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IGLL5_HUMAN
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   03-AUG-2022, entry version 91.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   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 human
RT   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 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).
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       Name=2;
CC         IsoId=B9A064-2; Sequence=VSP_040709, VSP_040710;
CC   -!- TISSUE SPECIFICITY: Contrary to IGLL1, not expressed in pre-B-cells.
CC       {ECO:0000269|PubMed:1703205, ECO:0000269|PubMed:1900243}.
CC   -!- MISCELLANEOUS: Located within the immunoglobulin lambda locus, but does
CC       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   AlphaFoldDB; B9A064; -.
DR   SMR; B9A064; -.
DR   BioGRID; 1148096; 160.
DR   IntAct; B9A064; 20.
DR   MINT; B9A064; -.
DR   STRING; 9606.ENSP00000431254; -.
DR   CarbonylDB; B9A064; -.
DR   GlyGen; B9A064; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; B9A064; -.
DR   PhosphoSitePlus; B9A064; -.
DR   BioMuta; IGLL5; -.
DR   jPOST; B9A064; -.
DR   MassIVE; B9A064; -.
DR   MaxQB; B9A064; -.
DR   PaxDb; B9A064; -.
DR   PeptideAtlas; B9A064; -.
DR   PRIDE; B9A064; -.
DR   ProteomicsDB; 7509; -. [B9A064-1]
DR   Antibodypedia; 57108; 87 antibodies from 15 providers.
DR   DNASU; 100423062; -.
DR   Ensembl; ENST00000526893.6; ENSP00000431254.1; ENSG00000254709.8. [B9A064-1]
DR   Ensembl; ENST00000531372.1; ENSP00000434368.1; ENSG00000254709.8. [B9A064-2]
DR   GeneID; 100423062; -.
DR   KEGG; hsa:100423062; -.
DR   MANE-Select; ENST00000526893.6; ENSP00000431254.1; NM_001178126.2; NP_001171597.1.
DR   UCSC; uc011aiw.3; human. [B9A064-1]
DR   CTD; 100423062; -.
DR   DisGeNET; 100423062; -.
DR   GeneCards; IGLL5; -.
DR   HGNC; HGNC:38476; IGLL5.
DR   HPA; ENSG00000254709; Tissue enhanced (intestine, lymphoid tissue, stomach).
DR   neXtProt; NX_B9A064; -.
DR   OpenTargets; ENSG00000254709; -.
DR   VEuPathDB; HostDB:ENSG00000254709; -.
DR   eggNOG; ENOG502SS4M; Eukaryota.
DR   GeneTree; ENSGT00940000153307; -.
DR   HOGENOM; CLU_2526772_0_0_1; -.
DR   InParanoid; B9A064; -.
DR   OrthoDB; 1568661at2759; -.
DR   PhylomeDB; B9A064; -.
DR   TreeFam; TF335549; -.
DR   PathwayCommons; B9A064; -.
DR   SignaLink; B9A064; -.
DR   BioGRID-ORCS; 100423062; 10 hits in 1060 CRISPR screens.
DR   ChiTaRS; IGLL5; human.
DR   GenomeRNAi; 100423062; -.
DR   Pharos; B9A064; Tbio.
DR   PRO; PR:B9A064; -.
DR   Proteomes; UP000005640; Chromosome 22.
DR   RNAct; B9A064; protein.
DR   Bgee; ENSG00000254709; Expressed in duodenum and 88 other tissues.
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; Disulfide bond; Immunoglobulin domain;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..214
FT                   /note="Immunoglobulin lambda-like polypeptide 5"
FT                   /id="PRO_0000405596"
FT   DOMAIN          115..209
FT                   /note="Ig-like C1-type"
FT   REGION          98..109
FT                   /note="J region (By similarity to lambda light-chain)"
FT   REGION          110..214
FT                   /note="C region (By similarity to lambda light-chain)"
FT   DISULFID        136..195
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   VAR_SEQ         70..84
FT                   /note="LLLQPSPQRADPRCW -> SAQGQPHCHSVPALL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:1900243"
FT                   /id="VSP_040709"
FT   VAR_SEQ         85..214
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:1900243"
FT                   /id="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
 
 
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