SIA7A_CHICK
ID SIA7A_CHICK Reviewed; 566 AA.
AC Q92183;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 1;
DE EC=2.4.99.3 {ECO:0000269|PubMed:8288607};
DE AltName: Full=GalNAc alpha-2,6-sialyltransferase I;
DE AltName: Full=ST6GalNAc I;
DE Short=ST6GalNAcI;
DE AltName: Full=Sialyltransferase 7A;
DE Short=SIAT7-A;
GN Name=ST6GALNAC1; Synonyms=SIAT7A;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=8288607; DOI=10.1016/s0021-9258(17)42272-1;
RA Kurosawa N., Hamamoto T., Lee Y.-C., Nakaoka T., Kojima N., Tsuji S.;
RT "Molecular cloning and expression of GalNAc alpha 2,6-sialyltransferase.";
RL J. Biol. Chem. 269:1402-1409(1994).
CC -!- FUNCTION: Protein sialyltransferase specifically expressed in goblet
CC cells that plays a key role in intestinal host-commensal homeostasis
CC (By similarity). Conjugates sialic acid with an alpha-2-6 linkage to N-
CC acetylgalactosamine (GalNAc) glycan chains linked to serine or
CC threonine in glycoproteins (PubMed:8288607).
CC {ECO:0000250|UniProtKB:Q9NSC7, ECO:0000269|PubMed:8288607}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl
CC derivative + CMP-N-acetyl-beta-neuraminate = a beta-D-galactosyl-
CC (1->3)-[N-acetyl-alpha-neuraminyl-(2->6)]-N-acetyl-alpha-D-
CC galactosaminyl derivative + CMP + H(+); Xref=Rhea:RHEA:11136,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:133470, ChEBI:CHEBI:140764; EC=2.4.99.3;
CC Evidence={ECO:0000269|PubMed:8288607};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11137;
CC Evidence={ECO:0000269|PubMed:8288607};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:8288607}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9NSC7}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q9NSC7}.
CC -!- TISSUE SPECIFICITY: Heart, kidney, testes, brain, liver and lung.
CC {ECO:0000269|PubMed:8288607}.
CC -!- DEVELOPMENTAL STAGE: Embryo. {ECO:0000269|PubMed:8288607}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
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DR EMBL; X74946; CAA52902.1; -; mRNA.
DR PIR; A49880; A49880.
DR RefSeq; NP_990571.1; NM_205240.1.
DR AlphaFoldDB; Q92183; -.
DR SMR; Q92183; -.
DR STRING; 9031.ENSGALP00000002878; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR PaxDb; Q92183; -.
DR Ensembl; ENSGALT00000002882; ENSGALP00000002878; ENSGALG00000001862.
DR GeneID; 396168; -.
DR KEGG; gga:396168; -.
DR CTD; 55808; -.
DR VEuPathDB; HostDB:geneid_396168; -.
DR eggNOG; KOG2692; Eukaryota.
DR GeneTree; ENSGT00940000159930; -.
DR HOGENOM; CLU_032020_4_1_1; -.
DR InParanoid; Q92183; -.
DR OMA; DKYLVVH; -.
DR OrthoDB; 891104at2759; -.
DR PhylomeDB; Q92183; -.
DR TreeFam; TF354325; -.
DR Reactome; R-GGA-4085001; Sialic acid metabolism.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q92183; -.
DR Proteomes; UP000000539; Chromosome 18.
DR Bgee; ENSGALG00000001862; Expressed in colon and 8 other tissues.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0001665; F:alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016740; F:transferase activity; IBA:GO_Central.
DR GO; GO:0048874; P:host-mediated regulation of intestinal microbiota composition; ISS:UniProtKB.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IDA:UniProtKB.
DR Gene3D; 3.90.1480.20; -; 1.
DR InterPro; IPR001675; Glyco_trans_29.
DR InterPro; IPR038578; GT29-like_sf.
DR Pfam; PF00777; Glyco_transf_29; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Membrane; Reference proteome; Repeat; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..566
FT /note="Alpha-N-acetylgalactosaminide alpha-2,6-
FT sialyltransferase 1"
FT /id="PRO_0000149271"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..566
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REPEAT 247..254
FT /note="1"
FT REPEAT 330..337
FT /note="2"
FT REGION 138..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..337
FT /note="2 X 8 AA repeats of S-S-S-X-V-S-T-C"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 254..337
FT /evidence="ECO:0000250|UniProtKB:Q9UJ37"
FT DISULFID 340..508
FT /evidence="ECO:0000250|UniProtKB:Q9UJ37"
SQ SEQUENCE 566 AA; 64781 MW; E529CA94027757DF CRC64;
MGFLIRRLPK DSRIFRWLLI LTVFSFIITS FSALFGMEKS IFRQLKIYQS IAHMLQVDTQ
DQQGSNYSAN GRISKVGLER DIAWLELNTA VSTPSGEGKE EQKKTVKPVA KVEEAKEKVT
VKPFPEVMGI TNTTASTASV VERTKEKTTA RPVPGVGEAD GKRTTIALPS MKEDKEKATV
KPSFGMKVAH ANSTSKDKPK AEEPPASVKA IRPVTQAATV TEKKKLRAAD FKTEPQWDFD
DEYILDSSSP VSTCSESVRA KAAKSDWLRD LFLPNITLFI DKSYFNVSEW DRLEHFAPPY
GFMELNYSLV EEVMSRLPPN PHQQLLLANS SSNVSTCISC AVVGNGGILN NSGMGQEIDS
HDYVFRVSGA VIKGYEKDVG TKTSFYGFTA YSLVSSLQNL GHKGFKKIPQ GKHIRYIHFL
EAVRDYEWLK ALLLDKDIRK GFLNYYGRRP RERFDEDFTM NKYLVAHPDF LRYLKNRFLK
SKNLQKPYWR LYRPTTGALL LLTALHLCDR VSAYGYITEG HQKYSDHYYD KEWKRLVFYV
NHDFNLEKQV WKRLHDENIM KLYQRS
