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P01876

- IGHA1_HUMAN

UniProt

P01876 - IGHA1_HUMAN

Protein

Ig alpha-1 chain C region

Gene

IGHA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 2 (01 Feb 1991)
      Previous versions | rss
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    Functioni

    Ig alpha is the major immunoglobulin class in body secretions. It may serve both to defend against local infection and to prevent access of foreign antigens to the general immunologic system.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei352 – 3521Multimeric 3-hydroxykynurenine chromophore (covalent); in form alpha-1-microglobulin complex

    GO - Molecular functioni

    1. antigen binding Source: UniProtKB

    GO - Biological processi

    1. antibacterial humoral response Source: UniProt
    2. glomerular filtration Source: UniProt
    3. immune response Source: UniProtKB
    4. positive regulation of respiratory burst Source: UniProt
    5. protein-chromophore linkage Source: UniProtKB-KW
    6. retina homeostasis Source: UniProt

    Keywords - Ligandi

    Chromophore

    Enzyme and pathway databases

    ReactomeiREACT_160163. Scavenging of heme from plasma.

    Protein family/group databases

    MEROPSiI43.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ig alpha-1 chain C region
    Gene namesi
    Name:IGHA1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:5478. IGHA1.

    Subcellular locationi

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. extracellular region Source: Reactome
    3. extracellular space Source: UniProt
    4. extracellular vesicular exosome Source: UniProt
    5. monomeric IgA immunoglobulin complex Source: UniProt
    6. secretory dimeric IgA immunoglobulin complex Source: UniProt
    7. secretory IgA immunoglobulin complex Source: UniProt

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving IGHA1 is found in multiple myeloma (MM) cell lines. Translocation t(1;14)(q21;q32) that forms a FCRL4-IGHA1 fusion protein.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini‹1 – 353›353Ig alpha-1 chain C regionPRO_0000153566Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi14 – 14Interchain (with light chain)
    Disulfide bondi26 ↔ 85
    Disulfide bondi77 ↔ 101
    Glycosylationi105 – 1051O-linked (GalNAc...)
    Glycosylationi111 – 1111O-linked (GalNAc...)
    Glycosylationi113 – 1131O-linked (GalNAc...)
    Glycosylationi119 – 1191O-linked (GalNAc...)
    Glycosylationi121 – 1211O-linked (GalNAc...)
    Disulfide bondi122 – 122Interchain (with heavy chain)
    Disulfide bondi123 ↔ 180Or C-123 with C-182
    Glycosylationi144 – 1441N-linked (GlcNAc...) (complex)4 Publications
    Disulfide bondi147 ↔ 204
    Disulfide bondi182 – 182Interchain (with heavy chain) (or with C-180)
    Disulfide bondi192 – 192Interchain (with heavy chain of another subunit)Curated
    Disulfide bondi250 ↔ 313
    Glycosylationi340 – 3401N-linked (GlcNAc...) (complex)1 Publication
    Disulfide bondi352 – 352Interchain (with J chain); in oligomeric form

    Post-translational modificationi

    3-Hydroxykynurenine, an oxidized tryptophan metabolite that is common in biological fluids, reacts with alpha-1-microglobulin to form heterogeneous polycyclic chromophores including hydroxanthommatin. The chromophore reacts with accessible cysteines forming non-reducible thioether cross-links with Ig alpha-1 chain C region Cys-352.
    N- and O-glycosylated. N-glycan at Asn-144: Hex5HexNAc4.4 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP01876.
    PRIDEiP01876.

    PTM databases

    PhosphoSiteiP01876.

    Expressioni

    Gene expression databases

    BgeeiP01876.
    GenevestigatoriP01876.

    Interactioni

    Subunit structurei

    Monomeric or polymeric.

    Protein-protein interaction databases

    IntActiP01876. 44 interactions.
    STRINGi9606.ENSP00000374989.

