IGHD_HUMAN
ID IGHD_HUMAN Reviewed; 384 AA.
AC P01880; A0A087WUS7; Q6P4I8; Q8WU38;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 3.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Immunoglobulin heavy constant delta {ECO:0000303|PubMed:11340299, ECO:0000303|Ref.15};
DE AltName: Full=Ig delta chain C region {ECO:0000305};
DE AltName: Full=Ig delta chain C region NIG-65 {ECO:0000305|PubMed:6787589, ECO:0000305|PubMed:7092891};
DE AltName: Full=Ig delta chain C region WAH {ECO:0000305|PubMed:6787589, ECO:0000305|PubMed:6947220};
GN Name=IGHD {ECO:0000303|PubMed:11340299, ECO:0000303|Ref.15};
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 IGHD*01).
RX PubMed=3922054; DOI=10.1126/science.3922054;
RA White M.B., Shen A.L., Word C.J., Tucker P.W., Blattner F.R.;
RT "Human immunoglobulin D: genomic sequence of the delta heavy chain.";
RL Science 228:733-737(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (IMGT ALLELE IGHD*02).
RX PubMed=2518659; DOI=10.1093/intimm/1.3.296;
RA Word C.J., White M.B., Kuziel W.A., Shen A.L., Blattner F.R., Tucker P.W.;
RT "The human immunoglobulin C mu-C delta locus: complete nucleotide sequence
RT and structural analysis.";
RL Int. Immunol. 1:296-309(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE IGHD*02).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=B-cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 1-162, AND DISULFIDE BONDS.
RX PubMed=6947220; DOI=10.1073/pnas.78.10.6168;
RA Putnam F.W., Takahashi N., Tetaert D., Debuire B., Lin L.-C.;
RT "Amino acid sequence of the first constant region domain and the hinge
RT region of the delta heavy chain of human IgD.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:6168-6172(1981).
RN [6]
RP PROTEIN SEQUENCE OF 103-137, AND GLYCOSYLATION AT SER-109; SER-110;
RP THR-113; THR-126; THR-127; THR-131 AND THR-132.
RX PubMed=7092891; DOI=10.1016/0006-291x(82)91078-6;
RA Takayasu T., Suzuki S., Kametani F., Takahashi N., Shinoda T., Okuyama T.,
RA Munekata E.;
RT "Amino acid sequence of galactosamine-containing glycopeptides in the hinge
RT region of a human immunoglobulin D.";
RL Biochem. Biophys. Res. Commun. 105:1066-1071(1982).
RN [7]
RP PROTEIN SEQUENCE OF 158-383.
RX PubMed=6787589; DOI=10.1073/pnas.78.1.504;
RA Lin L.-C., Putnam F.W.;
RT "Primary structure of the Fc region of human immunoglobulin D: implications
RT for evolutionary origin and biological function.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:504-508(1981).
RN [8]
RP PROTEIN SEQUENCE OF 158-383.
RX PubMed=6785754; DOI=10.1073/pnas.78.2.785;
RA Shinoda T., Takahashi N., Takayasu T., Okuyama T., Shimizu A.;
RT "Complete amino acid sequence of the Fc region of a human delta chain.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:785-789(1981).
RN [9]
RP GLYCOSYLATION AT ASN-225; ASN-316 AND ASN-367.
RX PubMed=7008791; DOI=10.1016/0006-291x(80)90311-3;
RA Takayasu T., Takahashi N., Shinoda T.;
RT "Amino acid sequence and location of the three glycopeptides in the Fc
RT region of human immunoglobulin D.";
RL Biochem. Biophys. Res. Commun. 97:635-641(1980).
RN [10]
RP GLYCOSYLATION AT SER-109; THR-126; THR-127; THR-131; THR-132; ASN-225;
RP ASN-316 AND ASN-367.
RX PubMed=6619128; DOI=10.1016/s0021-9258(17)44263-3;
RA Mellis S.J., Baenziger J.U.;
RT "Structures of the O-glycosidically linked oligosaccharides of human IgD.";
RL J. Biol. Chem. 258:11557-11563(1983).
RN [11]
RP FUNCTION.
RX PubMed=8774350; DOI=10.1046/j.1365-2567.1996.d01-672.x;
RA Drenth J.P., Goertz J., Daha M.R., van der Meer J.W.;
RT "Immunoglobulin D enhances the release of tumor necrosis factor-alpha, and
RT interleukin-1 beta as well as interleukin-1 receptor antagonist from human
RT mononuclear cells.";
RL Immunology 88:355-362(1996).
RN [12]
RP REVIEW.
RX PubMed=10702483; DOI=10.1128/cdli.7.2.131-140.2000;
RA Vladutiu A.O.;
RT "Immunoglobulin D: properties, measurement, and clinical relevance.";
RL Clin. Diagn. Lab. Immunol. 7:131-140(2000).
RN [13]
RP REVIEW.
RX PubMed=11282392; DOI=10.1016/s0161-5890(01)00006-2;
RA Preud'homme J.L., Petit I., Barra A., Morel F., Lecron J.C., Lelievre E.;
RT "Structural and functional properties of membrane and secreted IgD.";
RL Mol. Immunol. 37:871-887(2000).
