Entry euk: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   10-MAY-2017, entry version 113.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE
RP   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.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   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.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   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.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 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
RT   protein 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;
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.
RL   (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
RT   Rise 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.,
RA   Schwager P., Steigemann W., Schramm H.J.;
RT   "The structure determination of the variable portion of the Bence-
RT   Jones 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
CC       (PubMed:24600447). Immunoglobulins, also known as antibodies, are
CC       membrane-bound or secreted glycoproteins produced by B
CC       lymphocytes. In the recognition phase of humoral immunity, the
CC       membrane-bound immunoglobulins serve as receptors which, upon
CC       binding of a specific antigen, trigger the clonal expansion and
CC       differentiation of B lymphocytes into immunoglobulins-secreting
CC       plasma cells. Secreted immunoglobulins mediate the effector phase
CC       of humoral immunity, which results in the elimination of bound
CC       antigens (PubMed:20176268, PubMed:22158414). The antigen binding
CC       site is formed by the variable domain of one heavy chain, together
CC       with that of its associated light chain. Thus, each immunoglobulin
CC       has two antigen binding sites with remarkable affinity for a
CC       particular antigen. The variable domains are assembled by a
CC       process called V-(D)-J rearrangement and can then be subjected to
CC       somatic hypermutations which, after exposure to antigen and
CC       selection, allow affinity maturation for a particular antigen
CC       (PubMed:20176268, PubMed:17576170). {ECO:0000303|PubMed:17576170,
CC       ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414,
CC       ECO:0000303|PubMed:24600447}.
CC   -!- SUBUNIT: Immunoglobulins are composed of two identical heavy
CC       chains and 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
CC       that of IMGT allele IGKV1-33*01.
CC   -!- CAUTION: For an example of a full length immunoglobulin kappa
CC       light 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   PDBsum; 1B0W; -.
DR   PDBsum; 1JV5; -.
DR   PDBsum; 1QP1; -.
DR   PDBsum; 2Q20; -.
DR   PDBsum; 3CDC; -.
DR   PDBsum; 3CDF; -.
DR   PDBsum; 3CDY; -.
DR   PDBsum; 4K07; -.
DR   ProteinModelPortal; P01594; -.
DR   SMR; P01594; -.
DR   DIP; DIP-58572N; -.
DR   IMGT_GENE-DB; IGKV1-33; -.
DR   DMDM; 125758; -.
DR   DMDM; 125767; -.
DR   PeptideAtlas; P01594; -.
DR   PRIDE; P01594; -.
DR   Ensembl; ENST00000473726; ENSP00000420020; ENSG00000242076.
DR   Ensembl; ENST00000632835; ENSP00000487732; ENSG00000282811.
DR   H-InvDB; HIX0161621; -.
DR   HGNC; HGNC:5737; IGKV1-33.
DR   neXtProt; NX_P01594; -.
DR   GeneTree; ENSGT00780000121852; -.
DR   HOVERGEN; HBG018013; -.
DR   PhylomeDB; 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-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR   EvolutionaryTrace; P01594; -.
DR   PRO; PR:P01594; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0003823; F:antigen binding; NAS:UniProtKB.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
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; NAS:UniProtKB.
DR   GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; 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; 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   Complete proteome; Direct protein sequencing; Disulfide bond;
KW   Immunity; Immunoglobulin domain; Immunoglobulin V region; Membrane;
KW   Polymorphism; Reference proteome; Secreted; Signal.
FT   SIGNAL        1     22       {ECO:0000269|PubMed:5028201}.
FT   CHAIN        23    117       Immunoglobulin kappa variable 1-33.
FT                                {ECO:0000255}.
FT                                /FTId=PRO_0000059738.
FT   DOMAIN       24   >117       Ig-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00114}.
FT   REGION       23     45       Framework-1.
FT   REGION       46     56       Complementarity-determining-1.
FT   REGION       57     71       Framework-2.
FT   REGION       72     78       Complementarity-determining-2.
FT   REGION       79    110       Framework-3.
FT   REGION      111   >117       Complementarity-determining-3.
FT   DISULFID     45    110       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   CONFLICT     32     32       S -> T (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     35     35       A -> V (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     46     46       Q -> E (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     50     53       DISN -> TVLS (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     53     53       N -> D (in Ref. 2; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     72     72       D -> A (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     75     75       N -> S (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     78     78       T -> S (in Ref. 2; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     87     87       S -> G (in Ref. 2; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     87     87       S -> Q (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     91     92       TD -> AH (in Ref. 2; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    100    100       L -> V (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    105    105       I -> F (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    114    115       DN -> LD (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    115    115       N -> Y (in Ref. 2; AA sequence).
FT                                {ECO:0000305}.
FT   NON_TER     117    117
FT   STRAND       26     29       {ECO:0000244|PDB:2Q20}.
FT   STRAND       31     35       {ECO:0000244|PDB:2Q20}.
FT   STRAND       41     49       {ECO:0000244|PDB:2Q20}.
FT   STRAND       55     60       {ECO:0000244|PDB:2Q20}.
FT   STRAND       66     71       {ECO:0000244|PDB:2Q20}.
FT   TURN         72     74       {ECO:0000244|PDB:2Q20}.
FT   STRAND       84     89       {ECO:0000244|PDB:2Q20}.
FT   STRAND       92     99       {ECO:0000244|PDB:2Q20}.
FT   HELIX       102    104       {ECO:0000244|PDB:2Q20}.
FT   STRAND      106    112       {ECO:0000244|PDB:2Q20}.
FT   STRAND      114    117       {ECO:0000244|PDB:2Q20}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        40    112       ismart:IGv [T]
FT   MYHIT        24    117       iprf:IG_LIKE [T]
FT   MYHIT        28    111       ipfam:V-set [T]
FT   MYHIT        30    116       ismart:IG [T]
SQ   SEQUENCE   117 AA;  12848 MW;  EE4F871C54A514FB CRC64;
     MDMRVPAQLL GLLLLWLSGA RCDIQMTQSP SSLSASVGDR VTITCQASQD ISNYLNWYQQ
     KPGKAPKLLI YDASNLETGV PSRFSGSGSG TDFTFTISSL QPEDIATYYC QQYDNLP
//