SIA7E_HUMAN
ID SIA7E_HUMAN Reviewed; 336 AA.
AC Q9BVH7; B1AK82;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 5;
DE EC=2.4.99.- {ECO:0000269|PubMed:12668675};
DE AltName: Full=GD1 alpha synthase;
DE AltName: Full=GalNAc alpha-2,6-sialyltransferase V;
DE AltName: Full=ST6GalNAc V {ECO:0000303|PubMed:12668675};
DE Short=ST6GalNAcV;
DE AltName: Full=Sialyltransferase 7E;
DE Short=SIAT7-E;
GN Name=ST6GALNAC5; Synonyms=SIAT7E;
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 Harduin-Lepers A.;
RT "Molecular cloning and expression of human ST6GALNAC V.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12668675; DOI=10.1074/jbc.m211034200;
RA Tsuchida A., Okajima T., Furukawa K., Ando T., Ishida H., Yoshida A.,
RA Nakamura Y., Kannagi R., Kiso M., Furukawa K.;
RT "Synthesis of disialyl Lewis a (Le(a)) structure in colon cancer cell lines
RT by a sialyltransferase, ST6GalNAc VI, responsible for the synthesis of
RT alpha-series gangliosides.";
RL J. Biol. Chem. 278:22787-22794(2003).
CC -!- FUNCTION: Predominantly catalyzes the biosynthesis of ganglioside
CC GD1alpha from GM1b in the brain, by transferring the sialyl group (N-
CC acetyl-alpha-neuraminyl or NeuAc) from CMP-NeuAc to the GalNAc residue
CC on the NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc sequence of GM1b
CC (PubMed:12668675). GD1alpha is a critical molecule in the communication
CC and interaction between neuronal cells and their supportive cells,
CC particularly in brain tissues, and functions as an adhesion molecule in
CC the process of metastasis (By similarity). Also shows activity towards
CC sialyl Lc4Cer (N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-galactosyl-
CC (1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-
CC beta-D-glucosyl-(1<->1')-N-acyl-sphing-4-enine) generating disialyl
CC Lc4Cer, which can lead to the synthesis of disialyl Lewis a (Le(a)),
CC suggested to be a cancer-associated antigen (PubMed:12668675).
CC {ECO:0000250|UniProtKB:Q9QYJ1, ECO:0000269|PubMed:12668675}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GM1b (d18:1(4E)) =
CC a ganglioside GD1alpha (d18:1(4E)) + CMP + H(+);
CC Xref=Rhea:RHEA:41968, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:78568, ChEBI:CHEBI:78569;
CC Evidence={ECO:0000269|PubMed:12668675};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41969;
CC Evidence={ECO:0000305|PubMed:12668675};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + N-acetyl-alpha-neuraminosyl-
CC (2->3)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-
CC beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-N-acyl-sphing-4-
CC enine = CMP + H(+) + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-
CC galactosyl-(1->3)-[N-acetyl-alpha-neuraminosyl-(2->6)]-N-acetyl-beta-
CC D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-
CC (1<->1')-N-acyl-sphing-4-enine; Xref=Rhea:RHEA:47884,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:88073, ChEBI:CHEBI:88079;
CC Evidence={ECO:0000269|PubMed:12668675};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47885;
CC Evidence={ECO:0000305|PubMed:12668675};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.56 mM for GMb1 {ECO:0000269|PubMed:12668675};
CC KM=0.90 mM for sialyl Lc4Cer {ECO:0000269|PubMed:12668675};
CC -!- PATHWAY: Glycolipid biosynthesis. {ECO:0000305|PubMed:12668675}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=ST6GalNAc
CC V;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_634";
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DR EMBL; AJ507292; CAD45372.1; -; mRNA.
DR EMBL; AK056241; BAB71127.1; -; mRNA.
DR EMBL; AC099060; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL035409; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX06386.1; -; Genomic_DNA.
DR EMBL; BC001201; AAH01201.1; -; mRNA.
DR CCDS; CCDS673.1; -.
DR RefSeq; NP_112227.1; NM_030965.2.
DR AlphaFoldDB; Q9BVH7; -.
DR BioGRID; 123600; 4.
DR IntAct; Q9BVH7; 2.
DR STRING; 9606.ENSP00000417583; -.
DR SwissLipids; SLP:000001365; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyGen; Q9BVH7; 2 sites.
