ID   IGLL5_HUMAN             Reviewed;         214 AA.
AC   B9A064;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 2.
DT   13-FEB-2019, entry version 74.
DE   RecName: Full=Immunoglobulin lambda-like polypeptide 5;
DE   AltName: Full=G lambda-1;
DE   AltName: Full=Germline immunoglobulin lambda 1;
DE   Flags: Precursor;
GN   Name=IGLL5;
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 2), AND TISSUE SPECIFICITY.
RX   PubMed=1900243; DOI=10.1002/eji.1830210237;
RA   Guglielmi P., Davi F.;
RT   "Expression of a novel type of immunoglobulin C lambda transcripts in
RT   human mature B lymphocytes producing kappa light chains.";
RL   Eur. J. Immunol. 21:501-508(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
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).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=B9A064-1; Sequence=Displayed;
CC         Note=No experimental confirmation available.;
CC       Name=2;
CC         IsoId=B9A064-2; Sequence=VSP_040709, VSP_040710;
CC   -!- TISSUE SPECIFICITY: Contrary to IGLL1, not expressed in pre-B-
CC       cells. {ECO:0000269|PubMed:1703205, ECO:0000269|PubMed:1900243}.
CC   -!- MISCELLANEOUS: Located within the immunoglobulin lambda locus, but
CC       does not require somatic rearrangement for expression.
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DR   EMBL; D87023; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS54506.1; -. [B9A064-1]
DR   RefSeq; NP_001171597.1; NM_001178126.1. [B9A064-1]
DR   UniGene; Hs.449574; -.
DR   UniGene; Hs.449585; -.
DR   UniGene; Hs.474325; -.
DR   UniGene; Hs.535668; -.
DR   UniGene; Hs.625768; -.
DR   UniGene; Hs.640434; -.
DR   UniGene; Hs.659929; -.
DR   UniGene; Hs.713252; -.
DR   UniGene; Hs.728722; -.
DR   UniGene; Hs.728758; -.
DR   UniGene; Hs.731137; -.
DR   ProteinModelPortal; B9A064; -.
DR   SMR; B9A064; -.
DR   BioGrid; 1148096; 26.
DR   IntAct; B9A064; 1.
DR   MINT; B9A064; -.
DR   STRING; 9606.ENSP00000431254; -.
DR   CarbonylDB; B9A064; -.
DR   iPTMnet; B9A064; -.
DR   PhosphoSitePlus; B9A064; -.
DR   BioMuta; IGLL5; -.
DR   jPOST; B9A064; -.
DR   MaxQB; B9A064; -.
DR   PaxDb; B9A064; -.
DR   PRIDE; B9A064; -.
DR   ProteomicsDB; 7509; -.
DR   ProteomicsDB; 7510; -. [B9A064-2]
DR   Ensembl; ENST00000526893; ENSP00000431254; ENSG00000254709. [B9A064-1]
DR   Ensembl; ENST00000531372; ENSP00000434368; ENSG00000254709. [B9A064-2]
DR   GeneID; 100423062; -.
DR   KEGG; hsa:100423062; -.
DR   UCSC; uc011aiw.3; human. [B9A064-1]
DR   CTD; 100423062; -.
DR   DisGeNET; 100423062; -.
DR   EuPathDB; HostDB:ENSG00000254709.7; -.
DR   GeneCards; IGLL5; -.
DR   HGNC; HGNC:38476; IGLL5.
DR   neXtProt; NX_B9A064; -.
DR   OpenTargets; ENSG00000254709; -.
DR   eggNOG; ENOG410J0XA; Eukaryota.
DR   eggNOG; ENOG410YZ00; LUCA.
DR   GeneTree; ENSGT00940000153307; -.
DR   HOVERGEN; HBG108319; -.
DR   InParanoid; B9A064; -.
DR   OrthoDB; 1568661at2759; -.
DR   PhylomeDB; B9A064; -.
DR   TreeFam; TF335549; -.
DR   ChiTaRS; IGLL5; human.
DR   GenomeRNAi; 100423062; -.
DR   PRO; PR:B9A064; -.
DR   Proteomes; UP000005640; Chromosome 22.
DR   Bgee; ENSG00000254709; Expressed in 82 organ(s), highest expression level in lymph node.
DR   ExpressionAtlas; B9A064; baseline and differential.
DR   Genevisible; B9A064; HS.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0042571; C:immunoglobulin complex, circulating; IBA:GO_Central.
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: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   2: Evidence at transcript level;
KW   Alternative splicing; Complete proteome; Disulfide bond;
KW   Immunoglobulin domain; Reference proteome; Secreted; Signal.
FT   SIGNAL        1     35       {ECO:0000255}.
FT   CHAIN        36    214       Immunoglobulin lambda-like polypeptide 5.
FT                                /FTId=PRO_0000405596.
FT   DOMAIN      115    209       Ig-like C1-type.
FT   REGION       98    109       J region (By similarity to lambda light-
FT                                chain).
FT   REGION      110    214       C region (By similarity to lambda light-
FT                                chain).
FT   DISULFID    136    195       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   VAR_SEQ      70     84       LLLQPSPQRADPRCW -> SAQGQPHCHSVPALL (in
FT                                isoform 2). {ECO:0000303|PubMed:1900243}.
FT                                /FTId=VSP_040709.
FT   VAR_SEQ      85    214       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:1900243}.
FT                                /FTId=VSP_040710.
SQ   SEQUENCE   214 AA;  23063 MW;  A29B29F09C063EBC CRC64;
     MRPKTGQVGC ETPEELGPGP RQRWPLLLLG LAMVAHGLLR PMVAPQSGDP DPGASVGSSR
     SSLRSLWGRL LLQPSPQRAD PRCWPRGFWS EPQSLCYVFG TGTKVTVLGQ PKANPTVTLF
     PPSSEELQAN KATLVCLISD FYPGAVTVAW KADGSPVKAG VETTKPSKQS NNKYAASSYL
     SLTPEQWKSH RSYSCQVTHE GSTVEKTVAP TECS
//