    Structurei

    Secondary structure

    1
    353
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi128 – 1303
    Helixi134 – 1396
    Beta strandi146 – 1494
    Beta strandi162 – 1643
    Beta strandi185 – 1884
    Turni190 – 1923
    Helixi193 – 1986
    Beta strandi201 – 2066
    Beta strandi215 – 2206
    Beta strandi229 – 2335
    Turni237 – 2415
    Beta strandi242 – 25817
    Beta strandi261 – 2666
    Helixi273 – 2753
    Beta strandi276 – 2783
    Beta strandi287 – 2893
    Beta strandi292 – 30110
    Helixi302 – 3076
    Beta strandi311 – 3166
    Beta strandi323 – 3253

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IGAX-ray-A/B1-353[»]
    1OW0X-ray3.10A/B122-335[»]
    2QEJX-ray3.20A/B123-336[»]
    3CHNX-ray-A/B/C/D2-353[»]
    ProteinModelPortaliP01876.
    SMRiP01876. Positions 1-102, 123-331.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP01876.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini6 – 9893Ig-like 1Add
    BLAST
    Domaini125 – 22096Ig-like 2Add
    BLAST
    Domaini228 – 330103Ig-like 3Add
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Immunoglobulin C region, Immunoglobulin domain, Repeat

    Phylogenomic databases

    eggNOGiNOG27314.
    HOVERGENiHBG005814.
    InParanoidiP01876.
    OMAiEVDGTCY.
    PhylomeDBiP01876.
    TreeFamiTF334176.

    Family and domain databases

    Gene3Di2.60.40.10. 3 hits.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003006. Ig/MHC_CS.
    IPR003597. Ig_C1-set.
    [Graphical view]
    PfamiPF07654. C1-set. 2 hits.
    [Graphical view]
    SMARTiSM00407. IGc1. 2 hits.
    [Graphical view]
    PROSITEiPS50835. IG_LIKE. 3 hits.
    PS00290. IG_MHC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P01876-1 [UniParc]FASTAAdd to Basket

    « Hide

    ASPTSPKVFP LSLCSTQPDG NVVIACLVQG FFPQEPLSVT WSESGQGVTA    50
    RNFPPSQDAS GDLYTTSSQL TLPATQCLAG KSVTCHVKHY TNPSQDVTVP 100
    CPVPSTPPTP SPSTPPTPSP SCCHPRLSLH RPALEDLLLG SEANLTCTLT 150
    GLRDASGVTF TWTPSSGKSA VQGPPERDLC GCYSVSSVLP GCAEPWNHGK 200
    TFTCTAAYPE SKTPLTATLS KSGNTFRPEV HLLPPPSEEL ALNELVTLTC 250
    LARGFSPKDV LVRWLQGSQE LPREKYLTWA SRQEPSQGTT TFAVTSILRV 300
    AAEDWKKGDT FSCMVGHEAL PLAFTQKTID RLAGKPTHVN VSVVMAEVDG 350
    TCY 353
    Length:353
    Mass (Da):37,655
    Last modified:February 1, 1991 - v2
    Checksum:iEBA11ECB7E85DB21
    GO

    Sequence cautioni

    The sequence AAC82528.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11
    Sequence conflicti163 – 1653TPS → PST AA sequence (PubMed:107164)Curated
    Sequence conflicti176 – 1761E → B AA sequence (PubMed:809331)Curated
    Sequence conflicti190 – 1901P → S AA sequence (PubMed:809331)Curated
    Sequence conflicti227 – 2271R → H AA sequence (PubMed:809331)Curated
    Sequence conflicti231 – 2311H → R AA sequence (PubMed:809331)Curated
    Sequence conflicti290 – 2901T → E AA sequence (PubMed:809331)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti176 – 1761E → D.
    Corresponds to variant rs1407 [ dbSNP | Ensembl ].
    VAR_014602

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J00220 Genomic DNA. Translation: AAC82528.1. Different initiation.
    PIRiA22360. A1HU.
    UniGeneiHs.699841.

    Genome annotation databases

    EnsembliENST00000390547; ENSP00000374989; ENSG00000211895.

    Polymorphism databases

    DMDMi113584.

    Keywords - Coding sequence diversityi

    Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Web resourcesi

    IMGT/GENE-DB

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J00220 Genomic DNA. Translation: AAC82528.1 . Different initiation.
    PIRi A22360. A1HU.
    UniGenei Hs.699841.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IGA X-ray - A/B 1-353 [» ]
    1OW0 X-ray 3.10 A/B 122-335 [» ]
    2QEJ X-ray 3.20 A/B 123-336 [» ]
    3CHN X-ray - A/B/C/D 2-353 [» ]
    ProteinModelPortali P01876.
    SMRi P01876. Positions 1-102, 123-331.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P01876. 44 interactions.
    STRINGi 9606.ENSP00000374989.

