ID   FUT1_MOUSE              Reviewed;         377 AA.
AC   O09160; P97327;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2020, sequence version 2.
DT   24-JAN-2024, entry version 139.
DE   RecName: Full=Galactoside alpha-(1,2)-fucosyltransferase 1 {ECO:0000305};
DE   AltName: Full=Alpha(1,2)FT 1;
DE   AltName: Full=Fucosyltransferase 1;
DE            Short=MFUT-1 {ECO:0000303|PubMed:11368156};
DE   AltName: Full=GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase 1;
DE   AltName: Full=Type 1 galactoside alpha-(1,2)-fucosyltransferase FUT1 {ECO:0000305};
DE            EC=2.4.1.69 {ECO:0000269|PubMed:14967068};
DE   AltName: Full=Type 2 galactoside alpha-(1,2)-fucosyltransferase FUT1 {ECO:0000305};
DE            EC=2.4.1.344 {ECO:0000250|UniProtKB:P19526};
GN   Name=Fut1 {ECO:0000312|MGI:MGI:109375};
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC   STRAIN=NIH Swiss;
RX   PubMed=9355741; DOI=10.1042/bj3270105;
RA   Domino S.E., Hiraiwa N., Lowe J.B.;
RT   "Molecular cloning, chromosomal assignment and tissue-specific expression
RT   of a murine alpha(1,2)fucosyltransferase expressed in thymic and epididymal
RT   epithelial cells.";
RL   Biochem. J. 327:105-115(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, CATALYTIC ACTIVITY,
RP   FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=11368156; DOI=10.1006/abbi.2001.2303;
RA   Lin B., Saito M., Sakakibara Y., Hayashi Y., Yanagisawa M., Iwamori M.;
RT   "Characterization of three members of murine alpha1,2-fucosyltransferases:
RT   change in the expression of the Se gene in the intestine of mice after
RT   administration of microbes.";
RL   Arch. Biochem. Biophys. 388:207-215(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ICR; TISSUE=Brain;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Vagina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/10;
RX   PubMed=18379136; DOI=10.1266/ggs.83.77;
RA   Liu Y., Takahashi A., Kitano T., Koide T., Shiroishi T., Moriwaki K.,
RA   Saitou N.;
RT   "Mosaic genealogy of the Mus musculus genome revealed by 21 nuclear genes
RT   from its three subspecies.";
RL   Genes Genet. Syst. 83:77-88(2008).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [7]
RP   CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=14967068; DOI=10.1042/bj20031668;
RA   Iwamori M., Domino S.E.;
RT   "Tissue-specific loss of fucosylated glycolipids in mice with targeted
RT   deletion of alpha(1,2)fucosyltransferase genes.";
RL   Biochem. J. 380:75-81(2004).
RN   [8]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=11713270; DOI=10.1128/mcb.21.24.8336-8345.2001;
RA   Domino S.E., Zhang L., Gillespie P.J., Saunders T.L., Lowe J.B.;
RT   "Deficiency of reproductive tract alpha(1,2)fucosylated glycans and normal
RT   fertility in mice with targeted deletions of the FUT1 or FUT2
RT   alpha(1,2)fucosyltransferase locus.";
RL   Mol. Cell. Biol. 21:8336-8345(2001).
RN   [9]
RP   FUNCTION.
RX   PubMed=16884711; DOI=10.1016/j.ydbio.2006.06.052;
RA   St John J.A., Claxton C., Robinson M.W., Yamamoto F., Domino S.E., Key B.;
RT   "Genetic manipulation of blood group carbohydrates alters development and
RT   pathfinding of primary sensory axons of the olfactory systems.";
RL   Dev. Biol. 298:470-484(2006).
