B3GN3_HUMAN
ID B3GN3_HUMAN Reviewed; 372 AA.
AC Q9Y2A9; B2RAS4; Q6NWU9; Q6NXU9; Q8WWR6; Q9C0J2;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 3;
DE EC=2.4.1.149 {ECO:0000269|PubMed:11042166};
DE AltName: Full=Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase;
DE EC=2.4.1.146 {ECO:0000269|PubMed:11439191};
DE AltName: Full=Beta-1,3-galactosyltransferase 8;
DE Short=Beta-1,3-GalTase 8;
DE Short=Beta3Gal-T8;
DE Short=Beta3GalT8;
DE Short=b3Gal-T8;
DE AltName: Full=Beta-3-Gx-T8;
DE AltName: Full=Core 1 extending beta-1,3-N-acetylglucosaminyltransferase {ECO:0000303|PubMed:11439191};
DE AltName: Full=Core1-beta3GlcNAcT {ECO:0000303|PubMed:11439191};
DE AltName: Full=Transmembrane protein 3;
DE AltName: Full=UDP-Gal:beta-GlcNAc beta-1,3-galactosyltransferase 8;
DE AltName: Full=UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 3;
DE Short=BGnT-3;
DE Short=Beta-1,3-Gn-T3;
DE Short=Beta-1,3-N-acetylglucosaminyltransferase 3;
DE Short=Beta3Gn-T3;
DE AltName: Full=UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase 8;
GN Name=B3GNT3; Synonyms=B3GALT8, TMEM3; ORFNames=UNQ637/PRO1266;
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], AND VARIANT HIS-328.
RX PubMed=10072769; DOI=10.1016/s0378-1119(99)00004-9;
RA Yokoyama-Kobayashi M., Yamaguchi T., Sekine S., Kato S.;
RT "Selection of cDNAs encoding putative type II membrane proteins on the cell
RT surface from a human full-length cDNA bank.";
RL Gene 228:161-167(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND VARIANT
RP HIS-328.
RX PubMed=11439191; DOI=10.1016/s0092-8674(01)00394-4;
RA Yeh J.-C., Hiraoka N., Petryniak B., Nakayama J., Ellies L.G., Rabuka D.,
RA Hindsgaul O., Marth J.D., Lowe J.B., Fukuda M.;
RT "Novel sulfated lymphocyte homing receptors and their control by a Core1
RT extension beta 1,3-N-acetylglucosaminyltransferase.";
RL Cell 105:957-969(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Gastric mucosa;
RX PubMed=11042166; DOI=10.1074/jbc.m004800200;
RA Shiraishi N., Natsume A., Togayachi A., Endo T., Akashima T., Yamada Y.,
RA Imai N., Nakagawa S., Koizumi S., Sekine S., Narimatsu H., Sasaki K.;
RT "Identification and characterization of three novel beta 1,3-N-
RT acetylglucosaminyltransferases structurally related to the beta 1,3-
RT galactosyltransferase family.";
RL J. Biol. Chem. 276:3498-3507(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT HIS-328.
RA Jensen M.A., Bennett E.P.;
RT "Cloning of a new member of the beta 1,3 galactosyltransferase family,
RT b1,3Gal-T6.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT HIS-328.
RA Bennett E.P.;
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-328.
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-328.
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 [10]
RP REVIEW.
RX PubMed=10580128; DOI=10.1016/s0304-4165(99)00168-3;
RA Amado M., Almeida R., Schwientek T., Clausen H.;
RT "Identification and characterization of large galactosyltransferase gene
RT families: galactosyltransferases for all functions.";
RL Biochim. Biophys. Acta 1473:35-53(1999).
RN [11]
RP VARIANT PHE-317.
RX PubMed=25787250; DOI=10.1073/pnas.1503696112;
RA Cromer M.K., Choi M., Nelson-Williams C., Fonseca A.L., Kunstman J.W.,
RA Korah R.M., Overton J.D., Mane S., Kenney B., Malchoff C.D., Stalberg P.,
RA Akerstroem G., Westin G., Hellman P., Carling T., Bjoerklund P.,
RA Lifton R.P.;
RT "Neomorphic effects of recurrent somatic mutations in Yin Yang 1 in
RT insulin-producing adenomas.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:4062-4067(2015).
