SIA4C_HUMAN
ID SIA4C_HUMAN Reviewed; 333 AA.
AC Q11206; A8K6B2; O60497; Q8N6A6; Q8NFG7; Q96QQ9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4;
DE Short=Alpha 2,3-ST 4;
DE Short=Beta-galactoside alpha-2,3-sialyltransferase 4;
DE EC=2.4.99.2 {ECO:0000269|PubMed:8288606};
DE EC=2.4.99.4 {ECO:0000269|PubMed:8288606};
DE AltName: Full=Alpha 2,3-sialyltransferase IV;
DE AltName: Full=Gal-NAc6S;
DE AltName: Full=Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase {ECO:0000303|PubMed:8288606};
DE AltName: Full=Gal-beta-1,4-GlcNAc-alpha-2,3-sialyltransferase {ECO:0000303|PubMed:8288606};
DE AltName: Full=N-acetyllactosaminide alpha-2,3-sialyltransferase;
DE EC=2.4.99.6 {ECO:0000269|PubMed:8288606, ECO:0000269|PubMed:8611500};
DE AltName: Full=SAT-3 {ECO:0000303|PubMed:8611500};
DE AltName: Full=ST-4;
DE AltName: Full=ST3Gal IV;
DE Short=ST3GalIV;
DE AltName: Full=ST3GalA.2;
DE AltName: Full=STZ {ECO:0000303|PubMed:8288606};
DE AltName: Full=Sialyltransferase 4C;
DE Short=SIAT4-C;
GN Name=ST3GAL4; Synonyms=CGS23, NANTA3, SIAT4C, STZ;
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].
RC TISSUE=Placenta;
RX PubMed=8557707; DOI=10.1074/jbc.271.2.931;
RA Kitagawa H., Mattei M.-G., Paulson J.C.;
RT "Genomic organization and chromosomal mapping of the Gal beta 1,3GalNAc/Gal
RT beta 1,4GlcNAc alpha 2,3-sialyltransferase.";
RL J. Biol. Chem. 271:931-938(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=8288606; DOI=10.1016/s0021-9258(17)42271-x;
RA Kitagawa H., Paulson J.C.;
RT "Cloning of a novel alpha 2,3-sialyltransferase that sialylates
RT glycoprotein and glycolipid carbohydrate groups.";
RL J. Biol. Chem. 269:1394-1401(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RX PubMed=7901202; DOI=10.1016/s0021-9258(18)41595-5;
RA Sasaki K., Watanabe E., Kawashima K., Sekine S., Dohi T., Oshima M.,
RA Hanai N., Nishi T., Hasegawa M.;
RT "Expression cloning of a novel Gal beta (1-3/1-4) GlcNAc alpha 2,3-
RT sialyltransferase using lectin resistance selection.";
RL J. Biol. Chem. 268:22782-22787(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 6 AND 7), AND ALTERNATIVE SPLICING.
RC TISSUE=Peripheral blood leukocyte;
RX PubMed=12441665; DOI=10.1023/a:1021199300718;
RA Grahn A., Larson G.;
RT "Identification of nine alternatively spliced alpha2,3-sialyltransferase,
RT ST3Gal IV, transcripts and analysis of their expression by RT-PCR and
RT laser-induced fluorescent capillary electrophoresis (LIF-CE) in twenty-one
RT human tissues.";
RL Glycoconj. J. 18:759-767(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Placenta;
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=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 48-314, FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Colon carcinoma;
RX PubMed=8611500; DOI=10.1021/bi960239l;
RA Basu S.S., Basu M., Li Z., Basu S.;
RT "Characterization of two glycolipid: alpha 2-3sialyltransferases, SAT-3
RT (CMP-NeuAc:nLcOse4Cer alpha 2-3sialyltransferase) and SAT-4 (CMP-
RT NeuAc:GgOse4Cer alpha 2-3sialyltransferase), from human colon carcinoma
RT (Colo 205) cell line.";
RL Biochemistry 35:5166-5174(1996).
RN [9]
RP FUNCTION.
