SIAT6_HUMAN
ID SIAT6_HUMAN Reviewed; 375 AA.
AC Q11203; A9Z1W2; D3DPX8; Q5T4W9; Q5T4X0; Q5T4X7; Q5T4X8; Q5T4X9; Q5T4Y0;
AC Q5T4Y2; Q5T4Y3; Q5T4Y4; Q86UR6; Q86UR7; Q86UR8; Q86UR9; Q86US0; Q86US1;
AC Q86US2; Q8IX41; Q8IX42; Q8IX43; Q8IX44; Q8IX45; Q8IX46; Q8IX47; Q8IX48;
AC Q8IX49; Q8IX50; Q8IX51; Q8IX52; Q8IX53; Q8IX54; Q8IX55; Q8IX56; Q8IX57;
AC Q8IX58;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase;
DE EC=2.4.99.6 {ECO:0000250|UniProtKB:P97325};
DE AltName: Full=Beta-galactoside alpha-2,3-sialyltransferase 3;
DE Short=Alpha 2,3-ST 3;
DE AltName: Full=Gal beta-1,3(4) GlcNAc alpha-2,3 sialyltransferase;
DE AltName: Full=N-acetyllactosaminide alpha-2,3-sialyltransferase;
DE AltName: Full=ST3Gal III;
DE Short=ST3GalIII;
DE AltName: Full=ST3N;
DE AltName: Full=Sialyltransferase 6;
GN Name=ST3GAL3; Synonyms=SIAT6;
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 B1).
RC TISSUE=Placenta;
RX PubMed=8333853; DOI=10.1006/bbrc.1993.1830;
RA Kitagawa H., Paulson J.C.;
RT "Cloning and expression of human Gal beta 1,3(4)GlcNAc alpha 2,3-
RT sialyltransferase.";
RL Biochem. Biophys. Res. Commun. 194:375-382(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A1; A7; A8; B1; B1-90; B1+32; B3; B4;
RP B4+173; B5+26; B5+173; B7; B8; C1; C7; C8; D2+26; E1 AND E3+32).
RA Grahn A., Larson G.;
RT "Structural variations of the alpha 2,3-sialyltransferase III, ST3GalIII,
RT transcripts in human peripheral white blood cells.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B10; C4; C5; C9; C11; C12 AND D5).
RC TISSUE=Fetal brain;
RA Grahn A., Larson G.;
RT "Structural variations of the alpha 2,3-sialyltransferase III, ST3GalIII,
RT transcripts in human fetal brain.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B1).
RC TISSUE=Brain;
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 [7]
RP VARIANTS MRT12 ASP-13 AND TYR-370, AND CHARACTERIZATION OF VARIANTS MRT12
RP ASP-13 AND TYR-370.
RX PubMed=21907012; DOI=10.1016/j.ajhg.2011.08.008;
RA Hu H., Eggers K., Chen W., Garshasbi M., Motazacker M.M., Wrogemann K.,
RA Kahrizi K., Tzschach A., Hosseini M., Bahman I., Hucho T., Muhlenhoff M.,
RA Gerardy-Schahn R., Najmabadi H., Ropers H.H., Kuss A.W.;
RT "ST3GAL3 mutations impair the development of higher cognitive functions.";
RL Am. J. Hum. Genet. 89:407-414(2011).
RN [8]
RP VARIANT DEE15 PRO-320, AND CHARACTERIZATION OF VARIANT DEE15 PRO-320.
RX PubMed=23252400; DOI=10.1111/epi.12050;
RA Edvardson S., Baumann A.M., Muehlenhoff M., Stephan O., Kuss A.W.,
RA Shaag A., He L., Zenvirt S., Tanzi R., Gerardy-Schahn R., Elpeleg O.;
RT "West syndrome caused by ST3Gal-III deficiency.";
RL Epilepsia 54:E24-E27(2013).
