KV401_HUMAN
ID KV401_HUMAN Reviewed; 121 AA.
AC P06312; P01625; P06313; P06314; P83593;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Immunoglobulin kappa variable 4-1 {ECO:0000303|PubMed:11549845, ECO:0000303|Ref.9};
DE AltName: Full=Ig kappa chain V-IV region B17 {ECO:0000305|PubMed:2997713};
DE AltName: Full=Ig kappa chain V-IV region JI {ECO:0000305|PubMed:50995};
DE AltName: Full=Ig kappa chain V-IV region Len {ECO:0000305|PubMed:50995};
DE AltName: Full=Ig kappa chain V-IV region STH {ECO:0000305|PubMed:9588180};
DE Flags: Precursor;
GN Name=IGKV4-1 {ECO:0000303|PubMed:11549845, ECO:0000303|Ref.9};
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=2997712; DOI=10.1093/nar/13.18.6515;
RA Klobeck H.G., Bornkamm G.W., Combriato G., Mocikat R., Pohlenz H.D.,
RA Zachau H.G.;
RT "Subgroup IV of human immunoglobulin K light chains is encoded by a single
RT germline gene.";
RL Nucleic Acids Res. 13:6515-6529(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2997713; DOI=10.1093/nar/13.18.6531;
RA Marsh P., Mills F., Gould H.;
RT "Detection of a unique human V kappa IV germline gene by a cloned cDNA
RT probe.";
RL Nucleic Acids Res. 13:6531-6544(1985).
RN [3]
RP SEQUENCE REVISION TO 76.
RA Marsh P.;
RL Submitted (OCT-1986) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE IGKV4-1*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 [5]
RP PROTEIN SEQUENCE OF 21-121.
RX PubMed=50995;
RA Schneider M., Hilschmann N.;
RT "The primary structure of a monoclonic immunoglobulin-L-chain of subgroup
RT IV of the kappa type (Bence-Jones protein Len).";
RL Hoppe-Seyler's Z. Physiol. Chem. 356:507-557(1975).
RN [6]
RP SEQUENCE REVISION TO 29.
RA Salomon A.;
RL Submitted (AUG-1996) to UniProtKB.
RN [7] {ECO:0000305}
RP PROTEIN SEQUENCE OF 21-121.
RC TISSUE=Abdominal adipose tissue {ECO:0000269|PubMed:9588180};
RX PubMed=9588180; DOI=10.1006/bbrc.1998.8515;
RA Olsen K.E., Sletten K., Westermark P.;
RT "Extended analysis of AL-amyloid protein from abdominal wall subcutaneous
RT fat biopsy: kappa IV immunoglobulin light chain.";
RL Biochem. Biophys. Res. Commun. 245:713-716(1998).
RN [8]
RP NOMENCLATURE.
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 [9]
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 [10]
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 [11]
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 [12]
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 [13]
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).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: V segment of the variable domain of immunoglobulins light
CC chain 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:22158414, PubMed:20176268). 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 IGKV4-1*01. {ECO:0000305}.
CC -!- CAUTION: For an example of a full-length immunoglobulin kappa light
CC chain see AC P0DOX7. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA26733.1; Type=Miscellaneous discrepancy; Note=Chimeric DNA corresponding to regions V and J of immunoglobulin kappa light chain.; Evidence={ECO:0000305};
CC Sequence=CAA77317.1; Type=Miscellaneous discrepancy; Note=Chimeric DNA corresponding to regions V and J of immunoglobulin kappa light chain.; Evidence={ECO:0000305};
CC Sequence=CAA77318.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z00022; CAA77317.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z00023; CAA77318.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X02990; CAA26733.1; ALT_SEQ; mRNA.
DR EMBL; AC244205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A01902; K4HU.
DR PIR; A01903; K4HULN.
DR PIR; A01904; K4HUJI.
DR PIR; A01905; K4HU17.
DR PIR; PH0869; PH0869.
DR PIR; S30523; S30523.
DR PIR; S34002; S34002.
DR PIR; S34003; S34003.
DR PDB; 1EEQ; X-ray; 1.50 A; A/B=21-121.
DR PDB; 1EEU; X-ray; 1.60 A; A/B=21-121.
DR PDB; 1EFQ; X-ray; 1.60 A; A=21-121.
DR PDB; 1EK3; X-ray; 1.90 A; A/B=21-121.
DR PDB; 1LVE; X-ray; 1.95 A; A=21-121.
DR PDB; 1QAC; X-ray; 1.80 A; A/B=21-121.
DR PDB; 2LVE; X-ray; 2.70 A; A=21-121.
DR PDB; 3LVE; X-ray; 2.00 A; A=21-121.
DR PDB; 4LVE; X-ray; 2.30 A; A/B=21-121.
DR PDB; 5LVE; X-ray; 2.00 A; A=21-121.
