ID MUC20_HUMAN Reviewed; 709 AA. AC Q8N307; Q6UX97; Q76I83; Q76I85; Q86ST8; Q8NBY6; Q96KA1; Q9P2I8; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2011, sequence version 3. DT 24-JAN-2024, entry version 142. DE RecName: Full=Mucin-20; DE Short=MUC-20; DE Flags: Precursor; GN Name=MUC20; Synonyms=KIAA1359; ORFNames=UNQ2782/PRO7170; 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 [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), VARIANTS RP 184-HIS--LEU-354 DEL; 241-HIS--LEU-354 DEL AND ILE-442, POLYMORPHISM, RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC TISSUE=Kidney; RX PubMed=14565953; DOI=10.1074/jbc.m304558200; RA Higuchi T., Orita T., Nakanishi S., Katsuya K., Watanabe H., Yamasaki Y., RA Waga I., Nanayama T., Yamamoto Y., Munger W., Sun H.-W., Falk R.J., RA Jennette J.C., Alcorta D.A., Li H., Yamamoto T., Saito Y., Nakamura M.; RT "Molecular cloning, genomic structure, and expression analysis of MUC20, a RT novel mucin protein, up-regulated in injured kidney."; RL J. Biol. Chem. 279:1968-1979(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS RP 184-HIS--LEU-354 DEL AND ILE-442. 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] (ISOFORM 1), AND VARIANTS RP 184-HIS--LEU-354 DEL; ILE-442 AND 483-THR--THR-533 DEL. RC TISSUE=Embryo, and 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS RP 184-HIS--LEU-354 DEL; 203-HIS--LEU-354 DEL; ILE-442 AND LEU-590. RC TISSUE=Brain, and Colon; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 26-638 (ISOFORM 1), AND VARIANT RP 241-HIS--LEU-354 DEL. RC TISSUE=Brain; RX PubMed=10718198; DOI=10.1093/dnares/7.1.65; RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XVI. The RT complete sequences of 150 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 7:65-73(2000). RN [7] RP FUNCTION, AND INTERACTION WITH MET. RX PubMed=15314156; DOI=10.1128/mcb.24.17.7456-7468.2004; RA Higuchi T., Orita T., Katsuya K., Yamasaki Y., Akiyama K., Li H., RA Yamamoto T., Saito Y., Nakamura M.; RT "MUC20 suppresses the hepatocyte growth factor-induced Grb2-Ras pathway by RT binding to a multifunctional docking site of met."; RL Mol. Cell. Biol. 24:7456-7468(2004). RN [8] RP TANDEM REPEATS POLYMORPHISM. RX PubMed=16508246; DOI=10.1159/000091785; RA Li G., Zhang H., Lv J., Hou P., Wang H.; RT "Tandem repeats polymorphism of MUC20 is an independent factor for the RT progression of immunoglobulin A nephropathy."; RL Am. J. Nephrol. 26:43-49(2006). RN [9] RP TISSUE SPECIFICITY. RX PubMed=16997931; DOI=10.1093/humrep/del164; RA Russo C.L., Spurr-Michaud S., Tisdale A., Pudney J., Anderson D., RA Gipson I.K.; RT "Mucin gene expression in human male urogenital tract epithelia."; RL Hum. Reprod. 21:2783-2793(2006). CC -!- FUNCTION: May regulate MET signaling cascade. Seems to decrease CC hepatocyte growth factor (HGF)-induced transient MAPK activation. CC Blocks GRB2 recruitment to MET thus suppressing the GRB2-RAS pathway. CC Inhibits HGF-induced proliferation of MMP1 and MMP9 expression. CC {ECO:0000269|PubMed:15314156}. CC -!- SUBUNIT: Interacts with MET; oligomerization increases affinity for CC MET. {ECO:0000269|PubMed:15314156}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Apical cell membrane CC {ECO:0000269|PubMed:14565953}. Basolateral cell membrane CC {ECO:0000269|PubMed:14565953}. Cell projection, microvillus membrane CC {ECO:0000269|PubMed:14565953}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=hMUC20-L; CC IsoId=Q8N307-1; Sequence=Displayed; CC Name=2; Synonyms=hMUC20-S; CC IsoId=Q8N307-3; Sequence=VSP_030980; CC -!