HV330_HUMAN
ID HV330_HUMAN Reviewed; 117 AA.
AC P01768; A0A0B4J2B7; P01769; P01770; P01773;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2016, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Immunoglobulin heavy variable 3-30 {ECO:0000303|PubMed:11340299, ECO:0000303|Ref.8};
DE AltName: Full=Ig heavy chain V-III region BUR {ECO:0000305|PubMed:107164};
DE AltName: Full=Ig heavy chain V-III region CAM {ECO:0000305|PubMed:6774332};
DE AltName: Full=Ig heavy chain V-III region GA {ECO:0000305|PubMed:4208843};
DE AltName: Full=Ig heavy chain V-III region NIE {ECO:0000305|PubMed:826475};
DE Flags: Precursor;
GN Name=IGHV3-30 {ECO:0000303|PubMed:11340299, ECO:0000303|Ref.8};
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 IGHV3-30*18).
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, AND PYROGLUTAMATE FORMATION AT GLN-20.
RX PubMed=4208843; DOI=10.1021/bi00709a004;
RA Florent G., Lehman D., Putnam F.W.;
RT "The switch point in mu heavy chains of human IgM immunoglobulins.";
RL Biochemistry 13:2482-2498(1974).
RN [3]
RP PROTEIN SEQUENCE OF 20-117, AND PYROGLUTAMATE FORMATION AT GLN-20.
RX PubMed=826475;
RA Ponstingl H., Hilschmann N.;
RT "The rule of antibody structure. The primary structure of a monoclonal IgG1
RT immunoglobulin (myeloma protein Nie). III. The chymotryptic peptides of the
RT H-chain, alignment of the tryptic peptides and discussion of the complete
RT structure.";
RL Hoppe-Seyler's Z. Physiol. Chem. 357:1571-1604(1976).
RN [4]
RP PROTEIN SEQUENCE OF 20-117, AND PYROGLUTAMATE FORMATION AT GLN-20.
RX PubMed=107164; DOI=10.1016/s0021-9258(17)30153-9;
RA Putnam F.W., Liu Y.-S.V., Low T.L.K.;
RT "Primary structure of a human IgA1 immunoglobulin. IV. Streptococcal IgA1
RT protease, digestion, Fab and Fc fragments, and the complete amino acid
RT sequence of the alpha 1 heavy chain.";
RL J. Biol. Chem. 254:2865-2874(1979).
RN [5]
RP PROTEIN SEQUENCE OF 20-117, AND PYROGLUTAMATE FORMATION AT GLN-20.
RX PubMed=6774332; DOI=10.1073/pnas.77.6.3239;
RA Lehman D.W., Putnam F.W.;
RT "Amino acid sequence of the variable region of a human mu chain: location
RT of a possible JH segment.";
RL Proc. Natl. Acad. Sci. U.S.A. 77:3239-3243(1980).
RN [6]
RP DISULFIDE BOND.
RX PubMed=1002129;
RA Dreker L., Schwarz J., Reichel W., Hilschmann N.;
RT "Rule of antibody structure. The primary structure of a monoclonal IgG1
RT immunoglobulin (myeloma protein Nie), I: purification and characterization
RT of the protein, the L- and H-chains, the cyanogen bromide cleavage
RT products, and the disulfide bridges.";
RL Hoppe-Seyler's Z. Physiol. Chem. 357:1515-1540(1976).
RN [7]
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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
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 IGHV3-30*18. {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; AC245166; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A02051; M3HUAM.
DR PIR; A02052; M3HUGA.
DR PIR; A02056; A1HUBR.
DR PIR; A91668; G1HUNI.
DR AlphaFoldDB; P01768; -.
DR SMR; P01768; -.
DR DrugBank; DB08396; 4-{[(Z)-(5-oxo-2-phenyl-1,3-oxazol-4(5H)-ylidene)methyl]amino}butanoic acid.
DR DrugBank; DB08635; N-(TRANS-4'-NITRO-4-STILBENYL)-N-METHYL-5-AMINO-PENTANOIC ACID.
DR IMGT_GENE-DB; IGHV3-30; -.
DR BioMuta; IGHV3-30; -.
DR DMDM; 123848; -.
DR jPOST; P01768; -.
DR MassIVE; P01768; -.
DR PeptideAtlas; P01768; -.
DR PRIDE; P01768; -.
DR Ensembl; ENST00000603660.1; ENSP00000474524.1; ENSG00000270550.1.
DR Ensembl; ENST00000633400.1; ENSP00000488205.1; ENSG00000282777.1.
DR GeneCards; IGHV3-30; -.
DR HGNC; HGNC:5591; IGHV3-30.
DR HPA; ENSG00000270550; Group enriched (intestine, lymphoid tissue, salivary gland, stomach, urinary bladder).
DR neXtProt; NX_P01768; -.
DR OpenTargets; ENSG00000270550; -.
DR VEuPathDB; HostDB:ENSG00000270550; -.
DR OMA; CARDTEC; -.
DR PhylomeDB; P01768; -.
DR PathwayCommons; P01768; -.
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; IGHV3-30; human.
DR Pharos; P01768; Tdark.
DR PRO; PR:P01768; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P01768; protein.
DR Bgee; ENSG00000270550; Expressed in duodenum and 90 other tissues.
DR ExpressionAtlas; P01768; baseline and differential.
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:0005615; C:extracellular space; HDA:UniProtKB.
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:107164,
FT ECO:0000269|PubMed:4208843, ECO:0000269|PubMed:6774332,
FT ECO:0000269|PubMed:826475"
FT CHAIN 20..117
FT /note="Immunoglobulin heavy variable 3-30"
FT /evidence="ECO:0000269|PubMed:107164,
FT ECO:0000269|PubMed:4208843, ECO:0000269|PubMed:6774332,
FT ECO:0000269|PubMed:826475"
FT /id="PRO_0000059919"
FT DOMAIN 20..>117
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:107164,
FT ECO:0000269|PubMed:4208843, ECO:0000269|PubMed:6774332,
FT ECO:0000269|PubMed:826475"
FT DISULFID 41..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:1002129"
FT CONFLICT 22
FT /note="Q -> E (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 25
FT /note="E -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="V -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 33..35
FT /note="PGR -> AGT (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="A -> T (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 45..50
FT /note="GFTFSS -> AFNLSD (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="T -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 50..53
FT /note="SYGM -> RYTI (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="S -> N (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="S -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="G -> A (in Ref. 2; AA sequence, 5; AA sequence and
FT 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="A -> P (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 67..68
FT /note="VA -> LS (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="V -> L (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="I -> M (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="D -> G (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="S -> B (in Ref. 2; AA sequence, 5; AA sequence and
FT 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="K -> T (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="K -> Z (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="Y -> H (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="D -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="K -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="K -> R (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 92..93
FT /note="DN -> ND (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="N -> I (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="L -> M (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="Q -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="Q -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 103..104
FT /note="NS -> KT (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="A -> P (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="A -> T (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="K -> R (in Ref. 5; AA sequence, 2; AA sequence and
FT 3; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 117
SQ SEQUENCE 117 AA; 12947 MW; CA8AF76424DC4208 CRC64;
MEFGLSWVFL VALLRGVQCQ VQLVESGGGV VQPGRSLRLS CAASGFTFSS YGMHWVRQAP
GKGLEWVAVI SYDGSNKYYA DSVKGRFTIS RDNSKNTLYL QMNSLRAEDT AVYYCAK
