SIA8F_HUMAN
ID SIA8F_HUMAN Reviewed; 398 AA.
AC P61647; B0YJ97; B9EH72; Q5VZH4;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Alpha-2,8-sialyltransferase 8F {ECO:0000305};
DE EC=2.4.99.-;
DE AltName: Full=Sialyltransferase 8F;
DE Short=SIAT8-F;
DE AltName: Full=Sialyltransferase St8Sia VI;
DE Short=ST8SiaVI;
GN Name=ST8SIA6 {ECO:0000312|HGNC:HGNC:23317}; Synonyms=SIAT8F;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Teintenier-Lelievre M., Delannoy P., Harduin-Lepers A.;
RT "Molecular cloning and expression of a sixth human alpha2,8-
RT sialyltransferase (hST8SiaVI).";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Alpha-2,8-sialyltransferase that prefers O-glycans to N-
CC glycans or glycolipids as acceptor substrates. The minimal acceptor
CC substrate is the NeuAc-alpha-2,3(6)-Gal sequence at the non-reducing
CC end of their carbohydrate groups. {ECO:0000250|UniProtKB:Q8K4T1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GM3 = CMP +
CC ganglioside GD3 + H(+); Xref=Rhea:RHEA:48288, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:79210,
CC ChEBI:CHEBI:79214; Evidence={ECO:0000250|UniProtKB:Q8K4T1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GM3 (d18:1(4E)) =
CC CMP + ganglioside GD3 (d18:1(4E)) + H(+); Xref=Rhea:RHEA:41760,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60065,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:78436;
CC Evidence={ECO:0000250|UniProtKB:Q8K4T1};
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:Q8K4T1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GD1a = CMP +
CC ganglioside GT1a + H(+); Xref=Rhea:RHEA:48912, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:82637,
CC ChEBI:CHEBI:90501; Evidence={ECO:0000250|UniProtKB:Q8K4T1};
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:Q8K4T1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GM1b = CMP +
CC ganglioside GD1c + H(+); Xref=Rhea:RHEA:48916, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:90151,
CC ChEBI:CHEBI:90856; Evidence={ECO:0000250|UniProtKB:Q8K4T1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GM4 (d18:1(4E)) =
CC CMP + H(+) + N-acetyl-alpha-neuraminosyl-(2->8)-N-acetyl-alpha-
CC neuraminosyl-(2->3)-beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine;
CC Xref=Rhea:RHEA:48924, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:78482, ChEBI:CHEBI:90858;
CC Evidence={ECO:0000250|UniProtKB:Q8K4T1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + N-acetyl-alpha-neuraminosyl-
CC (2->3)-beta-D-galactosyl-(1<->1')-ceramide = CMP + H(+) + N-acetyl-
CC alpha-neuraminosyl-(2->8)-N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-
CC galactosyl-(1<->1')-ceramide; Xref=Rhea:RHEA:48928,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:82643, ChEBI:CHEBI:90859;
CC Evidence={ECO:0000250|UniProtKB:Q8K4T1};
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:0000250|UniProtKB:Q8K4T1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GT1b = CMP +
CC ganglioside GQ1b + H(+); Xref=Rhea:RHEA:48932, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:82940,
CC ChEBI:CHEBI:90862; Evidence={ECO:0000250|UniProtKB:Q8K4T1};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=ST8Sia
CC VI;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_641";
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DR EMBL; AJ621583; CAF21722.1; -; mRNA.
DR EMBL; EF445032; ACA06074.1; -; Genomic_DNA.
DR EMBL; EF445032; ACA06075.1; -; Genomic_DNA.
DR EMBL; AL158164; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL160289; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC137102; AAI37103.1; -; mRNA.
DR EMBL; BC137103; AAI37104.1; -; mRNA.
DR CCDS; CCDS31158.1; -.
DR RefSeq; NP_001004470.1; NM_001004470.2.
DR AlphaFoldDB; P61647; -.
DR SMR; P61647; -.
DR BioGRID; 130764; 3.
DR STRING; 9606.ENSP00000366827; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyGen; P61647; 4 sites.
DR iPTMnet; P61647; -.
DR PhosphoSitePlus; P61647; -.
DR BioMuta; ST8SIA6; -.
DR DMDM; 48428578; -.
DR MassIVE; P61647; -.
