KV105_HUMAN
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 03-AUG-2022, entry version 158.
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}.
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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 AlphaFoldDB; P01602; -.
DR SMR; P01602; -.
DR IntAct; P01602; 9.
DR IMGT_GENE-DB; IGKV1-5; -.
DR GlyConnect; 1388; 3 N-Linked glycans (1 site).
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; 51404; -.
DR Ensembl; ENST00000496168.1; ENSP00000420436.1; ENSG00000243466.1.
DR Ensembl; ENST00000632205.1; ENSP00000488639.1; ENSG00000282801.1.
DR UCSC; uc061lqk.1; human.
DR GeneCards; IGKV1-5; -.
DR HGNC; HGNC:5741; IGKV1-5.
DR HPA; ENSG00000243466; Tissue enhanced (intestine, lymphoid tissue, urinary bladder).
DR neXtProt; NX_P01602; -.
DR OpenTargets; ENSG00000243466; -.
DR VEuPathDB; HostDB:ENSG00000243466; -.
DR GeneTree; ENSGT00940000153048; -.
DR InParanoid; P01602; -.
DR OMA; NCLASEN; -.
DR PhylomeDB; P01602; -.
DR PathwayCommons; 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-9664323; FCGR3A-mediated IL10 synthesis.
DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
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 SignaLink; P01602; -.
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 rectum and 93 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:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0006955; P:immune response; 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; 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 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
