MUC5A_HUMAN
ID MUC5A_HUMAN Reviewed; 5654 AA.
AC P98088; A0A096LPK4; O60460; O76065; Q13792; Q14425; Q658Q1; Q7M4S5; Q8N4M9;
AC Q8WWQ3; Q8WWQ4; Q8WWQ5;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 4.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Mucin-5AC {ECO:0000305};
DE Short=MUC-5AC {ECO:0000305};
DE AltName: Full=Gastric mucin {ECO:0000303|PubMed:8948439};
DE AltName: Full=Major airway glycoprotein {ECO:0000303|PubMed:7513696};
DE AltName: Full=Mucin-5 subtype AC, tracheobronchial;
DE AltName: Full=Tracheobronchial mucin {ECO:0000303|PubMed:2656675};
DE Short=TBM {ECO:0000303|PubMed:7513696};
DE Flags: Precursor;
GN Name=MUC5AC {ECO:0000303|PubMed:11535137, ECO:0000312|HGNC:HGNC:7515};
GN Synonyms=MUC5 {ECO:0000303|PubMed:7513696};
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 1-4589, NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF
RP 3025-4373, AND NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3081-4793.
RX PubMed=11535137; DOI=10.1042/0264-6021:3580763;
RA Escande F., Aubert J.-P., Porchet N., Buisine M.P.;
RT "Human mucin gene MUC5AC: organization of its 5'-region and central
RT repetitive region.";
RL Biochem. J. 358:763-772(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-1104.
RC TISSUE=Trachea;
RX PubMed=9506983; DOI=10.1074/jbc.273.12.6812;
RA Li D., Gallup M., Fan N., Szymkowski D.E., Basbaum C.B.;
RT "Cloning of the amino-terminal and 5'-flanking region of the human MUC5AC
RT mucin gene and transcriptional up-regulation by bacterial exoproducts.";
RL J. Biol. Chem. 273:6812-6820(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1005-1854.
RX PubMed=8948439; DOI=10.1042/bj3080831;
RA Klomp L.W., Van Rens L., Strous G.J.;
RT "Cloning and analysis of human gastric mucin cDNA reveals two types of
RT conserved cysteine-rich domains.";
RL Biochem. J. 308:831-838(1995).
RN [5]
RP PROTEIN SEQUENCE OF 1752-1773; 1796-1805; 2125-2146; 2169-2178; 3231-3252;
RP 3273-3284; 3529-3550; 3573-3582; 3962-3983; 4004-4015 AND 4636-4657.
RC TISSUE=Tracheobronchial mucosa;
RX PubMed=2656675; DOI=10.1016/s0021-9258(18)83168-4;
RA Rose M.C., Kaufman B., Martin B.M.;
RT "Proteolytic fragmentation and peptide mapping of human
RT carboxyamidomethylated tracheobronchial mucin.";
RL J. Biol. Chem. 264:8193-8199(1989).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 4574-5654.
RC TISSUE=Placenta, and Trachea;
RX PubMed=9620876; DOI=10.1042/bj3320729;
RA Buisine M.P., Desseyn J.-L., Porchet N., Degand P., Laine A., Aubert J.-P.;
RT "Genomic organization of the 3'-region of the human MUC5AC mucin gene:
RT additional evidence for a common ancestral gene for the 11p15.5 mucin gene
RT family.";
RL Biochem. J. 332:729-738(1998).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4614-5654, PARTIAL PROTEIN SEQUENCE, TISSUE
RP SPECIFICITY, AND VARIANT LEU-5521.
RC TISSUE=Nasal polyp;
RX PubMed=7513696; DOI=10.1016/s0021-9258(18)99965-5;
RA Meerzaman D., Charles P., Daskal E., Polymeropoulos M.H., Martin B.M.,
RA Rose M.C.;
RT "Cloning and analysis of cDNA encoding a major airway glycoprotein, human
RT tracheobronchial mucin (MUC5).";
RL J. Biol. Chem. 269:12932-12939(1994).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4705-5654, AND VARIANT LEU-5521.
RX PubMed=7775418; DOI=10.1074/jbc.270.23.13665;
RA Lesuffleur T., Roche F., Hill A.S., Lacasa M., Fox M., Swallow D.M.,
RA Zweibaum A., Real F.X.;
RT "Characterization of a mucin cDNA clone isolated from HT-29 mucus secreting
RT cells: the 3' end of MUC5AC?";
RL J. Biol. Chem. 270:13665-13673(1995).
RN [9]
RP PROTEIN SEQUENCE OF 4927-4936, PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF
RP ASP-4926.
RX PubMed=16787389; DOI=10.1042/bj20060443;
RA Lidell M.E., Hansson G.C.;
RT "Cleavage in the GDPH sequence of the C-terminal cysteine-rich part of the
RT human MUC5AC mucin.";
RL Biochem. J. 399:121-129(2006).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5081-5654.
RC TISSUE=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 [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5193-5654, AND VARIANT LEU-5521.
RC TISSUE=Stomach;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [12]
RP STRUCTURE OF O-LINKED CARBOHYDRATES.
RX PubMed=11445551; DOI=10.1093/glycob/11.6.459;
RA Silverman H.S., Parry S., Sutton-Smith M., Burdick M.D., McDermott K.,
RA Reid C.J., Batra S.K., Morris H.R., Hollingsworth M.A., Dell A., Harris A.;
RT "In vivo glycosylation of mucin tandem repeats.";
RL Glycobiology 11:459-471(2001).