CC -!- FUNCTION: Catalyzes the formation of the NeuAc-alpha-2,3-Gal-beta-1,4-
CC GlcNAc-, NeuAc-alpha-2,3-Gal-beta-1,3-GlcNAc- and NeuAc-alpha-2,3-Gal-
CC beta-1,3-GalNAc- sequences found in terminal carbohydrate groups of
CC glycoproteins and glycolipids. The highest activity is toward Gal-beta-
CC 1,3-GlcNAc and the lowest toward Gal-beta-1,3-GalNAc.
CC {ECO:0000250|UniProtKB:P97325}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl
CC derivative + CMP-N-acetyl-beta-neuraminate = an N-acetyl-alpha-
CC neuraminyl-(2->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-
CC glucosaminyl derivative + CMP + H(+); Xref=Rhea:RHEA:52316,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:133507, ChEBI:CHEBI:136545; EC=2.4.99.6;
CC Evidence={ECO:0000250|UniProtKB:P97325};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- INTERACTION:
CC Q11203; Q86TI2-2: DPP9; NbExp=3; IntAct=EBI-717142, EBI-21529239;
CC Q11203; Q8N7X4: MAGEB6; NbExp=3; IntAct=EBI-717142, EBI-6447163;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-
CC pass type II membrane protein. Secreted. Note=Membrane-bound form in
CC trans cisternae of Golgi. Secreted into the body fluid.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=26;
CC Name=B1;
CC IsoId=Q11203-1; Sequence=Displayed;
CC Name=A1;
CC IsoId=Q11203-2; Sequence=VSP_010591;
CC Name=A7;
CC IsoId=Q11203-3; Sequence=VSP_010591, VSP_010607, VSP_010609;
CC Name=A8;
CC IsoId=Q11203-4; Sequence=VSP_010591, VSP_010597;
CC Name=B1-90;
CC IsoId=Q11203-5; Sequence=VSP_010617;
CC Name=B1+32;
CC IsoId=Q11203-6; Sequence=VSP_010611, VSP_010614;
CC Name=B3;
CC IsoId=Q11203-7; Sequence=VSP_010598;
CC Name=B4;
CC IsoId=Q11203-8; Sequence=VSP_010618;
CC Name=B4+173;
CC IsoId=Q11203-9; Sequence=VSP_010600, VSP_010603;
CC Name=B5+26;
CC IsoId=Q11203-10; Sequence=VSP_010613;
CC Name=B5+173;
CC IsoId=Q11203-11; Sequence=VSP_010602, VSP_010605;
CC Name=B7;
CC IsoId=Q11203-12; Sequence=VSP_010607, VSP_010609;
CC Name=B8;
CC IsoId=Q11203-13; Sequence=VSP_010597;
CC Name=B10;
CC IsoId=Q11203-14; Sequence=VSP_010606, VSP_010608;
CC Name=C1;
CC IsoId=Q11203-15; Sequence=VSP_010594;
CC Name=C4;
CC IsoId=Q11203-16; Sequence=VSP_010594, VSP_010618;
CC Name=C5;
CC IsoId=Q11203-17; Sequence=VSP_010594, VSP_010610, VSP_010615;
CC Name=C7;
CC IsoId=Q11203-18; Sequence=VSP_010594, VSP_010607, VSP_010609;
CC Name=C8;
CC IsoId=Q11203-19; Sequence=VSP_010594, VSP_010597;
CC Name=C9;
CC IsoId=Q11203-20; Sequence=VSP_010594, VSP_010612, VSP_010616;
CC Name=C11;
CC IsoId=Q11203-21; Sequence=VSP_010594, VSP_010598, VSP_010618;
CC Name=C12;
CC IsoId=Q11203-22; Sequence=VSP_010594, VSP_010601, VSP_010604;
CC Name=D2+26;
CC IsoId=Q11203-23; Sequence=VSP_010593, VSP_010613;
CC Name=D5;
CC IsoId=Q11203-24; Sequence=VSP_010593, VSP_010610, VSP_010615;
CC Name=E1;
CC IsoId=Q11203-25; Sequence=VSP_010592, VSP_010596;
CC Name=E3+32;
CC IsoId=Q11203-26; Sequence=VSP_010595, VSP_010599;
CC -!- TISSUE SPECIFICITY: Highly expressed in adult skeletal muscle and in
CC all fetal tissues examined and to a much lesser extent in placenta,
CC lung and liver.
