MUC6_HUMAN
ID MUC6_HUMAN Reviewed; 2439 AA.
AC Q6W4X9; O15329; Q14394; Q2TUQ5; Q4L207; Q8N8I1; Q8NAK1;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 3.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Mucin-6;
DE Short=MUC-6;
DE AltName: Full=Gastric mucin-6;
DE Flags: Precursor;
GN Name=MUC6;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-1570.
RX PubMed=15081123; DOI=10.1016/j.ygeno.2003.11.003;
RA Rousseau K., Byrne C., Kim Y.S., Gum J.R. Jr., Swallow D.M., Toribara N.W.;
RT "The complete genomic organization of the human MUC6 and MUC2 mucin
RT genes.";
RL Genomics 83:936-939(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-119.
RA van Seuningen I.;
RT "Muc6 mucin exon1-exon3.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-116.
RA van Seuningen I., Desseyn J.-L.;
RT "Promotor characterization of the human MUC6.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1785-1998, AND VARIANT THR-1794.
RC TISSUE=Stomach;
RX PubMed=7680650; DOI=10.1016/s0021-9258(18)53402-5;
RA Toribara N.W., Roberton A.M., Ho S.B., Kuo W.-L., Gum E., Hicks J.W.,
RA Gum J.R. Jr., Byrd J.C., Siddiki B., Kim Y.S.;
RT "Human gastric mucin. Identification of a unique species by expression
RT cloning.";
RL J. Biol. Chem. 268:5879-5885(1993).
RN [6]
RP SEQUENCE REVISION TO 1954-1998.
RA Toribara N.W., Roberton A.M., Ho S.B., Kuo W.-L., Gum E., Hicks J.W.,
RA Gum J.R. Jr., Byrd J.C., Siddiki B., Kim Y.S.;
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1843-2439.
RC TISSUE=Prostate;
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 [MRNA] OF 2022-2439, AND SUBUNIT.
RX PubMed=9195947; DOI=10.1074/jbc.272.26.16398;
RA Toribara N.W., Ho S.B., Gum E., Gum J.R. Jr., Lau P., Kim Y.S.;
RT "The carboxyl-terminal sequence of the human secretory mucin, MUC6.
RT Analysis of the primary amino acid sequence.";
RL J. Biol. Chem. 272:16398-16403(1997).
RN [9]
RP TISSUE SPECIFICITY, AND POLYMORPHISM.
RX PubMed=9422745; DOI=10.1074/jbc.273.2.881;
RA Debailleul V., Laine A., Huet G., Mathon P., d'Hooghe M.C., Aubert J.-P.,
RA Porchet N.;
RT "Human mucin genes MUC2, MUC3, MUC4, MUC5AC, MUC5B, and MUC6 express stable
RT and extremely large mRNAs and exhibit a variable length polymorphism. An
RT improved method to analyze large mRNAs.";
RL J. Biol. Chem. 273:881-890(1998).
RN [10]
RP TISSUE SPECIFICITY, FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=10209489;
RX DOI=10.1002/(sici)1096-9896(199812)186:4<398::aid-path192>3.0.co;2-x;
RA Bartman A.E., Buisine M.-P., Aubert J.-P., Niehans G.A., Toribara N.W.,
RA Kim Y.S., Kelly E.J., Crabtree J.E., Ho S.B.;
RT "The MUC6 secretory mucin gene is expressed in a wide variety of epithelial
RT tissues.";
RL J. Pathol. 186:398-405(1998).
RN [11]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10330458; DOI=10.1177/002215549904700611;
RA Reid C.J., Harris A.;
RT "Expression of the MUC 6 mucin gene in development of the human kidney and
RT male genital ducts.";
RL J. Histochem. Cytochem. 47:817-822(1999).
RN [12]
RP FUNCTION, TISSUE SPECIFICITY, AND GLYCOSYLATION.
RX PubMed=11988092; DOI=10.1042/bj3640191;
RA Nordman H., Davies J.R., Lindell G., de Bolos C., Real F., Carlstedt I.;
RT "Gastric MUC5AC and MUC6 are large oligomeric mucins that differ in size,
RT glycosylation and tissue distribution.";
RL Biochem. J. 364:191-200(2002).
