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   16-JAN-2019, entry version 28.
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;
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   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.,
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   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   [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.
RL   (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
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 IGHV1-69D*01. {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}.
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DR   EMBL; AC245369; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PDB; 5WKZ; X-ray; 1.85 A; H=20-117.
DR   PDBsum; 5WKZ; -.
DR   ProteinModelPortal; A0A0B4J2H0; -.
DR   SMR; A0A0B4J2H0; -.
DR   IMGT_GENE-DB; IGHV1-69D; -.
DR   BioMuta; HGNC:49601; -.
DR   EPD; A0A0B4J2H0; -.
DR   jPOST; A0A0B4J2H0; -.
DR   Ensembl; ENST00000624687; ENSP00000485152; ENSG00000280411.
DR   Ensembl; ENST00000633446; ENSP00000488097; ENSG00000282399.
DR   EuPathDB; HostDB:ENSG00000280411.1; -.
DR   GeneCards; IGHV1-69D; -.
DR   HGNC; HGNC:49601; IGHV1-69D.
DR   neXtProt; NX_A0A0B4J2H0; -.
DR   OpenTargets; ENSG00000280411; -.
DR   GeneTree; ENSGT00940000153088; -.
DR   OMA; NTGGTEY; -.
DR   PRO; PR:A0A0B4J2H0; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   Bgee; ENSG00000280411; Expressed in 80 organ(s), highest expression level in lymph node.
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; Complete proteome;
KW   Disulfide bond; Immunity; Immunoglobulin domain;
KW   Immunoglobulin V region; Membrane; Polymorphism;
KW   Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   CHAIN        20    117       Immunoglobulin heavy variable 1-69D.
FT                                {ECO:0000255}.
FT                                /FTId=PRO_0000439568.
FT   DOMAIN       20   >117       Ig-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00114}.
FT   MOD_RES      20     20       Pyrrolidone carboxylic acid.
FT                                {ECO:0000250|UniProtKB:P01742}.
FT   DISULFID     41    115       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   NON_TER     117    117
FT   STRAND       22     25       {ECO:0000244|PDB:5WKZ}.
FT   STRAND       29     31       {ECO:0000244|PDB:5WKZ}.
FT   STRAND       37     44       {ECO:0000244|PDB:5WKZ}.
FT   STRAND       53     58       {ECO:0000244|PDB:5WKZ}.
FT   STRAND       64     71       {ECO:0000244|PDB:5WKZ}.
FT   HELIX        72     74       {ECO:0000244|PDB:5WKZ}.
FT   STRAND       76     79       {ECO:0000244|PDB:5WKZ}.
FT   HELIX        81     83       {ECO:0000244|PDB:5WKZ}.
FT   TURN         84     86       {ECO:0000244|PDB:5WKZ}.
FT   STRAND       87     92       {ECO:0000244|PDB:5WKZ}.
FT   TURN         93     96       {ECO:0000244|PDB:5WKZ}.
FT   STRAND       97    102       {ECO:0000244|PDB:5WKZ}.
FT   HELIX       107    109       {ECO:0000244|PDB:5WKZ}.
FT   STRAND      111    117       {ECO:0000244|PDB:5WKZ}.
SQ   SEQUENCE   117 AA;  12660 MW;  8787F1D4910590DD CRC64;
     MDWTWRFLFV VAAATGVQSQ VQLVQSGAEV KKPGSSVKVS CKASGGTFSS YAISWVRQAP
     GQGLEWMGGI IPIFGTANYA QKFQGRVTIT ADESTSTAYM ELSSLRSEDT AVYYCAR
//