IGHA1_HUMAN
ID IGHA1_HUMAN Reviewed; 353 AA.
AC P01876;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Immunoglobulin heavy constant alpha 1 {ECO:0000303|PubMed:11340299, ECO:0000303|Ref.12};
DE AltName: Full=Ig alpha-1 chain C region {ECO:0000305};
DE AltName: Full=Ig alpha-1 chain C region BUR {ECO:0000305|PubMed:107164};
DE AltName: Full=Ig alpha-1 chain C region TRO {ECO:0000305|PubMed:809331};
GN Name=IGHA1 {ECO:0000303|PubMed:11340299, ECO:0000303|Ref.12};
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 PROTEIN SEQUENCE.
RX PubMed=809331;
RA Kratzin H., Altevogt P., Ruban E., Kortt A., Staroscik K., Hilschmann N.;
RT "The primary structure of a monoclonal IgA-immunoglobulin (IgA Tro.), II.
RT The amino acid sequence of the H-chain, alpha-type, subgroup III; structure
RT of the complete IgA-molecule.";
RL Hoppe-Seyler's Z. Physiol. Chem. 356:1337-1342(1975).
RN [2]
RP PROTEIN SEQUENCE.
RX PubMed=107164; DOI=10.1016/s0021-9258(17)30153-9;
RA Putnam F.W., Liu Y.-S.V., Low T.L.K.;
RT "Primary structure of a human IgA1 immunoglobulin. IV. Streptococcal IgA1
RT protease, digestion, Fab and Fc fragments, and the complete amino acid
RT sequence of the alpha 1 heavy chain.";
RL J. Biol. Chem. 254:2865-2874(1979).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (IMGT ALLELE IGHA1*01).
RX PubMed=6811139; DOI=10.1016/0092-8674(82)90183-0;
RA Takahashi N., Ueda S., Obata M., Nikaido T., Nakai S., Honjo T.;
RT "Structure of human immunoglobulin gamma genes: implications for evolution
RT of a gene family.";
RL Cell 29:671-679(1982).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6421489; DOI=10.1016/0092-8674(84)90348-9;
RA Flanagan J.G., Lefranc M.-P., Rabbitts T.H.;
RT "Mechanisms of divergence and convergence of the human immunoglobulin alpha
RT 1 and alpha 2 constant region gene sequences.";
RL Cell 36:681-688(1984).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE IGHA1*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 [6]
RP PROTEIN SEQUENCE OF 345-353, AND BINDING TO CHROMOPHORE.
RX PubMed=7506257; DOI=10.1016/s0021-9258(17)42361-1;
RA Calero M., Escribano J., Grubb A., Mendez E.;
RT "Location of a novel type of interpolypeptide chain linkage in the human
RT protein HC-IgA complex (HC-IgA) and identification of a heterogeneous
RT chromophore associated with the complex.";
RL J. Biol. Chem. 269:384-389(1994).
RN [7]
RP GLYCOSYLATION AT SER-105; SER-111; SER-113; SER-119 AND SER-121.
RX PubMed=4373463; DOI=10.1016/s0021-9258(19)42101-7;
RA Baenziger J., Kornfeld S.;
RT "Structure of the carbohydrate units of IgA1 immunoglobulin. II. Structure
RT of the O-glycosidically linked oligosaccharide units.";
RL J. Biol. Chem. 249:7270-7281(1974).
RN [8]
RP DISULFIDE BONDS.
RX PubMed=393607;
RA Yang C.-Y., Kratzin H., Gotz H., Hilschmann N.;
RT "Rule of antibody structure. Primary structure of a human monoclonal IgA-
RT immunoglobulin (myeloma protein Tro). VII. Purification and
RT characterization of the disulfide bridges.";
RL Hoppe-Seyler's Z. Physiol. Chem. 360:1919-1940(1979).
RN [9]
RP REVIEW ON FUNCTION.
RX PubMed=2241915; DOI=10.1042/bj2710285;
RA Kerr M.A.;
RT "The structure and function of human IgA.";
RL Biochem. J. 271:285-296(1990).