DR PaxDb; P61647; -.
DR PeptideAtlas; P61647; -.
DR PRIDE; P61647; -.
DR Antibodypedia; 2510; 83 antibodies from 17 providers.
DR DNASU; 338596; -.
DR Ensembl; ENST00000377602.5; ENSP00000366827.4; ENSG00000148488.17.
DR GeneID; 338596; -.
DR KEGG; hsa:338596; -.
DR MANE-Select; ENST00000377602.5; ENSP00000366827.4; NM_001004470.3; NP_001004470.1.
DR UCSC; uc001ipd.4; human.
DR CTD; 338596; -.
DR DisGeNET; 338596; -.
DR GeneCards; ST8SIA6; -.
DR HGNC; HGNC:23317; ST8SIA6.
DR HPA; ENSG00000148488; Tissue enhanced (brain, lung).
DR MIM; 610139; gene.
DR neXtProt; NX_P61647; -.
DR OpenTargets; ENSG00000148488; -.
DR PharmGKB; PA134909138; -.
DR VEuPathDB; HostDB:ENSG00000148488; -.
DR eggNOG; KOG2692; Eukaryota.
DR GeneTree; ENSGT01030000234535; -.
DR HOGENOM; CLU_048583_1_1_1; -.
DR InParanoid; P61647; -.
DR OMA; EQASKCK; -.
DR OrthoDB; 825014at2759; -.
DR PhylomeDB; P61647; -.
DR TreeFam; TF323961; -.
DR BRENDA; 2.4.99.8; 2681.
DR PathwayCommons; P61647; -.
DR Reactome; R-HSA-4085001; Sialic acid metabolism.
DR Reactome; R-HSA-975577; N-Glycan antennae elongation.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 338596; 10 hits in 1076 CRISPR screens.
DR ChiTaRS; ST8SIA6; human.
DR GenomeRNAi; 338596; -.
DR Pharos; P61647; Tbio.
DR PRO; PR:P61647; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P61647; protein.
DR Bgee; ENSG00000148488; Expressed in substantia nigra and 103 other tissues.
DR ExpressionAtlas; P61647; baseline and differential.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
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:BHF-UCL.
DR GO; GO:0001835; P:blastocyst hatching; IEA:Ensembl.
DR GO; GO:0016051; P:carbohydrate biosynthetic process; ISS:BHF-UCL.
DR GO; GO:0001574; P:ganglioside biosynthetic process; ISS:BHF-UCL.
DR GO; GO:0009247; P:glycolipid biosynthetic process; ISS:BHF-UCL.
DR GO; GO:0009100; P:glycoprotein metabolic process; ISS:BHF-UCL.
DR GO; GO:0006491; P:N-glycan processing; IBA:GO_Central.
DR GO; GO:0009311; P:oligosaccharide metabolic process; ISS:BHF-UCL.
DR GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
DR GO; GO:0006493; P:protein O-linked glycosylation; ISS:BHF-UCL.
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..398
FT /note="Alpha-2,8-sialyltransferase 8F"
FT /id="PRO_0000149299"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 4..24
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..398
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 370
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 236..238
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 322..324
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 186..335
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT DISULFID 200..395
FT /evidence="ECO:0000250|UniProtKB:O43173"
SQ SEQUENCE 398 AA; 44836 MW; 48F58B82E4B69A26 CRC64;
MRPGGALLAL LASLLLLLLL RLLWCPADAP GRARILVEES REATHGTPAA LRTLRSPATA
VPRATNSTYL NEKSLQLTEK CKNLQYGIES FSNKTKGYSE NDYLQIITDI QSCPWKRQAE
EYANFRAKLA SCCDAVQNFV VSQNNTPVGT NMSYEVESKK EIPIKKNIFH MFPVSQPFVD
YPYNQCAVVG NGGILNKSLC GTEIDKSDFV FRCNLPPTTG DVSKDVGSKT NLVTINPSII
TLKYGNLKEK KALFLEDIAT YGDAFFLLPA FSFRANTGTS FKVYYTLEES KARQKVLFFH
PKYLKDLALF WRTKGVTAYR LSTGLMITSV AVELCKNVKL YGFWPFSKTV EDIPVSHHYY
DNKLPKHGFH QMPKEYSQIL QLHMKGILKL QFSKCEVA
