SIAT1_CHICK
ID SIAT1_CHICK Reviewed; 413 AA.
AC Q92182;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Beta-galactoside alpha-2,6-sialyltransferase 1;
DE Short=Alpha 2,6-ST 1;
DE EC=2.4.99.1 {ECO:0000269|PubMed:8307003};
DE AltName: Full=CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase 1;
DE AltName: Full=ST6Gal I;
DE Short=ST6GalI;
DE AltName: Full=Sialyltransferase 1;
GN Name=ST6GAL1; Synonyms=SIAT1;
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, PATHWAY, CATALYTIC ACTIVITY, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Embryo;
RX PubMed=8307003; DOI=10.1111/j.1432-1033.1994.tb19949.x;
RA Kurosawa N., Kawasaki M., Hamamoto T., Nakaoka T., Lee Y.-C., Arita M.,
RA Tsuji S.;
RT "Molecular cloning and expression of chick embryo Gal beta 1,4GlcNAc alpha
RT 2,6-sialyltransferase. Comparison with the mammalian enzyme.";
RL Eur. J. Biochem. 219:375-381(1994).
CC -!- FUNCTION: Transfers sialic acid from CMP-sialic acid to galactose-
CC containing acceptor substrates. {ECO:0000269|PubMed:8307003}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactoside + CMP-N-acetyl-beta-neuraminate = an N-
CC acetyl-alpha-neuraminyl-(2->6)-beta-D-galactosyl derivative + CMP +
CC H(+); Xref=Rhea:RHEA:52104, ChEBI:CHEBI:15378, ChEBI:CHEBI:28034,
CC ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:136398;
CC EC=2.4.99.1; Evidence={ECO:0000269|PubMed:8307003};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:8307003}.
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000250|UniProtKB:P15907}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000250|UniProtKB:P15907}; Single-pass type II membrane protein.
CC Secreted. Note=Membrane-bound form in trans cisternae of Golgi.
CC Secreted into the body fluid.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, brain and liver and to
CC a lesser extent in lung and heart. {ECO:0000269|PubMed:8307003}.
CC -!- PTM: The soluble form derives from the membrane form by proteolytic
CC processing. {ECO:0000250|UniProtKB:P13721}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P13721}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
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DR EMBL; X75558; CAA53235.1; -; mRNA.
DR PIR; S41114; S41114.
DR RefSeq; NP_990572.1; NM_205241.1.
DR AlphaFoldDB; Q92182; -.
DR SMR; Q92182; -.
DR STRING; 9031.ENSGALP00000008889; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR PaxDb; Q92182; -.
DR GeneID; 396169; -.
DR KEGG; gga:396169; -.
DR CTD; 6480; -.
DR VEuPathDB; HostDB:geneid_396169; -.
DR eggNOG; KOG2692; Eukaryota.
DR InParanoid; Q92182; -.
DR OrthoDB; 494294at2759; -.
DR PhylomeDB; Q92182; -.
DR BRENDA; 2.4.99.1; 1306.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q92182; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003835; F:beta-galactoside alpha-2,6-sialyltransferase activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0006054; P:N-acetylneuraminate metabolic process; ISS:UniProtKB.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; 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 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Membrane; Reference proteome; Secreted; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..413
FT /note="Beta-galactoside alpha-2,6-sialyltransferase 1"
FT /id="PRO_0000149252"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..413
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15907"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15907"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15907"
FT BINDING 329..331
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15907"
FT BINDING 360
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15907"
FT BINDING 372
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15907"
FT BINDING 376
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 377
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15907"
FT BINDING 383
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15907"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 148..413
FT /evidence="ECO:0000250|UniProtKB:P15907"
FT DISULFID 190..342
FT /evidence="ECO:0000250|UniProtKB:P15907"
FT DISULFID 360..371
FT /evidence="ECO:0000250|UniProtKB:P15907"
SQ SEQUENCE 413 AA; 47393 MW; 19B8CCD361ED137D CRC64;
MVHINVLKKF MCVLVVILIA LTVCLWKETR GSYYVPLKND GTQVHRALDK WNLLKSQGLL
HEAAGEMGQM PKALPNNQNK VKGITSGAVE KSRKAAEHVK VWDKDSSSRN LIPRLQKVRK
NYLSMNKYNV TYNGKMNAAK LSPEQLLCRL RDRVNVTMIR GSDGPFNSSE WQHYLPDKSL
NETVGRLGRC AVVSSAGSLK SSHLGPEIDS HDAVLRFNGA PVKGFQEDVG QKTTIRLVNS
QLVTVEEQQF LKDALYNTGI LIVWDPAPYH AEIHEWYRKP DYKFFEAYKS YRIRHPEQPF
YILNPKMQWQ LWDILQENSL EHIQPNPPSS GMLGIVIMMT LCDEVDVYEF LPSKRQTDIC
HYYQKFHDHA CTMGAYHPLL FEKNLVKHLN QGTDEDIYTH GKVTLPGFRN VHC
