ID A0A0F7RQX1_BRALA Unreviewed; 312 AA. AC A0A0F7RQX1; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 02-OCT-2024, entry version 30. 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}; DE Flags: Fragment; GN Name=2 {ECO:0000313|EMBL:CDI70285.1}; GN Synonyms=8 {ECO:0000313|EMBL:CDI70285.1}, st3gal1 GN {ECO:0000313|EMBL:CDI70285.1}; OS Branchiostoma lanceolatum (Common lancelet) (Amphioxus lanceolatum). OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes; OC Branchiostomatidae; Branchiostoma. OX NCBI_TaxID=7740 {ECO:0000313|EMBL:CDI70285.1}; RN [1] {ECO:0000313|EMBL:CDI70285.1} 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). CC -!- PATHWAY: Protein modification; protein glycosylation. CC {ECO:0000256|ARBA:ARBA00004922}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single- CC pass type II membrane protein {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; HG532006; CDI70285.1; -; mRNA. DR AlphaFoldDB; A0A0F7RQX1; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW. DR GO; GO:0016020; C: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:SF2; GAL BETA 1,3-GALNAC ALPHA-2,3-SIALYL TRANSFERASE-RELATED; 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:CDI70285.1}; KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Secreted {ECO:0000256|ARBA:ARBA00022525}; KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CDI70285.1}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 6..27 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DISULFID 165..304 FT /evidence="ECO:0000256|PIRSR:PIRSR005557-2" FT NON_TER 312 FT /evidence="ECO:0000313|EMBL:CDI70285.1" SQ SEQUENCE 312 AA; 35419 MW; ADE256D106ED33E3 CRC64; MIRMTVKLFV TAIVFVLIMV GAMYHFVQPG KSPLARSTTG VTVPPGEEVE NNSQLSRWWR RFQGDGEPVQ ANNSATVATA PEQPACKRVW QKGRSAWFDS RFDENIRPVW SRANIELPAD ARKWWMSLQS KKDEDPAPLL NALFDMGAPD VDPWATHNLT GCLRCAVVGN SGNLKQSNYG EEIDGYDLIF RMNDAPTKGW EKDVGHRTTH HFMYPESAIN LPDDVSFVLL NFKPLDLKWM KTALTDGSIT RTWTNVKGRI KTDKTKILVY NPAFFKYVND KWTEHHGRYS STGSLVILFA VHVCDEVDVY GY //