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Immunoglobulin kappa variable 2-30 (Ig kappa chain V-II region RPMI 6410)

 KV230_HUMAN             Reviewed;         120 AA.
P06310; A0A075B6S3;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
02-NOV-2016, sequence version 2.
20-JUN-2018, entry version 119.
RecName: Full=Immunoglobulin kappa variable 2-30 {ECO:0000303|PubMed:11549845, ECO:0000303|Ref.4};
AltName: Full=Ig kappa chain V-II region RPMI 6410 {ECO:0000305|PubMed:2997711};
Flags: Precursor;
Name=IGKV2-30 {ECO:0000303|PubMed:11549845, ECO:0000303|Ref.4};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2997711; DOI=10.1093/nar/13.18.6499;
Klobeck H.G., Meindl A., Combriato G., Solomon A., Zachau H.G.;
"Human immunoglobulin kappa light chain genes of subgroups II and
III.";
Nucleic Acids Res. 13:6499-6513(1985).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE
IGKV2-30*01).
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[3]
NOMEMCLATURE.
PubMed=11549845;
Lefranc M.P.;
"Nomenclature of the human immunoglobulin kappa (IGK) genes.";
Exp. Clin. Immunogenet. 18:161-174(2001).
[4]
NOMENCLATURE.
Lefranc M.P., Lefranc G.;
"The Immunoglobulin FactsBook.";
(In) Lefranc M.P., Lefranc G. (eds.);
The Immunoglobulin FactsBook., pp.1-458, Academic Press, London.
(2001).
[5]
REVIEW ON SOMATIC HYPERMUTATION.
PubMed=17576170; DOI=10.1146/annurev.genet.41.110306.130340;
Teng G., Papavasiliou F.N.;
"Immunoglobulin somatic hypermutation.";
Annu. Rev. Genet. 41:107-120(2007).
[6]
REVIEW ON IMMUNOGLOBULINS.
PubMed=20176268; DOI=10.1016/j.jaci.2009.09.046;
Schroeder H.W. Jr., Cavacini L.;
"Structure and function of immunoglobulins.";
J. Allergy Clin. Immunol. 125:S41-S52(2010).
[7]
REVIEW ON FUNCTION.
PubMed=22158414; DOI=10.1038/nri3128;
McHeyzer-Williams M., Okitsu S., Wang N., McHeyzer-Williams L.;
"Molecular programming of B cell memory.";
Nat. Rev. Immunol. 12:24-34(2012).
[8]
NOMENCLATURE.
PubMed=24600447; DOI=10.3389/fimmu.2014.00022;
Lefranc M.P.;
"Immunoglobulin and T Cell Receptor Genes: IMGT((R)) and the Birth and
Rise of Immunoinformatics.";
Front. Immunol. 5:22-22(2014).
-!- FUNCTION: V region of the variable domain of immunoglobulin light
chains that participates in the antigen recognition
(PubMed:24600447). Immunoglobulins, also known as antibodies, are
membrane-bound or secreted glycoproteins produced by B
lymphocytes. In the recognition phase of humoral immunity, the
membrane-bound immunoglobulins serve as receptors which, upon
binding of a specific antigen, trigger the clonal expansion and
differentiation of B lymphocytes into immunoglobulins-secreting
plasma cells. Secreted immunoglobulins mediate the effector phase
of humoral immunity, which results in the elimination of bound
antigens (PubMed:20176268, PubMed:22158414). The antigen binding
site is formed by the variable domain of one heavy chain, together
with that of its associated light chain. Thus, each immunoglobulin
has two antigen binding sites with remarkable affinity for a
particular antigen. The variable domains are assembled by a
process called V-(D)-J rearrangement and can then be subjected to
somatic hypermutations which, after exposure to antigen and
selection, allow affinity maturation for a particular antigen
(PubMed:20176268, PubMed:17576170). {ECO:0000303|PubMed:17576170,
ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414,
ECO:0000303|PubMed:24600447}.
-!- SUBUNIT: Immunoglobulins are composed of two identical heavy
chains and two identical light chains; disulfide-linked.
{ECO:0000303|PubMed:20176268}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268,
ECO:0000303|PubMed:22158414}. Cell membrane
{ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
-!- POLYMORPHISM: There are several alleles. The sequence shown is
that of IMGT allele IGKV2-30*01.
