ID   KV315_HUMAN             Reviewed;         115 AA.
AC   P01624; A0A0B4J1T9; P04207;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2016, sequence version 2.
DT   02-SEP-2026, entry version 142.
DE   RecName: Full=Immunoglobulin kappa variable 3-15 {ECO:0000303|PubMed:11549845, ECO:0000303|Ref.5};
DE   AltName: Full=Ig kappa chain V-III region CLL {ECO:0000303|PubMed:3083417};
DE   AltName: Full=Ig kappa chain V-III region POM {ECO:0000305|PubMed:60899};
DE   Flags: Precursor;
GN   Name=IGKV3-15 {ECO:0000303|PubMed:11549845, ECO:0000303|Ref.5};
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 [GENOMIC DNA].
RX   PubMed=3083417; DOI=10.1073/pnas.83.7.2195;
RA   Jirik F.R., Sorge J., Fong S., Heitzmann J.G., Curd J.G., Chen P.P.,
RA   Goldfien R., Carson D.A.;
RT   "Cloning and sequence determination of a human rheumatoid factor light-
RT   chain gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:2195-2199(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE IGKV3-15*01).
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [3]
RP   PROTEIN SEQUENCE OF 21-115.
RX   PubMed=60899;
RA   Klapper D.G., Capra J.D.;
RT   "The amino acid sequence of the variable regions of the light chains from
RT   two idiotypically cross reactive IgM anti-gamma globulins.";
RL   Ann. Immunol. (Paris) 127C:261-271(1976).
RN   [4]
RP   NOMEMCLATURE.
RX   PubMed=11549845; DOI=10.1159/000049195;
RA   Lefranc M.P.;
RT   "Nomenclature of the human immunoglobulin kappa (IGK) genes.";
RL   Exp. Clin. Immunogenet. 18:161-174(2001).
RN   [5]
RP   NOMENCLATURE.
RA   Lefranc M.P., Lefranc G.;
RT   "The Immunoglobulin FactsBook.";
RL   (In) Lefranc M.P., Lefranc G. (eds.);
RL   The Immunoglobulin FactsBook., pp.1-458, Academic Press, London. (2001).
RN   [6]
RP   REVIEW ON SOMATIC HYPERMUTATION.
RX   PubMed=17576170; DOI=10.1146/annurev.genet.41.110306.130340;
RA   Teng G., Papavasiliou F.N.;
RT   "Immunoglobulin somatic hypermutation.";
RL   Annu. Rev. Genet. 41:107-120(2007).
RN   [7]
RP   REVIEW ON IMMUNOGLOBULINS.
RX   PubMed=20176268; DOI=10.1016/j.jaci.2009.09.046;
RA   Schroeder H.W. Jr., Cavacini L.;
RT   "Structure and function of immunoglobulins.";
RL   J. Allergy Clin. Immunol. 125:S41-S52(2010).
RN   [8]
RP   REVIEW ON FUNCTION.
RX   PubMed=22158414; DOI=10.1038/nri3128;
RA   McHeyzer-Williams M., Okitsu S., Wang N., McHeyzer-Williams L.;
RT   "Molecular programming of B cell memory.";
RL   Nat. Rev. Immunol. 12:24-34(2012).
RN   [9]
RP   NOMENCLATURE.
RX   PubMed=24600447; DOI=10.3389/fimmu.2014.00022;
RA   Lefranc M.P.;
RT   "Immunoglobulin and T Cell Receptor Genes: IMGT((R)) and the Birth and Rise
RT   of Immunoinformatics.";
RL   Front. Immunol. 5:22-22(2014).
CC   -!- FUNCTION: V region of the variable domain of immunoglobulin light
CC       chains that participates in the antigen recognition (PubMed:24600447).
CC       Immunoglobulins, also known as antibodies, are membrane-bound or
CC       secreted glycoproteins produced by B lymphocytes. In the recognition
CC       phase of humoral immunity, the membrane-bound immunoglobulins serve as
CC       receptors which, upon binding of a specific antigen, trigger the clonal
CC       expansion and differentiation of B lymphocytes into immunoglobulins-
CC       secreting plasma cells. Secreted immunoglobulins mediate the effector
CC       phase of humoral immunity, which results in the elimination of bound
CC       antigens (PubMed:20176268, PubMed:22158414). The antigen binding site
CC       is formed by the variable domain of one heavy chain, together with that
CC       of its associated light chain. Thus, each immunoglobulin has two
CC       antigen binding sites with remarkable affinity for a particular
CC       antigen. The variable domains are assembled by a process called V-(D)-J
CC       rearrangement and can then be subjected to somatic hypermutations
CC       which, after exposure to antigen and selection, allow affinity
CC       maturation for a particular antigen (PubMed:17576170, PubMed:20176268).