CC   -!- FUNCTION: Catalyzes the transfer of L-fucose, from a guanosine
CC       diphosphate-beta-L-fucose, to the terminal galactose residue of
CC       glycoconjugates through an alpha(1,2) linkage leading to H antigen
CC       synthesis that is an intermediate substrate in the synthesis of ABO
CC       blood group antigens (PubMed:11368156, PubMed:14967068,
CC       PubMed:16884711). H antigen is essential for maturation of the
CC       glomerular layer of the main olfactory bulb, in cell migration and
CC       early cell-cell contacts during tumor associated angiogenesis
CC       (PubMed:16884711). Preferentially fucosylates soluble lactose and to a
CC       lesser extent, fucosylates glycolipids gangliosides GA1 and GM1a
CC       (PubMed:11368156, PubMed:14967068). {ECO:0000269|PubMed:11368156,
CC       ECO:0000269|PubMed:14967068, ECO:0000269|PubMed:16884711}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl
CC         derivative + GDP-beta-L-fucose = an alpha-L-Fuc-(1->2)-beta-D-Gal-
CC         (1->4)-beta-D-GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:50668,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC         ChEBI:CHEBI:133507, ChEBI:CHEBI:133510; EC=2.4.1.344;
CC         Evidence={ECO:0000250|UniProtKB:P19526};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ganglioside GA1 + GDP-beta-L-fucose = a ganglioside Fuc-GA1
CC         + GDP + H(+); Xref=Rhea:RHEA:48320, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:88069,
CC         ChEBI:CHEBI:90262; Evidence={ECO:0000269|PubMed:11368156,
CC         ECO:0000269|PubMed:14967068};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48321;
CC         Evidence={ECO:0000305|PubMed:11368156};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-
CC         beta-D-Glc-(1<->1')-Cer(d18:1(4E)) + GDP-beta-L-fucose = alpha-L-
CC         fucosyl-(1->2)- beta-D-galactosyl-(1->3)-N-acetyl-beta-D-
CC         glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-
CC         (1<->1')-N-acylsphing-4-enine + GDP + H(+); Xref=Rhea:RHEA:32175,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17292, ChEBI:CHEBI:28743,
CC         ChEBI:CHEBI:57273, ChEBI:CHEBI:58189; EC=2.4.1.69;
CC         Evidence={ECO:0000269|PubMed:14967068};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32176;
CC         Evidence={ECO:0000305|PubMed:14967068};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a neolactoside nLc4Cer(d18:1(4E)) + GDP-beta-L-fucose = a
CC         neolactoside IV(2)-alpha-Fuc-nLc4Cer(d18:1(4E)) + GDP + H(+);
CC         Xref=Rhea:RHEA:48304, ChEBI:CHEBI:15378, ChEBI:CHEBI:17006,
CC         ChEBI:CHEBI:28691, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000269|PubMed:14967068};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48305;
CC         Evidence={ECO:0000305|PubMed:14967068};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ganglioside GM1 + GDP-beta-L-fucose = a 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:F6Q1T7};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48293;
CC         Evidence={ECO:0000250|UniProtKB:F6Q1T7};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-galactosyl-(1->3)-N-acetyl-D-galactosamine + GDP-beta-
CC         L-fucose = alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-
CC         D-galactosamine + GDP + H(+); Xref=Rhea:RHEA:62964,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC         ChEBI:CHEBI:84728, ChEBI:CHEBI:546807;
CC         Evidence={ECO:0000250|UniProtKB:F6Q1T7};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62965;
CC         Evidence={ECO:0000250|UniProtKB:F6Q1T7};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=28.85 mM for phenyl-beta-D-Galactoside
CC         {ECO:0000269|PubMed:11368156};
CC         KM=29.09 mM for lactose {ECO:0000269|PubMed:11368156};
CC         KM=0.24 mM for ganglioside GA1 {ECO:0000269|PubMed:11368156};
CC         KM=22.5 uM for ganglioside GA1 {ECO:0000269|PubMed:14967068};
CC         KM=10.8 uM for nLc4Cer {ECO:0000269|PubMed:14967068};
CC         KM=6.2 uM for Lc4Cer {ECO:0000269|PubMed:14967068};
CC         KM=4.3 uM for GM1 {ECO:0000269|PubMed:14967068};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000250|UniProtKB:P19526}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC       {ECO:0000305}; Single-pass type II membrane protein
CC       {ECO:0000305|PubMed:11368156}. Note=Membrane-bound form in trans
CC       cisternae of Golgi. {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: In the adult, highly expressed in pancreas, testis
CC       and epididymis and to a lesser extent in thymus, lung, stomach, small
CC       intestine, colon, spleen and uterus. Not expressed in brain, heart,
CC       skeletal muscle, kidney, liver and bone marrow (PubMed:9355741).
CC       Expressed in epididymis and testis (PubMed:11368156).
CC       {ECO:0000269|PubMed:11368156, ECO:0000269|PubMed:9355741}.
CC   -!- DISRUPTION PHENOTYPE: Homozygous mutant knockout mice for Fut1 develop
CC       normally, exhibit no gross phenotypic abnormalities and the
CC       Fucalpha(1-->2)Galbeta epitope is absent from the epithelia of the
CC       epididymis mice. {ECO:0000269|PubMed:11713270}.
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   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC       Note=Fucosyltransferase 1;
CC       URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_611";
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DR   EMBL; U90553; AAC53492.1; -; Genomic_DNA.
DR   EMBL; AF113533; AAD25352.1; -; mRNA.
DR   EMBL; Y09883; CAA71009.1; -; Genomic_DNA.
DR   EMBL; AK137638; BAE23444.1; -; mRNA.
DR   EMBL; AB039104; BAB68628.1; -; Genomic_DNA.
DR   EMBL; AB039112; BAB68636.1; -; Genomic_DNA.
DR   EMBL; AB039111; BAB68635.1; -; Genomic_DNA.
DR   EMBL; AB039109; BAB68633.1; -; Genomic_DNA.
DR   EMBL; AB039105; BAB68629.1; -; Genomic_DNA.
DR   EMBL; AC149057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS21254.1; -.
DR   RefSeq; NP_001258910.1; NM_001271981.1.