RN [14]
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 [15]
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 [16]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-225 AND ASN-316.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [17]
RP REVIEW.
RX PubMed=16895553; DOI=10.1111/j.1365-2567.2006.02386.x;
RA Geisberger R., Lamers M., Achatz G.;
RT "The riddle of the dual expression of IgM and IgD.";
RL Immunology 118:429-437(2006).
RN [18]
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 [19]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-316.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [20]
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 [21]
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).
CC -!- FUNCTION: Constant region of immunoglobulin heavy chains.
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:17576170, PubMed:20176268).
CC IgD is the major antigen receptor isotype on the surface of most
CC peripheral B-cells, where it is coexpressed with IgM. The membrane-
CC bound IgD (mIgD) induces the phosphorylation of CD79A and CD79B by the
CC Src family of protein tyrosine kinases. Soluble IgD (sIgD)
CC concentration in serum below those of IgG, IgA, and IgM but much higher
CC than that of IgE. IgM and IgD molecules present on B cells have
CC identical V regions and antigen-binding sites. After the antigen binds
CC to the B-cell receptor, the secreted form sIgD is shut off. IgD is a
CC potent inducer of TNF, IL1B, and IL1RN. IgD also induces release of
CC IL6, IL10, and LIF from peripheral blood mononuclear cells. Monocytes
CC seem to be the main producers of cytokines in vitro in the presence of
CC IgD (PubMed:8774350, PubMed:10702483, PubMed:11282392).
CC {ECO:0000269|PubMed:8774350, ECO:0000303|PubMed:10702483,
CC ECO:0000303|PubMed:11282392, ECO:0000303|PubMed:17576170,
CC ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
CC -!- SUBUNIT: Immunoglobulins are composed of two identical heavy chains and
CC two identical light chains; disulfide-linked (PubMed:20176268). An IgD
CC molecule contains thus a delta heavy chain combined with either a kappa
CC or a lambda light chains. Kappa light chains are found predominantly on
CC the membrane IgD (mIgD) form and lambda on the secreted IgD (sIgD)
CC form, this fact is poorly understood. Membrane-bound IgD molecules are
CC non-covalently associated with a heterodimer of CD79A and CD79B
CC (PubMed:11282392). {ECO:0000303|PubMed:11282392,
CC ECO:0000303|PubMed:20176268}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Secreted
CC {ECO:0000303|PubMed:11282392}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Single-pass type I
CC membrane protein {ECO:0000303|PubMed:11282392}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Secreted, sIgD {ECO:0000303|PubMed:11282392};
CC IsoId=P01880-1; Sequence=Displayed;
CC Name=2; Synonyms=Membrane-bound, mIgD {ECO:0000303|PubMed:11282392};
CC IsoId=P01880-2; Sequence=VSP_034489;
CC -!- POLYMORPHISM: There are several alleles. The sequence shown is that of
CC IMGT allele IGHD*02. {ECO:0000305}.
CC -!- MISCELLANEOUS: IgD is not present in every species and this does not
CC relate to phylogeny and evolution. IgD is present in primates, dog,
CC mouse and rat whereas it is undetectable in rabbit, guinea pig, swine,
CC cattle, sheep and Xenopus.
CC -!- CAUTION: For an example of a full-length immunoglobulin delta heavy
CC chain see AC P0DOX3. {ECO:0000305}.
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DR EMBL; K02880; AAA52770.1; -; Genomic_DNA.
DR EMBL; K02875; AAA52770.1; JOINED; Genomic_DNA.
DR EMBL; K02876; AAA52770.1; JOINED; Genomic_DNA.
DR EMBL; K02877; AAA52770.1; JOINED; Genomic_DNA.
DR EMBL; K02878; AAA52770.1; JOINED; Genomic_DNA.
DR EMBL; K02879; AAA52770.1; JOINED; Genomic_DNA.
DR EMBL; X57331; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC246787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC021276; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC063384; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A02175; DHHU.
DR PIR; S21205; S21205.
DR PIR; S30532; S30532.
DR PDB; 1ZVO; X-ray; -; C/D=1-383.
DR PDBsum; 1ZVO; -.
DR AlphaFoldDB; P01880; -.
DR SMR; P01880; -.
DR ComplexPortal; CPX-6744; IgD - Ig kappa immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6906; IgD - Ig lambda 1 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6907; IgD - Ig lambda 2 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6908; IgD - Ig lambda 3 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6909; IgD - Ig lambda 6 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6910; IgD - Ig lambda 7 immunoglobulin complex, constant regions.
DR IntAct; P01880; 2.
DR IMGT_GENE-DB; IGHD; -.
DR GlyConnect; 1943; 93 N-Linked glycans (3 sites), 4 O-Linked glycans (5 sites).
DR GlyConnect; 2968; 25 N-Linked glycans.
DR GlyConnect; 2969; 23 N-Linked glycans.