CC       {ECO:0000303|PubMed:17576170, ECO:0000303|PubMed:20176268,
CC       ECO:0000303|PubMed:22158414, ECO:0000303|PubMed:24600447}.
CC   -!- SUBUNIT: Immunoglobulins are composed of two identical heavy chains and
CC       two identical light chains; disulfide-linked.
CC       {ECO:0000303|PubMed:20176268}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268,
CC       ECO:0000303|PubMed:22158414}. Cell membrane
CC       {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
CC   -!- POLYMORPHISM: There are several alleles. The sequence shown is that of
CC       IMGT allele IGKV3-15*01.
CC   -!- CAUTION: For an example of a full-length immunoglobulin kappa light
CC       chain see AC P0DOX7. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA58992.1; Type=Miscellaneous discrepancy; Note=Chimeric DNA corresponding to regions V and J of immunoglobulin kappa light chain.; Evidence={ECO:0000305};
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DR   EMBL; M12740; AAA58992.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC245015; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; A01897; K3HUPM.
DR   PIR; A01898; K3HUCL.
DR   PIR; A30553; A30553.
DR   PIR; I30608; I30608.
DR   AlphaFoldDB; P01624; -.
DR   EMDB; EMD-11812; -.
DR   EMDB; EMD-11813; -.
DR   EMDB; EMD-13550; -.
DR   EMDB; EMD-13563; -.
DR   EMDB; EMD-19014; -.
DR   EMDB; EMD-19015; -.
DR   EMDB; EMD-25655; -.
DR   EMDB; EMD-26653; -.
DR   EMDB; EMD-26655; -.
DR   EMDB; EMD-27139; -.
DR   EMDB; EMD-32427; -.
DR   EMDB; EMD-32429; -.
DR   EMDB; EMD-33019; -.
DR   EMDB; EMD-33202; -.
DR   EMDB; EMD-33552; -.
DR   EMDB; EMD-34126; -.
DR   EMDB; EMD-34127; -.
DR   EMDB; EMD-34132; -.
DR   EMDB; EMD-34133; -.
DR   EMDB; EMD-34134; -.
DR   EMDB; EMD-34135; -.
DR   EMDB; EMD-38283; -.
DR   EMDB; EMD-38284; -.
DR   EMDB; EMD-38914; -.
DR   EMDB; EMD-40854; -.
DR   EMDB; EMD-41048; -.
DR   EMDB; EMD-41464; -.
DR   EMDB; EMD-41465; -.
DR   EMDB; EMD-42985; -.
DR   EMDB; EMD-43149; -.
DR   EMDB; EMD-44321; -.
DR   EMDB; EMD-44322; -.
DR   EMDB; EMD-44539; -.
DR   EMDB; EMD-44903; -.
DR   EMDB; EMD-48515; -.
DR   EMDB; EMD-49097; -.
DR   EMDB; EMD-49462; -.
DR   EMDB; EMD-49708; -.
DR   EMDB; EMD-8240; -.
DR   EMDB; EMD-8241; -.
DR   EMDB; EMD-8242; -.
DR   EMDB; EMD-8730; -.
DR   SMR; P01624; -.
DR   FunCoup; P01624; 373.
DR   IMGT_GENE-DB; IGKV3-15; -.
DR   BioMuta; IGKV3-15; -.
DR   DMDM; 125809; -.
DR   jPOST; P01624; -.
DR   MassIVE; P01624; -.
DR   Ensembl; ENST00000390252.2; ENSP00000374787.2; ENSG00000244437.1.
DR   Ensembl; ENST00000632887.1; ENSP00000488086.1; ENSG00000282447.1.
DR   AGR; HGNC:5816; -.
DR   GeneCards; IGKV3-15; -.
DR   HGNC; HGNC:5816; IGKV3-15.
DR   HPA; ENSG00000244437; Tissue enhanced (intestine, lymphoid tissue, urinary bladder).
DR   OpenTargets; ENSG00000244437; -.