RN [13]
RP TISSUE SPECIFICITY.
RX PubMed=15280409; DOI=10.1136/jcp.2003.015487;
RA Xia H.H.-X., Yang Y., Lam S.K., Wong W.M., Leung S.Y., Yuen S.T., Elia G.,
RA Wright N.A., Wong B.C.-Y.;
RT "Aberrant epithelial expression of trefoil family factor 2 and mucin 6 in
RT Helicobacter pylori infected gastric antrum, incisura, and body and its
RT association with antralisation.";
RL J. Clin. Pathol. 57:861-866(2004).
RN [14]
RP INDUCTION.
RX PubMed=15979574; DOI=10.1016/j.bbrc.2005.06.037;
RA Sakai H., Jinawath A., Yamaoka S., Yuasa Y.;
RT "Upregulation of MUC6 mucin gene expression by NFkappaB and Sp factors.";
RL Biochem. Biophys. Res. Commun. 333:1254-1260(2005).
CC -!- FUNCTION: May provide a mechanism for modulation of the composition of
CC the protective mucus layer related to acid secretion or the presence of
CC bacteria and noxious agents in the lumen. Plays an important role in
CC the cytoprotection of epithelial surfaces and are used as tumor markers
CC in a variety of cancers. May play a role in epithelial organogenesis.
CC {ECO:0000269|PubMed:10209489, ECO:0000269|PubMed:10330458,
CC ECO:0000269|PubMed:11988092}.
CC -!- SUBUNIT: Multimer; disulfide-linked. {ECO:0000269|PubMed:9195947}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed in the regenerative zone of gastric
CC antrum, gastric body mucosa and gastric incisura mucosa. Expressed in
CC the deeper mucous glands of gastric antrum. Overexpressed in
CC Helicobacter pylori infected gastric epithelium. Highly expressed in
CC duodenal Brunner's glands, gall bladder, seminal vesicle, pancreatic
CC centroacinar cells and ducts, and periductal glands of the common bile
CC duct. {ECO:0000269|PubMed:10209489, ECO:0000269|PubMed:10330458,
CC ECO:0000269|PubMed:11988092, ECO:0000269|PubMed:15280409,
CC ECO:0000269|PubMed:9422745}.
CC -!- DEVELOPMENTAL STAGE: Early expressed in fetal development and was
CC observed in Brunner's glands and pancreatic ducts at 18-19 weeks and in
CC gastric glands at 20 weeks of gestation. Expressed transiently in the
CC nephrogenic zone of the kidney in the early mid-trimester of
CC development. Detected in the epithelium of ureteric buds at 13 weeks
CC and at lower levels from 17 to 23 weeks of gestation.
CC {ECO:0000269|PubMed:10209489, ECO:0000269|PubMed:10330458}.
CC -!- INDUCTION: Up-regulated by NFKB1. Repressed by mithramycin A which is
CC an inhibitor of binding of transcription factors.
CC {ECO:0000269|PubMed:15979574}.
CC -!- PTM: O-glycosylated. {ECO:0000269|PubMed:11988092}.
CC -!- POLYMORPHISM: The number of repeats is highly polymorphic and varies
CC among different alleles. These repeats are very similar but not
CC identical.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK092533; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC04860.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Mucin database;
CC URL="http://www.medkem.gu.se/mucinbiology/databases/";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/MUC6ID44115ch11p15.html";
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DR EMBL; AC139749; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY312160; AAQ82434.1; -; mRNA.
DR EMBL; AY458429; AAS13634.1; -; mRNA.
DR EMBL; AY500284; AAS76674.1; -; Genomic_DNA.
DR EMBL; L07517; AAA35866.2; -; mRNA.
DR EMBL; AK092533; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK096772; BAC04860.1; ALT_INIT; mRNA.
DR EMBL; U97698; AAC51370.1; -; mRNA.
DR CCDS; CCDS44513.1; -.
DR PIR; A46629; A46629.
DR RefSeq; NP_005952.2; NM_005961.2.
DR AlphaFoldDB; Q6W4X9; -.
DR SMR; Q6W4X9; -.
DR BioGRID; 110675; 3.
