GBGT1_HUMAN
ID GBGT1_HUMAN Reviewed; 347 AA.
AC Q8N5D6; A8K633; B2RA95; B7Z8S5; Q45F07; Q5T7U9; Q5T7V1; Q8N2K4; Q9UKI5;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Globoside alpha-1,3-N-acetylgalactosaminyltransferase 1 {ECO:0000305};
DE EC=2.4.1.- {ECO:0000269|PubMed:23255552, ECO:0000305|PubMed:10506200};
DE AltName: Full=Forssman glycolipid synthase-like protein;
GN Name=GBGT1 {ECO:0000312|HGNC:HGNC:20460}; ORFNames=UNQ2513/PRO6002;
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] (ISOFORM 1), LACK OF FORSSMAN SYNTHASE ACTIVITY,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Substantia nigra;
RX PubMed=10506200; DOI=10.1074/jbc.274.41.29390;
RA Xu H., Storch T., Yu M., Elliott S.P., Haslam D.B.;
RT "Characterization of the human Forssman synthetase gene: an evolving
RT association between glycolipid synthesis and host-microbial interactions.";
RL J. Biol. Chem. 274:29390-29398(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PHE-20.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT
RP PHE-20.
RC TISSUE=Adrenal gland, Embryo, and Lung;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PHE-20; GLY-21; PRO-79;
RP TRP-163; ASN-200; PRO-238; ILE-248 AND PHE-291.
RG SeattleSNPs variation discovery resource;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PHE-20.
RC TISSUE=Pancreas;
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 [8]
RP POLYMORPHISM, TISSUE SPECIFICITY, VARIANT GLN-296, AND CHARACTERIZATION OF
RP VARIANT GLN-296.
RX PubMed=23255552; DOI=10.1182/blood-2012-10-455055;
RA Svensson L., Hult A.K., Stamps R., Aangstroem J., Teneberg S., Storry J.R.,
RA Joergensen R., Rydberg L., Henry S.M., Olsson M.L.;
RT "Forssman expression on human erythrocytes: biochemical and genetic
RT evidence of a new histo-blood group system.";
RL Blood 121:1459-1468(2013).
CC -!- FUNCTION: Has lost the ability to synthesize Forssman glycolipid
CC antigen (FORS1/FG) (PubMed:10506200). Might have acquired an
CC alternative function in glycosphingolipid metabolism, but it remains to
CC be established. It appears to have drifted more slowly than confirmed
CC pseudogenes in the glycosyltransferase 6 family, suggesting that it has
CC remained under evolutionary pressure. {ECO:0000269|PubMed:10506200,
CC ECO:0000305}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P14769};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:P14769};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8N5D6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N5D6-2; Sequence=VSP_013750;
CC Name=3;
CC IsoId=Q8N5D6-3; Sequence=VSP_055375;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in
CC placenta, ovary and peripheral blood leukocyte, whereas it is weakly
CC expressed in liver, thymus, and testis (PubMed:10506200). Expressed in
CC bone marrow erythroid cells (PubMed:23255552).
CC {ECO:0000269|PubMed:10506200, ECO:0000269|PubMed:23255552}.
CC -!- DOMAIN: The conserved DXD motif is involved in cofactor binding. The
CC manganese ion interacts with the beta-phosphate group of UDP and may
CC also have a role in catalysis (By similarity). {ECO:0000250}.
CC -!- POLYMORPHISM: Common alleles GBGT1*01N.01 and GBGT1*01N.02 do not
CC synthesize Forssman glycolipid antigen (FORS1). A rare allele encoding
CC an arginine to glutamine change at residue 296 is associated with the
CC ability to synthesize Forssman antigen, which is expressed in
CC erythrocytes and is inheritable, thus defining a new histo-blood group
CC FORS, also known as Apae. This variation might have arised as a
CC consequence of the selective pressure exerted by microorganisms. For
CC instance, the uropathogenic E.coli expressing prsG adhesin only binds
CC and agglutinates FORS1-expressing erythrocytes. Thus, FORS1-positive
CC individuals might be more susceptible to certain pathogens.
CC {ECO:0000269|PubMed:23255552}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 6 family. {ECO:0000305}.
CC -!- CAUTION: The Forssman antigen (FORS1) is normally expressed on
CC erythrocytes of some non-primate mammals. However, in rare cases it is
CC expressed on human erythrocytes of histo-blood group FORS carriers.
