ID   A0A7J7EHY9_DICBM        Unreviewed;       342 AA.
AC   A0A7J7EHY9;
DT   07-APR-2021, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 1.
DT   27-MAR-2024, entry version 12.
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=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   -!- 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:ARBA00043673};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47561;
CC         Evidence={ECO:0000256|ARBA:ARBA00043673};
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:ARBA00043773};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18022;
CC         Evidence={ECO:0000256|ARBA:ARBA00043773};
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}.
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DR   EMBL; JACDTQ010002883; KAF5915303.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A7J7EHY9; -.
DR   Proteomes; UP000551758; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003836; F:beta-galactoside (CMP) alpha-2,3-sialyltransferase activity; IEA:UniProt.
DR   GO; GO:0043603; P:amide metabolic process; IEA:UniProt.
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   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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:ARBA00022679};
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
//