ID   SIAT9_HUMAN             Reviewed;         418 AA.
AC   Q9UNP4; B3KM82; D6W5L9; O94902; Q53QU1; Q6NZX4; Q6YFL1;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 4.
DT   24-JAN-2024, entry version 185.
DE   RecName: Full=Lactosylceramide alpha-2,3-sialyltransferase;
DE            EC=2.4.3.9 {ECO:0000269|PubMed:16934889, ECO:0000269|PubMed:9822625};
DE   AltName: Full=CMP-NeuAc:lactosylceramide alpha-2,3-sialyltransferase;
DE   AltName: Full=GM3 synthase {ECO:0000303|PubMed:16934889};
DE   AltName: Full=Ganglioside GM3 synthase {ECO:0000303|PubMed:9822625};
DE   AltName: Full=ST3Gal V;
DE            Short=ST3GalV;
DE   AltName: Full=Sialyltransferase 9;
GN   Name=ST3GAL5; Synonyms=SIAT9; ORFNames=UNQ2510/PRO5998;
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] (ISOFORM 1), VARIANT ARG-104, CHARACTERIZATION,
RP   FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX   PubMed=9822625; DOI=10.1074/jbc.273.48.31652;
RA   Ishii A., Ohta M., Watanabe Y., Matsuda K., Ishiyama K., Sakoe K.,
RA   Nakamura M., Inokuchi J., Sanai Y., Saito M.;
RT   "Expression cloning and functional characterization of human cDNA for
RT   ganglioside GM3 synthase.";
RL   J. Biol. Chem. 273:31652-31655(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ARG-104.
RC   TISSUE=Brain;
RA   Kapitonov D.;
RT   "Molecular cloning and expression of ceramide galactosyltransferases.
RT   Comparison with other glycosyltransferases.";
RL   Thesis (1999), Medical College of Viriginia, United States.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Fetal brain;
RA   Kim K.-W., Kim K.-S., Do S.-I., Kim C.-H., Lee Y.-C.;
RT   "Molecular cloning of CMP-NeuAc:lactosylceramide alpha-2,3-
RT   sialyltransferase cDNA from human fetal brain.";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, CATALYTIC ACTIVITY, AND
RP   GLYCOSYLATION.
RC   TISSUE=Placenta;
RX   PubMed=16934889; DOI=10.1016/j.bbaexp.2006.07.001;
RA   Berselli P., Zava S., Sottocornola E., Milani S., Berra B., Colombo I.;
RT   "Human GM3 synthase: a new mRNA variant encodes an NH2-terminal extended
RT   form of the protein.";
RL   Biochim. Biophys. Acta 1759:348-358(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [7]
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   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-104.
RC   TISSUE=Skin;
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   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-418 (ISOFORM 1).
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [10]
RP   INVOLVEMENT IN SPDRS.
RX   PubMed=15502825; DOI=10.1038/ng1460;
RA   Simpson M.A., Cross H., Proukakis C., Priestman D.A., Neville D.C.A.,
RA   Reinkensmeier G., Wang H., Wiznitzer M., Gurtz K., Verganelaki A.,
RA   Pryde A., Patton M.A., Dwek R.A., Butters T.D., Platt F.M., Crosby A.H.;
RT   "Infantile-onset symptomatic epilepsy syndrome caused by a homozygous loss-
RT   of-function mutation of GM3 synthase.";
RL   Nat. Genet. 36:1225-1229(2004).
