SIA4A_CHICK
ID SIA4A_CHICK Reviewed; 342 AA.
AC Q11200;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1;
DE Short=Alpha 2,3-ST 1;
DE Short=Beta-galactoside alpha-2,3-sialyltransferase 1;
DE EC=2.4.99.4 {ECO:0000250|UniProtKB:P54751};
DE AltName: Full=Gal-NAc6S;
DE AltName: Full=Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase;
DE AltName: Full=ST3Gal I;
DE Short=ST3GalI;
DE AltName: Full=ST3GalA.1;
DE AltName: Full=ST3O;
DE AltName: Full=Sialyltransferase 4A;
DE Short=SIAT4-A;
GN Name=ST3GAL1; Synonyms=SIAT4A;
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].
RC TISSUE=Embryonic brain;
RX PubMed=7766661; DOI=10.1016/0304-4165(95)00012-z;
RA Kurosawa N., Hamamoto T., Inoue M., Tsuji S.;
RT "Molecular cloning and expression of chick Gal beta 1,3GalNAc alpha 2,3-
RT sialyltransferase.";
RL Biochim. Biophys. Acta 1244:216-222(1995).
CC -!- FUNCTION: Responsible for the synthesis of the sequence NeuAc-alpha-
CC 2,3-Gal-beta-1,3-GalNAc- found on sugar chains O-linked to Thr or Ser
CC and also as a terminal sequence on certain gangliosides. SIAT4A and
CC SIAT4B sialylate the same acceptor substrates but exhibit different Km
CC values. {ECO:0000250|UniProtKB:P54751}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl
CC derivative + CMP-N-acetyl-beta-neuraminate = an N-acetyl-alpha-
CC neuraminyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl derivative + CMP + H(+); Xref=Rhea:RHEA:21616,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:133470, ChEBI:CHEBI:139596; EC=2.4.99.4;
CC Evidence={ECO:0000250|UniProtKB:P54751};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-
CC pass type II membrane protein. Secreted. Note=Membrane-bound form in
CC trans cisternae of Golgi. Secreted into the body fluid.
CC -!- DEVELOPMENTAL STAGE: Expressed in early embryonic stages.
CC -!- PTM: The soluble form derives from the membrane form by proteolytic
CC processing.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
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DR EMBL; X80503; CAA56666.1; -; mRNA.
DR PIR; S55675; S55675.
DR RefSeq; NP_990548.1; NM_205217.1.
DR RefSeq; XP_015138567.1; XM_015283081.1.
DR AlphaFoldDB; Q11200; -.
DR SMR; Q11200; -.
DR STRING; 9031.ENSGALP00000026083; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR PaxDb; Q11200; -.
DR Ensembl; ENSGALT00000049825; ENSGALP00000051730; ENSGALG00000037773.
DR GeneID; 396140; -.
DR KEGG; gga:396140; -.
DR CTD; 6482; -.
DR VEuPathDB; HostDB:geneid_396140; -.
DR eggNOG; KOG2692; Eukaryota.
DR GeneTree; ENSGT00940000154725; -.
DR HOGENOM; CLU_032020_2_1_1; -.
DR InParanoid; Q11200; -.
DR OMA; LLNYTHQ; -.
DR OrthoDB; 891104at2759; -.
DR PhylomeDB; Q11200; -.
DR TreeFam; TF354325; -.
DR BRENDA; 2.4.99.2; 1306.
DR Reactome; R-GGA-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-GGA-4085001; Sialic acid metabolism.
DR Reactome; R-GGA-977068; Termination of O-glycan biosynthesis.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q11200; -.
DR Proteomes; UP000000539; Chromosome 2.
DR Bgee; ENSGALG00000037773; Expressed in muscle tissue and 13 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0003836; F:beta-galactoside (CMP) alpha-2,3-sialyltransferase activity; ISS:UniProtKB.
DR GO; GO:0010706; P:ganglioside biosynthetic process via lactosylceramide; IBA:GO_Central.
DR GO; GO:0006054; P:N-acetylneuraminate metabolic process; ISS:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISS:UniProtKB.
DR GO; GO:0097503; P:sialylation; ISS:UniProtKB.
DR Gene3D; 3.90.1480.20; -; 1.
DR InterPro; IPR001675; Glyco_trans_29.
DR InterPro; IPR038578; GT29-like_sf.
DR InterPro; IPR012163; Sialyl_trans.
DR Pfam; PF00777; Glyco_transf_29; 1.
DR PIRSF; PIRSF005557; Sialyl_trans; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Membrane; Reference proteome; Secreted; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..342
FT /note="CMP-N-acetylneuraminate-beta-galactosamide-alpha-
FT 2,3-sialyltransferase 1"
FT /id="PRO_0000149257"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..342
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 272
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 301
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
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 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 61..66
FT /evidence="ECO:0000250"
FT DISULFID 63..141
FT /evidence="ECO:0000250"
FT DISULFID 144..283
FT /evidence="ECO:0000250"
SQ SEQUENCE 342 AA; 39540 MW; 59E657652F4FE949 CRC64;
MVTVRKRNVK VFTFAFVLIT VTSFLLNYKH QVTMTTWDPK HIISQFSEQV RKLIKFPRRP
CSCSTCISEL GHSLWFDQRF NSTMQPFLTS QNALIPEDSY RWWLKLQGEK SPKNINDTLK
ELFGIIPGDR DPLQERGTFS CRRCAVVGNS GNLRQSQYGQ DIDSHDFVLR MNRAPTIGYE
SDVGSKTTHH FVYPESYKEL AENVSMIVIP FKTLDLRWIV TALTTGTINF TYVPVPRKIK
VRKEKVLIYN PSFIKYVYEN WLQNHGRYPS TGLLSVIFAL HVCDEVNVYG FGADSKGHWH
HYWENNASAG AFRQTGVHDG DFEFNVTLTL ASIEKIKFFK GR
