KV139_HUMAN
ID KV139_HUMAN Reviewed; 117 AA.
AC P01597; A0A0B4J1Z7; A0A0C4DH57; A0A0U1RVJ5; P01600; P01606; P01612; P04431;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2016, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Immunoglobulin kappa variable 1-39 {ECO:0000303|PubMed:11549845, ECO:0000303|Ref.8};
DE AltName: Full=Ig kappa chain V-I region DEE {ECO:0000305|PubMed:5124396};
DE AltName: Full=Ig kappa chain V-I region Hau {ECO:0000305|PubMed:4097974};
DE AltName: Full=Ig kappa chain V-I region Mev {ECO:0000305|PubMed:6816713};
DE AltName: Full=Ig kappa chain V-I region OU {ECO:0000305|PubMed:5447531};
DE AltName: Full=Ig kappa chain V-I region Walker {ECO:0000305|PubMed:6091049};
DE Flags: Precursor;
GN Name=IGKV1-39 {ECO:0000303|PubMed:11549845, ECO:0000303|Ref.8};
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=6091049; DOI=10.1093/nar/12.18.6995;
RA Klobeck H.G., Combriato G., Zachau H.G.;
RT "Immunoglobulin genes of the kappa light chain type from two human lymphoid
RT cell lines are closely related.";
RL Nucleic Acids Res. 12:6995-7006(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE IGKV1-39*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 23-117.
RX PubMed=4097974;
RA Watanabe S., Hilschmann N.;
RT "The primary structure of a monoclonal kappa-type immunoglobulin L-chain of
RT subgroup I (Bence-Jones protein Hau): subdivision within subgroups.";
RL Hoppe-Seyler's Z. Physiol. Chem. 351:1291-1295(1970).
RN [4]
RP PROTEIN SEQUENCE OF 23-117.
RX PubMed=5447531; DOI=10.1126/science.169.3940.56;
RA Kohler H., Shimizu A., Paul C., Putnam F.W.;
RT "Macroglobulin structure: variable sequence of light and heavy chains.";
RL Science 169:56-59(1970).
RN [5]
RP PROTEIN SEQUENCE OF 23-117.
RX PubMed=5124396; DOI=10.1042/bj1230945;
RA Milstein C.P., Deverson E.V.;
RT "The amino acid sequence of a human kappa light chain.";
RL Biochem. J. 123:945-958(1971).
RN [6]
RP PROTEIN SEQUENCE OF 23-117.
RX PubMed=6816713; DOI=10.1515/bchm2.1982.363.2.1347;
RA Eulitz M., Linke R.P.;
RT "Primary structure of the variable part of an amyloidogenic Bence-Jones
RT protein (Mev). An unusual insertion in the third hypervariable region of a
RT human kappa-immunoglobulin light chain.";
RL Hoppe-Seyler's Z. Physiol. Chem. 363:1347-1358(1982).
RN [7]
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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
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).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 23-117, AND DISULFIDE BOND.
RX PubMed=12217656; DOI=10.1016/s1047-8477(02)00015-1;
RA Nymalm Y., Kravchuk Z., Salminen T., Chumanevich A.A., Dubnovitsky A.P.,
RA Kankare J., Pentikainen O., Lehtonen J., Arosio P., Martsev S.,
RA Johnson M.S.;
RT "Antiferritin VL homodimer binds human spleen ferritin with high
RT specificity.";
RL J. Struct. Biol. 138:171-186(2002).
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 IGKV1-39*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=CAA25477.1; Type=Miscellaneous discrepancy; Note==Chimeric DNA. A chimeric DNA corresponding to regions V and J of immunoglobulin kappa light chain.; Evidence={ECO:0000305};
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DR EMBL; X00965; CAA25477.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC244255; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A01865; K1HUDE.
DR PIR; A01868; K1HUHU.
DR PIR; A01872; K1HUOU.
DR PIR; A01879; K1HUMV.
DR PIR; A01883; K1HUWK.
DR PIR; A27594; A27594.
DR PDB; 1F6L; X-ray; 2.80 A; L=23-117.
DR PDB; 3UPA; X-ray; 1.80 A; A/B=23-117.
DR PDBsum; 1F6L; -.
DR PDBsum; 3UPA; -.
DR AlphaFoldDB; P01597; -.
DR SMR; P01597; -.
DR IntAct; P01597; 1.
DR IMGT_GENE-DB; IGKV1-39; -.
