KV117_HUMAN
ID KV117_HUMAN Reviewed; 117 AA.
AC P01599; A0A0B4J1Z4; P01610;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2016, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Immunoglobulin kappa variable 1-17 {ECO:0000303|PubMed:11549845, ECO:0000303|Ref.5};
DE AltName: Full=Ig kappa chain V-I region Gal {ECO:0000305|PubMed:4215718};
DE AltName: Full=Ig kappa chain V-I region WEA {ECO:0000305|PubMed:6410398};
DE Flags: Precursor;
GN Name=IGKV1-17 {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 [LARGE SCALE GENOMIC DNA] (IMGT ALLELE IGKV1-17*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 [2]
RP PROTEIN SEQUENCE OF 23-117.
RX PubMed=4215718;
RA Laure C.J., Watanabe S., Hilschmann N.;
RT "The primary structure of a monoclonal IgM-immunoglobulin (macroglobulin
RT Gal.), I. The amino acid sequence of the L-chain of kappa-type, subgroup
RT I.";
RL Hoppe-Seyler's Z. Physiol. Chem. 354:1503-1504(1973).
RN [3]
RP PROTEIN SEQUENCE OF 23-117.
RX PubMed=6410398; DOI=10.1073/pnas.80.15.4837;
RA Goni F., Frangione B.;
RT "Amino acid sequence of the Fv region of a human monoclonal IgM (protein
RT WEA) with antibody activity against 3,4-pyruvylated galactose in Klebsiella
RT polysaccharides K30 and K33.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:4837-4841(1983).
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: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 IGKV1-17*01.
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; AC245015; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A01867; K1HUGL.
DR PIR; A01876; K1HUWE.
DR AlphaFoldDB; P01599; -.
DR SMR; P01599; -.
DR IntAct; P01599; 1.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR IMGT_GENE-DB; IGKV1-17; -.
DR GlyGen; P01599; 1 site, 1 O-linked glycan (1 site).
DR BioMuta; IGKV1-17; -.
DR DMDM; 125763; -.
DR jPOST; P01599; -.
DR MassIVE; P01599; -.
DR PeptideAtlas; P01599; -.
DR PRIDE; P01599; -.
DR Ensembl; ENST00000490686.1; ENSP00000418357.1; ENSG00000240382.3.
DR Ensembl; ENST00000632229.1; ENSP00000488092.1; ENSG00000281978.1.
DR GeneCards; IGKV1-17; -.
DR HGNC; HGNC:5733; IGKV1-17.
DR HPA; ENSG00000240382; Tissue enhanced (intestine, lymphoid tissue).
DR neXtProt; NX_P01599; -.
DR OpenTargets; ENSG00000240382; -.
DR VEuPathDB; HostDB:ENSG00000240382; -.
DR GeneTree; ENSGT00940000153048; -.
DR OMA; TVTIACK; -.
DR PhylomeDB; P01599; -.
DR PathwayCommons; P01599; -.
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; P01599; -.
DR Pharos; P01599; Tdark.
DR PRO; PR:P01599; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P01599; protein.
DR Bgee; ENSG00000240382; Expressed in rectum and 84 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:4215718,
FT ECO:0000269|PubMed:6410398"
FT CHAIN 23..117
FT /note="Immunoglobulin kappa variable 1-17"
FT /evidence="ECO:0000269|PubMed:4215718,
FT ECO:0000269|PubMed:6410398"
FT /id="PRO_0000059743"
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:0000250|UniProtKB:P01602"
FT REGION 46..56
FT /note="Complementarity-determining-1"
FT /evidence="ECO:0000250|UniProtKB:P01602"
FT REGION 57..71
FT /note="Framework-2"
FT /evidence="ECO:0000250|UniProtKB:P01602"
FT REGION 72..78
FT /note="Complementarity-determining-2"
FT /evidence="ECO:0000250|UniProtKB:P01602"
FT REGION 79..110
FT /note="Framework-3"
FT /evidence="ECO:0000250|UniProtKB:P01602"
FT REGION 111..>117
FT /note="Complementarity-determining-2"
FT /evidence="ECO:0000250|UniProtKB:P01602"
FT DISULFID 45..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 44
FT /note="T -> I (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="G -> T (in Ref. 2; AA sequence and 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="K -> T (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="R -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 72..74
FT /note="AAS -> GAT (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="S -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="S -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="S -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 113..116
FT /note="HNSY -> YSSF (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="H -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 117
SQ SEQUENCE 117 AA; 12779 MW; 8F0682D45A41B4DF CRC64;
MDMRVPAQLL GLLLLWFPGA RCDIQMTQSP SSLSASVGDR VTITCRASQG IRNDLGWYQQ
KPGKAPKRLI YAASSLQSGV PSRFSGSGSG TEFTLTISSL QPEDFATYYC LQHNSYP
