ID A0A7J7EHY9_DICBM Unreviewed; 342 AA. AC A0A7J7EHY9; DT 07-APR-2021, integrated into UniProtKB/TrEMBL. DT 07-APR-2021, sequence version 1. DT 24-JAN-2024, entry version 11. DE RecName: Full=CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1 {ECO:0000256|ARBA:ARBA00040101}; DE EC=2.4.3.2 {ECO:0000256|ARBA:ARBA00039106}; DE EC=2.4.3.4 {ECO:0000256|ARBA:ARBA00039107}; DE AltName: Full=Gal-NAc6S {ECO:0000256|ARBA:ARBA00042991}; DE AltName: Full=Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase {ECO:0000256|ARBA:ARBA00042448}; DE AltName: Full=Monosialoganglioside sialyltransferase {ECO:0000256|ARBA:ARBA00042990}; DE AltName: Full=ST3Gal I {ECO:0000256|ARBA:ARBA00041997}; DE AltName: Full=ST3GalA.1 {ECO:0000256|ARBA:ARBA00042022}; DE AltName: Full=ST3O {ECO:0000256|ARBA:ARBA00041507}; DE AltName: Full=Sialyltransferase 4A {ECO:0000256|ARBA:ARBA00042682}; GN ORFNames=HPG69_011768 {ECO:0000313|EMBL:KAF5915303.1}; OS Diceros bicornis minor (South-central black rhinoceros). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Perissodactyla; Rhinocerotidae; Diceros. OX NCBI_TaxID=77932 {ECO:0000313|EMBL:KAF5915303.1, ECO:0000313|Proteomes:UP000551758}; RN [1] {ECO:0000313|EMBL:KAF5915303.1, ECO:0000313|Proteomes:UP000551758} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SBR-YM {ECO:0000313|EMBL:KAF5915303.1}; RC TISSUE=Skin {ECO:0000313|EMBL:KAF5915303.1}; RX PubMed=32585004; RA Moodley Y., Westbury M.V., Russo I.M., Gopalakrishnan S., Rakotoarivelo A., RA Olsen R.A., Prost S., Tunstall T., Ryder O.A., Dalen L., Bruford M.W.; RT "Interspecific Gene Flow and the Evolution of Specialization in Black and RT White Rhinoceros."; RL Mol. Biol. Evol. 37:3105-3117(2020). CC -!- CATALYTIC ACTIVITY: CC Reaction=a ganglioside GA1 (d18:1(4E)) + CMP-N-acetyl-beta-neuraminate CC = a ganglioside GM1b (d18:1(4E)) + CMP + 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:0000256|ARBA:ARBA00036734}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47561; CC Evidence={ECO:0000256|ARBA:ARBA00036734}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a ganglioside GM1 (d18:1(4E)) + CMP-N-acetyl-beta-neuraminate CC = a ganglioside GD1a (d18:1(4E)) + CMP + H(+); Xref=Rhea:RHEA:18021, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, CC ChEBI:CHEBI:77709, ChEBI:CHEBI:78445; EC=2.4.3.2; CC Evidence={ECO:0000256|ARBA:ARBA00035948}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18022; CC Evidence={ECO:0000256|ARBA:ARBA00035948}; CC -!- CATALYTIC ACTIVITY: CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GM1 CC (d18:1(4E)/18:0) = CMP + ganglioside GD1a (18:1(4E)/18:0) + H(+); CC Xref=Rhea:RHEA:48248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, CC ChEBI:CHEBI:60377, ChEBI:CHEBI:73110, ChEBI:CHEBI:90153; CC Evidence={ECO:0000256|ARBA:ARBA00036879}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48249; CC Evidence={ECO:0000256|ARBA:ARBA00036879}; 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=2.4.3.4; CC Evidence={ECO:0000256|ARBA:ARBA00036292}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21617; CC Evidence={ECO:0000256|ARBA:ARBA00036292}; CC -!- PATHWAY: Glycolipid biosynthesis. {ECO:0000256|ARBA:ARBA00004934}. CC -!- PATHWAY: Protein modification; protein glycosylation. CC {ECO:0000256|ARBA:ARBA00004922}. CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane CC {ECO:0000256|ARBA:ARBA00004447}; Single-pass type II membrane protein CC {ECO:0000256|ARBA:ARBA00004447}. Membrane CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein CC {ECO:0000256|ARBA:ARBA00004606}. Secreted CC {ECO:0000256|ARBA:ARBA00004613}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family. CC {ECO:0000256|ARBA:ARBA00006003}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KAF5915303.1}. 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; JACDTQ010002883; KAF5915303.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7J7EHY9; -. DR Proteomes; UP000551758; Unassembled WGS sequence. DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008373; F:sialyltransferase activity; IEA:InterPro. DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro. 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; PTHR46032; ALPHA-2,3-SIALYLTRANSFERASE ST3GAL I ISOFORM X1; 1. DR PANTHER; PTHR46032:SF6; CMP-N-ACETYLNEURAMINATE-BETA-GALACTOSAMIDE-ALPHA-2,3-SIALYLTRANSFERASE 1; 1. DR Pfam; PF00777; Glyco_transf_29; 1. DR PIRSF; PIRSF005557; Sialyl_trans; 1. PE 3: Inferred from homology; KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676}; KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Reference proteome {ECO:0000313|Proteomes:UP000551758}; KW Secreted {ECO:0000256|ARBA:ARBA00022525}; KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968}; KW Transferase {ECO:0000256|ARBA:ARBA00022676}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}. FT BINDING 107 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR005557-1" FT BINDING 149 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR005557-1" FT BINDING 172 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR005557-1" FT BINDING 232 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR005557-1" FT BINDING 268 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR005557-1" FT BINDING 272 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR005557-1" FT BINDING 292 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR005557-1" FT BINDING 301 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR005557-1" FT BINDING 318 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR005557-1" FT DISULFID 144..283 FT /evidence="ECO:0000256|PIRSR:PIRSR005557-2" SQ SEQUENCE 342 AA; 39234 MW; F660203D5F61A952 CRC64; MATTRKRILK LLTLLILFIF LTSFLLNYSN TMVATPWFPK QMVLELSENV KRLMRYPHRP CTCARCIGQR EVSSWFDERF NRSMQPLLTA QNALLEEDTY NWWLRLQREK QPNNLNDTIK ELFRVVPGNV DPLLEKRSVG CRRCAVVGNS GNLKESWYGP QIDSHDFVLR MNKAPTAGFE ADVGSKTTHH LVYPESFREL AENVSMVLVP FKTTDLEWVV SATTTGTISH TYVPVPAKIQ VKKDKILIYH PAFIKYVFDT WLQGHGRYPS TGILSVIFSL HICDEVDLYG FGADSRGNWH HYWENNPSAG AFRKTGVHDG DFESNVTATL ASIDKIRIFK GR //