RX PubMed=25498912; DOI=10.1182/blood-2014-07-588590;
RA Mondal N., Buffone A. Jr., Stolfa G., Antonopoulos A., Lau J.T.,
RA Haslam S.M., Dell A., Neelamegham S.;
RT "ST3Gal-4 is the primary sialyltransferase regulating the synthesis of E-,
RT P-, and L-selectin ligands on human myeloid leukocytes.";
RL Blood 125:687-696(2015).
CC -!- FUNCTION: A beta-galactoside alpha2-3 sialyltransferase involved in
CC terminal sialylation of glycoproteins and glycolipids (PubMed:8288606,
CC PubMed:8611500). Catalyzes the transfer of sialic acid (N-acetyl-
CC neuraminic acid; Neu5Ac) from the nucleotide sugar donor CMP-Neu5Ac
CC onto acceptor Galbeta-(1->3)-GalNAc- and Galbeta-(1->4)-GlcNAc-
CC terminated glycoconjugates through an alpha2-3 linkage (PubMed:8288606,
CC PubMed:8611500). Plays a major role in hemostasis. Responsible for
CC sialylation of plasma VWF/von Willebrand factor, preventing its
CC recognition by asialoglycoprotein receptors (ASGPR) and subsequent
CC clearance. Regulates ASGPR-mediated clearance of platelets (By
CC similarity). Participates in the biosynthesis of the sialyl Lewis X
CC epitopes, both on O- and N-glycans, which are recognized by SELE/E-
CC selectin, SELP/P-selectin and SELL/L-selectin. Essential for selectin-
CC mediated rolling and adhesion of leukocytes during extravasation
CC (PubMed:25498912). Contributes to adhesion and transendothelial
CC migration of neutrophils likely through terminal sialylation of CXCR2
CC (By similarity). In glycosphingolipid biosynthesis, sialylates GM1 and
CC GA1 gangliosides to form GD1a and GM1b, respectively (PubMed:8288606).
CC Metabolizes brain c-series ganglioside GT1c forming GQ1c (By
CC similarity). Synthesizes ganglioside LM1 (IV3Neu5Ac-nLc4Cer), a major
CC structural component of peripheral nerve myelin (PubMed:8611500).
CC {ECO:0000250|UniProtKB:P61131, ECO:0000250|UniProtKB:Q91Y74,
CC ECO:0000269|PubMed:25498912, ECO:0000269|PubMed:8288606,
CC ECO:0000269|PubMed:8611500}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-galactosaminyl
CC derivative + CMP-N-acetyl-beta-neuraminate = an N-acetyl-alpha-
CC neuraminyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-
CC galactosaminyl derivative + CMP + H(+); Xref=Rhea:RHEA:52380,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:136588, ChEBI:CHEBI:136589; EC=2.4.99.2;
CC Evidence={ECO:0000269|PubMed:8288606};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52381;
CC Evidence={ECO:0000305|PubMed:8288606};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl
CC derivative + CMP-N-acetyl-beta-neuraminate = an N-acetyl-alpha-
CC neuraminyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl derivative + CMP + H(+); Xref=Rhea:RHEA:21616,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:133470, ChEBI:CHEBI:139596; EC=2.4.99.4;
CC Evidence={ECO:0000269|PubMed:8288606};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21617;
CC Evidence={ECO:0000305|PubMed:8288606};
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:0000269|PubMed:8288606, ECO:0000269|PubMed:8611500};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52317;
CC Evidence={ECO:0000305|PubMed:8288606, ECO:0000305|PubMed:8611500};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GM1 (d18:1(4E)) =
CC CMP + ganglioside GD1a (d18:1(4E)) + H(+); Xref=Rhea:RHEA:18021,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:77709, ChEBI:CHEBI:78445; EC=2.4.99.2;
CC Evidence={ECO:0000269|PubMed:8288606};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18022;