RN [10]
RP CHROMOSOMAL TRANSLOCATION WITH FCRL4.
RX PubMed=11290337; DOI=10.1016/s1074-7613(01)00109-1;
RA Hatzivassiliou G., Miller I., Takizawa J., Palanisamy N., Rao P.H.,
RA Iida S., Tagawa S., Taniwaki M., Russo J., Neri A., Cattoretti G.,
RA Clynes R., Mendelsohn C., Chaganti R.S.K., Dalla-Favera R.;
RT "IRTA1 and IRTA2, novel immunoglobulin superfamily receptors expressed in B
RT cells and involved in chromosome 1q21 abnormalities in B cell malignancy.";
RL Immunity 14:277-289(2001).
RN [11]
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 [12]
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 [13]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-144.
RC TISSUE=Bile;
RX PubMed=15084671; DOI=10.1074/mcp.m400015-mcp200;
RA Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J.,
RA Argani P., Goggins M.G., Maitra A., Pandey A.;
RT "A proteomic analysis of human bile.";
RL Mol. Cell. Proteomics 3:715-728(2004).
RN [14]
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 [15]
RP GLYCOSYLATION AT ASN-144 AND ASN-340.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [16]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-144, AND STRUCTURE OF
RP CARBOHYDRATES.
RC TISSUE=Cerebrospinal fluid;
RX PubMed=19838169; DOI=10.1038/nmeth.1392;
RA Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G.,
RA Larson G.;
RT "Enrichment of glycopeptides for glycan structure and attachment site
RT identification.";
RL Nat. Methods 6:809-811(2009).
RN [17]
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 [18]
RP GLYCOSYLATION AT THR-106; THR-109; SER-111; SER-113 AND THR-117, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20823119; DOI=10.1074/mcp.m110.001834;
RA Takahashi K., Wall S.B., Suzuki H., Smith A.D. IV, Hall S., Poulsen K.,
RA Kilian M., Mobley J.A., Julian B.A., Mestecky J., Novak J., Renfrow M.B.;
RT "Clustered O-glycans of IgA1: defining macro- and microheterogeneity by use
RT of electron capture/transfer dissociation.";
RL Mol. Cell. Proteomics 9:2545-2557(2010).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [20]
RP GLYCOSYLATION AT ASN-144, STRUCTURE OF CARBOHYDRATES, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=22171320; DOI=10.1074/mcp.m111.013649;
RA Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
RT "Human urinary glycoproteomics; attachment site specific analysis of N- and
RT O-linked glycosylations by CID and ECD.";
RL Mol. Cell. Proteomics 11:1-17(2012).
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).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [23]
RP GLYCOSYLATION AT THR-106; THR-109; SER-111; SER-113; THR-114 AND THR-117,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=31959827; DOI=10.1038/s41598-020-57510-z;
RA Ohyama Y., Yamaguchi H., Nakajima K., Mizuno T., Fukamachi Y., Yokoi Y.,
RA Tsuboi N., Inaguma D., Hasegawa M., Renfrow M.B., Novak J., Yuzawa Y.,
RA Takahashi K.;
RT "Analysis of O-glycoforms of the IgA1 hinge region by sequential
RT deglycosylation.";
RL Sci. Rep. 10:671-671(2020).
RN [24]
RP STRUCTURE BY ELECTRON MICROSCOPY (2.90 ANGSTROMS) OF 123-353 IN COMPLEX
RP WITH PIGR AND JCHAIN, DISULFIDE BOND, AND SUBUNIT.
RX PubMed=32029686; DOI=10.1126/science.aaz5807;
RA Kumar N., Arthur C.P., Ciferri C., Matsumoto M.L.;
RT "Structure of the secretory immunoglobulin A core.";
RL Science 367:1008-1014(2020).
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 Ig alpha is the major immunoglobulin class in body secretions
CC (PubMed:2241915). {ECO:0000303|PubMed:17576170,
CC ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414,
CC ECO:0000303|PubMed:2241915}.
