ID A0A0F7RPZ0_PYTBI Unreviewed; 347 AA. AC A0A0F7RPZ0; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 10-FEB-2021, entry version 24. DE SubName: Full=Alpha2,3-sialyltransferase {ECO:0000313|EMBL:CDI70262.1}; GN Name=st3gal2 {ECO:0000313|EMBL:CDI70262.1}; 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} 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 ?2,3-Sialyltransferases (ST3Gal) Molecular and RT Functional Evolution in Deuterostomes: Significance of Lineage-Specific RT Losses."; RL Mol. Biol. Evol. 32:906-927(2015). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single- CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}. 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; 891104at2759; -. DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0008373; F:sialyltransferase activity; IEA:InterPro. DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro. 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 2: Evidence at transcript level; KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, KW ECO:0000313|EMBL:CDI70262.1}; KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; 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 /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR005557-1" FT BINDING 154 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR005557-1" FT BINDING 177 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR005557-1" FT BINDING 237 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR005557-1" FT BINDING 273 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR005557-1" FT BINDING 277 FT /note="Substrate; via amide nitrogen" FT /evidence="ECO:0000256|PIRSR:PIRSR005557-1" FT BINDING 297 FT /note="Substrate; via amide nitrogen" FT /evidence="ECO:0000256|PIRSR:PIRSR005557-1" FT BINDING 306 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR005557-1" FT BINDING 323 FT /note="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 //