HV323_HUMAN
ID HV323_HUMAN Reviewed; 117 AA.
AC P01764; A0A087WSX3; P01765; P01774; P01775; P01776; P01777; P01778; P01779;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2015, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Immunoglobulin heavy variable 3-23 {ECO:0000303|PubMed:11340299, ECO:0000303|Ref.8};
DE AltName: Full=Ig heavy chain V-III region LAY {ECO:0000305|PubMed:4139708};
DE AltName: Full=Ig heavy chain V-III region POM {ECO:0000305|PubMed:4139708};
DE AltName: Full=Ig heavy chain V-III region TEI {ECO:0000305|PubMed:4522793};
DE AltName: Full=Ig heavy chain V-III region TIL {ECO:0000305|PubMed:409716};
DE AltName: Full=Ig heavy chain V-III region TUR {ECO:0000305|PubMed:4522793};
DE AltName: Full=Ig heavy chain V-III region VH26 {ECO:0000305|PubMed:6450418};
DE AltName: Full=Ig heavy chain V-III region WAS {ECO:0000305|PubMed:4522793};
DE AltName: Full=Ig heavy chain V-III region ZAP {ECO:0000305|PubMed:4522793};
DE Flags: Precursor;
GN Name=IGHV3-23 {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 [GENOMIC DNA] (IMGT ALLELE IGHV3-23*02), AND VARIANTS
RP LEU-24 AND GLY-80.
RX PubMed=6450418; DOI=10.1073/pnas.77.11.6561;
RA Matthyssens G., Rabbitts T.H.;
RT "Structure and multiplicity of genes for the human immunoglobulin heavy
RT chain variable region.";
RL Proc. Natl. Acad. Sci. U.S.A. 77:6561-6565(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE IGHV3-23*04).
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 [3]
RP PROTEIN SEQUENCE OF 20-117, AND VARIANT LEU-24.
RX PubMed=4522793; DOI=10.1073/pnas.71.3.845;
RA Capra J.D., Kehoe J.M.;
RT "Variable region sequences of five human immunoglobulin heavy chains of the
RT VH3 subgroup: definitive identification of four heavy chain hypervariable
RT regions.";
RL Proc. Natl. Acad. Sci. U.S.A. 71:845-848(1974).
RN [4]
RP PROTEIN SEQUENCE OF 20-117, AND VARIANT LEU-24.
RX PubMed=4139708; DOI=10.1073/pnas.71.10.4032;
RA Capra J.D., Kehoe J.M.;
RT "Structure of antibodies with shared idiotypy: the complete sequence of the
RT heavy chain variable regions of two immunoglobulin M anti-gamma
RT globulins.";
RL Proc. Natl. Acad. Sci. U.S.A. 71:4032-4036(1974).
RN [5]
RP PROTEIN SEQUENCE OF 20-117, AND VARIANT LEU-24.
RX PubMed=409716; DOI=10.1016/s0021-9258(19)66954-1;
RA Wang A.-C., Wang I.Y., Fudenberg H.H.;
RT "Immunoglobulin structure and genetics. Identity between variable regions
RT of a mu and a gamma2 chain.";
RL J. Biol. Chem. 252:7192-7199(1977).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-117.
RX PubMed=7681398; DOI=10.1002/eji.1830230412;
RA Mariette X., Tsapis A., Brouet J.C.;
RT "Nucleotidic sequence analysis of the variable domains of four human
RT monoclonal IgM with an antibody activity to myelin-associated
RT glycoprotein.";
RL Eur. J. Immunol. 23:846-851(1993).
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).
RN [13]
RP 3D-STRUCTURE MODELING OF 20-117.
RX PubMed=3866244; DOI=10.1073/pnas.82.24.8624;
RA Toyonaga B., Yoshikai Y., Vadasz V., Chin B., Mak T.W.;
RT "Organization and sequences of the diversity, joining, and constant region
RT genes of the human T-cell receptor beta chain.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:8624-8628(1985).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 20-116, AND DISULFIDE BONDS.
