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UniProtKB/Swiss-Prot entry P01876


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name IGHA1_HUMAN
Primary accession number P01876
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on February 1, 1991 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 92)
Name and origin of the protein
Protein name Ig alpha-1 chain C region
Synonyms None
Gene name
Name: IGHA1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0092-8674(84)90348-9; PubMed=6421489 [NCBI, ExPASy, EBI, Israel, Japan]
Flanagan J.G., Lefranc M.-P., Rabbitts T.H.;
"Mechanisms of divergence and convergence of the human immunoglobulin alpha 1 and alpha 2 constant region gene sequences.";
Cell 36:681-688(1984).
[2]
PROTEIN SEQUENCE (MYELOMA PROTEIN BUR), AND DISULFIDE BONDS.
PubMed=107164 [NCBI, ExPASy, EBI, Israel, Japan]
Putnam F.W., Liu Y.-S.V., Low T.L.K.;
"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.";
J. Biol. Chem. 254:2865-2874(1979).
[3]
PROTEIN SEQUENCE (MYELOMA PROTEIN TRO).
PubMed=809331 [NCBI, ExPASy, EBI, Israel, Japan]
Kratzin H., Altevogt P., Ruban E., Kortt A., Staroscik K., Hilschmann N.;
"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.";
Hoppe-Seyler's Z. Physiol. Chem. 356:1337-1342(1975).
[4]
DISULFIDE BONDS.
PubMed=393607 [NCBI, ExPASy, EBI, Israel, Japan]
Yang C.-Y., Kratzin H., Gotz H., Hilschmann N.;
"Rule of antibody structure. Primary structure of a human monoclonal IgA-immunoglobulin (myeloma protein Tro). VII. Purification and characterization of the disulfide bridges.";
Hoppe-Seyler's Z. Physiol. Chem. 360:1919-1940(1979).
[5]
PROTEIN SEQUENCE OF 345-353, AND BINDING TO CHROMOPHORE.
PubMed=7506257 [NCBI, ExPASy, EBI, Israel, Japan]
Calero M., Escribano J., Grubb A., Mendez E.;
"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.";
J. Biol. Chem. 269:384-389(1994).
[6]
REVIEW.
PubMed=2241915 [NCBI, ExPASy, EBI, Israel, Japan]
Kerr M.A.;
"The structure and function of human IgA.";
Biochem. J. 271:285-296(1990).
[7]
CHROMOSOMAL TRANSLOCATION WITH FCRL4.
DOI=10.1016/S1074-7613(01)00109-1; PubMed=11290337 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"IRTA1 and IRTA2, novel immunoglobulin superfamily receptors expressed in B cells and involved in chromosome 1q21 abnormalities in B cell malignancy.";
Immunity 14:277-289(2001).
[8]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-144, AND MASS SPECTROMETRY.
TISSUE=Bile;
DOI=10.1074/mcp.M400015-MCP200; PubMed=15084671 [NCBI, ExPASy, EBI, Israel, Japan]
Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.;
"A proteomic analysis of human bile.";
Mol. Cell. Proteomics 3:715-728(2004).
Comments
  • FUNCTION: 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.
  • SUBUNIT: Monomeric or polymeric.
  • INTERACTION:
    O14519:CDK2AP1; NbExp=1; IntAct=EBI-727651, EBI-1052532;
    Q96JB5:CDK5RAP3; NbExp=1; IntAct=EBI-727651, EBI-718818;
  • PTM: 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.
  • DISEASE: 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.
  • SIMILARITY: Contains 3 Ig-like (immunoglobulin-like) domains.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
J00220; AAC82528.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A22360; A1HU.
UniGene Hs.648398
3D structure databases
PDB
1IGA; X-ray; -; A/B=1-353.[ExPASy / RCSB / EBI]
1OW0; X-ray; 3.10 A; A/B=123-335.[ExPASy / RCSB / EBI]
2QEJ; X-ray; 3.20 A; A/B=123-336.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1IGA; -.
1OW0; -.
2QEJ; -.
ModBase P01876.
Protein-protein interaction databases
IntAct P01876; -.
Protein family/group databases
IMGT J00220.
Organism-specific databases
HGNC HGNC:5478; IGHA1.
GenAtlas IGHA1.
HPA CAB008641; -.
MIM 146900; gene. [NCBI / EBI]
PharmGKB PA29710; -.
GeneCards P01876.
Gene expression databases
ArrayExpress P01876; -.
GermOnline ENSG00000130076; Homo sapiens.
Ontologies
GO
GO:0003823; Molecular function: antigen binding (non-traceable author statement from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006955; Biological process: immune response (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR007110; Ig-like.