CC -!- PTM: The soluble form derives from the membrane form by proteolytic
CC processing.
CC -!- DISEASE: Intellectual developmental disorder, autosomal recessive 12
CC (MRT12) [MIM:611090]: A disorder characterized by significantly below
CC average general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period.
CC {ECO:0000269|PubMed:21907012}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Developmental and epileptic encephalopathy 15 (DEE15)
CC [MIM:615006]: A form of epilepsy that manifests in the neonatal or the
CC early infantile period as severely impaired cognitive and motor
CC development, due to recurrent clinical seizures or prominent interictal
CC epileptiform discharges. Patients develop infantile spasms, mainly of
CC the flexor type, between 3 and 7 months of age, which are accompanied
CC by hypsarrhythmia on EEG. Other features include poor eye contact,
CC hypotonia, primitive reflexes, and irritability. Seizures evolve
CC clinically to Lennox-Gastaut syndrome. {ECO:0000269|PubMed:23252400}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- MISCELLANEOUS: [Isoform B1+32]: May be produced at very low levels due
CC to a premature stop codon in the mRNA, leading to nonsense-mediated
CC mRNA decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform B4+173]: May be produced at very low levels due
CC to a premature stop codon in the mRNA, leading to nonsense-mediated
CC mRNA decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform B5+173]: May be produced at very low levels due
CC to a premature stop codon in the mRNA, leading to nonsense-mediated
CC mRNA decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform B10]: May be produced at very low levels due to
CC a premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform C9]: May be produced at very low levels due to
CC a premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform E1]: May be produced at very low levels due to
CC a premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform E3+32]: May be produced at very low levels due
CC to a premature stop codon in the mRNA, leading to nonsense-mediated
CC mRNA decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=ST3Gal
CC III;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_624";
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DR EMBL; L23768; AAA35778.1; -; mRNA.
DR EMBL; AF425851; AAO13859.1; -; mRNA.
DR EMBL; AF425852; AAO13860.1; -; mRNA.
DR EMBL; AF425853; AAO13861.1; -; mRNA.
DR EMBL; AF425854; AAO13862.1; -; mRNA.
DR EMBL; AF425855; AAO13863.1; -; mRNA.
DR EMBL; AF425856; AAO13864.1; -; mRNA.
DR EMBL; AF425857; AAO13865.1; -; mRNA.
DR EMBL; AF425858; AAO13866.1; -; mRNA.
DR EMBL; AF425859; AAO13867.1; -; mRNA.
DR EMBL; AF425860; AAO13868.1; -; mRNA.
DR EMBL; AF425861; AAO13869.1; -; mRNA.
DR EMBL; AF425862; AAO13870.1; -; mRNA.
DR EMBL; AF425863; AAO13871.1; -; mRNA.
DR EMBL; AF425864; AAO13872.1; -; mRNA.
DR EMBL; AF425865; AAO13873.1; -; mRNA.
DR EMBL; AF425866; AAO13874.1; -; mRNA.
DR EMBL; AF425867; AAO13875.1; -; mRNA.
DR EMBL; AF425868; AAO13876.1; -; mRNA.
DR EMBL; AF425869; AAO13877.1; -; mRNA.
DR EMBL; AY167992; AAO38806.1; -; mRNA.
DR EMBL; AY167993; AAO38807.1; -; mRNA.