CC   -!- FUNCTION: Transfers the sialyl group (N-acetyl-alpha-neuraminyl or
CC       NeuAc) from CMP-NeuAc to the non-reducing terminal galactose (Gal) of
CC       glycosphingolipids forming gangliosides (important molecules involved
CC       in the regulation of multiple cellular processes, including cell
CC       proliferation and differentiation, apoptosis, embryogenesis,
CC       development, and oncogenesis) (PubMed:9822625, PubMed:16934889). Mainly
CC       involved in the biosynthesis of ganglioside GM3 but can also use
CC       different glycolipids as substrate acceptors such as D-
CC       galactosylceramide (GalCer), asialo-GM2 (GA2) and asialo-GM1 (GA1),
CC       although less preferentially than beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-
CC       Cer (LacCer) (PubMed:16934889). {ECO:0000269|PubMed:16934889,
CC       ECO:0000269|PubMed:9822625}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + CMP-N-
CC         acetyl-beta-neuraminate = a ganglioside GM3 (d18:1(4E)) + CMP + H(+);
CC         Xref=Rhea:RHEA:18417, ChEBI:CHEBI:15378, ChEBI:CHEBI:17950,
CC         ChEBI:CHEBI:57812, ChEBI:CHEBI:60065, ChEBI:CHEBI:60377; EC=2.4.3.9;
CC         Evidence={ECO:0000269|PubMed:16934889, ECO:0000269|PubMed:9822625};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18418;
CC         Evidence={ECO:0000305|PubMed:16934889, ECO:0000305|PubMed:9822625};
CC   -!- CATALYTIC ACTIVITY: [Isoform 3]:
CC       Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GA2
CC         (d18:1(4E)/18:0) = CMP + ganglioside GM2 (d18:1(4E)/18:0) + H(+);
CC         Xref=Rhea:RHEA:41776, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812,
CC         ChEBI:CHEBI:60377, ChEBI:CHEBI:78485, ChEBI:CHEBI:78486;
CC         Evidence={ECO:0000269|PubMed:16934889};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41777;
CC         Evidence={ECO:0000305|PubMed:16934889};
CC   -!- CATALYTIC ACTIVITY: [Isoform 3]:
CC       Reaction=beta-D-Gal-(1<->1')-Cer + CMP-N-acetyl-beta-neuraminate = CMP
CC         + H(+) + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-galactosyl-
CC         (1<->1')-ceramide; Xref=Rhea:RHEA:41780, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:82643,
CC         ChEBI:CHEBI:143593; Evidence={ECO:0000269|PubMed:16934889};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41781;
CC         Evidence={ECO:0000305|PubMed:16934889};
CC   -!- CATALYTIC ACTIVITY: [Isoform 3]:
CC       Reaction=a beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine + CMP-N-
CC         acetyl-beta-neuraminate = a ganglioside GM4 (d18:1(4E)) + CMP + H(+);
CC         Xref=Rhea:RHEA:47600, ChEBI:CHEBI:15378, ChEBI:CHEBI:18390,
CC         ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:78482;
CC         Evidence={ECO:0000305|PubMed:16934889};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47601;
CC         Evidence={ECO:0000305|PubMed:16934889};
CC   -!- CATALYTIC ACTIVITY: [Isoform 3]:
CC       Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GA1
CC         (d18:1(4E)/18:0) = CMP + ganglioside GM1 (d18:1(4E)/18:0) + H(+);
CC         Xref=Rhea:RHEA:41784, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812,
CC         ChEBI:CHEBI:60377, ChEBI:CHEBI:73110, ChEBI:CHEBI:78484;
CC         Evidence={ECO:0000269|PubMed:16934889};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41785;
CC         Evidence={ECO:0000305|PubMed:16934889};
CC   -!- PATHWAY: Glycolipid biosynthesis. {ECO:0000305|PubMed:16934889,
CC       ECO:0000305|PubMed:9822625}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC       pass type II membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9UNP4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UNP4-2; Sequence=VSP_033686;
CC       Name=3;
CC         IsoId=Q9UNP4-3; Sequence=VSP_033687, VSP_033688;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. High expression in brain, skeletal
CC       muscle, placenta, and testis. mRNA widely distributed in human brain,
CC       but slightly elevated expression was observed in the cerebral cortex,
CC       temporal lobe, and putamen. {ECO:0000269|PubMed:9822625}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:16934889}.
CC   -!- DISEASE: Salt and pepper developmental regression syndrome (SPDRS)
CC       [MIM:609056]: A rare autosomal recessive disorder characterized by
CC       infantile onset of severe, recurrent and refractory seizures, failure
CC       to thrive, psychomotor delay, developmental stagnation, and cortical
CC       blindness. Deafness is observed in some patients. Affected individuals
CC       have patches of skin hypo- or hyperpigmentation on the trunk, face, and
CC       extremities. {ECO:0000269|PubMed:15502825}. Note=The disease is caused
CC       by variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD14634.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAF66146.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAQ89463.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAY24147.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAA33950.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=ST3Gal V;
CC       URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_626";
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DR   EMBL; AB018356; BAA33950.1; ALT_INIT; mRNA.
DR   EMBL; AF119415; AAF66146.1; ALT_INIT; mRNA.
DR   EMBL; AY152815; AAO16866.2; -; mRNA.
DR   EMBL; AF105026; AAD14634.1; ALT_INIT; mRNA.
DR   EMBL; AK001340; BAG50894.1; -; mRNA.
DR   EMBL; AC105053; AAY24147.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CH471053; EAW99475.1; -; Genomic_DNA.
DR   EMBL; CH471053; EAW99479.1; -; Genomic_DNA.
DR   EMBL; BC065936; AAH65936.2; -; mRNA.