CC Evidence={ECO:0000305|PubMed:8288606};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GA1 (d18:1(4E)) =
CC CMP + ganglioside GM1b (d18:1(4E)) + H(+); Xref=Rhea:RHEA:47560,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:27938, ChEBI:CHEBI:57812,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:78568;
CC Evidence={ECO:0000269|PubMed:8288606};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47561;
CC Evidence={ECO:0000305|PubMed:8288606};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GT1c (d18:1(4E)) =
CC CMP + ganglioside GQ1c (d18:1(4E)) + H(+); Xref=Rhea:RHEA:47588,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:87789, ChEBI:CHEBI:87791;
CC Evidence={ECO:0000250|UniProtKB:P61131};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47589;
CC Evidence={ECO:0000250|UniProtKB:P61131};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside nLc4Cer + CMP-N-acetyl-beta-neuraminate = a
CC neolactoside IV(3)-alpha-NeuAc-nLc4Cer + CMP + H(+);
CC Xref=Rhea:RHEA:65432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:90376, ChEBI:CHEBI:90390;
CC Evidence={ECO:0000269|PubMed:8611500};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65433;
CC Evidence={ECO:0000305|PubMed:8611500};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside nLc4Cer(d18:1(4E)) + CMP-N-acetyl-beta-
CC neuraminate = a neolactoside IV(3)-alpha-NeuAc-nLc4Cer(d18:1(4E)) +
CC CMP + H(+); Xref=Rhea:RHEA:18913, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17006, ChEBI:CHEBI:57812, ChEBI:CHEBI:58665,
CC ChEBI:CHEBI:60377; EC=2.4.99.6;
CC Evidence={ECO:0000305|PubMed:8611500};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18914;
CC Evidence={ECO:0000305|PubMed:8611500};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.2 mM for Gal-beta-1,3-GalNAc {ECO:0000269|PubMed:8288606};
CC KM=0.3 mM for Gal-beta-1,4-GlcNAc {ECO:0000269|PubMed:8288606};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000305|PubMed:8288606}.
CC -!- PATHWAY: Glycolipid biosynthesis. {ECO:0000305|PubMed:8288606}.
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=7;
CC Name=1; Synonyms=B1;
CC IsoId=Q11206-1; Sequence=Displayed;
CC Name=2; Synonyms=A1;
CC IsoId=Q11206-2; Sequence=VSP_001784;
CC Name=3; Synonyms=A2;
CC IsoId=Q11206-3; Sequence=VSP_001785;
CC Name=4; Synonyms=C;
CC IsoId=Q11206-4; Sequence=VSP_001786;
CC Name=5;
CC IsoId=Q11206-5; Sequence=VSP_021104;
CC Name=6;
CC IsoId=Q11206-6; Sequence=VSP_001784, VSP_021104;
CC Name=7;
CC IsoId=Q11206-7; Sequence=VSP_001785, VSP_021104;
CC -!- TISSUE SPECIFICITY: Highly expressed in adult placenta, heart and
CC kidney. {ECO:0000269|PubMed:8288606}.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal tissues, with highest levels in
CC heart, lung, and kidney. {ECO:0000269|PubMed:8288606}.
CC -!- PTM: The soluble form derives from the membrane form by proteolytic
CC processing.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=ST3Gal
CC IV;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_625";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L23767; AAA16460.1; -; mRNA.
DR EMBL; X74570; CAA52662.1; -; mRNA.
DR EMBL; AF516603; AAM66432.1; -; mRNA.
DR EMBL; AF516604; AAM66433.1; -; mRNA.
DR EMBL; AY040826; AAK93790.1; -; mRNA.
DR EMBL; AK291577; BAF84266.1; -; mRNA.
DR EMBL; AP000806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010645; AAH10645.1; -; mRNA.
DR EMBL; AF035249; AAC14162.1; -; mRNA.
DR CCDS; CCDS58193.1; -. [Q11206-1]
DR CCDS; CCDS58194.1; -. [Q11206-2]
DR CCDS; CCDS8474.1; -. [Q11206-5]
DR PIR; A48715; A48715.
DR PIR; A49879; A49879.