-!- CAUTION: For an example of a full-length immunoglobulin kappa
light chain see AC P0DOX7. {ECO:0000305}.
-!- SEQUENCE CAUTION:
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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EMBL; AC244255; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z00020; CAA77315.1; ALT_SEQ; Genomic_DNA.
PIR; A01890; K2HURP.
ProteinModelPortal; P06310; -.
SMR; P06310; -.
DrugBank; DB00693; Fluorescein.
IMGT_GENE-DB; IGKV2-30; -.
DMDM; 125792; -.
PeptideAtlas; P06310; -.
PRIDE; P06310; -.
ProteomicsDB; 51884; -.
Ensembl; ENST00000468494; ENSP00000418138; ENSG00000243238.
Ensembl; ENST00000632910; ENSP00000488685; ENSG00000281933.
EuPathDB; HostDB:ENSG00000243238.1; -.
GeneCards; IGKV2-30; -.
HGNC; HGNC:5785; IGKV2-30.
neXtProt; NX_P06310; -.
OpenTargets; ENSG00000243238; -.
GeneTree; ENSGT00860000133683; -.
HOVERGEN; HBG018013; -.
OMA; MLWITGS; -.
PhylomeDB; P06310; -.
Reactome; R-HSA-166663; Initial triggering of complement.
Reactome; R-HSA-173623; Classical antibody-mediated complement activation.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
Reactome; R-HSA-2029481; FCGR activation.
Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-HSA-2029485; Role of phospholipids in phagocytosis.
Reactome; R-HSA-2168880; Scavenging of heme from plasma.
Reactome; R-HSA-2454202; Fc epsilon receptor (FCERI) signaling.
Reactome; R-HSA-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-5690714; CD22 mediated BCR regulation.
Reactome; R-HSA-977606; Regulation of Complement cascade.
Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
ChiTaRS; IGKV2-30; human.
PRO; PR:P06310; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000243238; -.
GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0003823; F:antigen binding; NAS:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
GO; GO:0006956; P:complement activation; TAS:Reactome.
GO; GO:0006958; P:complement activation, classical pathway; TAS:Reactome.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
GO; GO:0006955; P:immune response; NAS:UniProtKB.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome.
GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013106; Ig_V-set.
Pfam; PF07686; V-set; 1.
SMART; SM00406; IGv; 1.
SUPFAM; SSF48726; SSF48726; 1.
PROSITE; PS50835; IG_LIKE; 1.
3: Inferred from homology;
Adaptive immunity; Cell membrane; Complete proteome; Disulfide bond;
Immunity; Immunoglobulin domain; Immunoglobulin V region; Membrane;
Polymorphism; Reference proteome; Secreted; Signal.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 120 Immunoglobulin kappa variable 2-30.
{ECO:0000255}.
/FTId=PRO_0000015173.
DOMAIN 21 >120 Ig-like. {ECO:0000255|PROSITE-
ProRule:PRU00114}.
REGION 21 43 Framework-1.
{ECO:0000303|PubMed:2997711}.
REGION 44 59 Complementarity-determining-1.
{ECO:0000303|PubMed:2997711}.
REGION 60 74 Framework-2.
{ECO:0000303|PubMed:2997711}.
REGION 75 81 Complementarity-determining-2.
{ECO:0000303|PubMed:2997711}.
REGION 82 113 Framework-3.
{ECO:0000303|PubMed:2997711}.
REGION 114 >120 Complementarity-determining-3.
{ECO:0000303|PubMed:2997711}.
DISULFID 43 113 {ECO:0000255|PROSITE-ProRule:PRU00114}.
CONFLICT 120 120 P -> S (in Ref. 1; CAA77315).
{ECO:0000305}.
NON_TER 120 120
SEQUENCE 120 AA; 13185 MW; CBC23C12D0848080 CRC64;
MRLPAQLLGL LMLWVPGSSG DVVMTQSPLS LPVTLGQPAS ISCRSSQSLV YSDGNTYLNW
FQQRPGQSPR RLIYKVSNRD SGVPDRFSGS GSGTDFTLKI SRVEAEDVGV YYCMQGTHWP


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