- TISSUE SPECIFICITY: Highly expressed in kidney, moderately in placenta, CC lung, prostate, liver, and digestive system. In the kidney, localized CC in the proximal tubules but not in the glomerulus or distal tubules. CC Detected in most of the male urogenital tract epithelia, with the CC exception of epididymis. {ECO:0000269|PubMed:14565953, CC ECO:0000269|PubMed:16997931}. CC -!- POLYMORPHISM: The region encoding the tandem repeats is highly CC polymorphic. Divergence of the number of tandem repeats was seen in CC different cDNA libraries. CC -!- SEQUENCE CAUTION: CC Sequence=AAQ88814.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAA92597.1; Type=Miscellaneous discrepancy; Note=Dubious isoform. Probable cloning artifact.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Mucin database; CC URL="http://www.medkem.gu.se/mucinbiology/databases/"; 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; AB098731; BAD06718.1; -; mRNA. DR EMBL; AB098733; BAD06720.1; -; Genomic_DNA. DR EMBL; AY358449; AAQ88814.1; ALT_FRAME; mRNA. DR EMBL; AK027314; BAB55035.1; -; mRNA. DR EMBL; AK075138; BAC11428.1; -; mRNA. DR EMBL; AC069513; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC029267; AAH29267.1; -; mRNA. DR EMBL; BC044243; AAH44243.1; -; mRNA. DR EMBL; AB037780; BAA92597.1; ALT_SEQ; mRNA. DR CCDS; CCDS63877.1; -. [Q8N307-1] DR RefSeq; NP_001269435.1; NM_001282506.1. [Q8N307-1] DR RefSeq; NP_001278762.1; NM_001291833.1. DR RefSeq; NP_065841.1; NM_020790.1. DR RefSeq; NP_689886.3; NM_152673.3. DR AlphaFoldDB; Q8N307; -. DR BioGRID; 128360; 49. DR IntAct; Q8N307; 23. DR STRING; 9606.ENSP00000414350; -. DR GlyCosmos; Q8N307; 4 sites, 1 glycan. DR GlyGen; Q8N307; 13 sites, 2 O-linked glycans (10 sites). DR iPTMnet; Q8N307; -. DR PhosphoSitePlus; Q8N307; -. DR BioMuta; MUC20; -. DR DMDM; 317373415; -. DR jPOST; Q8N307; -. DR MassIVE; Q8N307; -. DR PaxDb; 9606-ENSP00000414350; -. DR PeptideAtlas; Q8N307; -. DR ProteomicsDB; 71749; -. [Q8N307-1] DR ProteomicsDB; 71750; -. [Q8N307-3] DR Antibodypedia; 35139; 233 antibodies from 24 providers. DR DNASU; 200958; -. DR Ensembl; ENST00000445522.6; ENSP00000405629.2; ENSG00000176945.18. [Q8N307-3] DR Ensembl; ENST00000447234.7; ENSP00000414350.2; ENSG00000176945.18. [Q8N307-1] DR Ensembl; ENST00000610415.4; ENSP00000479947.1; ENSG00000278114.4. [Q8N307-1] DR Ensembl; ENST00000615394.4; ENSP00000483878.1; ENSG00000276583.4. [Q8N307-1] DR Ensembl; ENST00000620530.4; ENSP00000479182.1; ENSG00000275501.4. [Q8N307-1] DR Ensembl; ENST00000625274.2; ENSP00000485837.1; ENSG00000278114.4. [Q8N307-3] DR Ensembl; ENST00000627739.2; ENSP00000485855.1; ENSG00000276583.4. [Q8N307-3] DR Ensembl; ENST00000630334.2; ENSP00000485921.1; ENSG00000275501.4. [Q8N307-3] DR GeneID; 200958; -. DR KEGG; hsa:200958; -. DR MANE-Select; ENST00000447234.7; ENSP00000414350.2; NM_001282506.2; NP_001269435.1. DR UCSC; uc032soi.2; human. [Q8N307-1] DR AGR; HGNC:23282; -. DR CTD; 200958; -. DR DisGeNET; 200958; -. DR GeneCards; MUC20; -. DR HGNC; HGNC:23282; MUC20. DR HPA; ENSG00000176945; Low tissue specificity. DR MIM; 610360; gene. DR neXtProt; NX_Q8N307; -. DR OpenTargets; ENSG00000176945; -. DR PharmGKB; PA134939730; -. DR VEuPathDB; HostDB:ENSG00000176945; -. DR eggNOG; ENOG502SVUK; Eukaryota. DR GeneTree; ENSGT00730000111453; -. DR InParanoid; Q8N307; -. DR OrthoDB; 5267050at2759; -. DR