DR   RefSeq; NP_032077.2; NM_008051.6.
DR   RefSeq; XP_006540679.1; XM_006540616.3.
DR   AlphaFoldDB; O09160; -.
DR   STRING; 10090.ENSMUSP00000008605; -.
DR   SwissLipids; SLP:000001425; -.
DR   CAZy; GT11; Glycosyltransferase Family 11.
DR   GlyCosmos; O09160; 3 sites, No reported glycans.
DR   GlyGen; O09160; 3 sites.
DR   iPTMnet; O09160; -.
DR   PhosphoSitePlus; O09160; -.
DR   PaxDb; 10090-ENSMUSP00000008605; -.
DR   ProteomicsDB; 271650; -.
DR   ProteomicsDB; 328835; -.
DR   Antibodypedia; 31803; 162 antibodies from 24 providers.
DR   DNASU; 14343; -.
DR   Ensembl; ENSMUST00000008605.6; ENSMUSP00000008605.6; ENSMUSG00000008461.7.
DR   GeneID; 14343; -.
DR   KEGG; mmu:14343; -.
DR   UCSC; uc009gwg.2; mouse.
DR   AGR; MGI:109375; -.
DR   CTD; 2523; -.
DR   MGI; MGI:109375; Fut1.
DR   VEuPathDB; HostDB:ENSMUSG00000008461; -.
DR   eggNOG; ENOG502S316; Eukaryota.
DR   GeneTree; ENSGT00390000001450; -.
DR   HOGENOM; CLU_043399_0_1_1; -.
DR   InParanoid; O09160; -.
DR   OMA; WPPSHRQ; -.
DR   OrthoDB; 2959824at2759; -.
DR   PhylomeDB; O09160; -.
DR   TreeFam; TF315810; -.
DR   BRENDA; 2.4.1.69; 3474.
DR   Reactome; R-MMU-9033807; ABO blood group biosynthesis.
DR   SABIO-RK; O09160; -.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 14343; 0 hits in 79 CRISPR screens.
DR   PRO; PR:O09160; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; O09160; Protein.
DR   Bgee; ENSMUSG00000008461; Expressed in lip and 30 other cell types or tissues.
DR   ExpressionAtlas; O09160; baseline and differential.
DR   GO; GO:0005794; C:Golgi apparatus; IMP:MGI.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031127; F:alpha-(1,2)-fucosyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0008417; F:fucosyltransferase activity; IMP:MGI.
DR   GO; GO:0008107; F:galactoside 2-alpha-L-fucosyltransferase activity; IDA:MGI.
DR   GO; GO:0036065; P:fucosylation; IDA:UniProtKB.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0021772; P:olfactory bulb development; IMP:UniProtKB.
DR   GO; GO:0009312; P:oligosaccharide biosynthetic process; IMP:MGI.
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   GO; GO:0030155; P:regulation of cell adhesion; IDA:UniProtKB.
DR   GO; GO:0001936; P:regulation of endothelial cell proliferation; IMP:UniProtKB.
DR   CDD; cd11301; Fut1_Fut2_like; 1.
DR   InterPro; IPR002516; Glyco_trans_11.
DR   PANTHER; PTHR11927; GALACTOSIDE 2-L-FUCOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR11927:SF4; GALACTOSIDE ALPHA-(1,2)-FUCOSYLTRANSFERASE 1; 1.
DR   Pfam; PF01531; Glyco_transf_11; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Glycosyltransferase; Golgi apparatus; Lipid metabolism;
KW   Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..377
FT                   /note="Galactoside alpha-(1,2)-fucosyltransferase 1"
FT                   /id="PRO_0000149098"
FT   TOPO_DOM        1..8
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        9..26
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        27..377
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        67
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        303
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        329
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        12
FT                   /note="A -> T (in Ref. 1; AAC53492)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        210..213
FT                   /note="GIRP -> SPA (in Ref. 1; AAC53492)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   377 AA;  42394 MW;  9B17542B1F7A969A CRC64;
     MWTPSRRQLC LAFLLVCVLS AGSFFFHLNG GNFFRNGLTL SVLCSDYHLL KSPVAMVCLP
     HPLQTSNGSP SCPEQSSSLS GTWTITPGGR FGNQMGQYAT LLALAQLNGR QAFIQPEMHA
     ALAPVFRISL PVLDPEVDSL TPWQHLVLHD WMSEEYSHLE DPFLKLSGFP CSWTFFHHLR
     EQIRREFTLH NHLREGAQYL LSGLRIGPAG IRPHTFVGVH VRRGDYLEVM PNRWKGVVGD
     RAYLQQAMDW FRARHKDPIF VVTSNGMKWC LENIDTSHGD VVFAGNGQEG TPGKDFALLT
     QCNHTIMTIG TFGFWAAYLA GGDTVYLANF TLPDSEFLKI FRPEAAFLPE WVGINADLSP
     LQAQFDPWKP DSLFRLV
//