RX PubMed=15033359; DOI=10.1016/j.jmb.2004.02.013;
RA Jespers L., Schon O., James L.C., Veprintsev D., Winter G.;
RT "Crystal structure of HEL4, a soluble, refoldable human V(H) single domain
RT with a germ-line scaffold.";
RL J. Mol. Biol. 337:893-903(2004).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 20-116, AND DISULFIDE BONDS.
RX PubMed=24892548; DOI=10.1371/journal.pone.0098178;
RA Kim D.S., Song H.N., Nam H.J., Kim S.G., Park Y.S., Park J.C., Woo E.J.,
RA Lim H.K.;
RT "Directed evolution of human heavy chain variable domain (VH) using in vivo
RT protein fitness filter.";
RL PLoS ONE 9:E98178-E98192(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 IGHV3-23*04. {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; M35415; AAA58735.1; -; Genomic_DNA.
DR EMBL; AC245166; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A02047; H3HU26.
DR PIR; A02048; H3HUTL.
DR PIR; A02057; M3HUPM.
DR PIR; A02058; M3HULY.
DR PIR; A02059; G1HUWS.
DR PIR; A02060; G1HUTE.
DR PIR; A02061; A1HUZP.
DR PIR; A02062; A1HUTU.
DR PDB; 1OHQ; X-ray; 2.00 A; A/B=20-116.
DR PDB; 3BN9; X-ray; 2.17 A; D/F=21-116.
DR PDB; 3UPC; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J=22-117.
DR PDB; 3ZHD; X-ray; 1.96 A; A/B=20-116.
DR PDB; 3ZHK; X-ray; 1.96 A; A/B=20-116.
DR PDB; 3ZHL; X-ray; 2.47 A; A=20-116.
DR PDB; 4KFZ; X-ray; 2.80 A; C/D=20-116.
DR PDBsum; 1OHQ; -.
DR PDBsum; 3BN9; -.
DR PDBsum; 3UPC; -.
DR PDBsum; 3ZHD; -.
DR PDBsum; 3ZHK; -.
DR PDBsum; 3ZHL; -.
DR PDBsum; 4KFZ; -.
DR AlphaFoldDB; P01764; -.
DR SMR; P01764; -.
DR IntAct; P01764; 2.
DR DrugBank; DB04147; Dodecyldimethylamine N-oxide.
DR IMGT_GENE-DB; IGHV3-23; -.
DR BioMuta; IGHV3-23; -.
DR DMDM; 123854; -.
DR jPOST; P01764; -.
DR MassIVE; P01764; -.
DR PeptideAtlas; P01764; -.
DR PRIDE; P01764; -.
DR Ensembl; ENST00000390609.3; ENSP00000375018.2; ENSG00000211949.3.
DR Ensembl; ENST00000632630.1; ENSP00000487761.1; ENSG00000281962.1.
DR UCSC; uc059gga.1; human.
DR GeneCards; IGHV3-23; -.
DR HGNC; HGNC:5588; IGHV3-23.
DR HPA; ENSG00000211949; Tissue enhanced (intestine, lymphoid tissue).
DR neXtProt; NX_P01764; -.
DR OpenTargets; ENSG00000211949; -.
DR VEuPathDB; HostDB:ENSG00000211949; -.
DR GeneTree; ENSGT01050000244871; -.
DR InParanoid; P01764; -.
DR OMA; YCARRTD; -.
DR PhylomeDB; P01764; -.
DR PathwayCommons; P01764; -.
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 SignaLink; P01764; -.
DR ChiTaRS; IGHV3-23; human.
DR EvolutionaryTrace; P01764; -.
DR Pharos; P01764; Tdark.
DR PRO; PR:P01764; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P01764; protein.
