SIA8E_RAT
ID SIA8E_RAT Reviewed; 376 AA.
AC Q6ZXC8; A0A0G2JV41; E9PU47;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 22-APR-2020, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Alpha-2,8-sialyltransferase 8E {ECO:0000305};
DE EC=2.4.99.- {ECO:0000269|PubMed:1606358};
DE AltName: Full=Sialyltransferase 8E;
DE Short=SIAT8-E;
DE AltName: Full=Sialyltransferase St8Sia V;
DE Short=SATV {ECO:0000303|PubMed:1606358};
DE Short=ST8SiaV;
GN Name=St8sia5 {ECO:0000312|RGD:1302934};
GN Synonyms=Siat8e {ECO:0000312|EMBL:CAG27884.1}, St8siav;
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 {ECO:0000312|EMBL:CAG27884.1};
RN [1] {ECO:0000312|EMBL:CAG27884.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:CAG27884.1};
RX PubMed=15843597; DOI=10.1093/glycob/cwi063;
RA Harduin-Lepers A., Mollicone R., Delannoy P., Oriol R.;
RT "The animal sialyltransferases and sialyltransferase-related genes: a
RT phylogenetic approach.";
RL Glycobiology 15:805-817(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=1606358; DOI=10.1093/glycob/2.2.137;
RA Iber H., Zacharias C., Sandhoff K.;
RT "The c-series gangliosides GT3, GT2 and GP1c are formed in rat liver Golgi
RT by the same set of glycosyltransferases that catalyse the biosynthesis of
RT asialo-, a- and b-series gangliosides.";
RL Glycobiology 2:137-142(1992).
CC -!- FUNCTION: Involved in the synthesis of gangliosides GD1c, GT1a, GQ1b,
CC GP1c and GT3 from GD1a, GT1b, GM1b and GD3 respectively.
CC {ECO:0000269|PubMed:1606358}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GT1b (d18:1(4E)) =
CC CMP + ganglioside GQ1b (d18:1(4E)) + H(+); Xref=Rhea:RHEA:41772,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:78452, ChEBI:CHEBI:78455;
CC Evidence={ECO:0000269|PubMed:1606358};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41773;
CC Evidence={ECO:0000269|PubMed:1606358};
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:0000269|PubMed:1606358};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47593;
CC Evidence={ECO:0000269|PubMed:1606358};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GD3 (d18:1(4E)) =
CC CMP + ganglioside GT3 (d18:1(4E)) + H(+); Xref=Rhea:RHEA:41764,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:78436, ChEBI:CHEBI:78438;
CC Evidence={ECO:0000269|PubMed:1606358};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41765;
CC Evidence={ECO:0000269|PubMed:1606358};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GD1a (d18:1(4E)) =
CC CMP + ganglioside GT1a (d18:1(4E)) + H(+); Xref=Rhea:RHEA:41768,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:78445, ChEBI:CHEBI:78447;
CC Evidence={ECO:0000250|UniProtKB:O15466};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41769;
CC Evidence={ECO:0000250|UniProtKB:O15466};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GM1b (d18:1(4E)) =
CC CMP + ganglioside GD1c (d18:1(4E)) + H(+); Xref=Rhea:RHEA:47576,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:78568, ChEBI:CHEBI:87787;
CC Evidence={ECO:0000250|UniProtKB:O15466};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47577;
CC Evidence={ECO:0000250|UniProtKB:O15466};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=120 uM for GD3 {ECO:0000269|PubMed:1606358};
CC KM=130 uM for GD1a {ECO:0000269|PubMed:1606358};
CC Vmax=1.7 nmol/h/mg enzyme towards GD3 {ECO:0000269|PubMed:1606358};
CC Vmax=0.7 nmol/h/mg enzyme towards GD1a {ECO:0000269|PubMed:1606358};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:1606358}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:1606358}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=Q6ZXC8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZXC8-2; Sequence=VSP_060566;
CC -!- TISSUE SPECIFICITY: Expressed in liver. {ECO:0000269|PubMed:1606358}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000255}.
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DR EMBL; AJ699422; CAG27884.1; -; mRNA.
DR EMBL; AC139391; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_998793.1; NM_213628.1.
DR RefSeq; XP_006255030.1; XM_006254968.3. [Q6ZXC8-2]
DR AlphaFoldDB; Q6ZXC8; -.
DR SMR; Q6ZXC8; -.
DR STRING; 10116.ENSRNOP00000033363; -.
DR SwissLipids; SLP:000001441; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyGen; Q6ZXC8; 2 sites.
DR Ensembl; ENSRNOT00000035317; ENSRNOP00000033363; ENSRNOG00000022691. [Q6ZXC8-1]
DR Ensembl; ENSRNOT00000077679; ENSRNOP00000069340; ENSRNOG00000022691. [Q6ZXC8-2]
DR GeneID; 364901; -.
DR KEGG; rno:364901; -.
DR CTD; 29906; -.
DR RGD; 1302934; St8sia5.
DR eggNOG; KOG2692; Eukaryota.
DR GeneTree; ENSGT01030000234535; -.
DR HOGENOM; CLU_048583_1_1_1; -.
DR OMA; FEFNSTA; -.
DR OrthoDB; 825014at2759; -.
DR PhylomeDB; Q6ZXC8; -.
DR Reactome; R-RNO-4085001; Sialic acid metabolism.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q6ZXC8; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000022691; Expressed in frontal cortex and 6 other tissues.
DR Genevisible; Q6ZXC8; RN.
DR GO; GO:0000139; C:Golgi membrane; IDA: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; ISO:RGD.
DR GO; GO:0008373; F:sialyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006688; P:glycosphingolipid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
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 Alternative initiation; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Lipid metabolism; Membrane; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..376
FT /note="Alpha-2,8-sialyltransferase 8E"
FT /id="PRO_0000449514"
FT TRANSMEM 17..37
FT /note="Helical"
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 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 164..313
FT /evidence="ECO:0000255|PIRSR:PIRSR005557-2"
FT DISULFID 178..373
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT VAR_SEQ 43
FT /note="K -> KRGFQFGWQRGDQQANWTGLFNASGSLTEQNISDSSS (in
FT isoform 2)"
FT /id="VSP_060566"
FT CONFLICT 271..272
FT /note="RQ -> GE (in Ref. 1; CAG27884)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="Q -> H (in Ref. 1; CAG27884)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 43840 MW; 869DEF3748B4E1D4 CRC64;
MRYADPSANR DLLGNRTLLF IFICAFALVT LLQQILYSKS YIKRYFEFYK EPLEFNSTRC
LELRQEILEV KVLSMVKQSE LFERWKSLQI CKWAMDASEA SLFKSTLSRC CNAPNFLFTT
QKNTPVETNL RYEVESSGLY HIDQEIFKMF PKEMPYYRSQ FKKCAVVGNG GILKNSGCGK
EINSADFVFR CNLPPISGIY TTDVGEKTDV VTVNPSIIID RFHKLEKWRR PFFSVLQRYE
NASVLLPAFY NVRNTLVSFR VKYMLDDFQS RQPVYFFHPQ YLSSVSRYWL SLGVRARRIS
TGLILVTAAL ELCEEVHLFG FWAFPMNPSG FFITHHYYDN VKPKPGFHAM PSEIFTFLRM
HSRGILRVHT GTCNCC