DR   EMBL; AY359105; AAQ89463.1; ALT_INIT; mRNA.
DR   CCDS; CCDS1986.2; -. [Q9UNP4-1]
DR   CCDS; CCDS42705.1; -. [Q9UNP4-3]
DR   CCDS; CCDS86856.1; -. [Q9UNP4-2]
DR   RefSeq; NP_001035902.1; NM_001042437.1. [Q9UNP4-3]
DR   RefSeq; NP_003887.3; NM_003896.3. [Q9UNP4-1]
DR   AlphaFoldDB; Q9UNP4; -.
DR   SMR; Q9UNP4; -.
DR   BioGRID; 114389; 16.
DR   IntAct; Q9UNP4; 3.
DR   STRING; 9606.ENSP00000491316; -.
DR   DrugBank; DB05867; 99mTc-14 F7 Mab.
DR   DrugBank; DB04339; Carbocisteine.
DR   SwissLipids; SLP:000000751; -. [Q9UNP4-3]
DR   SwissLipids; SLP:000000776; -.
DR   SwissLipids; SLP:000000868; -.
DR   SwissLipids; SLP:000000877; -. [Q9UNP4-3]
DR   CAZy; GT29; Glycosyltransferase Family 29.
DR   GlyCosmos; Q9UNP4; 3 sites, No reported glycans.
DR   GlyGen; Q9UNP4; 3 sites.
DR   iPTMnet; Q9UNP4; -.
DR   PhosphoSitePlus; Q9UNP4; -.
DR   SwissPalm; Q9UNP4; -.
DR   BioMuta; ST3GAL5; -.
DR   DMDM; 189047140; -.
DR   jPOST; Q9UNP4; -.
DR   MassIVE; Q9UNP4; -.
DR   MaxQB; Q9UNP4; -.
DR   PaxDb; 9606-ENSP00000366549; -.
DR   PeptideAtlas; Q9UNP4; -.
DR   ProteomicsDB; 85318; -. [Q9UNP4-1]
DR   ProteomicsDB; 85319; -. [Q9UNP4-2]
DR   ProteomicsDB; 85320; -. [Q9UNP4-3]
DR   Antibodypedia; 31972; 174 antibodies from 25 providers.
DR   DNASU; 8869; -.
DR   Ensembl; ENST00000393805.6; ENSP00000377394.1; ENSG00000115525.18. [Q9UNP4-2]
DR   Ensembl; ENST00000393808.8; ENSP00000377397.3; ENSG00000115525.18. [Q9UNP4-3]
DR   Ensembl; ENST00000638572.2; ENSP00000491316.1; ENSG00000115525.18. [Q9UNP4-1]
DR   Ensembl; ENST00000638986.1; ENSP00000491853.1; ENSG00000115525.18. [Q9UNP4-2]
DR   Ensembl; ENST00000639432.1; ENSP00000491828.1; ENSG00000115525.18. [Q9UNP4-2]
DR   Ensembl; ENST00000640322.1; ENSP00000491564.1; ENSG00000115525.18. [Q9UNP4-2]
DR   Ensembl; ENST00000640982.1; ENSP00000492299.1; ENSG00000115525.18. [Q9UNP4-2]
DR   Ensembl; ENST00000640992.1; ENSP00000492753.1; ENSG00000115525.18. [Q9UNP4-2]
DR   GeneID; 8869; -.
DR   KEGG; hsa:8869; -.
DR   MANE-Select; ENST00000638572.2; ENSP00000491316.1; NM_003896.4; NP_003887.3.
DR   UCSC; uc002sqp.2; human. [Q9UNP4-1]
DR   AGR; HGNC:10872; -.
DR   CTD; 8869; -.
DR   DisGeNET; 8869; -.
DR   GeneCards; ST3GAL5; -.
DR   GeneReviews; ST3GAL5; -.
DR   HGNC; HGNC:10872; ST3GAL5.
DR   HPA; ENSG00000115525; Low tissue specificity.
DR   MalaCards; ST3GAL5; -.
DR   MIM; 604402; gene.
DR   MIM; 609056; phenotype.
DR   neXtProt; NX_Q9UNP4; -.
DR   OpenTargets; ENSG00000115525; -.
DR   Orphanet; 370933; GM3 synthase deficiency.
DR   PharmGKB; PA35773; -.
DR   VEuPathDB; HostDB:ENSG00000115525; -.
DR   eggNOG; KOG2692; Eukaryota.
DR   GeneTree; ENSGT00940000157929; -.
DR   HOGENOM; CLU_032020_3_2_1; -.