DR EMBL; AY167994; AAO38808.1; -; mRNA.
DR EMBL; AY167995; AAO38809.1; -; mRNA.
DR EMBL; AY167996; AAO38810.1; -; mRNA.
DR EMBL; AY167997; AAO38811.1; -; mRNA.
DR EMBL; AY167998; AAO38812.1; -; mRNA.
DR EMBL; AL357079; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL451062; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL592548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07082.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07083.1; -; Genomic_DNA.
DR EMBL; BC050380; AAH50380.1; -; mRNA.
DR CCDS; CCDS492.1; -. [Q11203-1]
DR CCDS; CCDS493.1; -. [Q11203-4]
DR CCDS; CCDS494.1; -. [Q11203-2]
DR CCDS; CCDS495.1; -. [Q11203-8]
DR CCDS; CCDS496.1; -. [Q11203-13]
DR CCDS; CCDS497.1; -. [Q11203-15]
DR CCDS; CCDS498.1; -. [Q11203-19]
DR CCDS; CCDS499.1; -. [Q11203-3]
DR CCDS; CCDS500.1; -. [Q11203-12]
DR CCDS; CCDS53310.1; -. [Q11203-18]
DR CCDS; CCDS57988.1; -. [Q11203-5]
DR CCDS; CCDS57989.1; -. [Q11203-7]
DR CCDS; CCDS57990.1; -. [Q11203-16]
DR CCDS; CCDS57991.1; -. [Q11203-17]
DR CCDS; CCDS57992.1; -. [Q11203-22]
DR CCDS; CCDS57993.1; -. [Q11203-24]
DR CCDS; CCDS57994.1; -. [Q11203-23]
DR CCDS; CCDS85964.1; -. [Q11203-21]
DR PIR; JN0618; JN0618.
DR RefSeq; NP_001257388.1; NM_001270459.1. [Q11203-5]
DR RefSeq; NP_001257389.1; NM_001270460.1. [Q11203-7]
DR RefSeq; NP_001257390.1; NM_001270461.1. [Q11203-16]
DR RefSeq; NP_001257391.1; NM_001270462.1. [Q11203-21]
DR RefSeq; NP_001257392.1; NM_001270463.1. [Q11203-24]
DR RefSeq; NP_001257393.1; NM_001270464.1. [Q11203-17]
DR RefSeq; NP_001257394.1; NM_001270465.1. [Q11203-23]
DR RefSeq; NP_001257395.1; NM_001270466.1. [Q11203-22]
DR RefSeq; NP_006270.1; NM_006279.3. [Q11203-1]
DR RefSeq; NP_777623.2; NM_174963.3. [Q11203-4]
DR RefSeq; NP_777624.1; NM_174964.2. [Q11203-2]
DR RefSeq; NP_777625.1; NM_174965.2. [Q11203-3]
DR RefSeq; NP_777626.1; NM_174966.2. [Q11203-8]
DR RefSeq; NP_777627.1; NM_174967.2. [Q11203-12]
DR RefSeq; NP_777628.2; NM_174968.3. [Q11203-13]
DR RefSeq; NP_777629.1; NM_174969.2. [Q11203-15]
DR RefSeq; NP_777630.1; NM_174970.2. [Q11203-18]
DR RefSeq; NP_777631.2; NM_174971.3. [Q11203-19]
DR RefSeq; XP_016857602.1; XM_017002113.1. [Q11203-1]
DR AlphaFoldDB; Q11203; -.
DR SMR; Q11203; -.
DR BioGRID; 112379; 19.
DR IntAct; Q11203; 7.
DR ChEMBL; CHEMBL3596076; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyGen; Q11203; 2 sites.
DR iPTMnet; Q11203; -.
DR PhosphoSitePlus; Q11203; -.
DR BioMuta; ST3GAL3; -.
DR DMDM; 1705561; -.
DR MassIVE; Q11203; -.