DR Bgee; ENSG00000211949; Expressed in duodenum and 94 other tissues.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
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 3D-structure; Adaptive immunity; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Immunity; Immunoglobulin; Immunoglobulin domain; Membrane;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:409716,
FT ECO:0000269|PubMed:4139708, ECO:0000269|PubMed:4522793"
FT CHAIN 20..117
FT /note="Immunoglobulin heavy variable 3-23"
FT /evidence="ECO:0000269|PubMed:409716,
FT ECO:0000269|PubMed:4139708, ECO:0000269|PubMed:4522793"
FT /id="PRO_0000015249"
FT DOMAIN 20..>117
FT /note="Ig-like"
FT DISULFID 41..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:15033359, ECO:0000269|PubMed:24892548,
FT ECO:0007744|PDB:1OHQ, ECO:0007744|PDB:3BN9,
FT ECO:0007744|PDB:3UPC, ECO:0007744|PDB:3ZHD,
FT ECO:0007744|PDB:3ZHK, ECO:0007744|PDB:3ZHL"
FT VARIANT 24
FT /note="V -> L (in IMGT allele IGHV3-23*02)"
FT /evidence="ECO:0000269|PubMed:6450418"
FT /id="VAR_073326"
FT VARIANT 80
FT /note="A -> G (in IMGT allele IGHV3-23*02)"
FT /evidence="ECO:0000269|PubMed:6450418"
FT /id="VAR_073327"
FT CONFLICT 20
FT /note="E -> A (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="G -> A (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="L -> G (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 47..54
FT /note="TFSSYAMS -> SFSTDAMY (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 50..53
FT /note="SYAM -> RVLS (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 50..52
FT /note="SYA -> TYV (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="S -> A (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="S -> T (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 51..54
FT /note="YAMS -> TSAVY (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 51..54
FT /note="YAMS -> TTSRF (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="Y -> S (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 68..84
FT /note="SAISGSGGSTYYADSVK -> AWKYQEASNSHFADTVN (in Ref. 3;
FT AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 68..84
FT /note="SAISGSGGSTYYADSVK -> GWRYEGSSLTHYAVSVQ (in Ref. 3;
FT AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 68..78
FT /note="SAISGSGGSTY -> AWKYENGNDKH (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 68..78
FT /note="SAISGSGGSTY -> EFRVQGSAISH (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="S -> G (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 69..84
FT /note="AISGSGGSTYYADSVK -> GRLNASSNLHFAVSAQ (in Ref. 3; AA
FT sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 71..78
FT /note="SGSGGSTY -> ZGLSVSZS (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 84..85
FT /note="KG -> QA (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="K -> N (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 92..93
FT /note="DN -> ND (in Ref. 4; AA sequence and 3; AA
FT sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 93..101
FT /note="NSKNTLYLQ -> DSKNT (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="Q -> L (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 103..107
FT /note="NSLRA -> LSLEP (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 103..106
FT /note="NSLR -> LSLQ (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 104..105
FT /note="SL -> TG (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="S -> G (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="S -> R (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="R -> E (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="R -> Q (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 109..112
FT /note="DTAV -> VSAI (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="V -> L (in Ref. 3; AA sequence and 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="K -> R (in Ref. 4; AA sequence and 3; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 117
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:3ZHD"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:3ZHD"
FT STRAND 37..46
FT /evidence="ECO:0007829|PDB:3ZHD"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:3ZHD"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:3ZHD"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:1OHQ"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:3ZHD"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:3ZHD"
FT TURN 81..86
FT /evidence="ECO:0007829|PDB:3ZHD"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:3ZHD"
FT TURN 93..96
FT /evidence="ECO:0007829|PDB:3ZHD"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:3ZHD"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:3ZHD"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:3ZHD"
SQ SEQUENCE 117 AA; 12582 MW; E96D8794FA22F0B5 CRC64;
MEFGLSWLFL VAILKGVQCE VQLVESGGGL VQPGGSLRLS CAASGFTFSS YAMSWVRQAP
GKGLEWVSAI SGSGGSTYYA DSVKGRFTIS RDNSKNTLYL QMNSLRAEDT AVYYCAK
