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Protein

Ig alpha-2 chain C region

Gene

IGHA2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.

GO - Molecular functioni

  • antigen binding Source: UniProtKB

GO - Biological processi

  • antibacterial humoral response Source: UniProtKB
  • B cell receptor signaling pathway Source: GO_Central
  • complement activation, classical pathway Source: GO_Central
  • glomerular filtration Source: UniProtKB
  • immune response Source: UniProtKB
  • innate immune response Source: GO_Central
  • phagocytosis, engulfment Source: GO_Central
  • phagocytosis, recognition Source: GO_Central
  • positive regulation of B cell activation Source: GO_Central
  • positive regulation of respiratory burst Source: UniProtKB
  • receptor-mediated endocytosis Source: Reactome
  • retina homeostasis Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-HSA-2168880. Scavenging of heme from plasma.

Names & Taxonomyi

Protein namesi
Recommended name:
Ig alpha-2 chain C region
Gene namesi
Name:IGHA2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:5479. IGHA2.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • external side of plasma membrane Source: GO_Central
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • monomeric IgA immunoglobulin complex Source: UniProtKB
  • secretory dimeric IgA immunoglobulin complex Source: UniProtKB
  • secretory IgA immunoglobulin complex Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Polymorphism and mutation databases

DMDMi218512088.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 340›340Ig alpha-2 chain C regionPRO_0000153567Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 ↔ 85Curated
Glycosylationi47 – 471N-linked (GlcNAc...)1 Publication
Glycosylationi92 – 921N-linked (GlcNAc...) (complex)2 Publications
Disulfide bondi101 – 101Interchain (with light chain)Curated
Disulfide bondi109 – 109Interchain (with heavy chain)Curated
Disulfide bondi110 ↔ 167Curated
Glycosylationi131 – 1311N-linked (GlcNAc...)2 Publications
Disulfide bondi134 ↔ 191Curated
Disulfide bondi169 – 169Interchain (with heavy chain)Curated
Disulfide bondi179 – 179Interchain (with heavy chain of another subunit)PROSITE-ProRule annotation
Glycosylationi205 – 2051N-linked (GlcNAc...) (complex)5 Publications
Disulfide bondi237 ↔ 300Curated
Glycosylationi327 – 3271N-linked (GlcNAc...) (complex)3 Publications
Disulfide bondi339 – 339Interchain (with J chain)Curated

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiP01877.
MaxQBiP01877.
PeptideAtlasiP01877.
PRIDEiP01877.

PTM databases

iPTMnetiP01877.
PhosphoSiteiP01877.
UniCarbKBiP01877.

Interactioni

Subunit structurei

Monomeric or polymeric.

Protein-protein interaction databases

IntActiP01877. 19 interactions.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CM9X-ray-A/B/C/D2-340[»]
ProteinModelPortaliP01877.
SMRiP01877. Positions 1-102, 110-318.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 9893Ig-like 1Add
BLAST
Domaini112 – 20796Ig-like 2Add
BLAST
Domaini215 – 317103Ig-like 3Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin C region, Immunoglobulin domain, Repeat

Phylogenomic databases

HOVERGENiHBG005814.
InParanoidiP01877.
PhylomeDBiP01877.

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.
IPR013151. Immunoglobulin.
[Graphical view]
PfamiPF07654. C1-set. 2 hits.
PF00047. ig. 1 hit.
[Graphical view]
SMARTiSM00407. IGc1. 3 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 3 hits.
PROSITEiPS50835. IG_LIKE. 3 hits.
PS00290. IG_MHC. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P01877-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
ASPTSPKVFP LSLDSTPQDG NVVVACLVQG FFPQEPLSVT WSESGQNVTA
60 70 80 90 100
RNFPPSQDAS GDLYTTSSQL TLPATQCPDG KSVTCHVKHY TNPSQDVTVP
110 120 130 140 150
CPVPPPPPCC HPRLSLHRPA LEDLLLGSEA NLTCTLTGLR DASGATFTWT
160 170 180 190 200
PSSGKSAVQG PPERDLCGCY SVSSVLPGCA QPWNHGETFT CTAAHPELKT
210 220 230 240 250
PLTANITKSG NTFRPEVHLL PPPSEELALN ELVTLTCLAR GFSPKDVLVR
260 270 280 290 300
WLQGSQELPR EKYLTWASRQ EPSQGTTTFA VTSILRVAAE DWKKGDTFSC
310 320 330 340
MVGHEALPLA FTQKTIDRMA GKPTHVNVSV VMAEVDGTCY
Length:340
Mass (Da):36,526
Last modified:December 16, 2008 - v3
Checksum:i98922700756EE906
GO

