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   26-FEB-2020, entry version 148.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (IMGT ALLELE IGKV1-5*01), AND VARIANT
RP   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 kappa
RT   genes and a pseudogene.";
RL   Nature 288:730-733(1980).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (IMGT ALLELE IGKV1-5*01), AND VARIANT
RP   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 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., 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   [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 acid
RT   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 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. Intrachain
RT   disulfide bonds.";
RL   Biochemistry 9:3188-3196(1970).
RN   [8]
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   [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. (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 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:20176268, PubMed:17576170).
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 IGKV1-5*03.
CC   -!- CAUTION: For an example of a full-length immunoglobulin kappa light
CC       chain see AC P0DOX7. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   SMR; P01602; -.
DR   IntAct; P01602; 7.
DR   IMGT_GENE-DB; IGKV1-5; -.
DR   GlyConnect; 1388; -.
DR   GlyConnect; 2049; -.
DR   iPTMnet; P01602; -.
DR   PhosphoSitePlus; P01602; -.
DR   BioMuta; IGKV1-5; -.
DR   DMDM; 125760; -.
DR   jPOST; P01602; -.
DR   MassIVE; P01602; -.
DR   PeptideAtlas; P01602; -.
DR   PRIDE; P01602; -.
DR   ProteomicsDB; 51398; -.
DR   ProteomicsDB; 51400; -.
DR   ProteomicsDB; 51404; -.
DR   ProteomicsDB; 51406; -.
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; ENSGT00940000153048; -.
DR   InParanoid; P01602; -.
DR   OMA; YLQSGIP; -.
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-977606; Regulation of Complement cascade.
DR   Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR   ChiTaRS; IGKV1-5; human.
DR   Pharos; P01602; Tdark.
DR   PRO; PR:P01602; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; P01602; protein.
DR   Bgee; ENSG00000243466; Expressed in lymph node and 82 other tissues.
DR   GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0019814; C:immunoglobulin complex; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0003823; F:antigen binding; NAS:UniProtKB.
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; IBA:GO_Central.
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:0030449; P:regulation of complement activation; 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; IPR036179; Ig-like_dom_sf.
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; Direct protein sequencing;
KW   Disulfide bond; Immunity; Immunoglobulin; Immunoglobulin domain; Membrane;
KW   Polymorphism; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:112021,
FT                   ECO:0000269|PubMed:4216454, ECO:0000269|PubMed:5489770"
FT   CHAIN           23..117
FT                   /note="Immunoglobulin kappa variable 1-5"
FT                   /evidence="ECO:0000269|PubMed:112021,
FT                   ECO:0000269|PubMed:4216454, ECO:0000269|PubMed:5489770"
FT                   /id="PRO_0000015169"
FT   DOMAIN          24..>117
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   REGION          23..45
FT                   /note="Framework-1"
FT                   /evidence="ECO:0000303|PubMed:6779204"
FT   REGION          46..56
FT                   /note="Complementarity-determining-1"
FT                   /evidence="ECO:0000303|PubMed:6779204"
FT   REGION          57..71
FT                   /note="Framework-2"
FT                   /evidence="ECO:0000303|PubMed:6779204"
FT   REGION          72..78
FT                   /note="Complementarity-determining-2"
FT                   /evidence="ECO:0000303|PubMed:6779204"
FT   REGION          79..110
FT                   /note="Framework-3"
FT                   /evidence="ECO:0000303|PubMed:6779204"
FT   REGION          111..>117
FT                   /note="Complementarity-determining-3"
FT                   /evidence="ECO:0000303|PubMed:6779204"
FT   DISULFID        45..110
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT                   ECO:0000269|PubMed:4923144"
FT   VARIANT         72
FT                   /note="K -> D (in IMGT allele IGKV1-5*01; requires 2
FT                   nucleotide substitutions)"
FT                   /evidence="ECO:0000269|PubMed:6087279,
FT                   ECO:0000269|PubMed:6779204"
FT                   /id="VAR_073349"
FT   CONFLICT        33..34
FT                   /note="LS -> QP (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        42
FT                   /note="T -> A (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        50
FT                   /note="S -> N (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        52..53
FT                   /note="SS -> NI (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        52..53
FT                   /note="SS -> NT (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        63
FT                   /note="G -> E (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        68
FT                   /note="L -> V (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        70
FT                   /note="I -> M (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        73
FT                   /note="A -> S (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        75..78
FT                   /note="SLES -> TLET (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        85
FT                   /note="S -> I (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        92
FT                   /note="E -> D (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        98
FT                   /note="S -> N (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        114..117
FT                   /note="NSYS -> SRYP (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        115..117
FT                   /note="SYS -> TFF (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        116
FT                   /note="Y -> D (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         117
SQ   SEQUENCE   117 AA;  12782 MW;  1BCDF3A40AFD9868 CRC64;
     MDMRVPAQLL GLLLLWLPGA KCDIQMTQSP STLSASVGDR VTITCRASQS ISSWLAWYQQ
     KPGKAPKLLI YKASSLESGV PSRFSGSGSG TEFTLTISSL QPDDFATYYC QQYNSYS
//