CC -!- SUBUNIT: Immunoglobulins are composed of two identical heavy chains and
CC two identical light chains; disulfide-linked (PubMed:20176268).
CC Monomeric or polymeric (PubMed:2241915). Part of the secretory IgA
CC (sIgA) complex that consists of two, four or five IgA monomers, and two
CC additional non-Ig polypeptides, namely the JCHAIN and the secretory
CC component (the proteoytic product of PIGR).
CC {ECO:0000269|PubMed:32029686, ECO:0000303|PubMed:20176268,
CC ECO:0000303|PubMed:2241915}.
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 -!- PTM: 3-Hydroxykynurenine, an oxidized tryptophan metabolite that is
CC common in biological fluids, reacts with alpha-1-microglobulin to form
CC heterogeneous polycyclic chromophores including hydroxanthommatin. The
CC chromophore reacts with accessible cysteines forming non-reducible
CC thioether cross-links with Ig alpha-1 chain C region Cys-352.
CC {ECO:0000269|PubMed:7506257}.
CC -!- PTM: N- and O-glycosylated. N-glycan at Asn-144: Hex5HexNAc4.
CC {ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:19139490,
CC ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22171320}.
CC -!- POLYMORPHISM: There are several alleles. The sequence shown is that of
CC IMGT allele IGHA1*02. {ECO:0000305}.
CC -!- DISEASE: Note=A chromosomal aberration involving IGHA1 is found in
CC multiple myeloma (MM) cell lines. Translocation t(1;14)(q21;q32) that
CC forms a FCRL4-IGHA1 fusion protein. {ECO:0000269|PubMed:11290337}.
CC -!- CAUTION: For an example of a full-length immunoglobulin alpha heavy
CC chain see AC P0DOX2. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC82528.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; J00220; AAC82528.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL901608; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL928768; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A22360; A1HU.
DR PDB; 1IGA; X-ray; -; A/B=1-353.
DR PDB; 1OW0; X-ray; 3.10 A; A/B=122-335.
DR PDB; 2ESG; X-ray; -; A/B=1-353.
DR PDB; 2QEJ; X-ray; 3.20 A; A/B=123-336.
DR PDB; 3CHN; X-ray; -; A/B/C/D=2-353.
DR PDB; 6LX3; EM; 3.15 A; A/B/C/D=122-353.
DR PDB; 6LXW; EM; 3.27 A; A/B/C/D=122-353.
DR PDB; 6UE7; EM; 2.90 A; A/B/F/G=123-353.
DR PDB; 6XJA; EM; 4.00 A; A/B=122-331.
DR PDBsum; 1IGA; -.
DR PDBsum; 1OW0; -.
DR PDBsum; 2ESG; -.
DR PDBsum; 2QEJ; -.
DR PDBsum; 3CHN; -.
DR PDBsum; 6LX3; -.
DR PDBsum; 6LXW; -.
DR PDBsum; 6UE7; -.
DR PDBsum; 6XJA; -.
DR AlphaFoldDB; P01876; -.
DR SMR; P01876; -.
DR ComplexPortal; CPX-6955; IgA1 - Ig kappa immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6956; IgA1 - Ig lambda 1 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6958; IgA1 - Ig lambda 2 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6959; IgA1 - Ig lambda 3 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6960; IgA1 - Ig lambda 6 immunoglobulin complex, constant regions.
DR ComplexPortal; CPX-6961; IgA1 - Ig lambda 7 immunoglobulin complex, constant regions.
DR IntAct; P01876; 88.
DR MINT; P01876; -.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR IMGT_GENE-DB; IGHA1; -.
DR CarbonylDB; P01876; -.
DR GlyConnect; 227; 58 N-Linked glycans (1 site), 1 O-Linked glycan.
DR GlyConnect; 230; 150 N-Linked glycans (2 sites), 49 O-Linked glycans (9 sites).
DR GlyConnect; 2965; 44 N-Linked glycans.
DR GlyConnect; 2966; 49 N-Linked glycans.
DR GlyGen; P01876; 12 sites, 128 N-linked glycans (3 sites), 63 O-linked glycans (10 sites).
