KVD28_HUMAN
ID KVD28_HUMAN Reviewed; 120 AA.
AC P01615; A0A0A0MTQ6; P01616; P01617; P06309;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2016, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Immunoglobulin kappa variable 2D-28 {ECO:0000303|PubMed:11549845, ECO:0000303|Ref.8};
DE AltName: Full=Ig kappa chain V-II region FR {ECO:0000305|PubMed:821524};
DE AltName: Full=Ig kappa chain V-II region GM607 {ECO:0000305|PubMed:6325927};
DE AltName: Full=Ig kappa chain V-II region MIL {ECO:0000305|Ref.3};
DE AltName: Full=Ig kappa chain V-II region TEW {ECO:0000305|PubMed:4596149, ECO:0000305|PubMed:4700495};
DE Flags: Precursor;
GN Name=IGKV2D-28 {ECO:0000303|PubMed:11549845, ECO:0000303|Ref.8};
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 IGKV2D-28*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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 17-120.
RX PubMed=6325927; DOI=10.1038/309073a0;
RA Klobeck H.G., Solomon A., Zachau H.G.;
RT "Contribution of human V kappa II germ-line genes to light-chain
RT diversity.";
RL Nature 309:73-76(1984).
RN [3]
RP PROTEIN SEQUENCE OF 21-120.
RA Dreyer W.J., Gray W.R., Hood L.E.;
RT "The genetic, molecular, and cellular basis of antibody formation: some
RT facts and a unifying hypothesis.";
RL Cold Spring Harb. Symp. Quant. Biol. 32:353-367(1967).
RN [4]
RP PROTEIN SEQUENCE OF 21-120.
RX PubMed=4596149; DOI=10.1021/bi00743a028;
RA Putnam F.W., Whitley E.J. Jr., Paul C., Davidson J.N.;
RT "Amino acid sequence of a kappa Bence Jones protein from a case of primary
RT amyloidosis.";
RL Biochemistry 12:3763-3780(1973).
RN [5]
RP PROTEIN SEQUENCE OF 21-120.
RX PubMed=821524; DOI=10.1021/bi00662a028;
RA Riesen W.F., Jaton J.-C.;
RT "Variable region sequence of the light chain from a Waldenstroms IgM with
RT specificity for phosphorylcholine.";
RL Biochemistry 15:3829-3833(1976).
RN [6]
RP PROTEIN SEQUENCE OF 21-47.
RX PubMed=4700495; DOI=10.1172/jci107295;
RA Terry W.D., Page D.L., Kimura S., Isobe T., Osserman E.F., Glenner G.G.;
RT "Structural identity of Bence Jones and amyloid fibril proteins in a
RT patient with plasma cell dyscrasia and amyloidosis.";
RL J. Clin. Invest. 52:1276-1281(1973).
RN [7]
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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
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 IGKV2D-28*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; AC233264; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z00009; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A01886; K2HUFR.
DR PIR; A01887; K2HUML.
DR PIR; A01889; K2HUGM.
DR PIR; A90370; K2HUTW.
DR AlphaFoldDB; P01615; -.
DR SMR; P01615; -.
DR IntAct; P01615; 1.
DR DrugBank; DB08562; 4-(4-STYRYL-PHENYLCARBAMOYL)-BUTYRIC ACID.
DR IMGT_GENE-DB; IGKV2D-28; -.
DR iPTMnet; P01615; -.
DR PhosphoSitePlus; P01615; -.
DR BioMuta; IGKV2D-28; -.
DR DMDM; 125786; -.
DR jPOST; P01615; -.
DR MassIVE; P01615; -.
DR PeptideAtlas; P01615; -.
DR PRIDE; P01615; -.
DR Ensembl; ENST00000453166.2; ENSP00000393492.2; ENSG00000242534.3.
DR GeneCards; IGKV2D-28; -.
DR HGNC; HGNC:5799; IGKV2D-28.
DR HPA; ENSG00000242534; Tissue enhanced (intestine, lymphoid tissue, salivary gland).
DR neXtProt; NX_P01615; -.
DR OpenTargets; ENSG00000244116; -.
DR VEuPathDB; HostDB:ENSG00000242534; -.
DR GeneTree; ENSGT00940000154039; -.
DR OMA; RMEPENV; -.
DR PhylomeDB; P01615; -.
DR PathwayCommons; P01615; -.
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; P01615; -.
DR Pharos; P01615; Tdark.
DR PRO; PR:P01615; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P01615; protein.
DR Bgee; ENSG00000242534; Expressed in duodenum and 89 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 1: Evidence at protein level;
KW Adaptive immunity; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Immunity; Immunoglobulin; Immunoglobulin domain; Membrane;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:4596149,
FT ECO:0000269|PubMed:4700495, ECO:0000269|PubMed:821524,
FT ECO:0000269|Ref.3"
FT CHAIN 20..120
FT /note="Immunoglobulin kappa variable 2D-28"
FT /evidence="ECO:0000269|PubMed:4596149,
FT ECO:0000269|PubMed:821524, ECO:0000269|Ref.3"
FT /id="PRO_0000059759"
FT DOMAIN 20..>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:6325927"
FT REGION 44..59
FT /note="Complementarity-determining-1"
FT /evidence="ECO:0000303|PubMed:6325927"
FT REGION 60..74
FT /note="Framework-2"
FT /evidence="ECO:0000303|PubMed:6325927"
FT REGION 75..81
FT /note="Complementarity-determining-2"
FT /evidence="ECO:0000303|PubMed:6325927"
FT REGION 82..113
FT /note="Framework-3"
FT /evidence="ECO:0000303|PubMed:6325927"
FT REGION 114..>120
FT /note="Complementarity-determining-3"
FT /evidence="ECO:0000303|PubMed:6325927"
FT DISULFID 43..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 22
FT /note="I -> V (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="M -> L (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="S -> F (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="P -> L (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="S -> Q (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="S -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 50..52
FT /note="LHS -> VYR (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="H -> Z (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 53..56
FT /note="NGYN -> DGFD (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 55..56
FT /note="YN -> BT (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="Missing (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="D -> N (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="G -> Q (in Ref. 2; Z00009)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="Q -> E (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 75..76
FT /note="LG -> AL (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 76..80
FT /note="GSNRA -> SSYRD (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="D -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="G -> D (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="S -> T (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="E -> Q (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="A -> G (in Ref. 2; Z00009)"
FT /evidence="ECO:0000305"
FT CONFLICT 117..119
FT /note="LQT -> TZS (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="T -> A (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 120
SQ SEQUENCE 120 AA; 12957 MW; 0B78BEF46FFB1F97 CRC64;
MRLPAQLLGL LMLWVSGSSG DIVMTQSPLS LPVTPGEPAS ISCRSSQSLL HSNGYNYLDW
YLQKPGQSPQ LLIYLGSNRA SGVPDRFSGS GSGTDFTLKI SRVEAEDVGV YYCMQALQTP