DR   InParanoid; Q9UNP4; -.
DR   OMA; TPLHWVD; -.
DR   OrthoDB; 5404317at2759; -.
DR   PhylomeDB; Q9UNP4; -.
DR   TreeFam; TF352819; -.
DR   BioCyc; MetaCyc:HS03904-MONOMER; -.
DR   BRENDA; 2.4.99.9; 2681.
DR   PathwayCommons; Q9UNP4; -.
DR   Reactome; R-HSA-4085001; Sialic acid metabolism.
DR   SignaLink; Q9UNP4; -.
DR   SIGNOR; Q9UNP4; -.
DR   BioGRID-ORCS; 8869; 20 hits in 1167 CRISPR screens.
DR   ChiTaRS; ST3GAL5; human.
DR   GeneWiki; ST3GAL5; -.
DR   GenomeRNAi; 8869; -.
DR   Pharos; Q9UNP4; Tbio.
DR   PRO; PR:Q9UNP4; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q9UNP4; Protein.
DR   Bgee; ENSG00000115525; Expressed in right adrenal gland and 180 other cell types or tissues.
DR   ExpressionAtlas; Q9UNP4; baseline and differential.
DR   GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR   GO; GO:0016020; C:membrane; TAS:ProtInc.
DR   GO; GO:0003836; F:beta-galactoside (CMP) alpha-2,3-sialyltransferase activity; TAS:Reactome.
DR   GO; GO:0047291; F:lactosylceramide alpha-2,3-sialyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0008373; F:sialyltransferase activity; TAS:ProtInc.
DR   GO; GO:0001574; P:ganglioside biosynthetic process; IC:UniProtKB.
DR   GO; GO:0006688; P:glycosphingolipid biosynthetic process; TAS:ProtInc.
DR   GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
DR   Gene3D; 3.90.1480.20; Glycosyl transferase family 29; 1.
DR   InterPro; IPR001675; Glyco_trans_29.
DR   InterPro; IPR038578; GT29-like_sf.
DR   InterPro; IPR012163; Sialyl_trans.
DR   PANTHER; PTHR13713:SF60; LACTOSYLCERAMIDE ALPHA-2,3-SIALYLTRANSFERASE; 1.
DR   PANTHER; PTHR13713; SIALYLTRANSFERASE; 1.
DR   Pfam; PF00777; Glyco_transf_29; 1.
DR   PIRSF; PIRSF005557; Sialyl_trans; 1.
DR   Genevisible; Q9UNP4; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Disulfide bond; Epilepsy; Glycoprotein;
KW   Glycosyltransferase; Golgi apparatus; Intellectual disability;
KW   Lipid metabolism; Membrane; Reference proteome; Signal-anchor; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..418
FT                   /note="Lactosylceramide alpha-2,3-sialyltransferase"
FT                   /id="PRO_0000149302"
FT   TOPO_DOM        1..61
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        62..82
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        83..418
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        86
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        236
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        390
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        195..353
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..28
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_033686"
FT   VAR_SEQ         1..23
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16934889"
FT                   /id="VSP_033687"
FT   VAR_SEQ         24..28
FT                   /note="PAGRA -> MASVP (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16934889"
FT                   /id="VSP_033688"
FT   VARIANT         104
FT                   /note="H -> R (in dbSNP:rs1138484)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:9822625, ECO:0000269|Ref.2"
FT                   /id="VAR_025510"
SQ   SEQUENCE   418 AA;  47990 MW;  B423540B31C27A8A CRC64;
     MRTKAAGCAE RRPLQPRTEA AAAPAGRAMP SEYTYVKLRS DCSRPSLQWY TRAQSKMRRP
     SLLLKDILKC TLLVFGVWIL YILKLNYTTE ECDMKKMHYV DPDHVKRAQK YAQQVLQKEC
     RPKFAKTSMA LLFEHRYSVD LLPFVQKAPK DSEAESKYDP PFGFRKFSSK VQTLLELLPE
     HDLPEHLKAK TCRRCVVIGS GGILHGLELG HTLNQFDVVI RLNSAPVEGY SEHVGNKTTI
     RMTYPEGAPL SDLEYYSNDL FVAVLFKSVD FNWLQAMVKK ETLPFWVRLF FWKQVAEKIP
     LQPKHFRILN PVIIKETAFD ILQYSEPQSR FWGRDKNVPT IGVIAVVLAT HLCDEVSLAG
     FGYDLNQPRT PLHYFDSQCM AAMNFQTMHN VTTETKFLLK LVKEGVVKDL SGGIDREF
//