FUT1_HUMAN
ID FUT1_HUMAN Reviewed; 365 AA.
AC P19526; O14505; O14506; O14507;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Galactoside alpha-(1,2)-fucosyltransferase 1 {ECO:0000305};
DE AltName: Full=Alpha(1,2)FT 1;
DE AltName: Full=Blood group H alpha 2-fucosyltransferase;
DE AltName: Full=Fucosyltransferase 1;
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:0000250|UniProtKB:O09160};
DE EC=2.4.1.69 {ECO:0000250|UniProtKB:O09160};
DE AltName: Full=Type 2 galactoside alpha-(1,2)-fucosyltransferase FUT1 {ECO:0000305};
DE EC=2.4.1.344 {ECO:0000269|PubMed:2118655};
GN Name=FUT1 {ECO:0000312|HGNC:HGNC:4012}; Synonyms=H, HSC;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=2118655; DOI=10.1073/pnas.87.17.6674;
RA Larsen R.D., Ernst L.K., Nair R.P., Lowe J.B.;
RT "Molecular cloning, sequence, and expression of a human GDP-L-fucose:beta-
RT D-galactoside 2-alpha-L-fucosyltransferase cDNA that can form the H blood
RT group antigen.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:6674-6678(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INVOLVEMENT IN BOMBAY PHENOTYPE, AND
RP VARIANTS CYS-154; CYS-171; GLU-259; VAL-315 AND CYS-349.
RX PubMed=9122901; DOI=10.1046/j.1537-2995.1997.37397240210.x;
RA Wagner F.F., Flegel W.A.;
RT "Polymorphism of the h allele and the population frequency of sporadic
RT nonfunctional alleles.";
RL Transfusion 37:284-290(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INVOLVEMENT IN BOMBAY AND PARA-BOMBAY
RP PHENOTYPES, AND VARIANTS TYR-148; HIS-154; HIS-241 AND LYS-348.
RX PubMed=9226185;
RA Kaneko M., Nishihara S., Shinya N., Kudo T., Iwasaki H., Seno T., Okubo Y.,
RA Narimatsu H.;
RT "Wide variety of point mutations in the H gene of Bombay and para-Bombay
RT individuals which inactivate H enzyme.";
RL Blood 90:839-849(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-12.
RG SeattleSNPs variation discovery resource;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, AND INDUCTION.
RX PubMed=18205178; DOI=10.1002/jcp.21285;
RA Moehler T.M., Sauer S., Witzel M., Andrulis M., Garcia-Vallejo J.J.,
RA Grobholz R., Willhauck-Fleckenstein M., Greiner A., Goldschmidt H.,
RA Schwartz-Albiez R.;
RT "Involvement of alpha 1-2-fucosyltransferase I (FUT1) and surface-expressed
RT Lewis(y) (CD174) in first endothelial cell-cell contacts during
RT angiogenesis.";
RL J. Cell. Physiol. 215:27-36(2008).
RN [8]
RP INVOLVEMENT IN BOMBAY AND PARA-BOMBAY PHENOTYPES, AND VARIANT HIS-164.
RX PubMed=7912436; DOI=10.1073/pnas.91.13.5843;
RA Kelly R.J., Ernst L.K., Larsen R.D., Bryant J.G., Robinson J.S., Lowe J.B.;
RT "Molecular basis for H blood group deficiency in Bombay (Oh) and para-
RT Bombay individuals.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:5843-5847(1994).
RN [9]
RP INVOLVEMENT IN BOMBAY PHENOTYPE, AND VARIANT ARG-242.
RX PubMed=9299444; DOI=10.1006/bbrc.1997.7232;
RA Koda Y., Soejima M., Johnson P.H., Smart E., Kimura H.;
RT "Missense mutation of FUT1 and deletion of FUT2 are responsible for Indian
RT Bombay phenotype of ABO blood group system.";
RL Biochem. Biophys. Res. Commun. 238:21-25(1997).
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:2118655). H antigen is essential for
CC maturation of the glomerular layer of the main olfactory bulb, in cell
CC migration and early cell-cell contacts during tumor associated
CC angiogenesis (PubMed:18205178). Preferentially fucosylates soluble
CC lactose and to a lesser extent fucosylates glycolipids gangliosides GA1
CC and GM1a (By similarity). {ECO:0000250|UniProtKB:O09160,
CC ECO:0000269|PubMed:18205178, ECO:0000269|PubMed:2118655}.
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:0000269|PubMed:2118655};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GA1 + GDP-beta-L-fucose = 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:0000250|UniProtKB:O09160};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48321;
CC Evidence={ECO:0000250|UniProtKB:O09160};
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:0000250|UniProtKB:O09160};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32176;
CC Evidence={ECO:0000250|UniProtKB:O09160};
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:0000250|UniProtKB:O09160};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48305;
CC Evidence={ECO:0000250|UniProtKB:O09160};
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: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=2.4 mM for phenyl beta-D-galactoside {ECO:0000269|PubMed:2118655};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:2118655}.
