IGHA_EQUAS
ID IGHA_EQUAS Reviewed; 346 AA.
AC P0DUB3;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 07-OCT-2020, sequence version 1.
DT 25-MAY-2022, entry version 4.
DE RecName: Full=Immunoglobulin heavy constant alpha;
DE AltName: Full=Ig alpha chain C region {ECO:0000303|PubMed:32251747};
DE AltName: Full=IgA constant region {ECO:0000303|PubMed:32251747};
DE Flags: Fragment;
GN Name=IGHA;
OS Equus asinus (Donkey) (Equus africanus asinus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9793;
RN [1]
RP IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION AT ASN-134 AND ASN-333,
RP AND SUBCELLULAR LOCATION.
RX PubMed=32251747; DOI=10.1016/j.ijbiomac.2020.03.253;
RA Gnanesh Kumar B.S., Rawal A.;
RT "Sequence characterization and N-glycoproteomics of secretory
RT immunoglobulin A from donkey milk.";
RL Int. J. Biol. Macromol. 155:605-613(2020).
RN [2]
RP PROTEIN SEQUENCE OF 15-41; 252-263; 267-276; 300-320 AND 325-346,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=21645650; DOI=10.1016/j.jprot.2011.05.036;
RA Cunsolo V., Muccilli V., Fasoli E., Saletti R., Righetti P.G., Foti S.;
RT "Poppea's bath liquor: the secret proteome of she-donkey's milk.";
RL J. Proteomics 74:2083-2099(2011).
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. The antigen binding site is formed by the variable domain of
CC one heavy chain, together with that of its associated light chain.
CC Thus, each immunoglobulin has two antigen binding sites with remarkable
CC affinity for a particular antigen. The variable domains are assembled
CC by a process called V-(D)-J rearrangement and can then be subjected to
CC somatic hypermutations which, after exposure to antigen and selection,
CC allow affinity maturation for a particular antigen. Ig alpha is the
CC major immunoglobulin class in body secretions.
CC {ECO:0000250|UniProtKB:P01876, ECO:0000250|UniProtKB:P01877}.
CC -!- SUBUNIT: Immunoglobulins are composed of two identical heavy chains and
CC two identical light chains; disulfide-linked. Monomeric or polymeric.
CC Part of the secretory IgA (sIgA) complex that consists of two, four or
CC five IgA monomers, and two additional non-Ig polypeptides, namely the
CC JCHAIN and the secretory component (the proteoytic product of PIGR).
CC {ECO:0000250|UniProtKB:P01876, ECO:0000250|UniProtKB:P01877}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21645650,
CC ECO:0000269|PubMed:32251747}. Cell membrane
CC {ECO:0000250|UniProtKB:P01876, ECO:0000250|UniProtKB:P01877}.
CC -!- PTM: N-glycosylated. N-glycans attached to Asn-134 varies from
CC differentially fucosylated complex and hybrid to sialylated with N-
CC glycoyl neuraminic acid types: GlcNAc2Man3GlcNAc2(Fuc);
CC GlcNAc1Man4GlcNAc2(Fuc); GlcNAc1Man4GlcNAc2;
CC Gal1GlcNAc2Man3GlcNAc2(Fuc); GlcNAc2Man3GlcNAc2;
CC Gal1GlcNAc2Man3GlcNAc2; GlcNAc1Man3GlcNAc2; GlcNAc1Man2GlcNAc2 and
CC NeuGc1Gal1GlcNAc2Man3GlcNAc2(Fuc). N-glycans attached to Asn-333 are
CC mainly fucosylated complex types: GlcNAc2Man3GlcNAc2;
CC GlcNAc1Man3GlcNAc2; GlcNAc1Man3GlcNAc2(Fuc); GlcNAc2Man3GlcNAc2(Fuc);
CC Gal1GlcNAc2Man3GlcNAc2(Fuc); NeuGc1Gal1GlcNAc1Man3GlcNAc2(Fuc);
CC NeuGc1Gal1GlcNAc2Man3GlcNAc2(Fuc) and
CC NeuAc1Gal1GlcNAc2Man3GlcNAc2(Fuc). {ECO:0000269|PubMed:32251747}.
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DR AlphaFoldDB; P0DUB3; -.
DR SMR; P0DUB3; -.
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; -; 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; 3.
DR SMART; SM00407; IGc1; 3.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
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..346
FT /note="Immunoglobulin heavy constant alpha"
FT /id="PRO_0000451038"
FT DOMAIN 6..96
FT /note="Ig-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 118..212
FT /note="Ig-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 221..323
FT /note="Ig-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:32251747"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:32251747"
FT DISULFID 26..83
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 139..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 174
FT /note="Interchain (with heavy chain)"
FT /evidence="ECO:0000250|UniProtKB:P01876,
FT ECO:0000250|UniProtKB:P01877"
FT DISULFID 184
FT /note="Interchain (with heavy chain of another subunit) (or
FT with C-505 of PIGR/the secretory component)"
FT /evidence="ECO:0000250|UniProtKB:P01876,
FT ECO:0000250|UniProtKB:P01877"
FT DISULFID 243..306
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 345
FT /note="Interchain (with J chain); in oligomeric form"
FT /evidence="ECO:0000250|UniProtKB:P01876,
FT ECO:0000250|UniProtKB:P01877"
FT NON_TER 1
SQ SEQUENCE 346 AA; 37322 MW; E9D9D4C92CDA4B3F CRC64;
ASVTSPSIFP LSLRKADSGD PVVIACLIKG FFPLGFPEPV KVTWGKSGVV TNYLPSEAGG
LYTVISQLSL RADQCPDDAS VKCEVQHYTS PSKSVDVPCI VCPPPPPCPC ECLLSTVPRL
SLSPPAEDLL LSSNASLTCT LRGLRDPKGA TFTWSPSSGN VPVLQEPKLE PSGCYSVSSV
LPGCAEPWSK KETFSCTASH PELKKSQTVS ITKPKEPLFQ PQVHVLPPPS EELALNELVT
LTCLVRGFSP KEVLVLWLQG HEKLPREKYL VFKPLREPGQ SVPTFAVTSL LRVEAEAWLR
GDVFSCMVGH EALPLSFTQK SIDRLSGKPT HVNVSVVMAE ADGTCY