PhylomeDB; Q8N307; -. DR TreeFam; TF338458; -. DR PathwayCommons; Q8N307; -. DR Reactome; R-HSA-5083625; Defective GALNT3 causes HFTC. DR Reactome; R-HSA-5083632; Defective C1GALT1C1 causes TNPS. DR Reactome; R-HSA-5083636; Defective GALNT12 causes CRCS1. DR Reactome; R-HSA-5621480; Dectin-2 family. DR Reactome; R-HSA-8851805; MET activates RAS signaling. DR Reactome; R-HSA-913709; O-linked glycosylation of mucins. DR Reactome; R-HSA-977068; Termination of O-glycan biosynthesis. DR SignaLink; Q8N307; -. DR BioGRID-ORCS; 200958; 54 hits in 1103 CRISPR screens. DR ChiTaRS; MUC20; human. DR GeneWiki; MUC20; -. DR GenomeRNAi; 200958; -. DR Pharos; Q8N307; Tbio. DR PRO; PR:Q8N307; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q8N307; Protein. DR Bgee; ENSG00000176945; Expressed in right uterine tube and 117 other cell types or tissues. DR ExpressionAtlas; Q8N307; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009925; C:basal plasma membrane; IDA:MGI. DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome. DR GO; GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0042802; F:identical protein binding; IPI:MGI. DR GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; IBA:GO_Central. DR InterPro; IPR034551; MUC20. DR PANTHER; PTHR37358; MUCIN-20; 1. DR PANTHER; PTHR37358:SF1; MUCIN-20; 1. DR Genevisible; Q8N307; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Cell projection; Glycoprotein; KW Membrane; Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1..25 FT /evidence="ECO:0000255" FT CHAIN 26..709 FT /note="Mucin-20" FT /id="PRO_0000317469" FT REPEAT 173..192 FT /note="1" FT /evidence="ECO:0000269|PubMed:16508246" FT REPEAT 193..211 FT /note="2" FT /evidence="ECO:0000269|PubMed:16508246" FT REPEAT 212..230 FT /note="3" FT /evidence="ECO:0000269|PubMed:16508246" FT REPEAT 231..249 FT /note="4" FT /evidence="ECO:0000269|PubMed:16508246" FT REPEAT 250..268 FT /note="5" FT /evidence="ECO:0000269|PubMed:16508246" FT REPEAT 269..287 FT /note="6" FT /evidence="ECO:0000269|PubMed:16508246" FT REPEAT 288..306 FT /note="7" FT /evidence="ECO:0000269|PubMed:16508246" FT REPEAT 307..325 FT /note="8" FT /evidence="ECO:0000269|PubMed:16508246" FT REPEAT 326..344 FT /note="9" FT /evidence="ECO:0000269|PubMed:16508246" FT REPEAT 345..363 FT /note="10" FT /evidence="ECO:0000269|PubMed:16508246" FT REPEAT 364..382 FT /note="11" FT /evidence="ECO:0000269|PubMed:16508246" FT REPEAT 383..400 FT /note="12; approximate" FT /evidence="ECO:0000269|PubMed:16508246" FT REGION 57..92 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 170..403 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 173..400 FT /note="12 X 20 AA approximate tandem repeats of S-S-E-S-S- FT A-S-S-D-S-P-H-P-V-I-T-P-S-R-A" FT REGION 434..515 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 450..656 FT /note="Involved in oligomerization" FT REGION 583..657 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 657..709 FT /note="Interaction with MET" FT /evidence="ECO:0000269|PubMed:15314156" FT COMPBIAS 57..71 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 434..461 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 475..515 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 609..655 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 423 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 616 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 622 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 1..35 