SEC1_MOUSE
ID SEC1_MOUSE Reviewed; 368 AA.
AC P97353; Q91V73; Q920T3; Q920T4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 138.
DE RecName: Full=Galactoside 2-alpha-L-fucosyltransferase Sec1;
DE EC=2.4.1.-;
DE AltName: Full=Alpha(1,2)FT 3;
DE AltName: Full=GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase 3;
DE AltName: Full=Secretory blood group protein 1 {ECO:0000312|MGI:MGI:1928893};
GN Name=Sec1 {ECO:0000312|MGI:MGI:1928893};
GN Synonyms=Fut3 {ECO:0000312|MGI:MGI:1928893};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ICR;
RA Hitoshi S., Kusunoki S., Kanazawa I., Tsuji S.;
RT "Molecular cloning and expression of a mouse GDP-L-Fucose: beta-D-
RT galactoside 2-alpha-L-Fucosyltransferase.";
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ICR; TISSUE=Gastrointestinal tract;
RX PubMed=11018479; DOI=10.1016/s1388-1981(00)00103-7;
RA Lin B., Hayashi Y., Saito M., Sakakibara Y., Yanagisawa M., Iwamori M.;
RT "GDP-fucose: beta-galactoside alpha1,2-fucosyltransferase, MFUT-II, and not
RT MFUT-I or -III, is induced in a restricted region of the digestive tract of
RT germ-free mice by host-microbe interactions and cycloheximide.";
RL Biochim. Biophys. Acta 1487:275-285(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Ola;
RX PubMed=11323419; DOI=10.1074/jbc.m100735200;
RA Domino S.E., Zhang L., Lowe J.B.;
RT "Molecular cloning, genomic mapping, and expression of two secretor blood
RT group alpha (1,2)fucosyltransferase genes differentially regulated in mouse
RT uterine epithelium and gastrointestinal tract.";
RL J. Biol. Chem. 276:23748-23756(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BFM/2Msf, BLG2/Msf, C57BL/10SnJ, CAST/EiJ, HMI/Msf, MSM/Msf,
RC NJL/Msf, pgn2, and SWN/Msf;
RA Liu Y., Kitano T., Koide T., Shiroishi T., Moriwaki K., Saitou N.;
RT "Conspicuous differences among gene genealogies of 21 nuclear genes of five
RT Mus musculus subspecies.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the transfer of alpha 1,2-linked fucose to
CC ganglioside GM1 and galacto-N-biose (By similarity).
CC {ECO:0000250|UniProtKB:Q9TTY3}.
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:0000250|UniProtKB:Q9TTY3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48293;
CC Evidence={ECO:0000250|UniProtKB:Q9TTY3};
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 -!- MISCELLANEOUS: In mouse, there are three genes (Fut1, Fut2 and Sec1)
CC which encode galactoside 2-L-fucosyltransferase.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 11 family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be Fut2. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Secretory
CC blood group protein 1;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_621";
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DR EMBL; Y09882; CAA71008.1; -; Genomic_DNA.
DR EMBL; AF113532; AAD25351.1; -; mRNA.
DR EMBL; AF214657; AAF45147.1; -; Genomic_DNA.
DR EMBL; AF214658; AAF45148.1; -; Genomic_DNA.
DR EMBL; AB039204; BAB68728.1; -; Genomic_DNA.
DR EMBL; AB039205; BAB68729.1; -; Genomic_DNA.
DR EMBL; AB039206; BAB68730.1; -; Genomic_DNA.
DR EMBL; AB039207; BAB68731.1; -; Genomic_DNA.
DR EMBL; AB039208; BAB68732.1; -; Genomic_DNA.
DR EMBL; AB039209; BAB68733.1; -; Genomic_DNA.
DR EMBL; AB039210; BAB68734.1; -; Genomic_DNA.
DR EMBL; AB039211; BAB68735.1; -; Genomic_DNA.
DR EMBL; AB039212; BAB68736.1; -; Genomic_DNA.
DR AlphaFoldDB; P97353; -.
DR STRING; 10090.ENSMUSP00000045229; -.
DR CAZy; GT11; Glycosyltransferase Family 11.
DR GlyGen; P97353; 3 sites.
DR MaxQB; P97353; -.
DR PaxDb; P97353; -.
DR PRIDE; P97353; -.
DR ProteomicsDB; 261145; -.
DR DNASU; 56546; -.
DR MGI; MGI:1928893; Sec1.
DR eggNOG; ENOG502S316; Eukaryota.
DR InParanoid; P97353; -.
DR BRENDA; 2.4.1.69; 3474.
DR UniPathway; UPA00378; -.
DR ChiTaRS; Sec1; mouse.
DR PRO; PR:P97353; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P97353; protein.
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:0008417; F:fucosyltransferase activity; IDA:MGI.
DR GO; GO:0008107; F:galactoside 2-alpha-L-fucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0036065; P:fucosylation; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0021772; P:olfactory bulb development; ISS:UniProtKB.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; ISS:UniProtKB.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISS:UniProtKB.
DR GO; GO:1904906; P:positive regulation of endothelial cell-matrix adhesion via fibronectin; ISS:UniProtKB.
DR GO; GO:1903672; P:positive regulation of sprouting angiogenesis; ISS:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IDA:UniProtKB.
DR InterPro; IPR002516; Glyco_trans_11.
DR PANTHER; PTHR11927; PTHR11927; 1.
DR Pfam; PF01531; Glyco_transf_11; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Lipid metabolism;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..368
FT /note="Galactoside 2-alpha-L-fucosyltransferase Sec1"
FT /id="PRO_0000149115"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..41
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..368
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 46
FT /note="G -> S (in strain: BFM/2Msf, C57BL/10SnJ and pgn2)"
FT VARIANT 50
FT /note="A -> G (in strain: BFM/2Msf, C57BL/10SnJ and pgn2)"
FT VARIANT 62
FT /note="P -> A (in strain: CAST/Ei)"
FT VARIANT 150
FT /note="H -> Q (in strain: BFM/2Msf and C57BL/10SnJ)"
FT VARIANT 214
FT /note="R -> H (in strain: pgn2)"
SQ SEQUENCE 368 AA; 41464 MW; 4093E853EB37303B CRC64;
MPSDSCLLSL TVLQRLRAIC PPLSTFYLFF VIFVVSTIFH CHRRLGLVPA PWASPSLVVF
PPRHMPREGM FTIRVKGRLG NQMGEYATLF ALARMNGRLA FIPASMHSTL APIFRISLPV
LHSDTAKRIP WQNYHLNDWM EERYRHIPGH YVRFTGYPCS WTFYHHLRPE ILKEFTLHDH
VREEAQAFLR GLQVNGSQPS TFVGVHVRRG DYVRVMPKVW KGVVADRGYL EKALDRFRAR
YSSPVFVVTS DDMAWCRKSI TASRGDVAFA GNGLQGSPAK DIALLMQCNH TVITLGTFGI
WAAYLTGGDT VYLANFTQPN SPFHTVFKPE AAYLPEWVGI AADLGQPNTV GSGHASARAP
KRHWGALL
