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Immunoglobulin lambda-like polypeptide 1 (CD179 antigen-like family member B) (Ig lambda-5) (Immunoglobulin omega polypeptide) (Immunoglobulin-related protein 14.1) (CD antigen CD179b)

 IGLL1_HUMAN             Reviewed;         213 AA.
P15814; Q0P681;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
27-SEP-2017, entry version 166.
RecName: Full=Immunoglobulin lambda-like polypeptide 1;
AltName: Full=CD179 antigen-like family member B;
AltName: Full=Ig lambda-5;
AltName: Full=Immunoglobulin omega polypeptide;
AltName: Full=Immunoglobulin-related protein 14.1;
AltName: CD_antigen=CD179b;
Flags: Precursor;
Name=IGLL1; Synonyms=IGL1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2501791; DOI=10.1073/pnas.86.14.5552;
Hollis G.F., Evans R.J., Stafford-Hollis J.M., Korsmeyer S.J.,
McKearn J.P.;
"Immunoglobulin lambda light-chain-related genes 14.1 and 16.1 are
expressed in pre-B cells and may encode the human immunoglobulin omega
light-chain protein.";
Proc. Natl. Acad. Sci. U.S.A. 86:5552-5556(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Lymphoid tissue;
PubMed=1703205; DOI=10.1084/jem.173.2.305;
Evans R.J., Hollis G.F.;
"Genomic structure of the human Ig lambda 1 gene suggests that it may
be expressed as an Ig lambda 14.1-like protein or as a canonical B
cell Ig lambda light chain: implications for Ig lambda gene
evolution.";
J. Exp. Med. 173:305-311(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-193, AND TISSUE SPECIFICITY.
PubMed=2128466; DOI=10.1093/intimm/2.3.201;
Schiff C., Bensmana M., Guglielmi P., Milili M., Lefranc M.-P.,
Fougereau M.;
"The immunoglobulin lambda-like gene cluster (14.1, 16.1 and F lambda
1) contains gene(s) selectively expressed in pre-B cells and is the
human counterpart of the mouse lambda 5 gene.";
Int. Immunol. 2:201-207(1990).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 95-213.
PubMed=3003227; DOI=10.1084/jem.163.2.425;
Chang H., Dmitrovsky E., Hieter P.A., Mitchell K., Leder P.,
Turoczi L., Kirsch I.R., Hollis G.F.;
"Identification of three new Ig lambda-like genes in man.";
J. Exp. Med. 163:425-435(1986).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND VARIANT AGM2 LEU-142.
PubMed=9419212; DOI=10.1084/jem.187.1.71;
Minegishi Y., Coustan-Smith E., Wang Y.H., Cooper M.D., Campana D.,
Conley M.E.;
"Mutations in the human lambda5/14.1 gene result in B cell deficiency
and agammaglobulinemia.";
J. Exp. Med. 187:71-77(1998).
[8]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 93-209 IN COMPLEX WITH
VPREB1, SUBUNIT, AND DISULFIDE BOND.
PubMed=17431183; DOI=10.1126/science.1139412;
Bankovich A.J., Raunser S., Juo Z.S., Walz T., Davis M.M.,
Garcia K.C.;
"Structural insight into pre-B cell receptor function.";
Science 316:291-294(2007).
-!- FUNCTION: Critical for B-cell development.
{ECO:0000269|PubMed:9419212}.
-!- SUBUNIT: Associates non-covalently with VPREB1.
{ECO:0000269|PubMed:17431183}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9419212}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P15814-1; Sequence=Displayed;
Name=2;
IsoId=P15814-2; Sequence=VSP_042748;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed only in pre-B-cells and a special B-
cell line (which is surface Ig negative).
{ECO:0000269|PubMed:2128466}.
-!- DISEASE: Agammaglobulinemia 2, autosomal recessive (AGM2)
[MIM:613500]: A primary immunodeficiency characterized by
profoundly low or absent serum antibodies and low or absent
circulating B cells due to an early block of B-cell development.
Affected individuals develop severe infections in the first years
of life. {ECO:0000269|PubMed:9419212}. Note=The disease is caused
by mutations affecting the gene represented in this entry.
-!- WEB RESOURCE: Name=IGLL1base; Note=IGLL1 mutation db;
URL="http://structure.bmc.lu.se/idbase/IGLL1base/";
-!- WEB RESOURCE: Name=Wikipedia; Note=IGLL1;
URL="https://en.wikipedia.org/wiki/IGLL1";
-----------------------------------------------------------------------
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EMBL; M27749; AAA36100.1; -; mRNA.
EMBL; M34513; AAA36096.1; -; Genomic_DNA.
EMBL; M34511; AAA36096.1; JOINED; Genomic_DNA.
EMBL; M34512; AAA36096.1; JOINED; Genomic_DNA.
EMBL; AP000345; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC030239; AAH30239.2; -; mRNA.
EMBL; BC012293; AAH12293.1; -; mRNA.
EMBL; X03528; CAA27229.1; -; Genomic_DNA.
EMBL; X03530; CAA27231.1; -; Genomic_DNA.
CCDS; CCDS13809.1; -. [P15814-1]
CCDS; CCDS13810.1; -. [P15814-2]
PIR; A33911; A33911.
RefSeq; NP_064455.1; NM_020070.3. [P15814-1]
RefSeq; NP_690594.1; NM_152855.2. [P15814-2]
UniGene; Hs.348935; -.
PDB; 2H32; X-ray; 2.70 A; B=93-213.
PDB; 2H3N; X-ray; 2.30 A; B/D=94-209.
PDB; 2LKQ; NMR; -; A=59-82.
PDBsum; 2H32; -.
PDBsum; 2H3N; -.
PDBsum; 2LKQ; -.
