ID A0A0F7RPZ0_PYTBI Unreviewed; 347 AA. AC A0A0F7RPZ0; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 02-OCT-2024, entry version 38. DE RecName: Full=beta-galactoside alpha-2,3-sialyltransferase {ECO:0000256|ARBA:ARBA00039107}; 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}; GN Name=st3gal2 {ECO:0000313|EMBL:CDI70262.1}; GN Synonyms=ST3GAL2 {ECO:0000313|RefSeq:NP_001306578.1}; OS Python bivittatus (Burmese python) (Python molurus bivittatus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera; OC Serpentes; Henophidia; Pythonidae; Python. OX NCBI_TaxID=176946 {ECO:0000313|EMBL:CDI70262.1}; RN [1] {ECO:0000313|EMBL:CDI70262.1, ECO:0000313|RefSeq:NP_001306578.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=25534026; DOI=10.1093/molbev/msu395; RA Petit D., Teppa E., Mir A.M., Vicogne D., Thisse C., Thisse B., Filloux C., RA Harduin-Lepers A.; RT "Integrative view of alpha2,3-sialyltransferases (ST3Gal) molecular and RT functional evolution in deuterostomes: significance of lineage-specific RT losses."; RL Mol. Biol. Evol. 32:906-927(2015). RN [2] {ECO:0000313|RefSeq:NP_001306578.1} RP IDENTIFICATION. RG RefSeq; RL Submitted (JUN-2024) to UniProtKB. 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 --------------------------------------------------------------------------- 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; HG531981; CDI70262.1; -; mRNA. DR RefSeq; NP_001306578.1; NM_001319649.1. DR GeneID; 103061993; -. DR KEGG; pbi:103061993; -. DR CTD; 6483; -. DR OrthoDB; 5348004at2759; -. DR Proteomes; UP000695026; Unplaced. 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:0006486; P:protein glycosylation; IEA:InterPro. DR Gene3D; 3.90.1480.20; Glycosyl transferase family 29; 1. DR InterPro; IPR051757; Beta-gal_alpha2-3_sialyltrans. 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:SF4; CMP-N-ACETYLNEURAMINATE-BETA-GALACTOSAMIDE-ALPHA-2,3-SIALYLTRANSFERASE 2; 1. DR Pfam; PF00777; Glyco_transf_29; 1. DR PIRSF; PIRSF005557; Sialyl_trans; 1. PE 2: Evidence at transcript level; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Glycosyltransferase {ECO:0000313|EMBL:CDI70262.1}; KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Reference proteome {ECO:0000313|Proteomes:UP000695026}; KW Secreted {ECO:0000256|ARBA:ARBA00022525}; KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CDI70262.1}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}. FT BINDING 113 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR005557-1" FT BINDING 154 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR005557-1" FT BINDING 177 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR005557-1" FT BINDING 237 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR005557-1" FT BINDING 273 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR005557-1" FT BINDING 277 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR005557-1" FT BINDING 297 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR005557-1" FT BINDING 306 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR005557-1" FT BINDING 323 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR005557-1" FT DISULFID 149..288 FT /evidence="ECO:0000256|PIRSR:PIRSR005557-2" SQ SEQUENCE 347 AA; 40034 MW; AB2CF98D945E0915 CRC64; MKFSLRFWFL STAFLLVFVM SLLFTYSHHS MAYLDLSGLN GLHRVKLVPS YAGMQRLSKE GLLVKRCACH RCAIESIDTS WFDNRYDSNI SPVWTKENVD LPLDVQRWWM MLQPQFKSHN LNEVLSKLFQ IVPGENPYSS RESQSCRRCA VVGNSGNLRG SSYGQEINGH DFIMRMNQAP TVGFEADVGS RTTHHFMYPE SAKNLPANVS FVLVPFKALD LLWIASALST GQIRFTYAPV KPFLRVDKER VQIYNPAFFK YIHDRWTEHH GRYPSTGMLV LFFALHVCDE VNVFGFGADS HGNWHHYWEN NRYAGEFRKT GVHDADFEAH IVDILEKTNK ISVYRGN //