HV205_HUMAN
ID HV205_HUMAN Reviewed; 119 AA.
AC P01817; A0A0A0MS10; P01818;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 07-SEP-2016, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Immunoglobulin heavy variable 2-5 {ECO:0000303|PubMed:11340299, ECO:0000303|Ref.5};
DE AltName: Full=Ig heavy chain V-II region HE {ECO:0000305|PubMed:5264153};
DE AltName: Full=Ig heavy chain V-II region MCE {ECO:0000305|PubMed:6780622};
DE Flags: Precursor;
GN Name=IGHV2-5 {ECO:0000303|PubMed:11340299, ECO:0000303|Ref.5};
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 IGHV2-5*02).
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 [2]
RP PROTEIN SEQUENCE OF 20-119, AND PYROGLUTAMATE FORMATION AT GLN-20.
RX PubMed=5264153; DOI=10.1073/pnas.64.3.997;
RA Cunningham B.A., Pflumm M.N., Rutishauser U., Edelman G.M.;
RT "Subgroups of amino acid sequences in the variable regions of
RT immunoglobulin heavy chains.";
RL Proc. Natl. Acad. Sci. U.S.A. 64:997-1003(1969).
RN [3]
RP PROTEIN SEQUENCE OF 20-119, AND PYROGLUTAMATE FORMATION AT GLN-20.
RX PubMed=6780622;
RA Gerber-Jenson B., Kazin A., Kehoe J.M., Scheffel C., Erickson B.W.,
RA Litman G.W.;
RT "Molecular basis for the temperature-dependent insolubility of
RT cryoglobulins. X. The amino acid sequence of the heavy chain variable
RT region of McE.";
RL J. Immunol. 126:1212-1216(1981).
RN [4]
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 [5]
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 [6]
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 [7]
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 [8]
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 [9]
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 IMGT allele IGHV2-5*02. {ECO:0000305}.
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; AC244226; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A02092; MHHUMC.
DR PIR; A02093; G1HUHE.
DR AlphaFoldDB; P01817; -.
DR SMR; P01817; -.
DR IMGT_GENE-DB; IGHV2-5; -.
DR BioMuta; IGHV2-5; -.
DR DMDM; 123825; -.
DR MassIVE; P01817; -.
DR PeptideAtlas; P01817; -.
DR PRIDE; P01817; -.
DR Ensembl; ENST00000390597.3; ENSP00000375006.2; ENSG00000211937.3.
DR Ensembl; ENST00000560724.3; ENSP00000473889.3; ENSG00000277318.2.
DR UCSC; uc059gfq.1; human.
DR GeneCards; IGHV2-5; -.
DR HGNC; HGNC:5576; IGHV2-5.
DR HPA; ENSG00000211937; Tissue enhanced (intestine, lymphoid tissue, stomach).
DR neXtProt; NX_P01817; -.
DR OpenTargets; ENSG00000211937; -.
DR VEuPathDB; HostDB:ENSG00000211937; -.
DR GeneTree; ENSGT01030000234536; -.
DR OMA; WPSAVTI; -.
DR PhylomeDB; P01817; -.
DR PathwayCommons; P01817; -.
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 ChiTaRS; IGHV2-5; human.
DR Pharos; P01817; Tdark.
DR PRO; PR:P01817; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P01817; protein.
DR Bgee; ENSG00000211937; Expressed in rectum and 86 other tissues.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0042571; C:immunoglobulin complex, circulating; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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:0006955; P:immune response; NAS:UniProtKB.
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 1: Evidence at protein level;
KW Adaptive immunity; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Immunity; Immunoglobulin; Immunoglobulin domain; Membrane;
KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:5264153,
FT ECO:0000269|PubMed:6780622"
FT CHAIN 20..119
FT /note="Immunoglobulin heavy variable 2-5"
FT /evidence="ECO:0000269|PubMed:5264153,
FT ECO:0000269|PubMed:6780622"
FT /id="PRO_0000059910"
FT DOMAIN 20..>119
FT /note="Ig-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT MOD_RES 20
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:5264153,
FT ECO:0000269|PubMed:6780622"
FT DISULFID 41..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 21..26
FT /note="ITLKES -> VTLKEN (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="Q -> E (in Ref. 3; AA sequence and 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 43..54
FT /note="FSGFSLSTSGVG -> LSGLSLTTDGVA (in Ref. 2; AA
FT sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 61..64
FT /note="PPGK -> GPGR (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="P -> R (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 71..78
FT /note="LIYWDDDK -> FINWDDDN (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 71..72
FT /note="LI -> WLL (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="Y -> F (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="K -> R (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 90..92
FT /note="ITK -> VTR (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="I -> G (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="K -> R (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="M -> I (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="A -> V (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 119
SQ SEQUENCE 119 AA; 13231 MW; 7403E23CE450BA92 CRC64;
MDTLCSTLLL LTIPSWVLSQ ITLKESGPTL VKPTQTLTLT CTFSGFSLST SGVGVGWIRQ
PPGKALEWLA LIYWDDDKRY SPSLKSRLTI TKDTSKNQVV LTMTNMDPVD TATYYCAHR