Sequence cautioni

The sequence AAB59396.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Sequence conflicti319 – 3191M → L in AAB59396 (PubMed:6421489).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti93 – 931P → S in A2M(2) allotype.
VAR_003879
Natural varianti102 – 1021P → R in A2M(2) allotype.
VAR_003880
Natural varianti279 – 2791F → Y in A2M(2) allotype.
VAR_003881
Natural varianti296 – 2961D → E in A2M(2) allotype.
VAR_003882
Natural varianti326 – 3261V → I in A2M(2) allotype.
VAR_003883
Natural varianti335 – 3351V → A in A2M(2) allotype.
VAR_003884

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00221 Genomic DNA. Translation: AAB59396.1. Different initiation.
AL928742 Genomic DNA. No translation available.
PIRiB22360.
UniGeneiHs.699841.

Cross-referencesi

Web resourcesi

IMGT/GENE-DB

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00221 Genomic DNA. Translation: AAB59396.1. Different initiation.
AL928742 Genomic DNA. No translation available.
PIRiB22360.
UniGeneiHs.699841.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CM9X-ray-A/B/C/D2-340[»]
ProteinModelPortaliP01877.
SMRiP01877. Positions 1-102, 110-318.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP01877. 19 interactions.

Protein family/group databases

IMGTiSearch...
Search...

PTM databases

iPTMnetiP01877.
PhosphoSiteiP01877.
UniCarbKBiP01877.

Polymorphism and mutation databases

DMDMi218512088.

Proteomic databases

EPDiP01877.
MaxQBiP01877.
PeptideAtlasiP01877.
PRIDEiP01877.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

GeneCardsiIGHA2.
HGNCiHGNC:5479. IGHA2.
MIMi147000. gene.
neXtProtiNX_P01877.
GenAtlasiSearch...

Phylogenomic databases

HOVERGENiHBG005814.
InParanoidiP01877.
PhylomeDBiP01877.

Enzyme and pathway databases

ReactomeiR-HSA-2168880. Scavenging of heme from plasma.

Miscellaneous databases

PROiP01877.
SOURCEiSearch...

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.
IPR013151. Immunoglobulin.
[Graphical view]
PfamiPF07654. C1-set. 2 hits.
PF00047. ig. 1 hit.
[Graphical view]
SMARTiSM00407. IGc1. 3 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 3 hits.
PROSITEiPS50835. IG_LIKE. 3 hits.
PS00290. IG_MHC. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Complete amino acid sequence of the alpha 2 heavy chain of a human IgA2 immunoglobulin of the A2m (2) allotype."
    Torano A., Putnam F.W.
    Proc. Natl. Acad. Sci. U.S.A. 75:966-969(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE (BUT).
  4. "Structure of the A2m(1) allotype of human IgA -- a recombinant molecule."
    Tsuzukida Y., Wang C.-C., Putnam F.W.
    Proc. Natl. Acad. Sci. U.S.A. 76:1104-1108(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE (MYELOMA PROTEIN LAN).
  5. "The structure and function of human IgA."
    Kerr M.A.
    Biochem. J. 271:285-296(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  6. Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-205.
    Tissue: Bile.
  7. "Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
    Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
    Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-131 AND ASN-205.
    Tissue: Plasma.
  8. "Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry."
    Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.
    J. Proteome Res. 5:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-205 AND ASN-327.
    Tissue: Saliva.
  9. "Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry."
    Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.
    Proteomics 8:3833-3847(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-47; ASN-92; ASN-131; ASN-205 AND ASN-327.
    Tissue: Milk.
  10. Cited for: GLYCOSYLATION AT ASN-92; ASN-327 AND ASN-205.
  11. Kolarich D.
    Submitted (JUL-2009) to UniProtKB
    Cited for: LACK OF GLYCOSYLATION AT ASN-92.

Entry informationi

Entry nameiIGHA2_HUMAN
AccessioniPrimary (citable) accession number: P01877
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: December 16, 2008
Last modified: July 6, 2016
This is version 142 of the entry and version 3 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

Miscellaneous

The sequence of the A2m1 allotype is shown.

Caution

N-glycosylation was reported in milk on the non-canonical Asn-92 site (PubMed:18780401). However, according to Ref. 11, N-glycosylation from the same tissue was found to be absent at this site.1 Publication

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.