DR RefSeq; NP_001241686.1; NM_001254757.1. [Q11206-1]
DR RefSeq; NP_001241687.1; NM_001254758.1. [Q11206-1]
DR RefSeq; NP_001241688.1; NM_001254759.1. [Q11206-2]
DR RefSeq; NP_001335328.1; NM_001348399.1. [Q11206-1]
DR RefSeq; NP_001335329.1; NM_001348400.1. [Q11206-5]
DR RefSeq; NP_006269.1; NM_006278.2. [Q11206-5]
DR AlphaFoldDB; Q11206; -.
DR SMR; Q11206; -.
DR BioGRID; 112377; 66.
DR IntAct; Q11206; 13.
DR STRING; 9606.ENSP00000436047; -.
DR SwissLipids; SLP:000001384; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyGen; Q11206; 4 sites.
DR iPTMnet; Q11206; -.
DR PhosphoSitePlus; Q11206; -.
DR BioMuta; ST3GAL4; -.
DR EPD; Q11206; -.
DR jPOST; Q11206; -.
DR MassIVE; Q11206; -.
DR MaxQB; Q11206; -.
DR PaxDb; Q11206; -.
DR PeptideAtlas; Q11206; -.
DR PRIDE; Q11206; -.
DR ProteomicsDB; 58900; -. [Q11206-1]
DR ProteomicsDB; 58901; -. [Q11206-2]
DR ProteomicsDB; 58902; -. [Q11206-3]
DR ProteomicsDB; 58903; -. [Q11206-4]
DR ProteomicsDB; 58904; -. [Q11206-5]
DR ProteomicsDB; 72151; -.
DR Antibodypedia; 33000; 167 antibodies from 25 providers.
DR DNASU; 6484; -.
DR Ensembl; ENST00000227495.10; ENSP00000227495.6; ENSG00000110080.20. [Q11206-5]
DR Ensembl; ENST00000392669.6; ENSP00000376437.2; ENSG00000110080.20. [Q11206-1]
DR Ensembl; ENST00000444328.7; ENSP00000394354.2; ENSG00000110080.20. [Q11206-1]
DR Ensembl; ENST00000449406.6; ENSP00000399444.2; ENSG00000110080.20. [Q11206-3]
DR Ensembl; ENST00000526727.5; ENSP00000436047.1; ENSG00000110080.20. [Q11206-1]
DR Ensembl; ENST00000530591.5; ENSP00000433989.1; ENSG00000110080.20. [Q11206-5]
DR Ensembl; ENST00000532243.5; ENSP00000434349.1; ENSG00000110080.20. [Q11206-2]
DR Ensembl; ENST00000534083.5; ENSP00000433318.1; ENSG00000110080.20. [Q11206-1]
DR Ensembl; ENST00000534457.5; ENSP00000434668.1; ENSG00000110080.20. [Q11206-6]
DR GeneID; 6484; -.
DR KEGG; hsa:6484; -.
DR MANE-Select; ENST00000444328.7; ENSP00000394354.2; NM_001254757.2; NP_001241686.1.
DR UCSC; uc001qds.4; human. [Q11206-1]
DR CTD; 6484; -.
DR DisGeNET; 6484; -.
DR GeneCards; ST3GAL4; -.
DR HGNC; HGNC:10864; ST3GAL4.
DR HPA; ENSG00000110080; Low tissue specificity.
DR MIM; 104240; gene.
DR neXtProt; NX_Q11206; -.
DR OpenTargets; ENSG00000110080; -.
DR PharmGKB; PA35766; -.
DR VEuPathDB; HostDB:ENSG00000110080; -.
DR eggNOG; KOG2692; Eukaryota.
DR GeneTree; ENSGT00940000158893; -.
DR HOGENOM; CLU_032020_1_0_1; -.
DR InParanoid; Q11206; -.
DR OMA; KSPPLCM; -.
DR OrthoDB; 891104at2759; -.
DR PhylomeDB; Q11206; -.
DR TreeFam; TF354325; -.
DR BioCyc; MetaCyc:HS03285-MON; -.
DR BRENDA; 2.4.99.2; 2681.
DR BRENDA; 2.4.99.6; 2681.
DR PathwayCommons; Q11206; -.