CC -!- FUNCTION: Beta-1,3-N-acetylglucosaminyltransferase involved in the
CC synthesis of poly-N-acetyllactosamine. Has activity for type 2
CC oligosaccharides (PubMed:11042166). Also acts as a core1-1,3-N-
CC acetylglucosaminyltransferase (Core1-beta3GlcNAcT) to form the 6-sulfo
CC sialyl Lewis x on extended core1 O-glycans (PubMed:11439191).
CC {ECO:0000269|PubMed:11042166, ECO:0000269|PubMed:11439191}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-{beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-
CC (1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-threonyl-[protein] + UDP-
CC N-acetyl-alpha-D-glucosamine = 3-O-{beta-D-GlcNAc-(1->3)-beta-D-Gal-
CC (1->3)-[beta-D-GlcNAc-(1->6)]-alpha-D-GalNAc}-L-threonyl-[protein] +
CC H(+) + UDP; Xref=Rhea:RHEA:56224, Rhea:RHEA-COMP:14420, Rhea:RHEA-
CC COMP:14422, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:139607, ChEBI:CHEBI:139612; EC=2.4.1.146;
CC Evidence={ECO:0000269|PubMed:11439191};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-{beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-
CC (1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-seryl-[protein] + UDP-N-
CC acetyl-alpha-D-glucosamine = 3-O-{beta-D-GlcNAc-(1->3)-beta-D-Gal-
CC (1->3)-[beta-D-GlcNAc-(1->6)]-alpha-D-GalNAc}-L-seryl-[protein] +
CC H(+) + UDP; Xref=Rhea:RHEA:56220, Rhea:RHEA-COMP:14419, Rhea:RHEA-
CC COMP:14421, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:139605, ChEBI:CHEBI:139611; EC=2.4.1.146;
CC Evidence={ECO:0000269|PubMed:11439191};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl
CC derivative + UDP-N-acetyl-alpha-D-glucosamine = an N-acetyl-beta-D-
CC glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-
CC glucosaminyl derivative + H(+) + UDP; Xref=Rhea:RHEA:14389,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:133507, ChEBI:CHEBI:134090; EC=2.4.1.149;
CC Evidence={ECO:0000269|PubMed:11042166};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in colon, jejunum, stomach, esophagus,
CC placenta and trachea. {ECO:0000269|PubMed:11042166}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC82374.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=UDP-
CC GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 3;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_536";
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DR EMBL; AB015630; BAA76497.1; -; mRNA.
DR EMBL; AF293973; AAK00849.1; -; mRNA.
DR EMBL; AB049585; BAB21531.1; -; mRNA.
DR EMBL; AJ130847; CAC45044.1; -; mRNA.
DR EMBL; AJ278961; CAC82374.1; ALT_FRAME; mRNA.
DR EMBL; AY358955; AAQ89314.1; -; mRNA.
DR EMBL; AK314323; BAG36971.1; -; mRNA.
DR EMBL; AC008761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC066876; AAH66876.1; -; mRNA.
DR EMBL; BC067423; AAH67423.1; -; mRNA.
DR CCDS; CCDS12364.1; -.
DR RefSeq; NP_055071.2; NM_014256.3.
DR RefSeq; XP_011525928.1; XM_011527626.2.
DR AlphaFoldDB; Q9Y2A9; -.
DR SMR; Q9Y2A9; -.
DR BioGRID; 115614; 139.
DR IntAct; Q9Y2A9; 10.
DR STRING; 9606.ENSP00000321874; -.
DR BindingDB; Q9Y2A9; -.
DR ChEMBL; CHEMBL3325305; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyGen; Q9Y2A9; 5 sites.
DR iPTMnet; Q9Y2A9; -.
DR PhosphoSitePlus; Q9Y2A9; -.
DR BioMuta; B3GNT3; -.
DR DMDM; 311033352; -.
DR EPD; Q9Y2A9; -.
DR jPOST; Q9Y2A9; -.
DR MassIVE; Q9Y2A9; -.
DR MaxQB; Q9Y2A9; -.
DR PaxDb; Q9Y2A9; -.
DR PeptideAtlas; Q9Y2A9; -.
DR PRIDE; Q9Y2A9; -.
DR ProteomicsDB; 85714; -.
DR Antibodypedia; 14471; 106 antibodies from 23 providers.
DR DNASU; 10331; -.
DR Ensembl; ENST00000318683.7; ENSP00000321874.5; ENSG00000179913.11.
DR Ensembl; ENST00000595387.1; ENSP00000472638.1; ENSG00000179913.11.
DR GeneID; 10331; -.
DR KEGG; hsa:10331; -.
