IGA2_HUMAN
ID IGA2_HUMAN Reviewed; 455 AA.
AC P0DOX2;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-JUL-2018, sequence version 2.
DT 25-MAY-2022, entry version 20.
DE RecName: Full=Immunoglobulin alpha-2 heavy chain {ECO:0000305};
DE AltName: Full=Immunoglobulin alpha-2 heavy chain BUT {ECO:0000305|PubMed:416441};
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, AND DISULFIDE BOND.
RX PubMed=416441; DOI=10.1073/pnas.75.2.966;
RA Torano A., Putnam F.W.;
RT "Complete amino acid sequence of the alpha 2 heavy chain of a human IgA2
RT immunoglobulin of the A2m (2) allotype.";
RL Proc. Natl. Acad. Sci. U.S.A. 75:966-969(1978).
RN [2]
RP GLYCOSYLATION AT ASN-162; ASN-207 AND ASN-246 AND ASN-442.
RX PubMed=407576; DOI=10.1073/pnas.74.6.2301;
RA Torano A., Tsuzukida Y., Liu Y.S., Putnam F.W.;
RT "Location and structural significance of the oligosaccharides in human Ig-
RT A1 and IgA2 immunoglobulins.";
RL Proc. Natl. Acad. Sci. U.S.A. 74:2301-2305(1977).
RN [3]
RP REVIEW ON FUNCTION AND SUBUNIT.
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 [4]
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 [5]
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 [6]
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: Immunoglobulins, also known as antibodies, are membrane-bound
CC or 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:20176268, PubMed:17576170).
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). {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 -!- CAUTION: This sequence is an example of a full-length immunoglobulin
CC alpha-2 heavy chain. {ECO:0000305}.
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DR AlphaFoldDB; P0DOX2; -.
DR SMR; P0DOX2; -.
DR GlyConnect; 2961; 32 N-Linked glycans.
DR GlyConnect; 2962; 35 N-Linked glycans.
DR GlyConnect; 2963; 38 N-Linked glycans.
DR iPTMnet; P0DOX2; -.
DR PhosphoSitePlus; P0DOX2; -.
DR jPOST; P0DOX2; -.
DR PRIDE; P0DOX2; -.
DR Pharos; P0DOX2; Tdark.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0019814; C:immunoglobulin complex; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; -; 4.
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; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR013151; Immunoglobulin.
DR Pfam; PF07654; C1-set; 2.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 4.
DR SMART; SM00407; IGc1; 3.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 4.
DR PROSITE; PS50835; IG_LIKE; 4.
DR PROSITE; PS00290; IG_MHC; 2.
PE 1: Evidence at protein level;
KW Adaptive immunity; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Immunity; Immunoglobulin;
KW Immunoglobulin domain; Membrane; Repeat; Secreted.
FT CHAIN 1..455
FT /note="Immunoglobulin alpha-2 heavy chain"
FT /id="PRO_0000439283"
FT DOMAIN 1..95
FT /note="Ig-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 121..213
FT /note="Ig-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 227..322
FT /note="Ig-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 330..432
FT /note="Ig-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 1..115
FT /note="Variable (V) domain, involved in antigen
FT recognition"
FT /evidence="ECO:0000305|PubMed:416441"
FT REGION 116..455
FT /note="Constant (C) domain"
FT /evidence="ECO:0000305|PubMed:416441"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:416441"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:416441"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:416441"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:416441"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:416441"
FT DISULFID 22..95
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000303|PubMed:416441"
FT DISULFID 141..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000303|PubMed:416441"
FT DISULFID 216
FT /note="Interchain (with light chain)"
FT /evidence="ECO:0000303|PubMed:416441"
FT DISULFID 224
FT /note="Interchain (with heavy chain)"
FT /evidence="ECO:0000303|PubMed:416441"
FT DISULFID 225..282
FT /evidence="ECO:0000303|PubMed:416441"
FT DISULFID 249..306
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000303|PubMed:416441"
FT DISULFID 284
FT /note="Interchain (with heavy chain)"
FT /evidence="ECO:0000303|PubMed:416441"
FT DISULFID 294
FT /note="Interchain (with heavy chain of another subunit)"
FT /evidence="ECO:0000303|PubMed:416441"
FT DISULFID 352..415
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000303|PubMed:416441"
FT DISULFID 454
FT /note="Interchain (with J chain)"
FT /evidence="ECO:0000303|PubMed:416441"
SQ SEQUENCE 455 AA; 48934 MW; FCAFE11CBF1C57AE CRC64;
EVQLVETGGG LIQPGGSLRL SCAASGFTVS NHSMSWVRQA PGKALEWVSA IYRGGTTYYA
DSVKGRFTIS RDDSRNTVYL QMNSLRAEDT AVYYCARDLA AARLFGKGTT VTVSSASPTS
PKVFPLSLDS TPQDGNVVVA CLVQGFFPQE PLSVTWSESG QNVTARNFPP SQDASGDLYT
TSSQLTLPAT QCPDGKSVTC HVKHYTNSSQ DVTVPCRVPP PPPCCHPRLS LHRPALEDLL
LGSEANLTCT LTGLRDASGA TFTWTPSSGK SAVEGPPERD LCGCYSVSSV LPGCAQPWNH
GETFTCTAAH PELKTPLTAN ITKSGNTFRP EVHLLPPPSE ELALNELVTL TCLARGFSPK
DVLVRWLQGS QELPREKYLT WASRQEPSQG TTTYAVTSIL RVAAEDWKKG ETFSCMVGHE
ALPLAFTQKT IDRLAGKPTH INVSVVMAEA DGTCY