DR Reactome; R-HSA-1912420; Pre-NOTCH Processing in Golgi.
DR Reactome; R-HSA-2022854; Keratan sulfate biosynthesis.
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-975577; N-Glycan antennae elongation.
DR Reactome; R-HSA-977068; Termination of O-glycan biosynthesis.
DR SignaLink; Q11206; -.
DR SIGNOR; Q11206; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 6484; 14 hits in 1081 CRISPR screens.
DR ChiTaRS; ST3GAL4; human.
DR GeneWiki; ST3GAL4; -.
DR GenomeRNAi; 6484; -.
DR Pharos; Q11206; Tbio.
DR PRO; PR:Q11206; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q11206; protein.
DR Bgee; ENSG00000110080; Expressed in lower esophagus mucosa and 169 other tissues.
DR ExpressionAtlas; Q11206; baseline and differential.
DR Genevisible; Q11206; 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:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0003836; F:beta-galactoside (CMP) alpha-2,3-sialyltransferase activity; IDA:BHF-UCL.
DR GO; GO:0047288; F:monosialoganglioside sialyltransferase activity; IDA:BHF-UCL.
DR GO; GO:0008118; F:N-acetyllactosaminide alpha-2,3-sialyltransferase activity; IMP:UniProtKB.
DR GO; GO:0004513; F:neolactotetraosylceramide alpha-2,3-sialyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008373; F:sialyltransferase activity; IBA:GO_Central.
DR GO; GO:0050890; P:cognition; IMP:UniProtKB.
DR GO; GO:0009247; P:glycolipid biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0009101; P:glycoprotein biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0018146; P:keratan sulfate biosynthetic process; TAS:Reactome.
DR GO; GO:0030259; P:lipid glycosylation; IDA:BHF-UCL.
DR GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0030194; P:positive regulation of blood coagulation; ISS:UniProtKB.
DR GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; IMP:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IDA:BHF-UCL.
DR GO; GO:1990743; P:protein sialylation; IDA:BHF-UCL.
DR GO; GO:0097503; P:sialylation; IDA:BHF-UCL.
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; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Lipid metabolism; Membrane; Reference proteome; Secreted;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..333
FT /note="CMP-N-acetylneuraminate-beta-galactosamide-alpha-
FT 2,3-sialyltransferase 4"
FT /id="PRO_0000149262"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..333
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 120..273
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..11
FT /note="Missing (in isoform 3 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:12441665"
FT /id="VSP_001785"
FT VAR_SEQ 1..6
FT /note="MVSKSR -> MCPAG (in isoform 2 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:12441665,
FT ECO:0000303|PubMed:8288606"
FT /id="VSP_001784"
FT VAR_SEQ 30..34
FT /note="RYIEL -> S (in isoform 5, isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:12441665,
FT ECO:0000303|PubMed:7901202"
FT /id="VSP_021104"
FT VAR_SEQ 61
FT /note="N -> KLSPLCS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12441665,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_001786"
FT CONFLICT 182..183
FT /note="NP -> KG (in Ref. 8; AAC14162)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="I -> T (in Ref. 8; AAC14162)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="M -> I (in Ref. 8; AAC14162)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 38045 MW; 15E4BCE1F4F5B3C3 CRC64;
MVSKSRWKLL AMLALVLVVM VWYSISREDR YIELFYFPIP EKKEPCLQGE AESKASKLFG
NYSRDQPIFL RLEDYFWVKT PSAYELPYGT KGSEDLLLRV LAITSSSIPK NIQSLRCRRC
VVVGNGHRLR NSSLGDAINK YDVVIRLNNA PVAGYEGDVG SKTTMRLFYP ESAHFDPKVE
NNPDTLLVLV AFKAMDFHWI ETILSDKKRV RKGFWKQPPL IWDVNPKQIR ILNPFFMEIA
ADKLLSLPMQ QPRKIKQKPT TGLLAITLAL HLCDLVHIAG FGYPDAYNKK QTIHYYEQIT
LKSMAGSGHN VSQEALAIKR MLEMGAIKNL TSF
