HV69D_HUMAN
ID HV69D_HUMAN Reviewed; 117 AA.
AC A0A0B4J2H0;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Immunoglobulin heavy variable 1-69D {ECO:0000303|PubMed:11340299, ECO:0000303|Ref.3};
DE Flags: Precursor;
GN Name=IGHV1-69D {ECO:0000303|PubMed:11340299, ECO:0000303|Ref.3};
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 IGHV1-69D*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 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 [3]
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 [4]
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 [5]
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 [6]
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 [7]
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 IGHV1-69D*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; AC245369; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PDB; 5C2B; X-ray; 1.40 A; H=20-117.
DR PDB; 5C6W; X-ray; 1.54 A; H/J=20-117.
DR PDB; 5CBA; X-ray; 2.50 A; A/C=20-117.
DR PDB; 5CBE; X-ray; 2.40 A; A/C=20-117.
DR PDB; 5WKZ; X-ray; 1.85 A; H=20-117.
DR PDBsum; 5C2B; -.
DR PDBsum; 5C6W; -.
DR PDBsum; 5CBA; -.
DR PDBsum; 5CBE; -.
DR PDBsum; 5WKZ; -.
DR AlphaFoldDB; A0A0B4J2H0; -.
DR SMR; A0A0B4J2H0; -.
DR IMGT_GENE-DB; IGHV1-69D; -.
DR BioMuta; HGNC:49601; -.
DR jPOST; A0A0B4J2H0; -.
DR MassIVE; A0A0B4J2H0; -.
DR PeptideAtlas; A0A0B4J2H0; -.
DR Ensembl; ENST00000624687.1; ENSP00000485152.1; ENSG00000280411.1.
DR Ensembl; ENST00000633446.1; ENSP00000488097.1; ENSG00000282399.1.
DR GeneCards; IGHV1-69D; -.
DR HGNC; HGNC:49601; IGHV1-69D.
DR HPA; ENSG00000280411; Tissue enhanced (lymphoid tissue, stomach).
DR neXtProt; NX_A0A0B4J2H0; -.
DR OpenTargets; ENSG00000280411; -.
DR VEuPathDB; HostDB:ENSG00000280411; -.
DR GeneTree; ENSGT00950000183013; -.
DR HOGENOM; CLU_077975_5_2_1; -.
DR OMA; IYAISWV; -.
DR ChiTaRS; IGHV1-69D; human.
DR Pharos; A0A0B4J2H0; Tdark.
DR PRO; PR:A0A0B4J2H0; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; A0A0B4J2H0; protein.
DR Bgee; ENSG00000280411; Expressed in vermiform appendix and 86 other tissues.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0042571; C:immunoglobulin complex, circulating; IBA:GO_Central.
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: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; Disulfide bond; Immunity;
KW Immunoglobulin; Immunoglobulin domain; Membrane;
KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..117
FT /note="Immunoglobulin heavy variable 1-69D"
FT /evidence="ECO:0000255"
FT /id="PRO_0000439568"
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:0000250|UniProtKB:P01742"
FT DISULFID 41..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT NON_TER 117
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:5C2B"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:5C2B"
FT STRAND 37..45
FT /evidence="ECO:0007829|PDB:5C2B"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:5C2B"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:5C2B"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:5C2B"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:5C2B"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:5C2B"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:5C2B"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:5C2B"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:5C2B"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:5C2B"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:5C2B"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:5C2B"
SQ SEQUENCE 117 AA; 12660 MW; 8787F1D4910590DD CRC64;
MDWTWRFLFV VAAATGVQSQ VQLVQSGAEV KKPGSSVKVS CKASGGTFSS YAISWVRQAP
GQGLEWMGGI IPIFGTANYA QKFQGRVTIT ADESTSTAYM ELSSLRSEDT AVYYCAR