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 -!- INDUCTION: Increased by TNF. {ECO:0000269|PubMed:18205178}.
CC -!- POLYMORPHISM: Genetic variations in FUT1 define the H blood group and
CC are responsible for the Bombay and para-Bombay phenotypes [MIM:616754].
CC Erythrocytes from individuals with the Bombay and para-Bombay blood
CC group phenotypes are deficient in H antigens.
CC {ECO:0000269|PubMed:7912436, ECO:0000269|PubMed:9122901,
CC ECO:0000269|PubMed:9226185, ECO:0000269|PubMed:9299444}.
CC -!- MISCELLANEOUS: There are two genes (FUT1 and FUT2) which encode
CC galactoside 2-L-fucosyltransferase. They are expressed in a tissue-
CC specific manner with expression restricted to cells of mesodermal or
CC endodermal origin respectively. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 11 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene mutation
CC database;
CC URL="https://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=hh";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/fut1/";
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_hum_598";
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DR EMBL; M35531; AAA52639.1; -; mRNA.
DR EMBL; Z69587; CAA93435.1; -; Genomic_DNA.
DR EMBL; AB004861; BAA20558.1; -; Genomic_DNA.
DR EMBL; AB004862; BAA20559.1; -; Genomic_DNA.
DR EMBL; AB004863; BAA20560.1; -; Genomic_DNA.
DR EMBL; AY923051; AAW82437.1; -; Genomic_DNA.
DR EMBL; AC009002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC074732; AAH74732.1; -; mRNA.
DR CCDS; CCDS12733.1; -.
DR PIR; A36047; A36047.
DR RefSeq; NP_000139.1; NM_000148.3.
DR RefSeq; NP_001316806.1; NM_001329877.1.
DR RefSeq; XP_016882042.1; XM_017026553.1.
DR AlphaFoldDB; P19526; -.
DR SMR; P19526; -.
DR BioGRID; 108799; 39.
DR IntAct; P19526; 16.
DR STRING; 9606.ENSP00000312021; -.
DR CAZy; GT11; Glycosyltransferase Family 11.
DR GlyGen; P19526; 2 sites.
DR iPTMnet; P19526; -.
DR PhosphoSitePlus; P19526; -.
DR BioMuta; FUT1; -.
DR EPD; P19526; -.
DR MassIVE; P19526; -.
DR PaxDb; P19526; -.
DR PeptideAtlas; P19526; -.
DR PRIDE; P19526; -.
DR ProteomicsDB; 53671; -.
DR Antibodypedia; 31803; 137 antibodies from 24 providers.
DR DNASU; 2523; -.
DR Ensembl; ENST00000645652.2; ENSP00000494643.1; ENSG00000174951.12.
DR GeneID; 2523; -.
DR KEGG; hsa:2523; -.
DR MANE-Select; ENST00000645652.2; ENSP00000494643.1; NM_001384359.1; NP_001371288.1.
DR CTD; 2523; -.
DR DisGeNET; 2523; -.
DR GeneCards; FUT1; -.
DR HGNC; HGNC:4012; FUT1.
DR HPA; ENSG00000174951; Tissue enhanced (pancreas, stomach).
DR MalaCards; FUT1; -.
DR MIM; 211100; gene.
DR MIM; 616754; phenotype.
DR neXtProt; NX_P19526; -.
DR OpenTargets; ENSG00000174951; -.
DR PharmGKB; PA28428; -.
DR VEuPathDB; HostDB:ENSG00000174951; -.
DR eggNOG; ENOG502S316; Eukaryota.
DR GeneTree; ENSGT00390000001450; -.
DR HOGENOM; CLU_043399_0_0_1; -.
DR InParanoid; P19526; -.
DR OMA; MWPPSHR; -.
DR OrthoDB; 1006406at2759; -.
DR PhylomeDB; P19526; -.
DR TreeFam; TF315810; -.
DR BioCyc; MetaCyc:HS10855-MON; -.
DR BRENDA; 2.4.1.344; 2681.
DR BRENDA; 2.4.1.69; 2681.
DR PathwayCommons; P19526; -.
DR Reactome; R-HSA-9033807; ABO blood group biosynthesis.
DR SABIO-RK; P19526; -.
DR SignaLink; P19526; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 2523; 21 hits in 1076 CRISPR screens.
DR ChiTaRS; FUT1; human.
DR GeneWiki; FUT1; -.
DR GenomeRNAi; 2523; -.
DR Pharos; P19526; Tbio.
DR PRO; PR:P19526; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P19526; protein.
DR Bgee; ENSG00000174951; Expressed in body of pancreas and 112 other tissues.
DR ExpressionAtlas; P19526; baseline and differential.