DR PeptideAtlas; Q11203; -.
DR PRIDE; Q11203; -.
DR ProteomicsDB; 58876; -. [Q11203-11]
DR Antibodypedia; 32385; 166 antibodies from 26 providers.
DR DNASU; 6487; -.
DR Ensembl; ENST00000262915.8; ENSP00000262915.3; ENSG00000126091.21. [Q11203-4]
DR Ensembl; ENST00000330208.6; ENSP00000333494.3; ENSG00000126091.21. [Q11203-22]
DR Ensembl; ENST00000335430.10; ENSP00000335633.7; ENSG00000126091.21. [Q11203-23]
DR Ensembl; ENST00000347631.8; ENSP00000317192.6; ENSG00000126091.21. [Q11203-1]
DR Ensembl; ENST00000351035.8; ENSP00000316999.6; ENSG00000126091.21. [Q11203-13]
DR Ensembl; ENST00000353126.8; ENSP00000330463.3; ENSG00000126091.21. [Q11203-8]
DR Ensembl; ENST00000361392.9; ENSP00000355341.5; ENSG00000126091.21. [Q11203-2]
DR Ensembl; ENST00000361400.9; ENSP00000354748.4; ENSG00000126091.21. [Q11203-15]
DR Ensembl; ENST00000361812.9; ENSP00000355201.4; ENSG00000126091.21. [Q11203-3]
DR Ensembl; ENST00000372362.6; ENSP00000361437.2; ENSG00000126091.21. [Q11203-12]
DR Ensembl; ENST00000372365.5; ENSP00000361440.1; ENSG00000126091.21. [Q11203-10]
DR Ensembl; ENST00000372366.6; ENSP00000361441.1; ENSG00000126091.21. [Q11203-23]
DR Ensembl; ENST00000372367.5; ENSP00000361442.1; ENSG00000126091.21. [Q11203-24]
DR Ensembl; ENST00000372369.5; ENSP00000361444.1; ENSG00000126091.21. [Q11203-5]
DR Ensembl; ENST00000372372.7; ENSP00000361447.2; ENSG00000126091.21. [Q11203-19]
DR Ensembl; ENST00000372374.7; ENSP00000361449.2; ENSG00000126091.21. [Q11203-7]
DR Ensembl; ENST00000469715.6; ENSP00000431700.2; ENSG00000126091.21. [Q11203-26]
DR Ensembl; ENST00000489897.6; ENSP00000437206.1; ENSG00000126091.21. [Q11203-11]
DR Ensembl; ENST00000490541.6; ENSP00000435018.2; ENSG00000126091.21. [Q11203-25]
DR Ensembl; ENST00000528371.5; ENSP00000434876.1; ENSG00000126091.21. [Q11203-17]
DR Ensembl; ENST00000530581.5; ENSP00000437293.1; ENSG00000126091.21. [Q11203-20]
DR Ensembl; ENST00000531451.5; ENSP00000435603.1; ENSG00000126091.21. [Q11203-18]
DR Ensembl; ENST00000531816.1; ENSP00000434378.1; ENSG00000126091.21. [Q11203-22]
DR Ensembl; ENST00000531993.6; ENSP00000432682.2; ENSG00000126091.21. [Q11203-21]
DR Ensembl; ENST00000533212.5; ENSP00000435621.1; ENSG00000126091.21. [Q11203-14]
DR Ensembl; ENST00000533997.6; ENSP00000432071.1; ENSG00000126091.21. [Q11203-9]
DR Ensembl; ENST00000545417.5; ENSP00000439634.1; ENSG00000126091.21. [Q11203-3]
DR Ensembl; ENST00000642504.1; ENSP00000494857.1; ENSG00000126091.21. [Q11203-9]
DR Ensembl; ENST00000642934.1; ENSP00000494146.1; ENSG00000126091.21. [Q11203-16]
DR Ensembl; ENST00000642949.1; ENSP00000495709.1; ENSG00000126091.21. [Q11203-6]
DR Ensembl; ENST00000644195.1; ENSP00000494201.1; ENSG00000126091.21. [Q11203-1]
DR Ensembl; ENST00000645142.1; ENSP00000496550.1; ENSG00000126091.21. [Q11203-6]
DR Ensembl; ENST00000645165.1; ENSP00000493660.1; ENSG00000126091.21. [Q11203-11]
DR Ensembl; ENST00000645640.1; ENSP00000494852.1; ENSG00000126091.21. [Q11203-11]
DR Ensembl; ENST00000646971.1; ENSP00000495887.1; ENSG00000126091.21. [Q11203-1]
DR GeneID; 6487; -.