DR MANE-Select; ENST00000318683.7; ENSP00000321874.5; NM_014256.4; NP_055071.2.
DR UCSC; uc002nhl.2; human.
DR CTD; 10331; -.
DR DisGeNET; 10331; -.
DR GeneCards; B3GNT3; -.
DR HGNC; HGNC:13528; B3GNT3.
DR HPA; ENSG00000179913; Tissue enhanced (intestine, salivary gland, stomach).
DR MIM; 605863; gene.
DR neXtProt; NX_Q9Y2A9; -.
DR OpenTargets; ENSG00000179913; -.
DR PharmGKB; PA25219; -.
DR VEuPathDB; HostDB:ENSG00000179913; -.
DR eggNOG; KOG2287; Eukaryota.
DR GeneTree; ENSGT00940000159134; -.
DR HOGENOM; CLU_036849_5_1_1; -.
DR InParanoid; Q9Y2A9; -.
DR OMA; YCAGGGF; -.
DR OrthoDB; 1037602at2759; -.
DR PhylomeDB; Q9Y2A9; -.
DR TreeFam; TF318639; -.
DR BioCyc; MetaCyc:ENSG00000179913-MON; -.
DR BRENDA; 2.4.1.146; 2681.
DR BRENDA; 2.4.1.149; 2681.
DR BRENDA; 2.4.99.6; 2681.
DR PathwayCommons; Q9Y2A9; -.
DR Reactome; R-HSA-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-HSA-913709; O-linked glycosylation of mucins.
DR SignaLink; Q9Y2A9; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 10331; 29 hits in 1064 CRISPR screens.
DR ChiTaRS; B3GNT3; human.
DR GeneWiki; Beta-1,3-N-acetylglucosaminyltransferase_3; -.
DR GenomeRNAi; 10331; -.
DR Pharos; Q9Y2A9; Tbio.
DR PRO; PR:Q9Y2A9; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9Y2A9; protein.
DR Bgee; ENSG00000179913; Expressed in mucosa of transverse colon and 95 other tissues.
DR ExpressionAtlas; Q9Y2A9; baseline and differential.
DR Genevisible; Q9Y2A9; HS.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0047223; F:beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008457; F:beta-galactosyl-N-acetylglucosaminylgalactosylglucosyl-ceramide beta-1,3-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008532; F:N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008499; F:UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity; TAS:Reactome.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0018146; P:keratan sulfate biosynthetic process; TAS:Reactome.
DR GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
DR GO; GO:0030311; P:poly-N-acetyllactosamine biosynthetic process; IDA:UniProtKB.
DR InterPro; IPR002659; Glyco_trans_31.
DR PANTHER; PTHR11214; PTHR11214; 1.
DR Pfam; PF01762; Galactosyl_T; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..372
FT /note="N-acetyllactosaminide beta-1,3-N-
FT acetylglucosaminyltransferase 3"
FT /id="PRO_0000219172"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..372
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 317
FT /note="I -> F"
FT /evidence="ECO:0000269|PubMed:25787250"
FT /id="VAR_074178"
FT VARIANT 328
FT /note="R -> H (in dbSNP:rs36686)"
FT /evidence="ECO:0000269|PubMed:10072769,
FT ECO:0000269|PubMed:11439191, ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.4,
FT ECO:0000269|Ref.5"
FT /id="VAR_022644"
FT CONFLICT 89
FT /note="C -> Y (in Ref. 9; AAH66876)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="W -> R (in Ref. 9; AAH67423)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 372 AA; 42534 MW; A6E3FE88B2F00F10 CRC64;
MKYLRHRRPN ATLILAIGAF TLLLFSLLVS PPTCKVQEQP PAIPEALAWP TPPTRPAPAP
CHANTSMVTH PDFATQPQHV QNFLLYRHCR HFPLLQDVPP SKCAQPVFLL LVIKSSPSNY
VRRELLRRTW GRERKVRGLQ LRLLFLVGTA SNPHEARKVN RLLELEAQTH GDILQWDFHD
SFFNLTLKQV LFLQWQETRC ANASFVLNGD DDVFAHTDNM VFYLQDHDPG RHLFVGQLIQ
NVGPIRAFWS KYYVPEVVTQ NERYPPYCGG GGFLLSRFTA AALRRAAHVL DIFPIDDVFL
GMCLELEGLK PASHSGIRTS GVRAPSQRLS SFDPCFYRDL LLVHRFLPYE MLLMWDALNQ
PNLTCGNQTQ IY