DR STRING; 9606.ENSP00000406861; -.
DR MEROPS; I08.952; -.
DR MEROPS; I08.955; -.
DR GlyConnect; 1521; 5 N-Linked glycans (3 sites).
DR GlyGen; Q6W4X9; 8 sites, 7 N-linked glycans (6 sites).
DR iPTMnet; Q6W4X9; -.
DR PhosphoSitePlus; Q6W4X9; -.
DR BioMuta; MUC6; -.
DR DMDM; 332278200; -.
DR jPOST; Q6W4X9; -.
DR MassIVE; Q6W4X9; -.
DR PaxDb; Q6W4X9; -.
DR PeptideAtlas; Q6W4X9; -.
DR PRIDE; Q6W4X9; -.
DR ProteomicsDB; 67744; -.
DR Antibodypedia; 22789; 358 antibodies from 23 providers.
DR DNASU; 4588; -.
DR Ensembl; ENST00000421673.7; ENSP00000406861.2; ENSG00000184956.16.
DR Ensembl; ENST00000636545.2; ENSP00000490759.1; ENSG00000283350.2.
DR GeneID; 4588; -.
DR KEGG; hsa:4588; -.
DR MANE-Select; ENST00000421673.7; ENSP00000406861.2; NM_005961.3; NP_005952.2.
DR UCSC; uc001lsw.3; human.
DR CTD; 4588; -.
DR DisGeNET; 4588; -.
DR GeneCards; MUC6; -.
DR HGNC; HGNC:7517; MUC6.
DR HPA; ENSG00000184956; Group enriched (pancreas, stomach).
DR MIM; 158374; gene.
DR neXtProt; NX_Q6W4X9; -.
DR OpenTargets; ENSG00000184956; -.
DR VEuPathDB; HostDB:ENSG00000184956; -.
DR eggNOG; KOG1216; Eukaryota.
DR GeneTree; ENSGT00940000161708; -.
DR HOGENOM; CLU_000076_1_0_1; -.
DR InParanoid; Q6W4X9; -.
DR OMA; PHSTARH; -.
DR OrthoDB; 12226at2759; -.
DR PhylomeDB; Q6W4X9; -.
DR TreeFam; TF300299; -.
DR PathwayCommons; Q6W4X9; -.
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-913709; O-linked glycosylation of mucins.
DR Reactome; R-HSA-977068; Termination of O-glycan biosynthesis.
DR SignaLink; Q6W4X9; -.
DR BioGRID-ORCS; 4588; 17 hits in 1060 CRISPR screens.
DR GeneWiki; MUC6; -.
DR GenomeRNAi; 4588; -.
DR Pharos; Q6W4X9; Tbio.
DR PRO; PR:Q6W4X9; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q6W4X9; protein.
DR Bgee; ENSG00000184956; Expressed in body of pancreas and 92 other tissues.
DR ExpressionAtlas; Q6W4X9; baseline and differential.
DR Genevisible; Q6W4X9; HS.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005201; F:extracellular matrix structural constituent; NAS:UniProtKB.
DR GO; GO:0030277; P:maintenance of gastrointestinal epithelium; NAS:UniProtKB.
DR InterPro; IPR006207; Cys_knot_C.
DR InterPro; IPR030124; MUC6.
DR InterPro; IPR036084; Ser_inhib-like_sf.
DR InterPro; IPR002919; TIL_dom.
DR InterPro; IPR014853; Unchr_dom_Cys-rich.
DR InterPro; IPR001007; VWF_dom.
DR InterPro; IPR001846; VWF_type-D.
DR PANTHER; PTHR11339:SF264; PTHR11339:SF264; 5.
DR Pfam; PF08742; C8; 3.
DR Pfam; PF01826; TIL; 2.
DR Pfam; PF00094; VWD; 3.
DR SMART; SM00832; C8; 3.
DR SMART; SM00041; CT; 1.
DR SMART; SM00215; VWC_out; 2.
DR SMART; SM00216; VWD; 3.
DR SUPFAM; SSF57567; SSF57567; 3.
DR PROSITE; PS01225; CTCK_2; 1.