DR iPTMnet; P01876; -.
DR PhosphoSitePlus; P01876; -.
DR BioMuta; IGHA1; -.
DR DMDM; 113584; -.
DR EPD; P01876; -.
DR jPOST; P01876; -.
DR MassIVE; P01876; -.
DR PeptideAtlas; P01876; -.
DR PRIDE; P01876; -.
DR ProteomicsDB; 51500; -.
DR Ensembl; ENST00000390547.3; ENSP00000374989.2; ENSG00000211895.5.
DR Ensembl; ENST00000633714.1; ENSP00000488021.1; ENSG00000282633.1.
DR UCSC; uc059gcy.1; human.
DR GeneCards; IGHA1; -.
DR HGNC; HGNC:5478; IGHA1.
DR HPA; ENSG00000211895; Group enriched (intestine, lymphoid tissue, salivary gland, stomach).
DR MIM; 146900; gene.
DR neXtProt; NX_P01876; -.
DR OpenTargets; ENSG00000211895; -.
DR VEuPathDB; HostDB:ENSG00000211895; -.
DR GeneTree; ENSGT00940000161516; -.
DR HOGENOM; CLU_030625_0_1_1; -.
DR InParanoid; P01876; -.
DR PhylomeDB; P01876; -.
DR TreeFam; TF334176; -.
DR PathwayCommons; P01876; -.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-HSA-2168880; Scavenging of heme from plasma.
DR SignaLink; P01876; -.
DR ChiTaRS; IGHA1; human.
DR EvolutionaryTrace; P01876; -.
DR Pharos; P01876; Tbio.
DR PRO; PR:P01876; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P01876; protein.
DR Bgee; ENSG00000211895; Expressed in duodenum and 91 other tissues.
DR ExpressionAtlas; P01876; baseline and differential.
DR Genevisible; P01876; HS.
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; IDA:UniProtKB.
DR GO; GO:0071745; C:IgA immunoglobulin complex; IC:ComplexPortal.
DR GO; GO:0071735; C:IgG immunoglobulin complex; IC:ComplexPortal.
DR GO; GO:0042571; C:immunoglobulin complex, circulating; IBA:GO_Central.
DR GO; GO:0071748; C:monomeric IgA immunoglobulin complex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IC:ComplexPortal.
DR GO; GO:0071752; C:secretory dimeric IgA immunoglobulin complex; IDA:UniProtKB.
DR GO; GO:0071751; C:secretory IgA immunoglobulin complex; IDA:UniProtKB.
DR GO; GO:0003823; F:antigen binding; IBA:GO_Central.
DR GO; GO:0002250; P:adaptive immune response; IC:ComplexPortal.
DR GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
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:0003094; P:glomerular filtration; IMP:UniProtKB.
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:0060267; P:positive regulation of respiratory burst; IDA:UniProtKB.
DR GO; GO:0001895; P:retina homeostasis; HEP: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 Pfam; PF07654; C1-set; 2.
DR SMART; SM00407; IGc1; 2.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS00290; IG_MHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Cell membrane; Chromophore;
KW Chromosomal rearrangement; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Immunity; Immunoglobulin; Immunoglobulin domain; Membrane;
KW Reference proteome; Secreted.
