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   27-MAR-2024, entry version 184.
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;
CC       Note=UDP-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   GlyCosmos; Q9Y2A9; 5 sites, No reported glycans.
DR   GlyGen; Q9Y2A9; 5 sites.
DR   iPTMnet; Q9Y2A9; -.
DR   PhosphoSitePlus; Q9Y2A9; -.
DR   SwissPalm; Q9Y2A9; -.
DR   BioMuta; B3GNT3; -.
DR   DMDM; 311033352; -.
DR   EPD; Q9Y2A9; -.
DR   jPOST; Q9Y2A9; -.
DR   MassIVE; Q9Y2A9; -.
DR   MaxQB; Q9Y2A9; -.
DR   PaxDb; 9606-ENSP00000321874; -.
DR   PeptideAtlas; Q9Y2A9; -.
DR   ProteomicsDB; 85714; -.
DR   Antibodypedia; 14471; 118 antibodies from 24 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   AGR; HGNC:13528; -.
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; VSYLQGH; -.
DR   OrthoDB; 532757at2759; -.
DR   PhylomeDB; Q9Y2A9; -.
DR   TreeFam; TF318639; -.
DR   BioCyc; MetaCyc:ENSG00000179913-MONOMER; -.
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; 37 hits in 1142 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 cell types or tissues.
DR   ExpressionAtlas; Q9Y2A9; baseline and differential.
DR   GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005886; C: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: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: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   GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
DR   Gene3D; 3.90.550.50; -; 1.
DR   InterPro; IPR002659; Glyco_trans_31.
DR   PANTHER; PTHR11214; BETA-1,3-N-ACETYLGLUCOSAMINYLTRANSFERASE; 1.
DR   PANTHER; PTHR11214:SF23; N-ACETYLLACTOSAMINIDE BETA-1,3-N-ACETYLGLUCOSAMINYLTRANSFERASE 3; 1.
DR   Pfam; PF01762; Galactosyl_T; 1.
DR   Genevisible; Q9Y2A9; HS.
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
//