DR GlyGen; P01880; 12 sites, 52 N-linked glycans (4 sites), 9 O-linked glycans (8 sites).
DR iPTMnet; P01880; -.
DR PhosphoSitePlus; P01880; -.
DR BioMuta; IGHD; -.
DR DMDM; 193806360; -.
DR jPOST; P01880; -.
DR MassIVE; P01880; -.
DR PeptideAtlas; P01880; -.
DR PRIDE; P01880; -.
DR ProteomicsDB; 51502; -. [P01880-1]
DR ProteomicsDB; 51503; -. [P01880-2]
DR GeneCards; IGHD; -.
DR HGNC; HGNC:5480; IGHD.
DR HPA; ENSG00000211898; Tissue enriched (lymphoid).
DR MIM; 147170; gene.
DR neXtProt; NX_P01880; -.
DR VEuPathDB; HostDB:ENSG00000211898; -.
DR InParanoid; P01880; -.
DR PhylomeDB; P01880; -.
DR PathwayCommons; P01880; -.
DR Reactome; R-HSA-5690714; CD22 mediated BCR regulation.
DR Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR SignaLink; P01880; -.
DR ChiTaRS; IGHD; human.
DR EvolutionaryTrace; P01880; -.
DR Pharos; P01880; Tdark.
DR PRO; PR:P01880; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P01880; protein.
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:0005615; C:extracellular space; IC:ComplexPortal.
DR GO; GO:0071738; C:IgD immunoglobulin complex; IC:ComplexPortal.
DR GO; GO:0042571; C:immunoglobulin complex, circulating; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0002250; P:adaptive immune response; IC:ComplexPortal.
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 GO; GO:0032732; P:positive regulation of interleukin-1 production; IDA:UniProtKB.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003006; Ig/MHC_CS.
DR InterPro; IPR003597; Ig_C1-set.
DR InterPro; IPR013151; Immunoglobulin.
DR Pfam; PF07654; C1-set; 2.
DR Pfam; PF00047; ig; 1.
DR SMART; SM00407; IGc1; 3.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS00290; IG_MHC; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Alternative splicing; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Immunity;
KW Immunoglobulin; Immunoglobulin domain; Membrane; Reference proteome;
KW Secreted; Transmembrane.
FT CHAIN <1..384
FT /note="Immunoglobulin heavy constant delta"
FT /id="PRO_0000153570"
FT DOMAIN 6..98
FT /note="Ig-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 175..263
FT /note="Ig-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 267..373
FT /note="Ig-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 96..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 109
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:6619128,
FT ECO:0000269|PubMed:7092891"
FT CARBOHYD 110
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:7092891"
FT CARBOHYD 113
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:7092891"
FT CARBOHYD 126
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:6619128,
FT ECO:0000269|PubMed:7092891"
FT CARBOHYD 127
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:6619128,
FT ECO:0000269|PubMed:7092891"
FT CARBOHYD 131
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:6619128,
FT ECO:0000269|PubMed:7092891"
FT CARBOHYD 132
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:6619128,
FT ECO:0000269|PubMed:7092891"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:6619128, ECO:0000269|PubMed:6785754,
FT ECO:0000269|PubMed:7008791"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:6619128,
FT ECO:0000269|PubMed:6785754, ECO:0000269|PubMed:7008791"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:6619128,
FT ECO:0000269|PubMed:6785754, ECO:0000269|PubMed:7008791"
FT DISULFID 15
FT /note="Interchain (with light chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:6947220"
FT DISULFID 28..84
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:6947220"
FT DISULFID 161
FT /note="Interchain (with heavy chain)"
FT /evidence="ECO:0000269|PubMed:6947220"
FT DISULFID 190..249
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 294..355
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 377..384
FT /note="VTDHGPMK -> LAMTPLIPQSKDENSDDYTTFDDVGSLWTTLSTFVALFIL
FT TLLYSGIVTFIKVK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034489"
FT CONFLICT 247
FT /note="V -> I (in Ref. 4; BC063384)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="R -> G (in Ref. 7; AA sequence and 8; AA sequence)"
FT NON_TER 1
SQ SEQUENCE 384 AA; 42353 MW; 726F08E73519DDDC CRC64;
APTKAPDVFP IISGCRHPKD NSPVVLACLI TGYHPTSVTV TWYMGTQSQP QRTFPEIQRR
DSYYMTSSQL STPLQQWRQG EYKCVVQHTA SKSKKEIFRW PESPKAQASS VPTAQPQAEG
SLAKATTAPA TTRNTGRGGE EKKKEKEKEE QEERETKTPE CPSHTQPLGV YLLTPAVQDL
WLRDKATFTC FVVGSDLKDA HLTWEVAGKV PTGGVEEGLL ERHSNGSQSQ HSRLTLPRSL
WNAGTSVTCT LNHPSLPPQR LMALREPAAQ APVKLSLNLL ASSDPPEAAS WLLCEVSGFS
PPNILLMWLE DQREVNTSGF APARPPPQPR STTFWAWSVL RVPAPPSPQP ATYTCVVSHE
DSRTLLNASR SLEVSYVTDH GPMK
