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 16-JAN-2019, entry version 101. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE RP 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., RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., RA 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., RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., RA Quetier F., 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 RT (macroglobulin Gal.), II: the amino acid sequence of the H-chain (mu- RT type), subgroup H 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 RT of the VH3 subgroup: definitive identification of four heavy chain RT hypervariable 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; 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. RL (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 RT Rise 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 CC (PubMed:24600447). Immunoglobulins, also known as antibodies, are CC membrane-bound or secreted glycoproteins produced by B CC lymphocytes. In the recognition phase of humoral immunity, the CC membrane-bound immunoglobulins serve as receptors which, upon CC binding of a specific antigen, trigger the clonal expansion and CC differentiation of B lymphocytes into immunoglobulins-secreting CC plasma cells. Secreted immunoglobulins mediate the effector phase CC of humoral immunity, which results in the elimination of bound CC antigens (PubMed:22158414, PubMed:20176268). The antigen binding CC site is formed by the variable domain of one heavy chain, together CC with that of its associated light chain. Thus, each immunoglobulin CC has two antigen binding sites with remarkable affinity for a CC particular antigen. The variable domains are assembled by a CC process called V-(D)-J rearrangement and can then be subjected to CC somatic hypermutations which, after exposure to antigen and CC selection, allow affinity maturation for a particular antigen CC (PubMed:20176268, PubMed:17576170). {ECO:0000303|PubMed:17576170, CC ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414, CC ECO:0000303|PubMed:24600447}. CC -!- SUBUNIT: Immunoglobulins are composed of two identical heavy CC chains and 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 CC that of IMGT allele IGHV3-7*03. {ECO:0000305}. CC -!- CAUTION: For examples of full-length immunoglobulin heavy chains CC (of different isotypes) see AC P0DOX2, AC P0DOX3, AC P0DOX4, AC CC P0DOX5 and AC P0DOX6. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- 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 ProteinModelPortal; 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 PeptideAtlas; P01780; -. DR PRIDE; P01780; -. DR ProteomicsDB; 51479; -. DR ProteomicsDB; 51480; -. DR ProteomicsDB; 57684; -. DR Ensembl; ENST00000390598; ENSP00000375007; ENSG00000211938. DR Ensembl; ENST00000633988; ENSP00000487659; ENSG00000282211. DR DisGeNET; 28452; -. DR EuPathDB; HostDB:ENSG00000211938.2; -. DR GeneCards; IGHV3-7; -. DR HGNC; HGNC:5620; IGHV3-7. DR neXtProt; NX_P01780; -. DR OpenTargets; ENSG00000211938; -. DR GeneTree; ENSGT00940000153134; -. DR HOVERGEN; HBG018013; -. DR OMA; WVANIKQ; -. DR PhylomeDB; 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-977606; Regulation of Complement cascade. DR Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers. DR ChiTaRS; IGHV3-7; human. DR PRO; PR:P01780; -. DR Proteomes; UP000005640; Chromosome 14. DR Bgee; ENSG00000211938; Expressed in 126 organ(s), highest expression level in lymph node. 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:0004252; F:serine-type endopeptidase activity; TAS:Reactome. DR GO; GO:0050853; P:B cell receptor signaling pathway; IBA:GO_Central. DR GO; GO:0006956; P:complement activation; TAS:Reactome. 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:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome. DR GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome. DR GO; GO:0006955; P:immune response; NAS:UniProtKB. DR GO; GO:0045087; P:innate immune response; IBA:GO_Central. DR GO; GO:0050900; P:leukocyte migration; TAS:Reactome. 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 GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome. DR GO; GO:0030449; P:regulation of complement activation; TAS:Reactome. DR GO; GO:0050776; P:regulation of immune response; TAS:Reactome. 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; Complete proteome; KW Direct protein sequencing; Disulfide bond; Immunity; KW Immunoglobulin domain; Immunoglobulin V region; Membrane; KW Polymorphism; Reference proteome; Secreted; Signal. FT SIGNAL 1 19 {ECO:0000269|PubMed:4522793, FT ECO:0000269|PubMed:4803843, FT ECO:0000269|PubMed:7737190}. FT CHAIN 20 117 Immunoglobulin heavy variable 3-7. FT {ECO:0000269|PubMed:4522793, FT ECO:0000269|PubMed:4803843, FT ECO:0000269|PubMed:7737190}. FT /FTId=PRO_0000059931. FT DOMAIN 20 >117 Ig-like. {ECO:0000255|PROSITE- FT ProRule:PRU00114}. FT DISULFID 41 115 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT CONFLICT 20 20 E -> D (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 29 29 G -> D (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 32 32 Q -> K (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 35 35 G -> E (in Ref. 5; AA sequence). FT {ECO:0000305}. FT CONFLICT 35 35 G -> R (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 38 38 R -> K (in Ref. 5; AA sequence). FT {ECO:0000305}. FT CONFLICT 42 42 A -> T (in Ref. 5; AA sequence). FT {ECO:0000305}. FT CONFLICT 47 54 TFSSYWMS -> BFBBLGMT (in Ref. 2; AA FT sequence). {ECO:0000305}. FT CONFLICT 47 54 TFSSYWMS -> SYSNYVMT (in Ref. 5; AA FT sequence). {ECO:0000305}. FT CONFLICT 50 51 SY -> TA (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 54 54 S -> K (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 68 75 ANIKQDGS -> VWRVEQVV (in Ref. 4; AA FT sequence). {ECO:0000305}. FT CONFLICT 68 68 A -> T (in Ref. 5; AA sequence). FT {ECO:0000305}. FT CONFLICT 71 75 KQDGS -> RPDET (in Ref. 5; AA sequence). FT {ECO:0000305}. FT CONFLICT 77 78 KY -> ZB (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 78 81 YYVD -> AFAN (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 78 80 YYV -> FYS (in Ref. 5; AA sequence). FT {ECO:0000305}. FT CONFLICT 84 85 Missing (in Ref. 5; AA sequence). FT {ECO:0000305}. FT CONFLICT 84 84 K -> N (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 89 89 I -> V (in Ref. 5; AA sequence). FT {ECO:0000305}. FT CONFLICT 92 94 DNA -> NDS (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 95 95 K -> R (in Ref. 5; AA sequence). FT {ECO:0000305}. FT CONFLICT 97 97 S -> T (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 98 107 LYLQMNSLRA -> VSNSMFLQRV (in Ref. 5; AA FT sequence). {ECO:0000305}. FT CONFLICT 103 107 NSLRA -> ISVTP (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 107 107 A -> V (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 112 112 V -> L (in Ref. 2; AA sequence). FT {ECO:0000305}. FT CONFLICT 112 112 V -> T (in Ref. 5; AA sequence). FT {ECO:0000305}. FT NON_TER 117 117 SQ SEQUENCE 117 AA; 12943 MW; 32001F95FCA6C2FC CRC64; MELGLSWVFL VAILEGVQCE VQLVESGGGL VQPGGSLRLS CAASGFTFSS YWMSWVRQAP GKGLEWVANI KQDGSEKYYV DSVKGRFTIS RDNAKNSLYL QMNSLRAEDT AVYYCAR //