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 29-MAY-2024, entry version 185. 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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 SIGNOR; 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; 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. 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 //