KV230_HUMAN
ID KV230_HUMAN Reviewed; 120 AA.
AC P06310; A0A075B6S3;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2016, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Immunoglobulin kappa variable 2-30 {ECO:0000303|PubMed:11549845, ECO:0000303|Ref.4};
DE AltName: Full=Ig kappa chain V-II region RPMI 6410 {ECO:0000305|PubMed:2997711};
DE Flags: Precursor;
GN Name=IGKV2-30 {ECO:0000303|PubMed:11549845, ECO:0000303|Ref.4};
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=2997711; DOI=10.1093/nar/13.18.6499;
RA Klobeck H.G., Meindl A., Combriato G., Solomon A., Zachau H.G.;
RT "Human immunoglobulin kappa light chain genes of subgroups II and III.";
RL Nucleic Acids Res. 13:6499-6513(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE IGKV2-30*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 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 [4]
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 [5]
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 [6]
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 [7]
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 [8]
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 IGKV2-30*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=CAA77315.1; Type=Miscellaneous discrepancy; Note=Chimeric DNA corresponding to regions V and J of immunoglobulin kappa light chain.; Evidence={ECO:0000305};
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DR EMBL; AC244255; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z00020; CAA77315.1; ALT_SEQ; Genomic_DNA.
DR PIR; A01890; K2HURP.
DR AlphaFoldDB; P06310; -.
DR SMR; P06310; -.
DR DrugBank; DB07375; Etiocholanedione.
DR DrugBank; DB00693; Fluorescein.
DR IMGT_GENE-DB; IGKV2-30; -.
DR BioMuta; IGKV2-30; -.
DR DMDM; 125792; -.
DR jPOST; P06310; -.
DR MassIVE; P06310; -.
DR PeptideAtlas; P06310; -.
DR PRIDE; P06310; -.
DR Ensembl; ENST00000468494.1; ENSP00000418138.1; ENSG00000243238.1.
DR Ensembl; ENST00000632910.1; ENSP00000488685.1; ENSG00000281933.1.
DR GeneCards; IGKV2-30; -.
DR HGNC; HGNC:5785; IGKV2-30.
DR HPA; ENSG00000243238; Tissue enhanced (intestine, lymphoid tissue, stomach).
DR neXtProt; NX_P06310; -.
DR OpenTargets; ENSG00000243238; -.
DR VEuPathDB; HostDB:ENSG00000243238; -.
DR GeneTree; ENSGT00940000153770; -.
DR OMA; SGRQRCA; -.
DR PhylomeDB; P06310; -.
DR PathwayCommons; P06310; -.
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; P06310; -.
DR Pharos; P06310; Tdark.
DR PRO; PR:P06310; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P06310; protein.
DR Bgee; ENSG00000243238; Expressed in duodenum and 91 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; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 3: Inferred from homology;
KW Adaptive immunity; Cell membrane; Disulfide bond; Immunity; Immunoglobulin;
KW Immunoglobulin domain; Membrane; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..120
FT /note="Immunoglobulin kappa variable 2-30"
FT /evidence="ECO:0000255"
FT /id="PRO_0000015173"
FT DOMAIN 21..>120
FT /note="Ig-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 21..43
FT /note="Framework-1"
FT /evidence="ECO:0000303|PubMed:2997711"
FT REGION 44..59
FT /note="Complementarity-determining-1"
FT /evidence="ECO:0000303|PubMed:2997711"
FT REGION 60..74
FT /note="Framework-2"
FT /evidence="ECO:0000303|PubMed:2997711"
FT REGION 75..81
FT /note="Complementarity-determining-2"
FT /evidence="ECO:0000303|PubMed:2997711"
FT REGION 82..113
FT /note="Framework-3"
FT /evidence="ECO:0000303|PubMed:2997711"
FT REGION 114..>120
FT /note="Complementarity-determining-3"
FT /evidence="ECO:0000303|PubMed:2997711"
FT DISULFID 43..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 120
FT /note="P -> S (in Ref. 1; CAA77315)"
FT /evidence="ECO:0000305"
FT NON_TER 120
SQ SEQUENCE 120 AA; 13185 MW; CBC23C12D0848080 CRC64;
MRLPAQLLGL LMLWVPGSSG DVVMTQSPLS LPVTLGQPAS ISCRSSQSLV YSDGNTYLNW
FQQRPGQSPR RLIYKVSNRD SGVPDRFSGS GSGTDFTLKI SRVEAEDVGV YYCMQGTHWP
