ID   SEC1_BOVIN              Reviewed;         368 AA.
AC   Q9TTY3;
DT   10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Galactoside 2-alpha-L-fucosyltransferase SEC1;
DE            EC=2.4.1.-;
DE   AltName: Full=Secretory blood group protein 1 {ECO:0000303|PubMed:10814703};
GN   Name=SEC1 {ECO:0000303|PubMed:10814703};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP   SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=10814703; DOI=10.1093/glycob/10.6.611;
RA   Barreaud J.P., Saunier K., Souchaire J., Delourme D., Oulmouden A.,
RA   Oriol R., Leveziel H., Julien R., Petit J.M.;
RT   "Three bovine alpha2-fucosyltransferase genes encode enzymes that
RT   preferentially transfer fucose on Galbeta1-3GalNAc acceptor substrates.";
RL   Glycobiology 10:611-621(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11606704; DOI=10.1093/oxfordjournals.molbev.a003749;
RA   Saunier K., Barreaud J.P., Eggen A., Oriol R., Leveziel H., Julien R.,
RA   Petit J.-M.;
RT   "Organization of the bovine alpha 2-fucosyltransferase gene cluster
RT   suggests that the Sec1 gene might have been shaped through a nonautonomous
RT   L1-retrotransposition event within the same locus.";
RL   Mol. Biol. Evol. 18:2083-2091(2001).
CC   -!- FUNCTION: Catalyzes the transfer of alpha 1,2-linked fucose to
CC       ganglioside GM1 and galacto-N-biose. {ECO:0000269|PubMed:10814703}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ganglioside GM1 + GDP-beta-L-fucose = ganglioside Fuc-GM1 +
CC         GDP + H(+); Xref=Rhea:RHEA:48292, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:82639,
CC         ChEBI:CHEBI:90189; Evidence={ECO:0000269|PubMed:10814703};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48293;
CC         Evidence={ECO:0000305|PubMed:10814703};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.60 uM for Galacto-N-biose {ECO:0000269|PubMed:10814703};
CC         KM=1.81 uM for ganglioside GM1 {ECO:0000269|PubMed:10814703};
CC         Vmax=28.2 pmol/min/mg enzyme towards Galacto-N-biose
CC         {ECO:0000269|PubMed:10814703};
CC         Vmax=37.9 pmol/min/mg enzyme towards ganglioside GM1
CC         {ECO:0000269|PubMed:10814703};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC       {ECO:0000250|UniProtKB:O09160}; Single-pass type II membrane protein
CC       {ECO:0000250|UniProtKB:O09160}. Note=Membrane-bound form in trans
CC       cisternae of Golgi. {ECO:0000250|UniProtKB:O09160}.
CC   -!- TISSUE SPECIFICITY: Kidney. {ECO:0000269|PubMed:10814703}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 11 family.
CC       {ECO:0000305}.
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DR   EMBL; AF187851; AAF03411.1; -; Genomic_DNA.
DR   EMBL; AH011100; AAL06322.1; -; mRNA.
DR   AlphaFoldDB; Q9TTY3; -.
DR   SMR; Q9TTY3; -.
DR   SwissLipids; SLP:000001423; -.
DR   CAZy; GT11; Glycosyltransferase Family 11.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031127; F:alpha-(1,2)-fucosyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0008107; F:galactoside 2-alpha-L-fucosyltransferase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR002516; Glyco_trans_11.
DR   PANTHER; PTHR11927; PTHR11927; 1.
DR   Pfam; PF01531; Glyco_transf_11; 1.
PE   1: Evidence at protein level;
KW   Glycosyltransferase; Golgi apparatus; Membrane; Reference proteome;
KW   Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..368
FT                   /note="Galactoside 2-alpha-L-fucosyltransferase SEC1"
FT                   /id="PRO_0000451808"
FT   TOPO_DOM        1..31
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        53..368
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   368 AA;  41649 MW;  166A7A7A78F6DE7F CRC64;
     MWDMRAVAPQ RPAAGHPRAG WPRKLKTAAT RFWATCPSSS TVCFLFVIFA VSTVFHCHRR
     LALVPAPWAY AGHVVLFPRH LPRGGVFTIN AKGRLGNQMG EYATLYALAK MNGRAAFIPP
     QMHSTLAPIF RITLPVLHDA TARSVPWQNY HLNDWMEEQY RHIPGEYVRL TGYPCSWTFY
     HHLRAEILQE FTLHAHVREE AQNFLRGLRV NGSRPSTYVG VHVRRGDYVR VMPTMWKGVL
     ADRGYLQQAL DWFRARHHSP LFVITSDDMA WCRRNINSSH RDVVFAGSGQ QGSPARDFAL
     LTQCNHTVIT VGTFGIWAAY LAGGSTVYLA NFTLPGSRFR MIFKPQAAFL PEWVGIAANL
     GQARESHP