FT CHAIN <1..353
FT /note="Immunoglobulin heavy constant alpha 1"
FT /id="PRO_0000153566"
FT DOMAIN 6..98
FT /note="Ig-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 125..220
FT /note="Ig-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 228..330
FT /note="Ig-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 96..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..122
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 352
FT /ligand="3-hydroxy-L-kynurenine"
FT /ligand_id="ChEBI:CHEBI:58125"
FT /ligand_note="multimeric 3-hydroxykynurenine chromophore"
FT /note="covalent; in form alpha-1-microglobulin complex"
FT CARBOHYD 105
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:4373463"
FT CARBOHYD 106
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:20823119,
FT ECO:0000269|PubMed:31959827"
FT CARBOHYD 109
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:20823119,
FT ECO:0000269|PubMed:31959827"
FT CARBOHYD 111
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:20823119,
FT ECO:0000269|PubMed:31959827, ECO:0000269|PubMed:4373463"
FT CARBOHYD 113
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:20823119,
FT ECO:0000269|PubMed:31959827, ECO:0000269|PubMed:4373463"
FT CARBOHYD 114
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:31959827"
FT CARBOHYD 117
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:20823119,
FT ECO:0000269|PubMed:31959827"
FT CARBOHYD 119
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:4373463"
FT CARBOHYD 121
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:4373463"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:15084671,
FT ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19838169,
FT ECO:0000269|PubMed:22171320"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:19139490"
FT DISULFID 14
FT /note="Interchain (with light chain)"
FT /evidence="ECO:0000269|PubMed:393607"
FT DISULFID 26..85
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 77..101
FT DISULFID 122
FT /note="Interchain (with heavy chain)"
FT /evidence="ECO:0000269|PubMed:393607"
FT DISULFID 123..180
FT /note="Or C-123 with C-182"
FT /evidence="ECO:0000269|PubMed:393607"
FT DISULFID 147..204
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 182
FT /note="Interchain (with heavy chain) (or with C-180)"
FT /evidence="ECO:0000269|PubMed:393607"
FT DISULFID 192
FT /note="Interchain (with heavy chain of another subunit) (or
FT with C-503 of PIGR/the secretory component)"
FT /evidence="ECO:0000269|PubMed:32029686,
FT ECO:0000269|PubMed:393607"
FT DISULFID 250..313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 352
FT /note="Interchain (with J chain); in oligomeric form"
FT /evidence="ECO:0000269|PubMed:393607"
FT VARIANT 176
FT /note="E -> D (in dbSNP:rs1407)"
FT /id="VAR_014602"
FT CONFLICT 163..165
FT /note="TPS -> PST (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="E -> B (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="P -> S (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="R -> H (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="H -> R (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="T -> E (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 1
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:6UE7"
FT HELIX 134..138
FT /evidence="ECO:0007829|PDB:6UE7"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:6UE7"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:1OW0"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:6LXW"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:6UE7"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:1OW0"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:1OW0"
FT HELIX 193..198
FT /evidence="ECO:0007829|PDB:6UE7"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:6UE7"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:6UE7"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:6UE7"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:6UE7"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:6LX3"
FT TURN 240..243
FT /evidence="ECO:0007829|PDB:6UE7"
FT STRAND 246..258
FT /evidence="ECO:0007829|PDB:6UE7"
FT STRAND 261..266
FT /evidence="ECO:0007829|PDB:6UE7"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:6UE7"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:6UE7"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:6UE7"
FT STRAND 292..300
FT /evidence="ECO:0007829|PDB:6UE7"
FT HELIX 302..307
FT /evidence="ECO:0007829|PDB:6UE7"
FT STRAND 311..316
FT /evidence="ECO:0007829|PDB:6UE7"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:6UE7"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:6UE7"
FT STRAND 340..343
FT /evidence="ECO:0007829|PDB:6UE7"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:6LX3"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:6UE7"
SQ SEQUENCE 353 AA; 37655 MW; EBA11ECB7E85DB21 CRC64;
ASPTSPKVFP LSLCSTQPDG NVVIACLVQG FFPQEPLSVT WSESGQGVTA RNFPPSQDAS
GDLYTTSSQL TLPATQCLAG KSVTCHVKHY TNPSQDVTVP CPVPSTPPTP SPSTPPTPSP
SCCHPRLSLH RPALEDLLLG SEANLTCTLT GLRDASGVTF TWTPSSGKSA VQGPPERDLC
GCYSVSSVLP GCAEPWNHGK TFTCTAAYPE SKTPLTATLS KSGNTFRPEV HLLPPPSEEL
ALNELVTLTC LARGFSPKDV LVRWLQGSQE LPREKYLTWA SRQEPSQGTT TFAVTSILRV
AAEDWKKGDT FSCMVGHEAL PLAFTQKTID RLAGKPTHVN VSVVMAEVDG TCY