    Protein family/group databases

    MEROPSi I43.001.
    IMGTi Search...

    PTM databases

    PhosphoSitei P01876.

    Polymorphism databases

    DMDMi 113584.

    Proteomic databases

    PaxDbi P01876.
    PRIDEi P01876.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000390547 ; ENSP00000374989 ; ENSG00000211895 .

    Organism-specific databases

    GeneCardsi GC14M106171.
    HGNCi HGNC:5478. IGHA1.
    MIMi 146900. gene.
    neXtProti NX_P01876.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG27314.
    HOVERGENi HBG005814.
    InParanoidi P01876.
    OMAi EVDGTCY.
    PhylomeDBi P01876.
    TreeFami TF334176.

    Enzyme and pathway databases

    Reactomei REACT_160163. Scavenging of heme from plasma.

    Miscellaneous databases

    EvolutionaryTracei P01876.
    PROi P01876.
    SOURCEi Search...

    Gene expression databases

    Bgeei P01876.
    Genevestigatori P01876.

    Family and domain databases

    Gene3Di 2.60.40.10. 3 hits.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003006. Ig/MHC_CS.
    IPR003597. Ig_C1-set.
    [Graphical view ]
    Pfami PF07654. C1-set. 2 hits.
    [Graphical view ]
    SMARTi SM00407. IGc1. 2 hits.
    [Graphical view ]
    PROSITEi PS50835. IG_LIKE. 3 hits.
    PS00290. IG_MHC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Mechanisms of divergence and convergence of the human immunoglobulin alpha 1 and alpha 2 constant region gene sequences."
      Flanagan J.G., Lefranc M.-P., Rabbitts T.H.
      Cell 36:681-688(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Primary structure of a human IgA1 immunoglobulin. IV. Streptococcal IgA1 protease, digestion, Fab and Fc fragments, and the complete amino acid sequence of the alpha 1 heavy chain."
      Putnam F.W., Liu Y.-S.V., Low T.L.K.
      J. Biol. Chem. 254:2865-2874(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE (MYELOMA PROTEIN BUR), DISULFIDE BONDS.
    3. "The primary structure of a monoclonal IgA-immunoglobulin (IgA Tro.), II. The amino acid sequence of the H-chain, alpha-type, subgroup III; structure of the complete IgA-molecule."
      Kratzin H., Altevogt P., Ruban E., Kortt A., Staroscik K., Hilschmann N.
      Hoppe-Seyler's Z. Physiol. Chem. 356:1337-1342(1975) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE (MYELOMA PROTEIN TRO).
    4. "Rule of antibody structure. Primary structure of a human monoclonal IgA-immunoglobulin (myeloma protein Tro). VII. Purification and characterization of the disulfide bridges."
      Yang C.-Y., Kratzin H., Gotz H., Hilschmann N.
      Hoppe-Seyler's Z. Physiol. Chem. 360:1919-1940(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BONDS.
    5. "Location of a novel type of interpolypeptide chain linkage in the human protein HC-IgA complex (HC-IgA) and identification of a heterogeneous chromophore associated with the complex."
      Calero M., Escribano J., Grubb A., Mendez E.
      J. Biol. Chem. 269:384-389(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 345-353, BINDING TO CHROMOPHORE.
    6. "The structure and function of human IgA."
      Kerr M.A.
      Biochem. J. 271:285-296(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    7. "IRTA1 and IRTA2, novel immunoglobulin superfamily receptors expressed in B cells and involved in chromosome 1q21 abnormalities in B cell malignancy."
      Hatzivassiliou G., Miller I., Takizawa J., Palanisamy N., Rao P.H., Iida S., Tagawa S., Taniwaki M., Russo J., Neri A., Cattoretti G., Clynes R., Mendelsohn C., Chaganti R.S.K., Dalla-Favera R.
      Immunity 14:277-289(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH FCRL4.
    8. Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-144.
      Tissue: Bile.
    9. Cited for: GLYCOSYLATION AT ASN-144 AND ASN-340.
    10. "Enrichment of glycopeptides for glycan structure and attachment site identification."
      Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.
      Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-144, STRUCTURE OF CARBOHYDRATES.
      Tissue: Cerebrospinal fluid.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
      Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
      Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-144, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiIGHA1_HUMAN
    AccessioniPrimary (citable) accession number: P01876
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 149 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3