HV333_HUMAN
ID HV333_HUMAN Reviewed; 117 AA.
AC P01772; A0A0B4J1V3; P01771;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2016, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Immunoglobulin heavy variable 3-33 {ECO:0000303|PubMed:11340299, ECO:0000303|Ref.5};
DE AltName: Full=Ig heavy chain V-III region HIL {ECO:0000305|PubMed:420800};
DE AltName: Full=Ig heavy chain V-III region KOL {ECO:0000305|PubMed:6884994};
DE Flags: Precursor;
GN Name=IGHV3-33 {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 IGHV3-33*01).
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=420800; DOI=10.1021/bi00571a001;
RA Chiu Y.-Y.H., Lopez de Castro J.A., Poljak R.J.;
RT "Amino acid sequence of the VH region of human myeloma cryoimmunoglobulin
RT IgG Hil.";
RL Biochemistry 18:553-560(1979).
RN [3]
RP PROTEIN SEQUENCE OF 20-117, PYROGLUTAMATE FORMATION AT GLN-20, AND
RP DISULFIDE BONDS.
RX PubMed=6884994;
RA Schmidt W.E., Jung H.-D., Palm W., Hilschmann N.;
RT "Three-dimensional structure determination of antibodies. Primary structure
RT of crystallized monoclonal immunoglobulin IgG1 KOL, I.";
RL Hoppe-Seyler's Z. Physiol. Chem. 364:713-747(1983).
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).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=7441755; DOI=10.1016/0022-2836(80)90252-1;
RA Marquart M., Deisenhofer J., Huber R., Palm W.;
RT "Crystallographic refinement and atomic models of the intact immunoglobulin
RT molecule Kol and its antigen-binding fragment at 3.0 A and 1.0-A
RT resolution.";
RL J. Mol. Biol. 141:369-391(1980).
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 IGHV3-33*01. {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; A02054; G1HUHL.
DR PIR; A02055; G1HUKL.
DR PDB; 2FB4; X-ray; 1.90 A; H=21-117.
DR PDB; 2IG2; X-ray; 3.00 A; H=21-117.
DR PDB; 2RCJ; X-ray; -; A/B/E/F/I/J/M/N/Q/R=20-117.
DR PDB; 7CZT; EM; 2.70 A; H/I=20-117.
DR PDBsum; 2FB4; -.
DR PDBsum; 2IG2; -.
DR PDBsum; 2RCJ; -.
DR PDBsum; 7CZT; -.
DR AlphaFoldDB; P01772; -.
DR SMR; P01772; -.
DR MINT; P01772; -.
DR IMGT_GENE-DB; IGHV3-33; -.
DR BioMuta; IGHV3-33; -.
DR DMDM; 123851; -.
DR jPOST; P01772; -.
DR MassIVE; P01772; -.
DR PeptideAtlas; P01772; -.
DR PRIDE; P01772; -.
DR Ensembl; ENST00000390615.2; ENSP00000375024.2; ENSG00000211955.2.
DR GeneCards; IGHV3-33; -.
DR HGNC; HGNC:5596; IGHV3-33.
DR HPA; ENSG00000211955; Tissue enhanced (intestine, lymphoid tissue, stomach).
DR neXtProt; NX_P01772; -.
DR OpenTargets; ENSG00000211955; -.
DR VEuPathDB; HostDB:ENSG00000211955; -.
DR GeneTree; ENSGT01050000244871; -.
DR OMA; WIGCIST; -.
DR PhylomeDB; P01772; -.
DR PathwayCommons; P01772; -.
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; IGHV3-33; human.
DR EvolutionaryTrace; P01772; -.
DR Pharos; P01772; Tdark.
DR PRO; PR:P01772; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P01772; protein.
DR Bgee; ENSG00000211955; Expressed in duodenum and 90 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 3D-structure; 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:420800,
FT ECO:0000269|PubMed:6884994"
FT CHAIN 20..117
FT /note="Immunoglobulin heavy variable 3-33"
FT /evidence="ECO:0000269|PubMed:420800,
FT ECO:0000269|PubMed:6884994"
FT /id="PRO_0000059923"
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:420800,
FT ECO:0000269|PubMed:6884994"
FT DISULFID 41..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:6884994"
FT CONFLICT 22
FT /note="Q -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 25..26
FT /note="ES -> QA (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 42..43
FT /note="AA -> SS (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="A -> I (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="T -> I (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="S -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 52..54
FT /note="GMH -> AMY (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="V -> I (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="Y -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 76..78
FT /note="NKY -> DQH (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 76..77
FT /note="NK -> RT (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="A -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="N -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="Y -> F (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="L -> M (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="N -> D (in Ref. 3; 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. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="A -> G (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="Y -> F (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 117
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:2FB4"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:7CZT"
FT STRAND 37..46
FT /evidence="ECO:0007829|PDB:2FB4"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:2FB4"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:2FB4"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:2FB4"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:7CZT"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:2FB4"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:2FB4"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:7CZT"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:2FB4"
FT TURN 93..96
FT /evidence="ECO:0007829|PDB:2FB4"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:2FB4"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:2FB4"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:2FB4"
SQ SEQUENCE 117 AA; 13074 MW; C00B376424DC474D CRC64;
MEFGLSWVFL VALLRGVQCQ VQLVESGGGV VQPGRSLRLS CAASGFTFSS YGMHWVRQAP
GKGLEWVAVI WYDGSNKYYA DSVKGRFTIS RDNSKNTLYL QMNSLRAEDT AVYYCAR
