ID   IGHA1_GORGO             Reviewed;         353 AA.
AC   P20758;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Ig alpha-1 chain C region;
GN   Name=IGHA1;
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Lymph node;
RX   PubMed=2506527; DOI=10.1093/nar/17.16.6732;
RA   Kawamura S., Omoto K., Ueda S.;
RT   "Nucleotide sequence of the gorilla immunoglobulin alpha 1 gene.";
RL   Nucleic Acids Res. 17:6732-6732(1989).
CC   -!- FUNCTION: Ig alpha is the major immunoglobulin class in body
CC       secretions. It may serve both to defend against local infection and to
CC       prevent access of foreign antigens to the general immunologic system
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Monomeric or polymeric. {ECO:0000250}.
CC   -!- PTM: 3-Hydroxykynurenine, an oxidized tryptophan metabolite that is
CC       common in biological fluids, reacts with alpha-1-microglobulin to form
CC       heterogeneous polycyclic chromophores including hydroxanthommatin. The
CC       chromophore reacts with accessible cysteines forming non-reducible
CC       thioether cross-links with Ig alpha-1 chain C region Cys-352 (By
CC       similarity). {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA33147.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X15045; CAA33147.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; P20758; -.
DR   SMR; P20758; -.
DR   STRING; 9593.ENSGGOP00000028297; -.
DR   PRIDE; P20758; -.
DR   eggNOG; ENOG502R54U; Eukaryota.
DR   InParanoid; P20758; -.
DR   Proteomes; UP000001519; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0003823; F:antigen binding; IBA:GO_Central.
DR   GO; GO:0050776; P:regulation of immune response; IBA:GO_Central.
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   InterPro; IPR013151; Immunoglobulin.
DR   Pfam; PF07654; C1-set; 2.
DR   Pfam; PF00047; ig; 1.
DR   SMART; SM00407; IGc1; 2.
DR   SUPFAM; SSF48726; SSF48726; 3.
DR   PROSITE; PS50835; IG_LIKE; 3.
DR   PROSITE; PS00290; IG_MHC; 1.
PE   1: Evidence at protein level;
KW   Chromophore; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW   Reference proteome; Repeat.
FT   CHAIN           <1..353
FT                   /note="Ig alpha-1 chain C region"
FT                   /id="PRO_0000153565"
FT   DOMAIN          6..98
FT                   /note="Ig-like 1"
FT   DOMAIN          125..220
FT                   /note="Ig-like 2"
FT   DOMAIN          228..330
FT                   /note="Ig-like 3"
FT   REGION          96..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..121
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         352
FT                   /ligand="3-hydroxy-L-kynurenine"
FT                   /ligand_id="ChEBI:CHEBI:58125"
FT                   /ligand_note="multimeric 3-hydroxykynurenine chromophore"
FT                   /note="covalent; in form alpha-1-microglobulin complex"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        144
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        340
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        14
FT                   /note="Interchain (with light chain)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        26..85
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        77..101
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        122
FT                   /note="Interchain (with heavy chain)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        123..180
FT                   /note="Or C-123 with C-182"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        147..204
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        182
FT                   /note="Interchain (with heavy chain) (or with C-180)"
FT   DISULFID        192
FT                   /note="Interchain (with heavy chain of another subunit)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        250..313
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        352
FT                   /note="Interchain (with J chain); in oligomeric form"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   NON_TER         1
SQ   SEQUENCE   353 AA;  37756 MW;  4820E8DB02AC7514 CRC64;
     ASPTSPKVFP LSLCSTQPDG DVVVACLVQG FFPQEPLSVT WSESGQGVTA RNFPPSQDAS
     GDLYTTSSQL TLPATQCPDG KSVTCHVNHY TNPSQDVTVP CRVPSTPPTP SPSTPPTPSP
     PCCHPRLSLH RPALEDLLLG SEANLTCTLT GLRDASGVTF TWTPSSGKSA VEGPPERDLC
     GCYSVSSVLP GCAEPWNHGK TFTCTAAYPE SKTPLTATLS KSGNMFRPEV HLLPPPSEEL
     ALNELVTLTC LARGFSPKDV LVRWLQGSQE LPREKYLTWA SRQEPSQGTT TFAVTSILRV
     AAEDWKKGDT FSCMVGHEAL PLAFTQKTID RLAGKPTHVN VSVVMAEVDG TCY