CC {ECO:0000305|PubMed:10506200, ECO:0000305|PubMed:23255552}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/gbgt1/";
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Globoside
CC alpha-1,3-N-acetylgalactosaminyltransferase 1;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_479";
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DR EMBL; AF163572; AAF06145.1; -; Transcribed_RNA.
DR EMBL; AY358175; AAQ88542.1; -; mRNA.
DR EMBL; AK074639; BAC11106.1; -; mRNA.
DR EMBL; AK291498; BAF84187.1; -; mRNA.
DR EMBL; AK303825; BAH14061.1; -; mRNA.
DR EMBL; AK314097; BAG36792.1; -; mRNA.
DR EMBL; DQ145941; AAZ38721.1; -; Genomic_DNA.
DR EMBL; AL162417; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW88045.1; -; Genomic_DNA.
DR EMBL; BC032499; AAH32499.1; -; mRNA.
DR CCDS; CCDS65175.1; -. [Q8N5D6-3]
DR CCDS; CCDS65176.1; -. [Q8N5D6-2]
DR CCDS; CCDS6960.1; -. [Q8N5D6-1]
DR RefSeq; NP_001269558.1; NM_001282629.1. [Q8N5D6-2]
DR RefSeq; NP_001269561.1; NM_001282632.1. [Q8N5D6-3]
DR RefSeq; NP_001275501.1; NM_001288572.1.
DR RefSeq; NP_001275502.1; NM_001288573.1.
DR RefSeq; NP_068836.2; NM_021996.5. [Q8N5D6-1]
DR AlphaFoldDB; Q8N5D6; -.
DR SMR; Q8N5D6; -.
DR BioGRID; 117677; 1.
DR IntAct; Q8N5D6; 1.
DR STRING; 9606.ENSP00000361110; -.
DR CAZy; GT6; Glycosyltransferase Family 6.
DR GlyGen; Q8N5D6; 1 site.
DR iPTMnet; Q8N5D6; -.
DR PhosphoSitePlus; Q8N5D6; -.
DR BioMuta; GBGT1; -.
DR DMDM; 67464687; -.
DR MassIVE; Q8N5D6; -.
DR PaxDb; Q8N5D6; -.
DR PeptideAtlas; Q8N5D6; -.
DR PRIDE; Q8N5D6; -.
DR Antibodypedia; 63936; 56 antibodies from 16 providers.
DR DNASU; 26301; -.
DR Ensembl; ENST00000372040.9; ENSP00000361110.3; ENSG00000148288.13. [Q8N5D6-1]
DR Ensembl; ENST00000372043.7; ENSP00000361113.3; ENSG00000148288.13. [Q8N5D6-2]
DR Ensembl; ENST00000540636.6; ENSP00000437663.1; ENSG00000148288.13. [Q8N5D6-3]
DR GeneID; 26301; -.
DR KEGG; hsa:26301; -.
DR MANE-Select; ENST00000372040.9; ENSP00000361110.3; NM_021996.6; NP_068836.2.
DR UCSC; uc004ccw.5; human. [Q8N5D6-1]
DR CTD; 26301; -.
DR DisGeNET; 26301; -.
DR GeneCards; GBGT1; -.
DR HGNC; HGNC:20460; GBGT1.
DR HPA; ENSG00000148288; Low tissue specificity.
DR MIM; 606074; gene.
DR neXtProt; NX_Q8N5D6; -.
DR OpenTargets; ENSG00000148288; -.
DR PharmGKB; PA134967297; -.
DR VEuPathDB; HostDB:ENSG00000148288; -.
DR eggNOG; ENOG502QQAJ; Eukaryota.
DR GeneTree; ENSGT00950000182858; -.
DR HOGENOM; CLU_062445_0_1_1; -.
DR InParanoid; Q8N5D6; -.
DR OMA; IHPGYFT; -.
DR PhylomeDB; Q8N5D6; -.
DR TreeFam; TF330991; -.
DR BioCyc; MetaCyc:ENSG00000148288-MON; -.
DR BRENDA; 2.4.1.88; 2681.
DR PathwayCommons; Q8N5D6; -.
DR SignaLink; Q8N5D6; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 26301; 39 hits in 1070 CRISPR screens.
DR GeneWiki; GBGT1; -.
DR GenomeRNAi; 26301; -.
DR Pharos; Q8N5D6; Tbio.
