ID   KV105_HUMAN             Reviewed;         117 AA.
AC   P01602; A0A075B6S8; P01596; P01598; P01604;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   24-JUN-2015, sequence version 2.
DT   15-MAR-2017, entry version 126.
DE   RecName: Full=Immunoglobulin kappa variable 1-5 {ECO:0000303|PubMed:11549845, ECO:0000303|Ref.9};
DE   AltName: Full=Ig kappa chain V-I region CAR {ECO:0000305|PubMed:4216454};
DE   AltName: Full=Ig kappa chain V-I region EU {ECO:0000305|PubMed:5489770};
DE   AltName: Full=Ig kappa chain V-I region HK102 {ECO:0000303|PubMed:6779204};
DE   AltName: Full=Ig kappa chain V-I region Kue {ECO:0000305|PubMed:112021};
DE   Flags: Precursor;
GN   Name=IGKV1-5 {ECO:0000303|PubMed:11549845, ECO:0000303|Ref.9};
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 [GENOMIC DNA] (IMGT ALLELE IGKV1-5*01), AND
RP   VARIANT ASP-72.
RX   PubMed=6779204; DOI=10.1038/288730a0;
RA   Bentley D.L., Rabbitts T.H.;
RT   "Human immunoglobulin variable region genes -- DNA sequences of two V
RT   kappa genes and a pseudogene.";
RL   Nature 288:730-733(1980).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (IMGT ALLELE IGKV1-5*01), AND
RP   VARIANT ASP-72.
RX   PubMed=6087279; DOI=10.1093/nar/12.13.5249;
RA   Jaenichen H.R., Pech M., Lindenmaier W., Wildgruber N., Zachau H.G.;
RT   "Composite human VK genes and a model of their evolution.";
RL   Nucleic Acids Res. 12:5249-5263(1984).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE
RP   IGKV1-5*03).
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   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.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   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.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [4]
RP   PROTEIN SEQUENCE OF 23-117.
RX   PubMed=5489770; DOI=10.1021/bi00818a007;
RA   Gottlieb P.D., Cunningham B.A., Rutishauser U., Edelman G.M.;
RT   "The covalent structure of a human gamma G-immunoglobulin. VI. Amino
RT   acid sequence of the light chain.";
RL   Biochemistry 9:3155-3161(1970).
RN   [5]
RP   PROTEIN SEQUENCE OF 23-117.
RX   PubMed=4216454; DOI=10.1111/j.1432-1033.1974.tb03843.x;
RA   Milstein C.P., Deverson E.V.;
RT   "Primary structure of kappa light chain from a human myeloma
RT   protein.";
RL   Eur. J. Biochem. 49:377-391(1974).
RN   [6]
RP   PROTEIN SEQUENCE OF 23-117.
RX   PubMed=112021;
RA   Eulitz M., Kley H.-P., Zeitler H.-J.;
RT   "The primary structure of the Bence-Jones protein Kue. The amino acid
RT   sequence of the variable part of a human L-chain of the kappa-type.";
RL   Hoppe-Seyler's Z. Physiol. Chem. 360:725-734(1979).
RN   [7]
RP   DISULFIDE BOND.
RX   PubMed=4923144; DOI=10.1021/bi00818a011;
RA   Gall W.E., Edelman G.M.;
RT   "The covalent structure of a human gamma G-immunoglobulin. X.
RT   Intrachain disulfide bonds.";
RL   Biochemistry 9:3188-3196(1970).
RN   [8]
RP   NOMEMCLATURE.
RX   PubMed=11549845;
RA   Lefranc M.P.;
RT   "Nomenclature of the human immunoglobulin kappa (IGK) genes.";
RL   Exp. Clin. Immunogenet. 18:161-174(2001).
RN   [9]
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.
RL   (2001).
RN   [10]
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   [11]
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   [12]
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   [13]
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
RT   Rise 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
CC       (PubMed:24600447). Immunoglobulins, also known as antibodies, are
CC       membrane-bound or secreted glycoproteins produced by B
CC       lymphocytes. In the recognition phase of humoral immunity, the
CC       membrane-bound immunoglobulins serve as receptors which, upon
CC       binding of a specific antigen, trigger the clonal expansion and
CC       differentiation of B lymphocytes into immunoglobulins-secreting
CC       plasma cells. Secreted immunoglobulins mediate the effector phase
CC       of humoral immunity, which results in the elimination of bound
CC       antigens (PubMed:20176268, PubMed:22158414). The antigen binding
CC       site is formed by the variable domain of one heavy chain, together
CC       with that of its associated light chain. Thus, each immunoglobulin
CC       has two antigen binding sites with remarkable affinity for a
CC       particular antigen. The variable domains are assembled by a
CC       process called V-(D)-J rearrangement and can then be subjected to
CC       somatic hypermutations which, after exposure to antigen and
CC       selection, allow affinity maturation for a particular antigen
CC       (PubMed:20176268, PubMed:17576170). {ECO:0000303|PubMed:17576170,
CC       ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414,
CC       ECO:0000303|PubMed:24600447}.
CC   -!- SUBUNIT: Immunoglobulins are composed of two identical heavy
CC       chains and 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
CC       that of IMGT allele IGKV1-5*03.
CC   -!- CAUTION: For an example of a full length immunoglobulin kappa
CC       light chain see AC P0DOX7. {ECO:0000305}.