IPR013783; Ig-like_fold.
IPR003006; Ig/MHC_CS.
IPR003597; Ig_C1-set.
Graphical view of domain structure.
Gene3D G3DSA:2.60.40.10; Ig-like_fold; 3.
Pfam PF07654; C1-set; 2.
Pfam graphical view of domain structure.
SMART SM00407; IGc1; 2.
SMART graphical view of domain structure.
PROSITE PS50835; IG_LIKE; 3.
PS00290; IG_MHC; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P01876.
ProtoNet P01876.
Genome annotation databases
Ensembl ENSG00000211895; Homo sapiens. [Contig view]
Phylogenomic databases
HOVERGEN P01876; -.
Other
LinkHub P01876; -.
SOURCE IGHA1; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Chromophore; Chromosomal rearrangement; Direct protein sequencing; Glycoprotein; Immunoglobulin C region; Immunoglobulin domain; Polymorphism; Repeat.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   <1   353  >353     Ig alpha-1 chain C region. PRO_0000153566
DOMAIN   6    98  93     Ig-like 1. 
DOMAIN   125   220  96     Ig-like 2. 
DOMAIN   228   330  103     Ig-like 3. 
BINDING   352   352        Multimeric 3-hydroxykynurenine chromophore (covalent); in form alpha-1-microglobulin complex. 
CARBOHYD   105   105        O-linked (GalNAc...). 
CARBOHYD   111   111        O-linked (GalNAc...). 
CARBOHYD   113   113        O-linked (GalNAc...). 
CARBOHYD   119   119        O-linked (GalNAc...). 
CARBOHYD   121   121        O-linked (GalNAc...). 
CARBOHYD   144   144        N-linked (GlcNAc...). 
CARBOHYD   340   340        N-linked (GlcNAc...). 
DISULFID   14    14        Interchain (with light chain). 
DISULFID   26    85         
DISULFID   77   101         
DISULFID   122   122        Interchain (with heavy chain). 
DISULFID   123   180        Or C-123 with C-182. 
DISULFID   147   204         
DISULFID   182   182        Interchain (with heavy chain) (or with C-180). 
DISULFID   192   192        Interchain (with heavy chain of another subunit) (Probable). 
DISULFID   250   313         
DISULFID   352   352        Interchain (with J chain); in oligomeric form. 
VARIANT   176   176  1     E -> D (in dbSNP:rs1407 [NCBI]). VAR_014602 
CONFLICT   163   165        TPS -> PST (in Ref. 2; AA sequence). 
CONFLICT   176   176        E -> B (in Ref. 3; AA sequence). 
CONFLICT   190   190        P -> S (in Ref. 3; AA sequence). 
CONFLICT   227   227        R -> H (in Ref. 3; AA sequence). 
CONFLICT   231   231        H -> R (in Ref. 3; AA sequence). 
CONFLICT   290   290        T -> E (in Ref. 3; AA sequence). 
NON_TER   1     1         
STRAND   128   130  3      
HELIX   134   139  6      
STRAND   146   149  4      
STRAND   162   164  3      
STRAND   185   188  4      
TURN   190   192  3      
HELIX   193   198  6      
STRAND   201   206  6      
STRAND   215   220  6      
STRAND   229   233  5      
TURN   237   241  5      
STRAND   242   258  17      
STRAND   261   266  6      
HELIX   273   275  3      
STRAND   276   278  3      
STRAND   287   289  3      
STRAND   292   301  10      
HELIX   302   307  6      
STRAND   311   316  6      
STRAND   323   325  3      
Sequence information
Length: 353 AA [This is the length of the unprocessed precursor] Molecular weight: 37655 Da [This is the MW of the unprocessed precursor] CRC64: EBA11ECB7E85DB21 [This is a checksum on the sequence]
        10         20         30         40         50         60 
ASPTSPKVFP LSLCSTQPDG NVVIACLVQG FFPQEPLSVT WSESGQGVTA RNFPPSQDAS 

        70         80         90        100        110        120 
GDLYTTSSQL TLPATQCLAG KSVTCHVKHY TNPSQDVTVP CPVPSTPPTP SPSTPPTPSP 

       130        140        150        160        170        180 
SCCHPRLSLH RPALEDLLLG SEANLTCTLT GLRDASGVTF TWTPSSGKSA VQGPPERDLC 

       190        200        210        220        230        240 
GCYSVSSVLP GCAEPWNHGK TFTCTAAYPE SKTPLTATLS KSGNTFRPEV HLLPPPSEEL 

       250        260        270        280        290        300 
ALNELVTLTC LARGFSPKDV LVRWLQGSQE LPREKYLTWA SRQEPSQGTT TFAVTSILRV 

       310        320        330        340        350 
AAEDWKKGDT FSCMVGHEAL PLAFTQKTID RLAGKPTHVN VSVVMAEVDG TCY 

P01876 in FASTA format

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