SIA8E_PANTR
ID SIA8E_PANTR Reviewed; 376 AA.
AC P61646;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Alpha-2,8-sialyltransferase 8E;
DE EC=2.4.99.-;
DE AltName: Full=Sialyltransferase 8E;
DE Short=SIAT8-E;
DE AltName: Full=Sialyltransferase St8Sia V;
DE Short=ST8SiaV;
GN Name=ST8SIA5; Synonyms=SIAT8E;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Harduin-Lepers A., Martinez-Duncker I., Mollicone R., Delannoy P.,
RA Oriol R.;
RT "Phylogeny of sialyltransferases.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the synthesis of gangliosides GD1c, GT1a, GQ1b,
CC GP1c and GT3 from GD1a, GT1b, GM1b and GD3 respectively.
CC {ECO:0000250|UniProtKB:O15466, ECO:0000250|UniProtKB:Q6ZXC8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GQ1c (d18:1(4E)) =
CC CMP + ganglioside GP1c (d18:1(4E)) + H(+); Xref=Rhea:RHEA:47592,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:87791, ChEBI:CHEBI:87792;
CC Evidence={ECO:0000250|UniProtKB:Q6ZXC8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47593;
CC Evidence={ECO:0000250|UniProtKB:Q6ZXC8};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:O15466}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q6ZXC8}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
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DR EMBL; AJ697662; CAG26900.1; -; mRNA.
DR RefSeq; NP_001009087.1; NM_001009087.1.
DR AlphaFoldDB; P61646; -.
DR SMR; P61646; -.
DR STRING; 9598.ENSPTRP00000016998; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR PaxDb; P61646; -.
DR Ensembl; ENSPTRT00000099353; ENSPTRP00000062453; ENSPTRG00000009997.
DR GeneID; 455402; -.
DR KEGG; ptr:455402; -.
DR CTD; 29906; -.
DR VGNC; VGNC:10459; ST8SIA5.
DR eggNOG; KOG2692; Eukaryota.
DR GeneTree; ENSGT01030000234535; -.
DR HOGENOM; CLU_048583_1_1_1; -.
DR InParanoid; P61646; -.
DR TreeFam; TF323961; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000002277; Chromosome 18.
DR Bgee; ENSPTRG00000009997; Expressed in dorsolateral prefrontal cortex and 14 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:0003828; F:alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity; IBA:GO_Central.
DR GO; GO:0008373; F:sialyltransferase activity; ISS:UniProtKB.
DR GO; GO:0006688; P:glycosphingolipid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006491; P:N-glycan processing; IBA:GO_Central.
DR GO; GO:0009311; P:oligosaccharide metabolic process; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
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 Lipid metabolism; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..376
FT /note="Alpha-2,8-sialyltransferase 8E"
FT /id="PRO_0000149298"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..38
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..376
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 348
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 214..216
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 300..302
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 164..313
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT DISULFID 178..373
FT /evidence="ECO:0000250|UniProtKB:O43173"
SQ SEQUENCE 376 AA; 43922 MW; CA49733EC502A345 CRC64;
MRYADPSANR DLLGNRTLLF IFICAFALVT LLQQILYGRN YIKRYFEFYE GPFEYNSTRC
LELRHEILEV KVLSMVKQSE LFDRWKSLQM CKWAMNISEA NQFKSTLSRC CNAPAFLFTT
QKNTPLGTKL KYEVDTSGIY HINQEIFRMF PKDMPYYRSQ FKKCAVVGNG GILKNSRCGR
EINSADFVFR CNLPPISEKY TMDVGVKTDV VTVNPSIITE RFHKLEKWRR PFYRVLQVYE
NASVLLPAFY NTRNTDVSIR VKYVLDDFES PQAVYYFHPQ YLVNVSRYWL SLGVRAKRIS
TGLILVTAAL ELCEEVHLFG FWAFPMNPSG LYITHHYYDN VKPRPGFHAM PSEIFNFLHL
HSRGILRVHT GTCSCC