DR PDBsum; 1EEQ; -.
DR PDBsum; 1EEU; -.
DR PDBsum; 1EFQ; -.
DR PDBsum; 1EK3; -.
DR PDBsum; 1LVE; -.
DR PDBsum; 1QAC; -.
DR PDBsum; 2LVE; -.
DR PDBsum; 3LVE; -.
DR PDBsum; 4LVE; -.
DR PDBsum; 5LVE; -.
DR AlphaFoldDB; P06312; -.
DR BMRB; P06312; -.
DR SMR; P06312; -.
DR IntAct; P06312; 3.
DR IMGT_GENE-DB; IGKV4-1; -.
DR iPTMnet; P06312; -.
DR PhosphoSitePlus; P06312; -.
DR BioMuta; IGKV4-1; -.
DR DMDM; 31340182; -.
DR jPOST; P06312; -.
DR MassIVE; P06312; -.
DR PeptideAtlas; P06312; -.
DR PRIDE; P06312; -.
DR ProteomicsDB; 51886; -.
DR Ensembl; ENST00000390243.2; ENSP00000374778.2; ENSG00000211598.2.
DR UCSC; uc061lqi.1; human.
DR GeneCards; IGKV4-1; -.
DR HGNC; HGNC:5834; IGKV4-1.
DR HPA; ENSG00000211598; Tissue enhanced (intestine, lymphoid tissue).
DR neXtProt; NX_P06312; -.
DR OpenTargets; ENSG00000211598; -.
DR VEuPathDB; HostDB:ENSG00000211598; -.
DR GeneTree; ENSGT00940000153094; -.
DR HOGENOM; CLU_077975_4_1_1; -.
DR InParanoid; P06312; -.
DR OMA; SCFLCTQ; -.
DR PhylomeDB; P06312; -.
DR TreeFam; TF352067; -.
DR PathwayCommons; P06312; -.
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; P06312; -.
DR ChiTaRS; IGKV4-1; human.
DR Pharos; P06312; Tdark.
DR PRO; PR:P06312; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P06312; protein.
DR Bgee; ENSG00000211598; Expressed in rectum and 122 other tissues.
DR Genevisible; P06312; HS.
DR GO; GO:0072562; C:blood microparticle; 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; 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; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Immunity; Immunoglobulin; Immunoglobulin domain; Membrane;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:50995,
FT ECO:0000269|PubMed:9588180"
FT CHAIN 21..121
FT /note="Immunoglobulin kappa variable 4-1"
FT /evidence="ECO:0000269|PubMed:50995,
FT ECO:0000269|PubMed:9588180"
FT /id="PRO_0000015181"
FT DOMAIN 21..>121
FT /note="Ig-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 21..43
FT /note="Framework-1"
FT /evidence="ECO:0000303|PubMed:2997712"
FT REGION 44..60
FT /note="Complementarity-determining-1"
FT /evidence="ECO:0000303|PubMed:2997712"
FT REGION 61..75
FT /note="Framework-2"
FT /evidence="ECO:0000303|PubMed:2997712"
FT REGION 76..82
FT /note="Complementarity-determining-2"
FT /evidence="ECO:0000303|PubMed:2997712"
FT REGION 83..114
FT /note="Framework-3"
FT /evidence="ECO:0000303|PubMed:2997712"
FT REGION 115..121
FT /note="Complementarity-determining-3"
FT /evidence="ECO:0000303|PubMed:2997712"
FT DISULFID 43..114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 32
FT /note="A -> V (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="K -> R (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="V -> I (in Ref. 2; CAA26733)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="N -> D (in Ref. 2; CAA26733)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="N -> S (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="P -> A (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 74..75
FT /note="IY -> FS (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 102..103
FT /note="SS -> PG (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 118..120
FT /note="YST -> DTI (in Ref. 1; CAA77317)"
FT /evidence="ECO:0000305"
FT CONFLICT 119..120
FT /note="ST -> NL (in Ref. 2; CAA26733)"
FT /evidence="ECO:0000305"
FT CONFLICT 119..120
FT /note="ST -> RI (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 121
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:1EEQ"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:1EEQ"
FT STRAND 39..47
FT /evidence="ECO:0007829|PDB:1EEQ"
FT TURN 52..55
FT /evidence="ECO:0007829|PDB:1EEQ"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:1EEQ"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:1EEQ"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:1EEQ"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:1EEQ"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:1EEQ"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:1EEQ"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:1EEQ"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:1EEQ"
SQ SEQUENCE 121 AA; 13380 MW; 9586AD4188D33974 CRC64;
MVLQTQVFIS LLLWISGAYG DIVMTQSPDS LAVSLGERAT INCKSSQSVL YSSNNKNYLA
WYQQKPGQPP KLLIYWASTR ESGVPDRFSG SGSGTDFTLT ISSLQAEDVA VYYCQQYYST
P