DR KEGG; hsa:6487; -.
DR MANE-Select; ENST00000347631.8; ENSP00000317192.6; NM_006279.5; NP_006270.1.
DR UCSC; uc001cjz.5; human. [Q11203-1]
DR CTD; 6487; -.
DR DisGeNET; 6487; -.
DR GeneCards; ST3GAL3; -.
DR HGNC; HGNC:10866; ST3GAL3.
DR HPA; ENSG00000126091; Tissue enhanced (skeletal muscle, tongue).
DR MalaCards; ST3GAL3; -.
DR MIM; 606494; gene.
DR MIM; 611090; phenotype.
DR MIM; 615006; phenotype.
DR neXtProt; NX_Q11203; -.
DR OpenTargets; ENSG00000126091; -.
DR Orphanet; 88616; Autosomal recessive non-syndromic intellectual disability.
DR Orphanet; 3451; Infantile spasms syndrome.
DR PharmGKB; PA35768; -.
DR VEuPathDB; HostDB:ENSG00000126091; -.
DR GeneTree; ENSGT00940000157285; -.
DR HOGENOM; CLU_032020_3_0_1; -.
DR InParanoid; Q11203; -.
DR OMA; NDINVGR; -.
DR PhylomeDB; Q11203; -.
DR TreeFam; TF354325; -.
DR BioCyc; MetaCyc:HS04994-MON; -.
DR BRENDA; 2.4.99.2; 2681.
DR BRENDA; 2.4.99.6; 2681.
DR PathwayCommons; Q11203; -.
DR Reactome; R-HSA-1912420; Pre-NOTCH Processing in Golgi.
DR Reactome; R-HSA-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-HSA-3656243; Defective ST3GAL3 causes MCT12 and EIEE15.
DR Reactome; R-HSA-4085001; Sialic acid metabolism.
DR Reactome; R-HSA-9037629; Lewis blood group biosynthesis.
DR Reactome; R-HSA-9683673; Maturation of protein 3a.
DR Reactome; R-HSA-9694548; Maturation of spike protein.
DR Reactome; R-HSA-9694719; Maturation of protein 3a.
DR Reactome; R-HSA-977068; Termination of O-glycan biosynthesis.
DR SignaLink; Q11203; -.
DR SIGNOR; Q11203; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 6487; 12 hits in 1072 CRISPR screens.
DR ChiTaRS; ST3GAL3; human.
DR GeneWiki; ST3GAL3; -.
DR GenomeRNAi; 6487; -.
DR Pharos; Q11203; Tbio.
DR PRO; PR:Q11203; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q11203; protein.
DR Bgee; ENSG00000126091; Expressed in hindlimb stylopod muscle and 115 other tissues.
DR ExpressionAtlas; Q11203; baseline and differential.
DR Genevisible; Q11203; HS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003836; F:beta-galactoside (CMP) alpha-2,3-sialyltransferase activity; TAS:Reactome.
DR GO; GO:0008118; F:N-acetyllactosaminide alpha-2,3-sialyltransferase activity; TAS:ProtInc.
DR GO; GO:0008373; F:sialyltransferase activity; IBA:GO_Central.
