HV307_HUMAN
ID HV307_HUMAN Reviewed; 117 AA.
AC P01780; A0A0B4J1U8; P01781; P80419;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2016, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Immunoglobulin heavy variable 3-7 {ECO:0000303|PubMed:11340299, ECO:0000303|Ref.7};
DE AltName: Full=Ig heavy chain V-III region GAL {ECO:0000305|PubMed:4803843};
DE AltName: Full=Ig heavy chain V-III region GAR {ECO:0000305|PubMed:7737190};
DE AltName: Full=Ig heavy chain V-III region JON {ECO:0000305|PubMed:4522793};
DE Flags: Precursor;
GN Name=IGHV3-7 {ECO:0000303|PubMed:11340299, ECO:0000303|Ref.7};
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 IGHV3-7*03).
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 20-117.
RX PubMed=4803843;
RA Watanabe S., Barnikol H.U., Horn J., Bertram J., Hilschmann N.;
RT "The primary structure of a monoclonal IgM-immunoglobulin (macroglobulin
RT Gal.), II: the amino acid sequence of the H-chain (mu-type), subgroup H
RT III. Architecture of the complete IgM-molecule.";
RL Hoppe-Seyler's Z. Physiol. Chem. 354:1505-1509(1973).
RN [3]
RP SEQUENCE REVISION TO 47-52.
RA Hilschmann N.;
RL Submitted (JUN-1975) to the PIR data bank.
RN [4]
RP PROTEIN SEQUENCE OF 20-117.
RX PubMed=4522793; DOI=10.1073/pnas.71.3.845;
RA Capra J.D., Kehoe J.M.;
RT "Variable region sequences of five human immunoglobulin heavy chains of the
RT VH3 subgroup: definitive identification of four heavy chain hypervariable
RT regions.";
RL Proc. Natl. Acad. Sci. U.S.A. 71:845-848(1974).
RN [5]
RP PROTEIN SEQUENCE OF 20-117.
RX PubMed=7737190; DOI=10.1111/j.1432-1033.1995.tb20336.x;
RA Stoppini M., Bellotti V., Negri A., Merlini G., Garver F., Ferri G.;
RT "Characterization of the two unique human anti-flavin monoclonal
RT immunoglobulins.";
RL Eur. J. Biochem. 228:886-893(1995).
RN [6]
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 [7]
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 [8]
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 [9]
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 [10]
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 [11]
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 IGHV3-7*03. {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; A02063; G3HUJN.
DR PIR; A02064; M3HUGL.
DR PIR; S69132; S69132.
DR PDB; 2FL5; X-ray; 3.00 A; B/D/F/H=20-117.
DR PDBsum; 2FL5; -.
DR AlphaFoldDB; P01780; -.
DR SMR; P01780; -.
DR IntAct; P01780; 1.
DR IMGT_GENE-DB; IGHV3-7; -.
DR BioMuta; IGHV3-7; -.
DR DMDM; 123859; -.
DR jPOST; P01780; -.
DR MassIVE; P01780; -.
DR PeptideAtlas; P01780; -.
DR PRIDE; P01780; -.
DR Ensembl; ENST00000390598.2; ENSP00000375007.2; ENSG00000211938.2.
DR Ensembl; ENST00000633988.1; ENSP00000487659.1; ENSG00000282211.1.
DR GeneCards; IGHV3-7; -.
DR HGNC; HGNC:5620; IGHV3-7.
DR HPA; ENSG00000211938; Tissue enhanced (intestine, lymphoid tissue).
DR neXtProt; NX_P01780; -.
DR OpenTargets; ENSG00000211938; -.
DR VEuPathDB; HostDB:ENSG00000211938; -.
DR GeneTree; ENSGT01050000244871; -.
DR OMA; YCARATA; -.
DR PhylomeDB; P01780; -.
DR PathwayCommons; P01780; -.
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; P01780; -.
DR ChiTaRS; IGHV3-7; human.
DR Pharos; P01780; Tdark.
DR PRO; PR:P01780; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P01780; protein.
DR Bgee; ENSG00000211938; Expressed in duodenum and 90 other tissues.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
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 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..19
FT /evidence="ECO:0000269|PubMed:4522793,
FT ECO:0000269|PubMed:4803843, ECO:0000269|PubMed:7737190"
FT CHAIN 20..117
FT /note="Immunoglobulin heavy variable 3-7"
FT /evidence="ECO:0000269|PubMed:4522793,
FT ECO:0000269|PubMed:4803843, ECO:0000269|PubMed:7737190"
FT /id="PRO_0000059931"
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 CONFLICT 20
FT /note="E -> D (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="G -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="Q -> K (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="G -> E (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="G -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="R -> K (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="A -> T (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 47..54
FT /note="TFSSYWMS -> BFBBLGMT (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 47..54
FT /note="TFSSYWMS -> SYSNYVMT (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 50..51
FT /note="SY -> TA (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="S -> K (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 68..75
FT /note="ANIKQDGS -> VWRVEQVV (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="A -> T (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 71..75
FT /note="KQDGS -> RPDET (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 77..78
FT /note="KY -> ZB (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 78..81
FT /note="YYVD -> AFAN (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 78..80
FT /note="YYV -> FYS (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 84..85
FT /note="Missing (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="K -> N (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="I -> V (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 92..94
FT /note="DNA -> NDS (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="K -> R (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="S -> T (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 98..107
FT /note="LYLQMNSLRA -> VSNSMFLQRV (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 103..107
FT /note="NSLRA -> ISVTP (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="A -> V (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="V -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="V -> T (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 117
SQ SEQUENCE 117 AA; 12943 MW; 32001F95FCA6C2FC CRC64;
MELGLSWVFL VAILEGVQCE VQLVESGGGL VQPGGSLRLS CAASGFTFSS YWMSWVRQAP
GKGLEWVANI KQDGSEKYYV DSVKGRFTIS RDNAKNSLYL QMNSLRAEDT AVYYCAR