DR   VEuPathDB; HostDB:ENSG00000244437; -.
DR   GeneTree; ENSGT00940000154413; -.
DR   InParanoid; P01624; -.
DR   OMA; DILMTQT; -.
DR   PAN-GO; P01624; 2 GO annotations based on evolutionary models.
DR   PhylomeDB; P01624; -.
DR   PathwayCommons; P01624; -.
DR   Reactome; R-HSA-166663; Initial triggering of complement.
DR   Reactome; R-HSA-173623; Classical antibody-mediated complement activation.
DR   Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR   Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR   Reactome; R-HSA-2029481; FCGR activation.
DR   Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR   Reactome; R-HSA-2029485; Role of phospholipids in phagocytosis.
DR   Reactome; R-HSA-2168880; Scavenging of heme from plasma.
DR   Reactome; R-HSA-2454202; Fc epsilon receptor (FCERI) signaling.
DR   Reactome; R-HSA-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
DR   Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
DR   Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
DR   Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR   Reactome; R-HSA-5690714; CD22 mediated BCR regulation.
DR   Reactome; R-HSA-9664323; FCGR3A-mediated IL10 synthesis.
DR   Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR   Reactome; R-HSA-9679191; Potential therapeutics for SARS.
DR   Reactome; R-HSA-977606; Regulation of Complement cascade.
DR   Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR   Agora; ENSG00000244437; -.
DR   ChiTaRS; IGKV3-15; human.
DR   Pharos; P01624; Tdark.
DR   PRO; PR:P01624; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; P01624; protein.
DR   Bgee; ENSG00000244437; Expressed in rectum and 88 other cell types or tissues.
DR   GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0019814; C:immunoglobulin complex; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0003823; F:antigen binding; NAS:UniProtKB.
DR   GO; GO:0006955; P:immune response; IBA:GO_Central.
DR   CDD; cd04980; IgV_L_kappa; 1.
DR   FunFam; 2.60.40.10:FF:000350; Immunoglobulin kappa chain variable 18-36; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR050150; IgV_Light_Chain.
DR   PANTHER; PTHR23267; IMMUNOGLOBULIN LIGHT CHAIN; 1.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00406; IGv; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   1: Evidence at protein level;
KW   Adaptive immunity; Cell membrane; Direct protein sequencing;
KW   Disulfide bond; Immunity; Immunoglobulin; Immunoglobulin domain; Membrane;
KW   Proteomics identification; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:60899"
FT   CHAIN           21..115
FT                   /note="Immunoglobulin kappa variable 3-15"
FT                   /evidence="ECO:0000269|PubMed:60899"
FT                   /id="PRO_0000059766"
FT   DOMAIN          21..>115
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   REGION          21..43
FT                   /note="Framework-1"
FT                   /evidence="ECO:0000250|UniProtKB:P01602"
FT   REGION          44..54
FT                   /note="Complementarity-determining-1"
FT                   /evidence="ECO:0000250|UniProtKB:P01602"
FT   REGION          55..69
FT                   /note="Framework-2"
FT                   /evidence="ECO:0000250|UniProtKB:P01602"
FT   REGION          70..76
FT                   /note="Complementarity-determining-2"
FT                   /evidence="ECO:0000250|UniProtKB:P01602"
FT   REGION          77..108
FT                   /note="Framework-3"
FT                   /evidence="ECO:0000250|UniProtKB:P01602"
FT   REGION          109..>115
FT                   /note="Complementarity-determining-3"
FT                   /evidence="ECO:0000250|UniProtKB:P01602"
FT   DISULFID        43..108
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   CONFLICT        29
FT                   /note="A -> V (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        49..52
FT                   /note="VSSN -> ISNSY (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        51
FT                   /note="S -> N (in Ref. 1; AAA58992)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        61..63
FT                   /note="GQA -> SGS (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        63
FT                   /note="A -> P (in Ref. 1; AAA58992)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        97
FT                   /note="S -> R (in Ref. 1; AAA58992)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         115
SQ   SEQUENCE   115 AA;  12496 MW;  EA850E228DE7FC25 CRC64;
     MEAPAQLLFL LLLWLPDTTG EIVMTQSPAT LSVSPGERAT LSCRASQSVS SNLAWYQQKP
     GQAPRLLIYG ASTRATGIPA RFSGSGSGTE FTLTISSLQS EDFAVYYCQQ YNNWP
//