DR GO; GO:0010706; P:ganglioside biosynthetic process via lactosylceramide; IEA:Ensembl.
DR GO; GO:0018146; P:keratan sulfate biosynthetic process; TAS:Reactome.
DR GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; TAS:Reactome.
DR GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
DR GO; GO:0019082; P:viral protein processing; TAS:Reactome.
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 splicing; Disease variant; Disulfide bond; Epilepsy;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Intellectual disability; Membrane; Reference proteome; Secreted;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..375
FT /note="CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-
FT 2,3-sialyltransferase"
FT /id="PRO_0000149266"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..375
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 160..314
FT /evidence="ECO:0000250"
FT VAR_SEQ 40..73
FT /note="NSVVLSFDSAGQTLGSEYDRLGFLLNLDSKLPAE -> SSPSQHPCSWMTPF
FT ASGLESGSSCRLLGSKVKTI (in isoform E3+32)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_010595"
FT VAR_SEQ 40..56
FT /note="NSVVLSFDSAGQTLGSE -> K (in isoform C1, isoform C4,
FT isoform C5, isoform C7, isoform C8, isoform C9, isoform C11
FT and isoform C12)"
FT /evidence="ECO:0000303|Ref.2, ECO:0000303|Ref.3"
FT /id="VSP_010594"
FT VAR_SEQ 40..55
FT /note="NSVVLSFDSAGQTLGS -> SKYSHSSSPQEKPVA (in isoform D5
FT and isoform D2+26)"
FT /evidence="ECO:0000303|Ref.2, ECO:0000303|Ref.3"
FT /id="VSP_010593"
FT VAR_SEQ 40..43
FT /note="NSVV -> SLLN (in isoform E1)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_010592"
FT VAR_SEQ 40
FT /note="N -> SKYSHSSSPQEKPVAD (in isoform A1, isoform A7 and
FT isoform A8)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_010591"
FT VAR_SEQ 44..375
FT /note="Missing (in isoform E1)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_010596"
FT VAR_SEQ 70
FT /note="L -> LSPRTLCTVVFGLDCILESPGEPKKLLMPASHPLEILKSLSEDTAFA
FT LGFLKLPR (in isoform A8, isoform B8 and isoform C8)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_010597"
FT VAR_SEQ 71..101
FT /note="Missing (in isoform B3 and isoform C11)"
FT /evidence="ECO:0000303|Ref.2, ECO:0000303|Ref.3"
FT /id="VSP_010598"
FT VAR_SEQ 74..375
FT /note="Missing (in isoform E3+32)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_010599"
FT VAR_SEQ 102..121
FT /note="FSKPAPMFLDDSFRKWARIR -> AKRNGAWRQKHIQAYVLRQR (in
FT isoform B5+173)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_010602"
FT VAR_SEQ 102..117
FT /note="FSKPAPMFLDDSFRKW -> PGRTISSERKSFCGSW (in isoform
FT C12)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_010601"
FT VAR_SEQ 102..115
FT /note="FSKPAPMFLDDSFR -> EKVRTFMAWLAWYG (in isoform
FT B4+173)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_010600"
FT VAR_SEQ 116..375
FT /note="Missing (in isoform B4+173)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_010603"
FT VAR_SEQ 118..375
FT /note="Missing (in isoform C12)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_010604"
FT VAR_SEQ 122..375
FT /note="Missing (in isoform B5+173)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_010605"
FT VAR_SEQ 133..155
FT /note="DNLIKAILSVTKEYRLTPALDSL -> VLDAQYPARERVSAEAGESSRHH
FT (in isoform A7, isoform B7 and isoform C7)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_010607"
FT VAR_SEQ 133..151