DR CarbonylDB; P01597; -.
DR BioMuta; IGKV1-39; -.
DR DMDM; 125779; -.
DR jPOST; P01597; -.
DR MassIVE; P01597; -.
DR PeptideAtlas; P01597; -.
DR PRIDE; P01597; -.
DR Ensembl; ENST00000498574.1; ENSP00000419058.1; ENSG00000242371.1.
DR Ensembl; ENST00000631411.1; ENSP00000488680.1; ENSG00000282120.1.
DR GeneCards; IGKV1-39; -.
DR HGNC; HGNC:5740; IGKV1-39.
DR HPA; ENSG00000242371; Group enriched (intestine, lymphoid tissue, salivary gland, stomach).
DR neXtProt; NX_P01597; -.
DR OpenTargets; ENSG00000242371; -.
DR OpenTargets; ENSG00000251546; -.
DR VEuPathDB; HostDB:ENSG00000242371; -.
DR OMA; DMMAPAQ; -.
DR PhylomeDB; P01597; -.
DR PathwayCommons; P01597; -.
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; P01597; -.
DR ChiTaRS; IGKV1-39; human.
DR Pharos; P01597; Tdark.
DR PRO; PR:P01597; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P01597; protein.
DR Bgee; ENSG00000242371; Expressed in duodenum and 80 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 3D-structure; 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:4097974,
FT ECO:0000269|PubMed:5124396, ECO:0000269|PubMed:5447531,
FT ECO:0000269|PubMed:6816713"
FT CHAIN 23..117
FT /note="Immunoglobulin kappa variable 1-39"
FT /evidence="ECO:0000269|PubMed:4097974,
FT ECO:0000269|PubMed:5124396, ECO:0000269|PubMed:5447531,
FT ECO:0000269|PubMed:6816713"
FT /id="PRO_0000059741"
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:6091049"
FT REGION 46..56
FT /note="Complementarity-determining-1"
FT /evidence="ECO:0000303|PubMed:6091049"
FT REGION 57..71
FT /note="Framework-2"
FT /evidence="ECO:0000303|PubMed:6091049"
FT REGION 72..78
FT /note="Complementarity-determining-2"
FT /evidence="ECO:0000303|PubMed:6091049"
FT REGION 79..110
FT /note="Framework-3"
FT /evidence="ECO:0000303|PubMed:6091049"
FT REGION 111..>117
FT /note="Complementarity-determining-3"
FT /evidence="ECO:0000303|PubMed:6091049"
FT DISULFID 45..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:12217656"
FT CONFLICT 24
FT /note="I -> D (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="T -> I (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="S -> G (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="S -> T (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 51..53
FT /note="ISS -> SVD (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 51..53
FT /note="ISS -> VNK (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="S -> N (in Ref. 1; CAA25477)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="N -> S (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="K -> B (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="K -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="L -> V (in Ref. 5; AA sequence and 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="Y -> F (in Ref. 5; AA sequence and 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 72..73
FT /note="AA -> DT (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 75..77
FT /note="SLQ -> BLH (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="S -> N (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="Q -> K (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="Q -> P (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="P -> T (in Ref. 1; CAA25477)"
FT /evidence="ECO:0000305"
FT CONFLICT 87..88
FT /note="SG -> GR (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="L -> F (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 99..101
FT /note="SLQ -> GLL (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="E -> D (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="F -> S (in Ref. 1; CAA25477)"
FT /evidence="ECO:0000305"
FT CONFLICT 113..115
FT /note="SYS -> NYI (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="S -> T (in Ref. 5; AA sequence and 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="T -> N (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="T -> S (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="P -> L (in Ref. 1; CAA25477)"
FT /evidence="ECO:0000305"
FT NON_TER 117
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:3UPA"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:3UPA"
FT STRAND 41..49
FT /evidence="ECO:0007829|PDB:3UPA"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:3UPA"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:3UPA"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:3UPA"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:3UPA"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:3UPA"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:3UPA"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:3UPA"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:3UPA"
SQ SEQUENCE 117 AA; 12737 MW; ED1DC5B0055AB9D4 CRC64;
MDMRVPAQLL GLLLLWLRGA RCDIQMTQSP SSLSASVGDR VTITCRASQS ISSYLNWYQQ
KPGKAPKLLI YAASSLQSGV PSRFSGSGSG TDFTLTISSL QPEDFATYYC QQSYSTP
