HV461_HUMAN
ID HV461_HUMAN Reviewed; 118 AA.
AC A0A0C4DH41;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Immunoglobulin heavy variable 4-61 {ECO:0000303|PubMed:11340299, ECO:0000303|Ref.3};
DE Flags: Precursor;
GN Name=IGHV4-61 {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 IGHV4-61*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 IGHV4-61*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; 7CZW; EM; 2.80 A; H/J=20-118.
DR PDB; 7D03; EM; 3.20 A; H=20-118.
DR PDBsum; 7CZW; -.
DR PDBsum; 7D03; -.
DR AlphaFoldDB; A0A0C4DH41; -.
DR SMR; A0A0C4DH41; -.
DR IMGT_GENE-DB; IGHV4-61; -.
DR BioMuta; IGHV4-61; -.
DR jPOST; A0A0C4DH41; -.
DR MassIVE; A0A0C4DH41; -.
DR PeptideAtlas; A0A0C4DH41; -.
DR Ensembl; ENST00000390630.3; ENSP00000375039.2; ENSG00000211970.3.
DR Ensembl; ENST00000632960.1; ENSP00000487694.1; ENSG00000282451.1.
DR GeneCards; IGHV4-61; -.
DR HGNC; HGNC:5655; IGHV4-61.
DR HPA; ENSG00000211970; Tissue enhanced (intestine, lymphoid tissue, stomach).
DR neXtProt; NX_A0A0C4DH41; -.
DR OpenTargets; ENSG00000211970; -.
DR VEuPathDB; HostDB:ENSG00000211970; -.
DR GeneTree; ENSGT01030000234536; -.
DR HOGENOM; CLU_077975_5_0_1; -.
DR OMA; CTTHAHS; -.
DR PhylomeDB; A0A0C4DH41; -.
DR ChiTaRS; IGHV4-61; human.
DR Pharos; A0A0C4DH41; Tdark.
DR PRO; PR:A0A0C4DH41; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; A0A0C4DH41; protein.
DR Bgee; ENSG00000211970; Expressed in duodenum and 91 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; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..118
FT /note="Immunoglobulin heavy variable 4-61"
FT /evidence="ECO:0000255"
FT /id="PRO_5007964481"
FT DOMAIN 20..>118
FT /note="Ig-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 41..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT NON_TER 118
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:7CZW"
FT STRAND 36..46
FT /evidence="ECO:0007829|PDB:7CZW"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:7CZW"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:7CZW"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:7CZW"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:7CZW"
FT TURN 83..87
FT /evidence="ECO:0007829|PDB:7CZW"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:7CZW"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:7CZW"
FT STRAND 98..105
FT /evidence="ECO:0007829|PDB:7CZW"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:7CZW"
FT STRAND 112..118
FT /evidence="ECO:0007829|PDB:7CZW"
SQ SEQUENCE 118 AA; 13066 MW; 351A25D958E48826 CRC64;
MKHLWFFLLL VAAPRWVLSQ VQLQESGPGL VKPSETLSLT CTVSGGSVSS GSYYWSWIRQ
PPGKGLEWIG YIYYSGSTNY NPSLKSRVTI SVDTSKNQFS LKLSSVTAAD TAVYYCAR