DR Genevisible; P19526; HS.
DR GO; GO:0005794; C:Golgi apparatus; TAS:UniProtKB.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0031127; F:alpha-(1,2)-fucosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008417; F:fucosyltransferase activity; TAS:Reactome.
DR GO; GO:0008107; F:galactoside 2-alpha-L-fucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:ProtInc.
DR GO; GO:0036065; P:fucosylation; ISS:UniProtKB.
DR GO; GO:0042355; P:L-fucose catabolic process; NAS:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0021772; P:olfactory bulb development; ISS:UniProtKB.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; TAS:Reactome.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IMP:UniProtKB.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IMP:UniProtKB.
DR GO; GO:1904906; P:positive regulation of endothelial cell-matrix adhesion via fibronectin; IMP:UniProtKB.
DR GO; GO:1903672; P:positive regulation of sprouting angiogenesis; IMP:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; ISS:UniProtKB.
DR GO; GO:0030155; P:regulation of cell adhesion; ISS:UniProtKB.
DR GO; GO:0001936; P:regulation of endothelial cell proliferation; ISS:UniProtKB.
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 Blood group antigen; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Lipid metabolism; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..365
FT /note="Galactoside alpha-(1,2)-fucosyltransferase 1"
FT /id="PRO_0000149095"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..25
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..365
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 12
FT /note="A -> V (in dbSNP:rs2071699)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_022268"
FT VARIANT 148
FT /note="D -> Y (found in individuals with para-Bombay
FT phenotype; allele H4; dbSNP:rs747442925)"
FT /evidence="ECO:0000269|PubMed:9226185"
FT /id="VAR_020536"
FT VARIANT 154
FT /note="Y -> C (found in individuals with Bombay phenotype)"
FT /evidence="ECO:0000269|PubMed:9122901"
FT /id="VAR_003417"
FT VARIANT 154
FT /note="Y -> H (found in individuals with para-Bombay
FT phenotype; allele H5; dbSNP:rs757349699)"
FT /evidence="ECO:0000269|PubMed:9226185"
FT /id="VAR_020537"
FT VARIANT 164
FT /note="L -> H (found in individuals with para-Bombay
FT phenotype; dbSNP:rs104894687)"
FT /evidence="ECO:0000269|PubMed:7912436"
FT /id="VAR_009708"
FT VARIANT 171
FT /note="W -> C (found in individuals with Bombay phenotype)"
FT /evidence="ECO:0000269|PubMed:9122901"
FT /id="VAR_003418"
FT VARIANT 241
FT /note="Y -> H (found in individuals with para-Bombay
FT phenotype; allele H3; dbSNP:rs765114567)"
FT /evidence="ECO:0000269|PubMed:9226185"
FT /id="VAR_020538"
FT VARIANT 242
FT /note="L -> R (found in individuals with Bombay phenotype;
FT dbSNP:rs28934588)"
FT /evidence="ECO:0000269|PubMed:9299444"
FT /id="VAR_009709"
FT VARIANT 259
FT /note="V -> E (found in individuals with Bombay phenotype)"
FT /evidence="ECO:0000269|PubMed:9122901"
FT /id="VAR_003419"
FT VARIANT 315
FT /note="A -> V (found in individuals with Bombay phenotype)"
FT /evidence="ECO:0000269|PubMed:9122901"
FT /id="VAR_003420"
FT VARIANT 348
FT /note="E -> K (found in individuals with para-Bombay
FT phenotype; allele H5; dbSNP:rs764739319)"
FT /evidence="ECO:0000269|PubMed:9226185"
FT /id="VAR_020539"
FT VARIANT 349
FT /note="W -> C (found in individuals with Bombay phenotype;
FT dbSNP:rs1438752561)"
FT /evidence="ECO:0000269|PubMed:9122901"
FT /id="VAR_003421"
SQ SEQUENCE 365 AA; 41251 MW; 4F4442EC375C9D9E CRC64;
MWLRSHRQLC LAFLLVCVLS VIFFLHIHQD SFPHGLGLSI LCPDRRLVTP PVAIFCLPGT
AMGPNASSSC PQHPASLSGT WTVYPNGRFG NQMGQYATLL ALAQLNGRRA FILPAMHAAL
APVFRITLPV LAPEVDSRTP WRELQLHDWM SEEYADLRDP FLKLSGFPCS WTFFHHLREQ
IRREFTLHDH LREEAQSVLG QLRLGRTGDR PRTFVGVHVR RGDYLQVMPQ RWKGVVGDSA
YLRQAMDWFR ARHEAPVFVV TSNGMEWCKE NIDTSQGDVT FAGDGQEATP WKDFALLTQC
NHTIMTIGTF GFWAAYLAGG DTVYLANFTL PDSEFLKIFK PEAAFLPEWV GINADLSPLW
TLAKP
