ID   KV137_HUMAN             Reviewed;         117 AA.
AC   A0A075B6S9; A0A0A0MT75; A0A0E3D6N1; A0A0U1RVJ2;
DT   13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2016, sequence version 7.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Probable non-functional immunoglobulinn kappa variable 1-37 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=IGKV1-37 {ECO:0000303|PubMed:11340299, ECO:0000303|Ref.4,
GN   ECO:0000312|HGNC:HGNC:5739};
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 IGKV1-37*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   CHARACTERIZATION.
RX   PubMed=9619395; DOI=10.1159/000019049;
RA   Lefranc M.P.;
RT   "IMGT (ImMunoGeneTics) locus on focus. A new section of Experimental and
RT   Clinical Immunogenetics.";
RL   Exp. Clin. Immunogenet. 15:1-7(1998).
RN   [3]
RP   NOMENCLATURE.
RX   PubMed=11340299; DOI=10.1159/000049189;
RA   Lefranc M.P.;
RT   "Nomenclature of the human immunoglobulin heavy (IGH) genes.";
RL   Exp. Clin. Immunogenet. 18:100-116(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: Probable non-functional open reading frame (ORF) of V region
CC       of the variable domain of immunoglobulin light chains
CC       (PubMed:24600447). Non-functional ORF generally cannot participate in
CC       the synthesis of a productive immunoglobulin chain due to altered V-
CC       (D)-J or switch recombination and/or splicing site (at mRNA level)
CC       and/or conserved amino acid change (protein level) (PubMed:9619395).
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       ECO:0000303|PubMed:9619395}.
CC   -!- SUBUNIT: Most probably, the immunoglobulin is not assembled due to
CC       incorrect folding of light chain (Probable). Immunoglobulins are
CC       composed of two identical heavy chains and two identical light chains;
CC       disulfide-linked. {ECO:0000303|PubMed:20176268, ECO:0000305}.
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 IGKV1-37*01. {ECO:0000305}.
CC   -!- CAUTION: Most probably a non-functional protein that cannot participate
CC       in the synthesis of a productive immunoglobulin chain due to a mutation
CC       at position 110, corresponding to the second cysteine from the
CC       disulfide bridge, potentially leading to uncorrect folding
CC       (PubMed:9619395). {ECO:0000303|PubMed:9619395, ECO:0000305}.
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DR   EMBL; AC244255; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A075B6S9; -.
DR   SMR; A0A075B6S9; -.
DR   BioMuta; IGKV1-37; -.
DR   jPOST; A0A075B6S9; -.
DR   MassIVE; A0A075B6S9; -.
DR   Ensembl; ENST00000465170.1; ENSP00000417427.1; ENSG00000239862.1.
DR   Ensembl; ENST00000632103.1; ENSP00000487793.1; ENSG00000282394.1.
DR   UCSC; uc061lrc.1; human.
DR   UCSC; uc061lrk.1; human.
DR   GeneCards; IGKV1-37; -.
DR   HGNC; HGNC:5739; IGKV1-37.
DR   HPA; ENSG00000239862; Tissue enhanced (intestine, lymphoid tissue, urinary bladder).
DR   neXtProt; NX_A0A075B6S9; -.
DR   VEuPathDB; HostDB:ENSG00000239862; -.
DR   HOGENOM; CLU_077975_4_1_1; -.
DR   OMA; CQQDASF; -.
DR   PhylomeDB; A0A075B6S9; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; A0A075B6S9; protein.
DR   Bgee; ENSG00000239862; Expressed in rectum and 61 other tissues.
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; IEA:UniProtKB-SubCell.
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; Immunity; Immunoglobulin;
KW   Immunoglobulin domain; Membrane; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..117
FT                   /note="Probable non-functional immunoglobulinn kappa
FT                   variable 1-37"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5014011168"
FT   DOMAIN          24..>117
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   NON_TER         117
SQ   SEQUENCE   117 AA;  12688 MW;  F4369E8FA981DA82 CRC64;
     MDMRVPAQLL GLLLLWVPGA RCDIQLTQSP SSLSASVGDR VTITCRVSQG ISSYLNWYRQ
     KPGKVPKLLI YSASNLQSGV PSRFSGSGSG TDFTLTISSL QPEDVATYYG QRTYNAP