FT /note="DNLIKAILSVTKEYRLTPA -> ECIGWLLEICGHSSAQGAP (in
FT isoform B10)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_010606"
FT VAR_SEQ 152..375
FT /note="Missing (in isoform B10)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_010608"
FT VAR_SEQ 156..375
FT /note="Missing (in isoform A7, isoform B7 and isoform C7)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_010609"
FT VAR_SEQ 186..202
FT /note="RLNSAPVKGFEKDVGSK -> SPGRTISSERKSFCGSW (in isoform
FT C5 and isoform D5)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_010610"
FT VAR_SEQ 187..375
FT /note="Missing (in isoform B5+26 and isoform D2+26)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_010613"
FT VAR_SEQ 187..244
FT /note="LNSAPVKGFEKDVGSKTTLRITYPEGAMQRPEQYERDSLFVLAGFKWQDFKW
FT LKYIVY -> VHRMASGNLWPLECPRSPLRFESSTHISSRRPPSPSLACPSTMASWAGG
FT TSLPLAVWQ (in isoform C9)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_010612"
FT VAR_SEQ 187..189
FT /note="LNS -> PRL (in isoform B1+32)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_010611"
FT VAR_SEQ 190..375
FT /note="Missing (in isoform B1+32)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_010614"
FT VAR_SEQ 203..375
FT /note="Missing (in isoform C5 and isoform D5)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_010615"
FT VAR_SEQ 245..375
FT /note="Missing (in isoform C9)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_010616"
FT VAR_SEQ 249..346
FT /note="Missing (in isoform B4, isoform C4 and isoform C11)"
FT /evidence="ECO:0000303|Ref.2, ECO:0000303|Ref.3"
FT /id="VSP_010618"
FT VAR_SEQ 249..278
FT /note="Missing (in isoform B1-90)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_010617"
FT VARIANT 13
FT /note="A -> D (in MRT12; most of the mutant protein is
FT improperly localized to the endoplasmic reticulum
FT preventing the protein from interacting with its substrates
FT in the Golgi and resulting in a loss-of-function;
FT dbSNP:rs387906943)"
FT /evidence="ECO:0000269|PubMed:21907012"
FT /id="VAR_066594"
FT VARIANT 320
FT /note="A -> P (in DEE15)"
FT /evidence="ECO:0000269|PubMed:23252400"
FT /id="VAR_069319"
FT VARIANT 370
FT /note="D -> Y (in MRT12; the mutant protein is improperly
FT localized to the endoplasmic reticulum preventing the
FT protein from interacting with its substrates in the Golgi
FT and resulting in a loss-of-function; shows a complete lack
FT of enzyme activity; secretion of the mutant protein is
FT dramatically reduced compared to wild-type)"
FT /evidence="ECO:0000269|PubMed:21907012"
FT /id="VAR_066595"
FT CONFLICT 38
FT /note="D -> N (in Ref. 3; AAO38806)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="L -> S (in Ref. 3; AAO38810)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="F -> L (in Ref. 3; AAO38810)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="N -> S (in Ref. 3; AAO38811)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 375 AA; 42171 MW; C9B7B61AD580EC2E CRC64;
MGLLVFVRNL LLALCLFLVL GFLYYSAWKL HLLQWEEDSN SVVLSFDSAG QTLGSEYDRL
GFLLNLDSKL PAELATKYAN FSEGACKPGY ASALMTAIFP RFSKPAPMFL DDSFRKWARI
REFVPPFGIK GQDNLIKAIL SVTKEYRLTP ALDSLRCRRC IIVGNGGVLA NKSLGSRIDD
YDIVVRLNSA PVKGFEKDVG SKTTLRITYP EGAMQRPEQY ERDSLFVLAG FKWQDFKWLK
YIVYKERVSA SDGFWKSVAT RVPKEPPEIR ILNPYFIQEA AFTLIGLPFN NGLMGRGNIP
TLGSVAVTMA LHGCDEVAVA GFGYDMSTPN APLHYYETVR MAAIKESWTH NIQREKEFLR
KLVKARVITD LSSGI