Entry sw: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   18-JAN-2017, entry version 110.
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   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       Immunoglobulins, also known as antibodies, are membrane-bound or
CC       secreted glycoproteins produced by B lymphocytes. In the
CC       recognition phase of humoral immunity, the membrane-bound
CC       immunoglobulins serve as receptors which, upon binding of a
CC       specific antigen, trigger the clonal expansion and differentiation
CC       of B lymphocytes into immunoglobulins-secreting plasma cells.
CC       Secreted immunoglobulins mediate the effector phase of humoral
CC       immunity, which results in the elimination of bound antigens
CC       (PubMed:20176268, PubMed:22158414). The antigen binding site is
CC       formed by the variable domain of one heavy chain, together with
CC       that of its associated light chain. Thus, each immunoglobulin has
CC       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   -!- SUBUNIT: Immunoglobulins are composed of two identical heavy
CC       chains and two identical light chains, linked by disulfide bonds.
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   -!- SIMILARITY: Contains 1 Ig-like (immunoglobulin-like) domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00114}.
CC   -!- WEB RESOURCE: Name=IMGT/GENE-DB;
CC       URL="http://www.imgt.org/IMGT_GENE-DB/GENElect?query=2+IGKV1-33&species=Homo+sapiens";
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=23-117.
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   DIP; DIP-58572N; -.
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   OpenTargets; ENSG00000239975; -.
DR   OpenTargets; ENSG00000242076; -.
DR   OpenTargets; ENSG00000282811; -.
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-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   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; NAS:UniProtKB.
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: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        28    111       ipfam:V-set [T]
FT   MYHIT        30    116       ismart:IG [T]
FT   MYHIT        40    112       ismart:IGv [T]
FT   MYHIT        24    117       iprf:IG_LIKE [T]
SQ   SEQUENCE   117 AA;  12848 MW;  EE4F871C54A514FB CRC64;
     MDMRVPAQLL GLLLLWLSGA RCDIQMTQSP SSLSASVGDR VTITCQASQD ISNYLNWYQQ
     KPGKAPKLLI YDASNLETGV PSRFSGSGSG TDFTFTISSL QPEDIATYYC QQYDNLP
//