DR PROSITE; PS51233; VWFD; 3.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..2439
FT /note="Mucin-6"
FT /id="PRO_0000259496"
FT DOMAIN 43..214
FT /note="VWFD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 302..357
FT /note="TIL"
FT DOMAIN 395..579
FT /note="VWFD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 866..1038
FT /note="VWFD 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT REPEAT 1561..1738
FT /note="1; truncated"
FT REPEAT 1785..1953
FT /note="2"
FT DOMAIN 2349..2438
FT /note="CTCK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT REGION 1202..1455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1471..1626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1607..1953
FT /note="Approximate repeats"
FT REGION 1642..1834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1868..1983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2033..2077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2090..2196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2233..2278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2323..2348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1212..1367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1380..1455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1471..1570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1579..1626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 486
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 659
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 975
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 45..176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 67..213
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 397..533
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 419..578
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 868..1002
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 890..1037
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 899..999
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 917..924
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 2349..2396
FT /evidence="ECO:0000250"
FT DISULFID 2363..2410
FT /evidence="ECO:0000250"
FT DISULFID 2372..2430
FT /evidence="ECO:0000250"
FT DISULFID 2376..2432
FT /evidence="ECO:0000250"
FT DISULFID ?..2437
FT /evidence="ECO:0000250"
FT VARIANT 1578
FT /note="P -> S (in dbSNP:rs10736904)"
FT /id="VAR_059542"
FT VARIANT 1794
FT /note="P -> T (in dbSNP:rs35549382)"
FT /evidence="ECO:0000269|PubMed:7680650"
FT /id="VAR_061488"
FT CONFLICT 81
FT /note="T -> S (in Ref. 2; AAQ82434)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="I -> G (in Ref. 2; AAQ82434)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="C -> Y (in Ref. 2; AAQ82434)"
FT /evidence="ECO:0000305"
FT CONFLICT 289..291
FT /note="RRW -> AL (in Ref. 2; AAQ82434)"