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DR   EMBL; J00245; AAA59087.1; -; Genomic_DNA.
DR   EMBL; Z00001; CAA77292.1; -; Genomic_DNA.
DR   EMBL; AC243970; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; A01864; K1HUAR.
DR   PIR; A01870; K1HUKU.
DR   PIR; A01882; K1HU12.
DR   PIR; A90562; K1HUEU.
DR   UniGene; Hs.449609; -.
DR   ProteinModelPortal; P01602; -.
DR   SMR; P01602; -.
DR   IntAct; P01602; 4.
DR   IMGT_GENE-DB; IGKV1-5; -.
DR   iPTMnet; P01598; -.
DR   DMDM; 125760; -.
DR   DMDM; 125762; -.
DR   DMDM; 125766; -.
DR   DMDM; 125768; -.
DR   PeptideAtlas; P01602; -.
DR   PRIDE; P01602; -.
DR   Ensembl; ENST00000496168; ENSP00000420436; ENSG00000243466.
DR   Ensembl; ENST00000632205; ENSP00000488639; ENSG00000282801.
DR   UCSC; uc061lqk.1; human.
DR   DisGeNET; 28299; -.
DR   GeneCards; IGKV1-5; -.
DR   HGNC; HGNC:5741; IGKV1-5.
DR   neXtProt; NX_P01602; -.
DR   OpenTargets; ENSG00000243466; -.
DR   GeneTree; ENSGT00780000121852; -.
DR   HOGENOM; HOG000059537; -.
DR   HOVERGEN; HBG018013; -.
DR   InParanoid; P01602; -.
DR   OMA; TITINCQ; -.
DR   PhylomeDB; P01602; -.
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-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR   PRO; PR:P01602; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0003823; F:antigen binding; NAS:UniProtKB.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
DR   GO; GO:0006956; P:complement activation; TAS:Reactome.
DR   GO; GO:0006958; P:complement activation, classical pathway; TAS:Reactome.
DR   GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
DR   GO; GO:0006955; P:immune response; NAS:UniProtKB.
DR   GO; GO:0002377; P:immunoglobulin production; IBA:GO_Central.
DR   GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome.
DR   GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR013106; Ig_V-set.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00406; IGv; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   1: Evidence at protein level;
KW   Adaptive immunity; Cell membrane; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; Immunity;
KW   Immunoglobulin domain; Immunoglobulin V region; Membrane;
KW   Polymorphism; Reference proteome; Secreted; Signal.
FT   SIGNAL        1     22       {ECO:0000269|PubMed:112021,
FT                                ECO:0000269|PubMed:4216454,
FT                                ECO:0000269|PubMed:5489770}.
FT   CHAIN        23    117       Immunoglobulin kappa variable 1-5.
FT                                {ECO:0000269|PubMed:112021,
FT                                ECO:0000269|PubMed:4216454,
FT                                ECO:0000269|PubMed:5489770}.
FT                                /FTId=PRO_0000015169.
FT   DOMAIN       24   >117       Ig-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00114}.
FT   REGION       23     45       Framework-1.
FT                                {ECO:0000303|PubMed:6779204}.
FT   REGION       46     56       Complementarity-determining-1.
FT                                {ECO:0000303|PubMed:6779204}.
FT   REGION       57     71       Framework-2.
FT                                {ECO:0000303|PubMed:6779204}.
FT   REGION       72     78       Complementarity-determining-2.
FT                                {ECO:0000303|PubMed:6779204}.
FT   REGION       79    110       Framework-3.
FT                                {ECO:0000303|PubMed:6779204}.
FT   REGION      111   >117       Complementarity-determining-3.
FT                                {ECO:0000303|PubMed:6779204}.
FT   DISULFID     45    110       {ECO:0000255|PROSITE-ProRule:PRU00114,
FT                                ECO:0000269|PubMed:4923144}.
FT   VARIANT      72     72       K -> D (in IMGT allele IGKV1-5*01;
FT                                requires 2 nucleotide substitutions).
FT                                {ECO:0000269|PubMed:6087279,
FT                                ECO:0000269|PubMed:6779204}.
FT                                /FTId=VAR_073349.
FT   CONFLICT     33     34       LS -> QP (in Ref. 6; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     42     42       T -> A (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     50     50       S -> N (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     52     53       SS -> NI (in Ref. 6; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     52     53       SS -> NT (in Ref. 4; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     63     63       G -> E (in Ref. 6; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     68     68       L -> V (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     70     70       I -> M (in Ref. 4; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     73     73       A -> S (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     75     78       SLES -> TLET (in Ref. 6; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     85     85       S -> I (in Ref. 4; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     92     92       E -> D (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     98     98       S -> N (in Ref. 6; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    114    117       NSYS -> SRYP (in Ref. 6; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    115    117       SYS -> TFF (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    116    116       Y -> D (in Ref. 4; AA sequence).
FT                                {ECO:0000305}.
FT   NON_TER     117    117
SQ   SEQUENCE   117 AA;  12782 MW;  1BCDF3A40AFD9868 CRC64;
     MDMRVPAQLL GLLLLWLPGA KCDIQMTQSP STLSASVGDR VTITCRASQS ISSWLAWYQQ
     KPGKAPKLLI YKASSLESGV PSRFSGSGSG TEFTLTISSL QPDDFATYYC QQYNSYS
//