KV133_HUMAN
ID KV133_HUMAN Reviewed; 117 AA.
AC P01594; A0A087WZH9; P01603;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2016, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Immunoglobulin kappa variable 1-33 {ECO:0000303|PubMed:11549845, ECO:0000303|Ref.5};
DE AltName: Full=Ig kappa chain V-I region AU {ECO:0000305|PubMed:5028201};
DE AltName: Full=Ig kappa chain V-I region Ka {ECO:0000305|PubMed:818073};
DE Flags: Precursor;
GN Name=IGKV1-33 {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 IGKV1-33*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=5028201;
RA Schiechl H., Hilschmann N.;
RT "Rule of antibody structure. The primary structure of a monoclonal
RT immunoglobulin L-chain of the kappa-type, subgroup I (Bence-Jones protein
RT Au).";
RL Hoppe-Seyler's Z. Physiol. Chem. 353:345-370(1972).
RN [3]
RP PROTEIN SEQUENCE OF 23-117.
RX PubMed=818073;
RA Shinoda T.;
RT "Comparative structural studies on the light chains of human
RT immunoglobulins. I. Protein Ka with the Inv(3) allotypic marker.";
RL J. Biochem. 77:1277-1296(1975).
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).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 23-117.
RX PubMed=1234024; DOI=10.1007/bf00539775;
RA Fehlhammer H., Schiffer M., Epp O., Colman P.M., Lattman E.E., Schwager P.,
RA Steigemann W., Schramm H.J.;
RT "The structure determination of the variable portion of the Bence-Jones
RT protein Au.";
RL Biophys. Struct. Mech. 1:139-146(1975).
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 -!- INTERACTION:
CC P01594; P01594: IGKV1-33; NbExp=3; IntAct=EBI-15853604, EBI-15853604;
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 IGKV1-33*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; AC244255; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A01869; K1HUKA.
DR PIR; A91653; K1HUAU.
DR PIR; S42265; S42265.
DR PDB; 1B0W; X-ray; 1.80 A; A/B/C=23-117.
DR PDB; 1JV5; X-ray; 2.20 A; A=23-117.
DR PDB; 1QP1; X-ray; 2.06 A; A/B/C=23-117.
DR PDB; 2Q20; X-ray; 1.30 A; A/B=23-117.
DR PDB; 3CDC; X-ray; 1.53 A; A/B=23-117.
DR PDB; 3CDF; X-ray; 1.53 A; A/B/C/D/E/F=23-117.
DR PDB; 3CDY; X-ray; 2.43 A; A/B=23-117.
DR PDB; 4K07; X-ray; 2.83 A; A/B/C/D/E/F/G/H/I/J=20-117.
DR PDB; 7CZQ; EM; 2.80 A; K/N=24-117.
DR PDB; 7CZU; EM; 3.40 A; K/N=24-117.
DR PDB; 7CZV; EM; 3.30 A; K/M/N=24-117.
DR PDBsum; 1B0W; -.
DR PDBsum; 1JV5; -.
DR PDBsum; 1QP1; -.
DR PDBsum; 2Q20; -.
DR PDBsum; 3CDC; -.
DR PDBsum; 3CDF; -.
DR PDBsum; 3CDY; -.
DR PDBsum; 4K07; -.
DR PDBsum; 7CZQ; -.
DR PDBsum; 7CZU; -.
DR PDBsum; 7CZV; -.
DR AlphaFoldDB; P01594; -.
DR SMR; P01594; -.
DR DIP; DIP-58572N; -.
DR IntAct; P01594; 4.
DR IMGT_GENE-DB; IGKV1-33; -.
DR BioMuta; IGKV1-33; -.
DR DMDM; 125767; -.
DR jPOST; P01594; -.
DR MassIVE; P01594; -.
DR PRIDE; P01594; -.
DR Ensembl; ENST00000473726.1; ENSP00000420020.1; ENSG00000242076.3.
DR Ensembl; ENST00000632835.1; ENSP00000487732.1; ENSG00000282811.1.
DR UCSC; uc061lra.1; human.
DR GeneCards; IGKV1-33; -.
DR HGNC; HGNC:5737; IGKV1-33.
DR HPA; ENSG00000242076; Tissue enhanced (lymphoid tissue, stomach, urinary bladder).
DR neXtProt; NX_P01594; -.
DR VEuPathDB; HostDB:ENSG00000242076; -.
DR GeneTree; ENSGT00940000162515; -.
DR PhylomeDB; P01594; -.
DR PathwayCommons; P01594; -.
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; P01594; -.
DR ChiTaRS; IGKV1-33; human.
DR EvolutionaryTrace; P01594; -.
DR Pharos; P01594; Tdark.
DR PRO; PR:P01594; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P01594; protein.
DR Bgee; ENSG00000242076; Expressed in rectum and 89 other tissues.
DR GO; GO:0072562; C:blood microparticle; 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:0042802; F:identical protein binding; IPI:IntAct.
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; Bence-Jones protein; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Immunity; Immunoglobulin;
KW Immunoglobulin domain; Membrane; Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:5028201"
FT CHAIN 23..117
FT /note="Immunoglobulin kappa variable 1-33"
FT /evidence="ECO:0000255"
FT /id="PRO_0000059738"
FT DOMAIN 24..>117
FT /note="Ig-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 23..45
FT /note="Framework-1"
FT REGION 46..56
FT /note="Complementarity-determining-1"
FT REGION 57..71
FT /note="Framework-2"
FT REGION 72..78
FT /note="Complementarity-determining-2"
FT REGION 79..110
FT /note="Framework-3"
FT REGION 111..>117
FT /note="Complementarity-determining-3"
FT DISULFID 45..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 32
FT /note="S -> T (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="A -> V (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="Q -> E (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 50..53
FT /note="DISN -> TVLS (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="D -> A (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="N -> S (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="T -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="S -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="S -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 91..92
FT /note="TD -> AH (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="L -> V (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="I -> F (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 114..115
FT /note="DN -> LD (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="N -> Y (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 117
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:2Q20"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:2Q20"
FT STRAND 41..49
FT /evidence="ECO:0007829|PDB:2Q20"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:2Q20"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:7CZQ"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:2Q20"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:2Q20"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:2Q20"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:2Q20"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:2Q20"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:2Q20"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:2Q20"
SQ SEQUENCE 117 AA; 12848 MW; EE4F871C54A514FB CRC64;
MDMRVPAQLL GLLLLWLSGA RCDIQMTQSP SSLSASVGDR VTITCQASQD ISNYLNWYQQ
KPGKAPKLLI YDASNLETGV PSRFSGSGSG TDFTFTISSL QPEDIATYYC QQYDNLP
