HV320_HUMAN
ID HV320_HUMAN Reviewed; 117 AA.
AC A0A0C4DH32;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 2.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Immunoglobulin heavy variable 3-20 {ECO:0000303|PubMed:11340299, ECO:0000303|Ref.4};
DE Flags: Precursor;
GN Name=IGHV3-20 {ECO:0000303|PubMed:11340299, 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] (IMGT ALLELE IGHV3-20*01).
RX PubMed=8490662; DOI=10.1038/ng0193-88;
RA Matsuda F., Shin E.K., Nagaoka H., Matsumura R., Haino M., Fukita Y.,
RA Taka-ishi S., Imai T., Riley J.H., Anand R.;
RT "Structure and physical map of 64 variable segments in the 3'0.8-megabase
RT region of the human immunoglobulin heavy-chain locus.";
RL Nat. Genet. 3:88-94(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE IGHV3-20*02),
RP AND VARIANT PHE-41.
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
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: V region of the variable domain of immunoglobulin heavy
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: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 the functional IMGT allele IGHV3-20*01 that is not represented on the
CC reference genome assembly (GRCh38/hg38). The sequence of the reference
CC genome assembly (GRCh38/hg38) is that of IMGT allele IGHV3-20*02 which
CC is considered as an open reading frame (ORF), but presents a mutation
CC at position 41, corresponding to the first cysteine from the disulfide
CC bridge, potentially leading to uncorrect folding.
CC {ECO:0000305|PubMed:11340299}.
CC -!- CAUTION: For examples of full-length immunoglobulin heavy chains (of
CC different isotypes) see AC P0DOX2, AC P0DOX3, AC P0DOX4, AC P0DOX5 and
CC AC P0DOX6. {ECO:0000305}.
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DR EMBL; M99657; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC245166; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A0C4DH32; -.
DR SMR; A0A0C4DH32; -.
DR IMGT_GENE-DB; IGHV3-20; -.
DR BioMuta; IGHV3-20; -.
DR jPOST; A0A0C4DH32; -.
DR MassIVE; A0A0C4DH32; -.
DR PeptideAtlas; A0A0C4DH32; -.
DR PRIDE; A0A0C4DH32; -.
DR Ensembl; ENST00000390606.3; ENSP00000375015.2; ENSG00000211946.3.
DR Ensembl; ENST00000632076.1; ENSP00000488747.1; ENSG00000282476.1.
DR GeneCards; IGHV3-20; -.
DR HGNC; HGNC:5585; IGHV3-20.
DR HPA; ENSG00000211946; Tissue enhanced (intestine, lymphoid tissue, stomach, urinary bladder).
DR neXtProt; NX_A0A0C4DH32; -.
DR VEuPathDB; HostDB:ENSG00000211946; -.
DR HOGENOM; CLU_077975_5_2_1; -.
DR PhylomeDB; A0A0C4DH32; -.
DR SignaLink; A0A0C4DH32; -.
DR ChiTaRS; IGHV3-20; human.
DR Pharos; A0A0C4DH32; Tdark.
DR PRO; PR:A0A0C4DH32; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; A0A0C4DH32; protein.
DR Bgee; ENSG00000211946; Expressed in duodenum and 94 other tissues.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0042571; C:immunoglobulin complex, circulating; IBA:GO_Central.
DR GO; GO:0003823; F:antigen binding; IBA:GO_Central.
DR GO; GO:0034987; F:immunoglobulin receptor binding; IBA:GO_Central.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0006958; P:complement activation, classical pathway; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0006911; P:phagocytosis, engulfment; IBA:GO_Central.
DR GO; GO:0006910; P:phagocytosis, recognition; IBA:GO_Central.
DR GO; GO:0050871; P:positive regulation of B cell activation; 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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..117
FT /note="Immunoglobulin heavy variable 3-20"
FT /evidence="ECO:0000255"
FT /id="PRO_0000439566"
FT DOMAIN 20..>117
FT /note="Ig-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 41..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 41
FT /note="C -> F (in IMGT allele IGHV3-20*02)"
FT /id="VAR_077934"
FT NON_TER 117
SQ SEQUENCE 117 AA; 12673 MW; E01A807666D786E9 CRC64;
MEFGLSWVFL VAILKGVQCE VQLVESGGGV VRPGGSLRLS CAASGFTFDD YGMSWVRQAP
GKGLEWVSGI NWNGGSTGYA DSVKGRFTIS RDNAKNSLYL QMNSLRAEDT ALYHCAR