FT /evidence="ECO:0000305"
FT CONFLICT 322..323
FT /note="PQ -> SE (in Ref. 2; AAQ82434)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="V -> D (in Ref. 2; AAQ82434)"
FT /evidence="ECO:0000305"
FT CONFLICT 569
FT /note="A -> D (in Ref. 2; AAQ82434)"
FT /evidence="ECO:0000305"
FT CONFLICT 614
FT /note="F -> I (in Ref. 2; AAQ82434)"
FT /evidence="ECO:0000305"
FT CONFLICT 619
FT /note="V -> M (in Ref. 2; AAQ82434)"
FT /evidence="ECO:0000305"
FT CONFLICT 757
FT /note="P -> L (in Ref. 2; AAQ82434)"
FT /evidence="ECO:0000305"
FT CONFLICT 818
FT /note="D -> Y (in Ref. 2; AAQ82434)"
FT /evidence="ECO:0000305"
FT CONFLICT 903
FT /note="D -> Y (in Ref. 2; AAQ82434)"
FT /evidence="ECO:0000305"
FT CONFLICT 1472
FT /note="T -> S (in Ref. 2; AAQ82434)"
FT /evidence="ECO:0000305"
FT CONFLICT 1544
FT /note="T -> S (in Ref. 2; AAQ82434)"
FT /evidence="ECO:0000305"
FT CONFLICT 1558
FT /note="V -> M (in Ref. 2; AAQ82434)"
FT /evidence="ECO:0000305"
FT CONFLICT 1806..1807
FT /note="TT -> SS (in Ref. 5; AAA35866)"
FT /evidence="ECO:0000305"
FT CONFLICT 1815
FT /note="V -> M (in Ref. 5; AAA35866)"
FT /evidence="ECO:0000305"
FT CONFLICT 1833
FT /note="H -> E (in Ref. 5; AAA35866)"
FT /evidence="ECO:0000305"
FT CONFLICT 1842
FT /note="S -> P (in Ref. 5; AAA35866)"
FT /evidence="ECO:0000305"
FT CONFLICT 1857
FT /note="I -> T (in Ref. 5; AAA35866)"
FT /evidence="ECO:0000305"
FT CONFLICT 1861
FT /note="T -> A (in Ref. 5; AAA35866)"
FT /evidence="ECO:0000305"
FT CONFLICT 1872
FT /note="M -> T (in Ref. 5; AAA35866)"
FT /evidence="ECO:0000305"
FT CONFLICT 1880..1885
FT /note="PTTIKA -> LTTLMN (in Ref. 5; AAA35866)"
FT /evidence="ECO:0000305"
FT CONFLICT 1895
FT /note="M -> V (in Ref. 5; AAA35866)"
FT /evidence="ECO:0000305"
FT CONFLICT 1905..1906
FT /note="SP -> AA (in Ref. 5; AAA35866)"
FT /evidence="ECO:0000305"
FT CONFLICT 1919..1920
FT /note="PY -> HS (in Ref. 5; AAA35866)"
FT /evidence="ECO:0000305"
FT CONFLICT 1934
FT /note="S -> A (in Ref. 5; AAA35866)"
FT /evidence="ECO:0000305"
FT CONFLICT 1937..1951
FT /note="NITPKHTSTGTRTPV -> KITTNPTSIGSSTPM (in Ref. 5;
FT AAA35866)"
FT /evidence="ECO:0000305"
FT CONFLICT 1940
FT /note="P -> F (in Ref. 6; BAC04860)"
FT /evidence="ECO:0000305"
FT CONFLICT 1958
FT /note="S -> T (in Ref. 5; AAA35866)"
FT /evidence="ECO:0000305"
FT CONFLICT 1963
FT /note="P -> T (in Ref. 5; AAA35866)"
FT /evidence="ECO:0000305"
FT CONFLICT 1972
FT /note="P -> S (in Ref. 5; AAA35866)"
FT /evidence="ECO:0000305"
FT CONFLICT 2091
FT /note="S -> SSWS (in Ref. 8; AAC51370)"
FT /evidence="ECO:0000305"
FT CONFLICT 2129
FT /note="S -> F (in Ref. 6; BAC04860)"
FT /evidence="ECO:0000305"
FT CONFLICT 2190..2192
FT /note="ASV -> GSG (in Ref. 8; AAC51370)"
FT /evidence="ECO:0000305"
FT CONFLICT 2272
FT /note="R -> G (in Ref. 8; AAC51370)"
FT /evidence="ECO:0000305"
FT CONFLICT 2318