DR PRO; PR:Q8N5D6; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q8N5D6; protein.
DR Bgee; ENSG00000148288; Expressed in body of stomach and 146 other tissues.
DR ExpressionAtlas; Q8N5D6; baseline and differential.
DR Genevisible; Q8N5D6; HS.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR GO; GO:0047277; F:globoside alpha-N-acetylgalactosaminyltransferase activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0009247; P:glycolipid biosynthetic process; TAS:ProtInc.
DR GO; GO:0030259; P:lipid glycosylation; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR005076; Glyco_trans_6.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR10462; PTHR10462; 1.
DR Pfam; PF03414; Glyco_transf_6; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Manganese; Membrane; Metal-binding; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..347
FT /note="Globoside alpha-1,3-N-
FT acetylgalactosaminyltransferase 1"
FT /id="PRO_0000157295"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 6..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..347
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 298
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 116..121
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 206..208
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 206
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 208
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 228..231
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 46..63
FT /note="FNMKLHYKREKPLQPVVW -> L (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055375"
FT VAR_SEQ 120..347
FT /note="KYTHFIQSFLESAEEFFMRGYRVHYYIFTDNPAAVPGVPLGPHRLLSSIPIQ
FT GHSHWEETSMRRMETISQHIAKRAHREVDYLFCLDVDMVFRNPWGPETLGDLVAAIHPS
FT YYAVPRQQFPYERRRVSTAFVADSEGDFYYGGAVFGGQVARVYEFTRGCHMAILADKAN
FT GIMAAWREESHLNRHFISNKPSKVLSPEYLWDDRKPQPPSLKLIRFSTLDKDISCLRS
FT -> NPSWSQPRSSSCVGTGCTTTSSLTTLQPFPGSRWVPTGFSAPSPSRVTPTGRRHPC
FT AGWRPSASTLLRGLTGRWTTSSALMWTWCFGTRGALRPWETWWLPFTQATTPFPASSSP
FT MSAGVFPLPLWQTAKGTSIMVGQSSGGRWPGYMSLLGAATWPSWRTRPMASWLPGGRKA
FT T (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_013750"
FT VARIANT 20
FT /note="L -> F (in dbSNP:rs2073924)"
FT /evidence="ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.4"
FT /id="VAR_022452"
FT VARIANT 21
FT /note="S -> G (in dbSNP:rs35578482)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_025068"
FT VARIANT 79
FT /note="L -> P (in dbSNP:rs12350913)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_025069"
FT VARIANT 163
FT /note="R -> W (in dbSNP:rs34260370)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_025070"
FT VARIANT 200
FT /note="D -> N (in dbSNP:rs34903033)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_025071"
FT VARIANT 238
FT /note="Q -> P (in dbSNP:rs35366884)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_025072"
FT VARIANT 248
FT /note="T -> I (in dbSNP:rs35184631)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_025073"
FT VARIANT 291
FT /note="I -> F (in dbSNP:rs35403335)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_025074"
FT VARIANT 296
FT /note="R -> Q (found in FORS blood group carriers;
FT reactivates Forssman antigen synthesis and expression in
FT erythrocytes; dbSNP:rs375748588)"
FT /evidence="ECO:0000269|PubMed:23255552"
FT /id="VAR_085166"
FT CONFLICT 163
FT /note="R -> Q (in Ref. 1; AAF06145)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="L -> F (in Ref. 1; AAF06145)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="S -> R (in Ref. 1; AAF06145)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 347 AA; 40127 MW; 99987D43B22344A0 CRC64;
MHRRRLALGL GFCLLAGTSL SVLWVYLENW LPVSYVPYYL PCPEIFNMKL HYKREKPLQP
VVWSQYPQPK LLEHRPTQLL TLTPWLAPIV SEGTFNPELL QHIYQPLNLT IGVTVFAVGK
YTHFIQSFLE SAEEFFMRGY RVHYYIFTDN PAAVPGVPLG PHRLLSSIPI QGHSHWEETS
MRRMETISQH IAKRAHREVD YLFCLDVDMV FRNPWGPETL GDLVAAIHPS YYAVPRQQFP
YERRRVSTAF VADSEGDFYY GGAVFGGQVA RVYEFTRGCH MAILADKANG IMAAWREESH
LNRHFISNKP SKVLSPEYLW DDRKPQPPSL KLIRFSTLDK DISCLRS
