ID CAG1_MOUSE STANDARD; PRT; 403 AA. AC Q64685; DT 01-NOV-1997 (REL. 35, CREATED) DT 01-NOV-1997 (REL. 35, LAST SEQUENCE UPDATE) DT 01-NOV-1997 (REL. 35, LAST ANNOTATION UPDATE) DE CMP-N-ACETYLNEURAMINATE-BETA-GALACTOSAMIDE-ALPHA-2,6-SIALYLTRANSFERASE DE (EC 2.4.99.1) (BETA-GALACTOSIDE ALPHA-2,6-SIALYLTRANSFERASE) DE (ALPHA 2,6-ST) (SIALYLTRANSFERASE 1) (ST6GALI). GN SIAT1. OS MUS MUSCULUS (MOUSE). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; MAMMALIA; EUTHERIA; OC RODENTIA; SCIUROGNATHI; MURIDAE; MURINAE; MUS. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=LIVER, AND BRAIN; RX MEDLINE; 94363344. RA HAMAMOTO T., KAWASAKI M., KUROSAWA N., NAKAOKA T., LEE Y.-C., RA TSUJI S.; RT "Two step single primer mediated polymerase chain reaction. RT Application to cloning of putative mouse, beta-galactoside alpha 2,6- RT sialyltransferase cDNA."; RL BIOORG. MED. CHEM. 1:141-145(1993). CC -!- FUNCTION: TRANSFERS SIALIC ACID FROM THE DONOR OF SUBSTRATE CMP- CC SIALIC ACID TO GALACTOSE CONTAINING ACCEPTOR SUBSTRATES. CC -!- CATALYTIC ACTIVITY: CMP-N-ACETYLNEURAMINATE + BETA-D-GALACTOSYL- CC 1,4-ACETYL-BETA-D-GLUCOSAMINE = CMP + ALPHA-N-ACETYLNEURAMINYL- CC 2,6-BETA-D-GALACTOSYL-1,4-N-ACETYL-BETA-D-GLUCOSAMINE. CC -!- PATHWAY: GLYCOSYLATION. CC -!- SUBCELLULAR LOCATION: TYPE II MEMBRANE PROTEIN. MEMBRANE-BOUND CC FORM IN TRANS CISTERNAE OF GOLGI, SOLUBLE FORM IN BODY FLUIDS. CC -!- PTM: THE SOLUBLE FORM DERIVES FROM THE MEMBRANE FORM BY CC PROTEOLYTIC PROCESSING. CC -!- SIMILARITY: BELONGS TO THE VERTEBRATE SIALYLTRANSFERASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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; D16106; G416229; -. DR MGD; MGI:108470; SIAT1. KW TRANSFERASE; GLYCOSYLTRANSFERASE; GLYCOPROTEIN; TRANSMEMBRANE; KW SIGNAL-ANCHOR; GOLGI STACK. FT DOMAIN 1 9 CYTOPLASMIC (POTENTIAL). FT TRANSMEM 10 26 SIGNAL-ANCHOR (TYPE-II MEMBRANE PROTEIN) FT (POTENTIAL). FT DOMAIN 27 403 LUMENAL, CATALYTIC (POTENTIAL). FT CARBOHYD 146 146 POTENTIAL. FT CARBOHYD 158 158 POTENTIAL. SQ SEQUENCE 403 AA; 46407 MW; 1E8FCF16 CRC32; MIHTNLKRKF SCFVLVFLLF AIICVWKKGS DYEALTLQAK VFQMPKSQEK VAVGPAPQAV FSNSKQDPKE GVQILSYPRV TAKVKPQPSL QVWDKDSTYS KLNPRLLKIW RNYLNMNKYK VSYKGPGPGV RFSVEGLRCH LRDHVNVSMI EATDSPFNTT EWEGYLPKET FRTKAGPCTK CAVVSSAGSL KNSQLGREID NHDAVLRFNG APTDNFQQDV GTKTTIRLVN SQLVTTEKRF LKDSLYTEGI LILWDPSVYH ADIPQWYQKP DYNFFETYKS YRRLHPSQPF YILKPQMPWE LWDIIQEISP DLIQPNPPSS GMLGIIIMMT LCDQVDIYEF LPSKRKTDVC YYHQKFFDSA CTMGAYHPLL FEKNMVKHLN EGTDEDIYLF GKATLSGFRN NRC //