109759; 8.
DR CORUM; P15814; -.
DR IntAct; P15814; 9.
DR MINT; P15814; -.
DR STRING; 9606.ENSP00000329312; -.
DR DrugBank; DB09130; Copper.
DR GlyGen; P15814; 2 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; P15814; -.
DR PhosphoSitePlus; P15814; -.
DR BioMuta; IGLL1; -.
DR DMDM; 123944; -.
DR jPOST; P15814; -.
DR MassIVE; P15814; -.
DR MaxQB; P15814; -.
DR PaxDb; P15814; -.
DR PeptideAtlas; P15814; -.
DR PRIDE; P15814; -.
DR ProteomicsDB; 53223; -. [P15814-1]
DR ProteomicsDB; 53224; -. [P15814-2]
DR Antibodypedia; 9342; 295 antibodies from 30 providers.
DR DNASU; 3543; -.
DR Ensembl; ENST00000249053.3; ENSP00000249053.3; ENSG00000128322.7. [P15814-2]
DR Ensembl; ENST00000330377.3; ENSP00000329312.2; ENSG00000128322.7. [P15814-1]
DR GeneID; 3543; -.
DR KEGG; hsa:3543; -.
DR MANE-Select; ENST00000330377.3; ENSP00000329312.2; NM_020070.4; NP_064455.1.
DR UCSC; uc002zxd.4; human. [P15814-1]
DR CTD; 3543; -.
DR DisGeNET; 3543; -.
DR GeneCards; IGLL1; -.
DR HGNC; HGNC:5870; IGLL1.
DR HPA; ENSG00000128322; Group enriched (bone marrow, testis).
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 VEuPathDB; HostDB:ENSG00000128322; -.
DR eggNOG; ENOG502SPNC; Eukaryota.
DR GeneTree; ENSGT00940000153307; -.
DR HOGENOM; CLU_2526772_0_0_1; -.
DR InParanoid; P15814; -.
DR OMA; PHSRYSC; -.
DR OrthoDB; 1568661at2759; -.
DR PhylomeDB; P15814; -.
DR TreeFam; TF335549; -.
DR PathwayCommons; P15814; -.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR SignaLink; P15814; -.
DR BioGRID-ORCS; 3543; 28 hits in 1071 CRISPR screens.
DR ChiTaRS; IGLL1; human.
DR EvolutionaryTrace; P15814; -.
DR GeneWiki; IGLL1; -.
DR GenomeRNAi; 3543; -.
DR Pharos; P15814; Tbio.
DR PRO; PR:P15814; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P15814; protein.
DR Bgee; ENSG00000128322; Expressed in bone marrow and 101 other tissues.
DR ExpressionAtlas; P15814; baseline and differential.
DR Genevisible; P15814; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
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: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; Disease variant; Disulfide bond;
KW Endoplasmic reticulum; Immunoglobulin domain; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..37
FT /evidence="ECO:0000255"
FT CHAIN 38..213
FT /note="Immunoglobulin lambda-like polypeptide 1"
FT /id="PRO_0000014777"
FT DOMAIN 114..208
FT /note="Ig-like C1-type"
FT REGION 97..108
FT /note="J region (By similarity to lambda light-chain)"
FT REGION 109..213
FT /note="C region (By similarity to lambda light-chain)"
FT DISULFID 135..194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:17431183"
FT DISULFID 212
FT /note="Interchain (with a heavy chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 70..213
FT /note="FLLQRGSWTGPRCWPRGFQSKHNSVTHVFGSGTQLTVLSQPKATPSVTLFPP
FT SSEELQANKATLVCLMNDFYPGILTVTWKADGTPITQGVEMTTPSKQSNNKYAASSYLS
FT LTPEQWRSRRSYSCQVMHEGSTVEKTVAPAECS -> SAQGHPLGHSVPAVL (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042748"
FT VARIANT 142
FT /note="P -> L (in AGM2; dbSNP:rs1064422)"
FT /evidence="ECO:0000269|PubMed:9419212"
FT /id="VAR_034869"
FT VARIANT 189
FT /note="R -> H (in dbSNP:rs8138122)"
FT /id="VAR_059392"
FT TURN 61..65
FT /evidence="ECO:0007829|PDB:2LKQ"
FT HELIX 66..70
FT /evidence="ECO:0007829|PDB:2LKQ"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:2LKQ"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:2H3N"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:2H3N"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:2H3N"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:2H3N"
FT STRAND 131..143
FT /evidence="ECO:0007829|PDB:2H3N"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:2H3N"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:2H3N"
FT STRAND 173..181
FT /evidence="ECO:0007829|PDB:2H3N"
FT HELIX 183..188
FT /evidence="ECO:0007829|PDB:2H3N"
FT STRAND 192..198
FT /evidence="ECO:0007829|PDB:2H3N"
FT STRAND 201..207
FT /evidence="ECO:0007829|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