FT /note="F -> S (in Ref. 8; AAC51370)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2439 AA; 257051 MW; 4A1A7E6A7C30F895 CRC64;
MVQRWLLLSC CGALLSAGLA NTSYTSPGLQ RLKDSPQTAP DKGQCSTWGA GHFSTFDHHV
YDFSGTCNYI FAATCKDAFP TFSVQLRRGP DGSISRIIVE LGASVVTVSE AIISVKDIGV
ISLPYTSNGL QITPFGQSVR LVAKQLELEL EVVWGPDSHL MVLVERKYMG QMCGLCGNFD
GKVTNEFVSE EGKFLEPHKF AALQKLDDPG EICTFQDIPS THVRQAQHAR ICTQLLTLVA
PECSVSKEPF VLSCQADVAA APQPGPQNSS CATLSEYSRQ CSMVGQPVRR WRSPGLCSVG
QCPANQVYQE CGSACVKTCS NPQHSCSSSC TFGCFCPEGT VLNDLSNNHT CVPVTQCPCV
LHGAMYAPGE VTIAACQTCR CTLGRWVCTE RPCPGHCSLE GGSFVTTFDA RPYRFHGTCT
YILLQSPQLP EDGALMAVYD KSGVSHSETS LVAVVYLSRQ DKIVISQDEV VTNNGEAKWL
PYKTRNITVF RQTSTHLQMA TSFGLELVVQ LRPIFQAYVT VGPQFRGQTR GLCGNFNGDT
TDDFTTSMGI AEGTASLFVD SWRAGNCPAA LERETDPCSM SQLNKVCAET HCSMLLRTGT
VFERCHATVN PAPFYKRCVY QACNYEETFP HICAALGDYV HACSLRGVLL WGWRSSVDNC
TIPCTGNTTF SYNSQACERT CLSLSDRATE CHHSAVPVDG CNCPDGTYLN QKGECVRKAQ
CPCILEGYKF ILAEQSTVIN GITCHCINGR LSCPQRPQMF LASCQAPKTF KSCSQSSENK
FGAACAPTCQ MLATGVACVP TKCEPGCVCA EGLYENADGQ CVPPEECPCE FSGVSYPGGA
ELHTDCRTCS CSRGRWACQQ GTHCPSTCTL YGEGHVITFD GQRFVFDGNC EYILATDVCG
VNDSQPTFKI LTENVICGNS GVTCSRAIKI FLGGLSVVLA DRNYTVTGEE PHVQLGVTPG
ALSLVVDISI PGRYNLTLIW NRHMTILIRI ARASQDPLCG LCGNFNGNMK DDFETRSRYV
ASSELELVNS WKESPLCGDV SFVTDPCSLN AFRRSWAERK CSVINSQTFA TCHSKVYHLP
YYEACVRDAC GCDSGGDCEC LCDAVAAYAQ ACLDKGVCVD WRTPAFCPIY CGFYNTHTQD
GHGEYQYTQE ANCTWHYQPC LCPSQPQSVP GSNIEGCYNC SQDEYFDHEE GVCVPCMPPT
TPQPPTTPQL PTTGSRPTQV WPMTGTSTTI GLLSSTGPSP SSNHTPASPT QTPLLPATLT
SSKPTASSGE PPRPTTAVTP QATSGLPPTA TLRSTATKPT VTQATTRATA STASPATTST
AQSTTRTTMT LPTPATSGTS PTLPKSTNQE LPGTTATQTT GPRPTPASTT GPTTPQPGQP
TRPTATETTQ TRTTTEYTTP QTPHTTHSPP TAGSPVPSTG PVTATSFHAT TTYPTPSHPE
TTLPTHVPPF STSLVTPSTH TVITPTHAQM ATSASNHSAP TGTIPPPTTL KATGSTHTAP
PITPTTSGTS QAHSSFSTNK TPTSLHSHTS STHHPEVTPT STTTITPNPT STRTRTPVAH
TNSATSSRPP PPFTTHSPPT GSSPFSSTGP MTATSFKTTT TYPTPSHPQT TLPTHVPPFS
TSLVTPSTHT VITPTHAQMA TSASIHSMPT GTIPPPTTLK ATGSTHTAPT MTLTTSGTSQ
ALSSLNTAKT STSLHSHTSS THHAEATSTS TTNITPNPTS TGTPPMTVTT SGTSQSRSSF
STAKTSTSLH SHTSSTHHPE VTSTSTTSIT PNHTSTGTRT PVAHTTSATS SRLPTPFTTH
SPPTGTTPIS STGPVTATSF QTTTTYPTPS HPHTTLPTHV PSFSTSLVTP STHTVIIPTH
TQMATSASIH SMPTGTIPPP TTIKATGSTH TAPPMTPTTS GTSQSPSSFS TAKTSTSLPY
HTSSTHHPEV TPTSTTNITP KHTSTGTRTP VAHTTSASSS RLPTPFTTHS PPTGSSPFSS
TGPMTATSFQ TTTTYPTPSH PQTTLPTHVP PFSTSLVTPS THTVIITTHT QMATSASIHS
TPTGTVPPPT TLKATGSTHT APPMTVTTSG TSQTHSSFST ATASSSFISS SSWLPQNSSS
RPPSSPITTQ LPHLSSATTP VSTTNQLSSS FSPSPSAPST VSSYVPSSHS SPQTSSPSVG
TSSSFVSAPV HSTTLSSGSH SSLSTHPTTA SVSASPLFPS SPAASTTIRA TLPHTISSPF
TLSALLPIST VTVSPTPSSH LASSTIAFPS TPRTTASTHT APAFSSQSTT SRSTSLTTRV
PTSGFVSLTS GVTGIPTSPV TNLTTRHPGP TLSPTTRFLT SSLTAHGSTP ASAPVSSLGT
PTPTSPGVCS VREQQEEITF KGCMANVTVT RCEGACISAA SFNIITQQVD ARCSCCRPLH
SYEQQLELPC PDPSTPGRRL VLTLQVFSHC VCSSVACGD