DR iPTMnet; Q9BVH7; -.
DR PhosphoSitePlus; Q9BVH7; -.
DR BioMuta; ST6GALNAC5; -.
DR DMDM; 21759442; -.
DR MassIVE; Q9BVH7; -.
DR PaxDb; Q9BVH7; -.
DR PeptideAtlas; Q9BVH7; -.
DR PRIDE; Q9BVH7; -.
DR ProteomicsDB; 79206; -.
DR Antibodypedia; 33478; 105 antibodies from 21 providers.
DR DNASU; 81849; -.
DR Ensembl; ENST00000477717.6; ENSP00000417583.1; ENSG00000117069.15.
DR GeneID; 81849; -.
DR KEGG; hsa:81849; -.
DR MANE-Select; ENST00000477717.6; ENSP00000417583.1; NM_030965.3; NP_112227.1.
DR UCSC; uc001dhi.4; human.
DR CTD; 81849; -.
DR DisGeNET; 81849; -.
DR GeneCards; ST6GALNAC5; -.
DR HGNC; HGNC:19342; ST6GALNAC5.
DR HPA; ENSG00000117069; Tissue enhanced (brain).
DR MIM; 610134; gene.
DR neXtProt; NX_Q9BVH7; -.
DR OpenTargets; ENSG00000117069; -.
DR PharmGKB; PA134924485; -.
DR VEuPathDB; HostDB:ENSG00000117069; -.
DR eggNOG; KOG2692; Eukaryota.
DR GeneTree; ENSGT00940000157634; -.
DR HOGENOM; CLU_061099_0_0_1; -.
DR InParanoid; Q9BVH7; -.
DR OMA; YGHDVGN; -.
DR OrthoDB; 817470at2759; -.
DR PhylomeDB; Q9BVH7; -.
DR TreeFam; TF323961; -.
DR BRENDA; 2.4.99.7; 2681.
DR PathwayCommons; Q9BVH7; -.
DR Reactome; R-HSA-4085001; Sialic acid metabolism.
DR SignaLink; Q9BVH7; -.
DR BioGRID-ORCS; 81849; 8 hits in 1061 CRISPR screens.
DR ChiTaRS; ST6GALNAC5; human.
DR GenomeRNAi; 81849; -.
DR Pharos; Q9BVH7; Tbio.
DR PRO; PR:Q9BVH7; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9BVH7; protein.
DR Bgee; ENSG00000117069; Expressed in CA1 field of hippocampus and 124 other tissues.
DR ExpressionAtlas; Q9BVH7; baseline and differential.
DR Genevisible; Q9BVH7; HS.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0001665; F:alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase activity; ISS:BHF-UCL.
DR GO; GO:0008373; F:sialyltransferase activity; ISS:BHF-UCL.
DR GO; GO:0001574; P:ganglioside biosynthetic process; IBA:GO_Central.
DR GO; GO:0006688; P:glycosphingolipid biosynthetic process; ISS:BHF-UCL.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; ISS:BHF-UCL.
DR GO; GO:0009311; P:oligosaccharide metabolic process; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
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 Lipid metabolism; Membrane; Reference proteome; Sialic acid; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..336
FT /note="Alpha-N-acetylgalactosaminide alpha-2,6-
FT sialyltransferase 5"
FT /id="PRO_0000149280"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..336
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 32..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 96..245
FT /evidence="ECO:0000250"
SQ SEQUENCE 336 AA; 38443 MW; F5FDD43D45CA11CE CRC64;
MKTLMRHGLA VCLALTTMCT SLLLVYSSLG GQKERPPQQQ QQQQQQQQQA SATGSSQPAA
ESSTQQRPGV PAGPRPLDGY LGVADHKPLK MHCRDCALVT SSGHLLHSRQ GSQIDQTECV
IRMNDAPTRG YGRDVGNRTS LRVIAHSSIQ RILRNRHDLL NVSQGTVFIF WGPSSYMRRD
GKGQVYNNLH LLSQVLPRLK AFMITRHKML QFDELFKQET GKDRKISNTW LSTGWFTMTI
ALELCDRINV YGMVPPDFCR DPNHPSVPYH YYEPFGPDEC TMYLSHERGR KGSHHRFITE
KRVFKNWART FNIHFFQPDW KPESLAINHP ENKPVF