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14565953" FT /id="VSP_030980" FT VARIANT 3 FT /note="C -> S (in dbSNP:rs7627924)" FT /id="VAR_038536" FT VARIANT 18 FT /note="V -> G (in dbSNP:rs1811139)" FT /id="VAR_038537" FT VARIANT 130..376 FT /note="Missing" FT /id="VAR_054139" FT VARIANT 184..354 FT /note="Missing" FT /evidence="ECO:0000269|PubMed:12975309, FT ECO:0000269|PubMed:14565953, ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334" FT /id="VAR_054140" FT VARIANT 203..354 FT /note="Missing" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_054141" FT VARIANT 241..354 FT /note="Missing" FT /evidence="ECO:0000269|PubMed:10718198, FT ECO:0000269|PubMed:14565953" FT /id="VAR_054142" FT VARIANT 442 FT /note="T -> I (in dbSNP:rs2550232)" FT /evidence="ECO:0000269|PubMed:12975309, FT ECO:0000269|PubMed:14565953, ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334" FT /id="VAR_038538" FT VARIANT 483..533 FT /note="Missing" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_054143" FT VARIANT 514 FT /note="G -> R (in dbSNP:rs3828410)" FT /id="VAR_056641" FT VARIANT 590 FT /note="P -> L (in dbSNP:rs3828408)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_038539" FT VARIANT 666 FT /note="R -> W (in dbSNP:rs11923495)" FT /id="VAR_038540" FT VARIANT 671 FT /note="S -> C (in dbSNP:rs3762739)" FT /id="VAR_038541" FT CONFLICT 75 FT /note="I -> V (in Ref. 5; AAH29267)" FT /evidence="ECO:0000305" FT CONFLICT 136 FT /note="R -> E (in Ref. 1; BAD06718/BAD06720, 2; AAQ88814, FT 3; BAB55035 and 5; AAH29267/AAH44243)" FT /evidence="ECO:0000305" FT CONFLICT 182 FT /note="S -> G (in Ref. 1; BAD06718/BAD06720, 2; AAQ88814, FT 3; BAB55035 and 5; AAH29267/AAH44243)" FT /evidence="ECO:0000305" FT CONFLICT 221 FT /note="P -> L (in Ref. 6; BAA92597)" FT /evidence="ECO:0000305" FT CONFLICT 407 FT /note="T -> A (in Ref. 3; BAB55035)" FT /evidence="ECO:0000305" FT CONFLICT 433 FT /note="T -> A (in Ref. 3; BAC11428)" FT /evidence="ECO:0000305" FT CONFLICT 444 FT /note="L -> P (in Ref. 5; AAH29267)" FT /evidence="ECO:0000305" FT CONFLICT 493 FT /note="D -> H (in Ref. 1; BAD06718/BAD06720, 2; AAQ88814, FT 3; BAC11428 and 5; AAH44243)" FT /evidence="ECO:0000305" FT CONFLICT 496 FT /note="V -> I (in Ref. 5; AAH29267)" FT /evidence="ECO:0000305" FT CONFLICT 505..506 FT /note="AT -> TI (in Ref. 5; AAH29267)" FT /evidence="ECO:0000305" FT CONFLICT 523..527 FT /note="VTVSR -> ATG (in Ref. 5; AAH29267)" FT /evidence="ECO:0000305" FT CONFLICT 592 FT /note="M -> T (in Ref. 5; AAH29267)" FT /evidence="ECO:0000305" FT CONFLICT 654 FT /note="V -> M (in Ref. 5; AAH29267)" FT /evidence="ECO:0000305" SQ SEQUENCE 709 AA; 71982 MW; DD344A6014D39172 CRC64; MGCLWGLALP LFFFCWEVGV SGSSAGPSTR RADTAMTTDD TEVPAMTLAP GHAALETQTL SAETSSRAST PAGPIPEAET RGAKRISPAR ETRSFTKTSP NFMVLIATSV ETSAASGSPE GAGMTTVQTI TGSDPREAIF DTLCTDDSSE EAKTLTMDIL TLAHTSTEAK GLSSESSASS DSPHPVITPS RASESSASSD GPHPVITPSR ASESSASSDG PHPVITPSRA SESSASSDGP HPVITPSRAS ESSASSDGPH PVITPSRASE SSASSDGPHP VITPSRASES SASSDGPHPV ITPSRASESS ASSDGPHPVI TPSRASESSA SSDGPHPVIT PSRASESSAS SDGLHPVITP SRASESSASS DGPHPVITPS RASESSASSD GPHPVITPSW SPGSDVTLLA EALVTVTNIE VINCSITEIE TTTSSIPGAS DTDLIPTEGV KASSTSDPPA LPDSTEAKPH ITEVTASAET LSTAGTTESA APDATVGTPL PTNSATEREV TAPGATTLSG ALVTVSRNPL EETSALSVET PSYVKVSGAA PVSIEAGSAV GKTTSFAGSS ASSYSPSEAA LKNFTPSETP TMDIATKGPF PTSRDPLPSV PPTTTNSSRG TNSTLAKITT SAKTTMKPPT ATPTTARTRP TTDVSAGENG GFLLLRLSVA SPEDLTDPRV AERLMQQLHR ELHAHAPHFQ VSLLRVRRG //