ProteinModelPortal; P15814; -.
SMR; P15814; -.
BioGrid; 109759; 3.
CORUM; P15814; -.
IntAct; P15814; 6.
MINT; MINT-4657105; -.
STRING; 9606.ENSP00000329312; -.
iPTMnet; P15814; -.
PhosphoSitePlus; P15814; -.
BioMuta; IGLL1; -.
DMDM; 123944; -.
MaxQB; P15814; -.
PaxDb; P15814; -.
PeptideAtlas; P15814; -.
PRIDE; P15814; -.
DNASU; 3543; -.
Ensembl; ENST00000249053; ENSP00000249053; ENSG00000128322. [P15814-2]
Ensembl; ENST00000330377; ENSP00000329312; ENSG00000128322. [P15814-1]
GeneID; 3543; -.
KEGG; hsa:3543; -.
UCSC; uc002zxd.4; human. [P15814-1]
CTD; 3543; -.
DisGeNET; 3543; -.
EuPathDB; HostDB:ENSG00000128322.6; -.
GeneCards; IGLL1; -.
HGNC; HGNC:5870; IGLL1.
HPA; HPA051134; -.
HPA; HPA071406; -.
MalaCards; IGLL1; -.
MIM; 146770; gene.
MIM; 613500; phenotype.
neXtProt; NX_P15814; -.
OpenTargets; ENSG00000128322; -.
Orphanet; 33110; Autosomal agammaglobulinemia.
PharmGKB; PA29756; -.
eggNOG; ENOG410J0XA; Eukaryota.
eggNOG; ENOG410YZ00; LUCA.
GeneTree; ENSGT00730000110696; -.
HOGENOM; HOG000113013; -.
HOVERGEN; HBG039526; -.
InParanoid; P15814; -.
KO; K06554; -.
OMA; KHNSVTH; -.
OrthoDB; EOG091G0XV9; -.
PhylomeDB; P15814; -.
TreeFam; TF335549; -.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
EvolutionaryTrace; P15814; -.
GeneWiki; IGLL1; -.
GenomeRNAi; 3543; -.
PRO; PR:P15814; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000128322; -.
CleanEx; HS_IGLL1; -.
ExpressionAtlas; P15814; baseline and differential.
Genevisible; P15814; HS.
GO; GO:0072562; C:blood microparticle; IBA:GO_Central.
GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0042571; C:immunoglobulin complex, circulating; IBA:GO_Central.
GO; GO:0016020; C:membrane; NAS:UniProtKB.
GO; GO:0003823; F:antigen binding; IBA:GO_Central.
GO; GO:0034987; F:immunoglobulin receptor binding; IBA:GO_Central.
GO; GO:0050853; P:B cell receptor signaling pathway; IBA:GO_Central.
GO; GO:0006958; P:complement activation, classical pathway; IBA:GO_Central.
GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
GO; GO:0006955; P:immune response; NAS:UniProtKB.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0006911; P:phagocytosis, engulfment; IBA:GO_Central.
GO; GO:0006910; P:phagocytosis, recognition; IBA:GO_Central.
GO; GO:0050871; P:positive regulation of B cell activation; IBA:GO_Central.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003006; Ig/MHC_CS.
InterPro; IPR003597; Ig_C1-set.
Pfam; PF07654; C1-set; 1.
SMART; SM00407; IGc1; 1.
SUPFAM; SSF48726; SSF48726; 1.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS00290; IG_MHC; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Disease mutation; Disulfide bond; Immunoglobulin domain; Polymorphism;
Reference proteome; Secreted; Signal.
SIGNAL 1 37 {ECO:0000255}.
CHAIN 38 213 Immunoglobulin lambda-like polypeptide 1.
/FTId=PRO_0000014777.
DOMAIN 114 208 Ig-like C1-type.
REGION 97 108 J region (By similarity to lambda light-
chain).
REGION 109 213 C region (By similarity to lambda light-
chain).
DISULFID 135 194 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:17431183}.
DISULFID 212 212 Interchain (with a heavy chain).
{ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 70 213 FLLQRGSWTGPRCWPRGFQSKHNSVTHVFGSGTQLTVLSQP
KATPSVTLFPPSSEELQANKATLVCLMNDFYPGILTVTWKA
DGTPITQGVEMTTPSKQSNNKYAASSYLSLTPEQWRSRRSY
SCQVMHEGSTVEKTVAPAECS -> SAQGHPLGHSVPAVL
(in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_042748.
VARIANT 142 142 P -> L (in AGM2; dbSNP:rs1064422).
{ECO:0000269|PubMed:9419212}.
/FTId=VAR_034869.
VARIANT 189 189 R -> H (in dbSNP:rs8138122).
/FTId=VAR_059392.
TURN 61 65 {ECO:0000244|PDB:2LKQ}.
HELIX 66 70 {ECO:0000244|PDB:2LKQ}.
HELIX 72 75 {ECO:0000244|PDB:2LKQ}.
STRAND 102 108 {ECO:0000244|PDB:2H3N}.
STRAND 115 119 {ECO:0000244|PDB:2H3N}.
HELIX 123 126 {ECO:0000244|PDB:2H3N}.
TURN 127 129 {ECO:0000244|PDB:2H3N}.
STRAND 131 143 {ECO:0000244|PDB:2H3N}.
STRAND 146 151 {ECO:0000244|PDB:2H3N}.
STRAND 158 162 {ECO:0000244|PDB:2H3N}.
STRAND 173 181 {ECO:0000244|PDB:2H3N}.
HELIX 183 188 {ECO:0000244|PDB:2H3N}.
STRAND 192 198 {ECO:0000244|PDB:2H3N}.
STRAND 201 207 {ECO:0000244|PDB:2H3N}.
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


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