SIA8B_RAT
ID SIA8B_RAT Reviewed; 375 AA.
AC Q07977; Q64688;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Alpha-2,8-sialyltransferase 8B;
DE EC=2.4.99.-;
DE AltName: Full=Sialyltransferase 8B;
DE Short=SIAT8-B;
DE AltName: Full=Sialyltransferase St8Sia II;
DE Short=ST8SiaII;
DE AltName: Full=Sialyltransferase X;
DE Short=STX;
GN Name=St8sia2; Synonyms=Siat8b, Stx;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=7685014; DOI=10.1016/s0021-9258(19)50227-7;
RA Livingston B.D., Paulson J.C.;
RT "Polymerase chain reaction cloning of a developmentally regulated member of
RT the sialyltransferase gene family.";
RL J. Biol. Chem. 268:11504-11507(1993).
CC -!- FUNCTION: May transfer sialic acid through alpha-2,8-linkages to the
CC alpha-2,3-linked and alpha-2,6-linked sialic acid of N-linked
CC oligosaccharides of glycoproteins and may be involved in PSA
CC (polysialic acid) expression.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed only in newborn brain.
CC -!- DEVELOPMENTAL STAGE: Newborn.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
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DR EMBL; L13445; AAA42147.1; -; mRNA.
DR PIR; A46727; A46727.
DR RefSeq; NP_476497.1; NM_057156.1.
DR AlphaFoldDB; Q07977; -.
DR SMR; Q07977; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyGen; Q07977; 6 sites.
DR iPTMnet; Q07977; -.
DR PhosphoSitePlus; Q07977; -.
DR PaxDb; Q07977; -.
DR Ensembl; ENSRNOT00000113519; ENSRNOP00000092932; ENSRNOG00000065528.
DR GeneID; 117523; -.
DR KEGG; rno:117523; -.
DR UCSC; RGD:621843; rat.
DR CTD; 8128; -.
DR RGD; 621843; St8sia2.
DR GeneTree; ENSGT01030000234535; -.
DR InParanoid; Q07977; -.
DR OrthoDB; 825014at2759; -.
DR PhylomeDB; Q07977; -.
DR Reactome; R-RNO-4085001; Sialic acid metabolism.
DR Reactome; R-RNO-419037; NCAM1 interactions.
DR Reactome; R-RNO-975577; N-Glycan antennae elongation.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q07977; -.
DR Proteomes; UP000002494; Chromosome 1.
DR GO; GO:0005769; C:early endosome; ISO:RGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0055037; C:recycling endosome; ISO:RGD.
DR GO; GO:0003828; F:alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity; ISO:RGD.
DR GO; GO:0008373; F:sialyltransferase activity; IMP:RGD.
DR GO; GO:0001574; P:ganglioside biosynthetic process; ISO:RGD.
DR GO; GO:0006491; P:N-glycan processing; ISO:RGD.
DR GO; GO:0030182; P:neuron differentiation; IEP:RGD.
DR GO; GO:1990138; P:neuron projection extension; IMP:RGD.
DR GO; GO:0009311; P:oligosaccharide metabolic process; ISO:RGD.
DR GO; GO:1901216; P:positive regulation of neuron death; IDA:RGD.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IMP:RGD.
DR GO; GO:0006486; P:protein glycosylation; ISO:RGD.
DR GO; GO:0042220; P:response to cocaine; IEP:RGD.
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; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..375
FT /note="Alpha-2,8-sialyltransferase 8B"
FT /id="PRO_0000149288"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..23
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..375
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 346
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 206..208
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 294..296
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 329..330
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 157..307
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT DISULFID 171..371
FT /evidence="ECO:0000250|UniProtKB:O43173"
SQ SEQUENCE 375 AA; 42400 MW; F7B3AC1E1E503675 CRC64;
MQLQFRSWML AALTLLVVFL IFADISEIEE EIGNSGGRGT IRSAVNSLHS KSNRAEVVIN
GSSLPAVADR SNESLKHSIQ PASSKWRHNQ TLSLRIRKQI LKFLDAEKDI SVLKGTLKPG
DIIHYIFDRD STMNVSQNLY ELLPRTSPLK NKHFQTCAIV GNSGVLLNSG CGQEIDTHSF
VIRCNLAPVQ EYARDVGLKT DLVTMNPSVI QRAFEDLVNA TWREKLLQRL HGLNGSILWI
PAFMARGGKE RVEWVNALIL KHHVNVRTAY PSLRLLHAVR GYWLTNKVHI KRPTTGLLMY
TLATRFCNQI YLYGFWPFPL DQNQNPVKYH YYDSLKYGYT SQASPHTMPL EFKALKSLHE
QGALKLTVGQ CDGAT