RN [13]
RP FUNCTION, TISSUE SPECIFICITY, AND GLYCOSYLATION.
RX PubMed=14535999; DOI=10.1046/j.1523-5378.2003.00173.x;
RA Van de Bovenkamp J.H., Mahdavi J., Korteland-Van Male A.M., Bueller H.A.,
RA Einerhand A.W., Boren T., Dekker J.;
RT "The MUC5AC glycoprotein is the primary receptor for Helicobacter pylori in
RT the human stomach.";
RL Helicobacter 8:521-532(2003).
RN [14]
RP GLYCOSYLATION AT TRP-2122, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP TRP-2122.
RX PubMed=14718370; DOI=10.1093/glycob/cwh041;
RA Perez-Vilar J., Randell S.H., Boucher R.C.;
RT "C-Mannosylation of MUC5AC and MUC5B Cys subdomains.";
RL Glycobiology 14:325-337(2004).
RN [15]
RP GLYCOSYLATION.
RX PubMed=22186971; DOI=10.1093/glycob/cwr183;
RA Raman J., Guan Y., Perrine C.L., Gerken T.A., Tabak L.A.;
RT "UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-
RT acetylgalactosaminyltransferases: completion of the family tree.";
RL Glycobiology 22:768-777(2012).
RN [16]
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=31732694; DOI=10.26508/lsa.201900462;
RA Simoes F.B., Quaresma M.C., Clarke L.A., Silva I.A., Pankonien I.,
RA Railean V., Kmit A., Amaral M.D.;
RT "TMEM16A chloride channel does not drive mucus production.";
RL Life. Sci Alliance 2:0-0(2019).
RN [17] {ECO:0007744|PDB:5AJN, ECO:0007744|PDB:5AJO, ECO:0007744|PDB:5AJP}
RP X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF GLYCOPEPTIDE REPEAT IN COMPLEX
RP WITH GALNT2, AND GLYCOSYLATION AT THR-2395; THR-2405; THR-2451; THR-2461;
RP THR-2531; THR-2541; THR-2571; THR-2581; THR-2699; THR-2709; THR-2883;
RP THR-2893; THR-2979; THR-2989; THR-3067; THR-3077; THR-4224; THR-4234;
RP THR-4296; THR-4306; THR-4320; THR-4330; THR-4376; THR-4386; THR-4440;
RP THR-4450; THR-4480; THR-4490; THR-4512; THR-4522; THR-4568 AND THR-4578.
RX PubMed=25939779; DOI=10.1038/ncomms7937;
RA Lira-Navarrete E., de Las Rivas M., Companon I., Pallares M.C., Kong Y.,
RA Iglesias-Fernandez J., Bernardes G.J., Peregrina J.M., Rovira C.,
RA Bernado P., Bruscolini P., Clausen H., Lostao A., Corzana F.,
RA Hurtado-Guerrero R.;
RT "Dynamic interplay between catalytic and lectin domains of GalNAc-
RT transferases modulates protein O-glycosylation.";
RL Nat. Commun. 6:6937-6937(2015).
CC -!- FUNCTION: Gel-forming glycoprotein of gastric and respiratory tract
CC epithelia that protects the mucosa from infection and chemical damage
CC by binding to inhaled microorganisms and particles that are
CC subsequently removed by the mucociliary system (PubMed:14535999,
CC PubMed:14718370). Interacts with H.pylori in the gastric epithelium,
CC Barrett's esophagus as well as in gastric metaplasia of the duodenum
CC (GMD) (PubMed:14535999). {ECO:0000269|PubMed:14535999,
CC ECO:0000303|PubMed:14535999, ECO:0000303|PubMed:14718370}.
CC -!- SUBUNIT: Multimeric. {ECO:0000303|PubMed:14718370}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14718370,
CC ECO:0000269|PubMed:31732694}.
CC -!- TISSUE SPECIFICITY: Highly expressed in surface mucosal cells of
CC respiratory tract and stomach epithelia. Overexpressed in a number of
CC carcinomas. Also expressed in Barrett's esophagus epithelium and in the
CC proximal duodenum. {ECO:0000269|PubMed:14535999,
CC ECO:0000269|PubMed:7513696}.
CC -!- DEVELOPMENTAL STAGE: In airway epithelial cells, expression increases
CC significantly during cell differentiation (at protein level).
CC {ECO:0000269|PubMed:31732694}.
CC -!- INDUCTION: By IL4. {ECO:0000269|PubMed:31732694}.
CC -!- DOMAIN: The cysteine residues in the Cys-rich subdomain repeats are not
CC involved in disulfide bonding.
CC -!- PTM: C-, O- and N-glycosylated (PubMed:14718370). O-glycosylated on the
CC second and last Thr of the Thr-/Ser-rich tandem repeats TTPSPVPTTSTTSA
CC (PubMed:25939779, PubMed:14718370, PubMed:22186971). One form of
CC glycosylation is also known as Lewis B (LeB) blood group antigen, a
CC tetrasaccharide consisting of N-acetylglucosamine having a fucosyl
CC residue attached (PubMed:14535999). It has a role as an epitope and
CC antigen and functions as a receptor for H.pylori binding and
CC facilitates infection (PubMed:14535999). C-mannosylation in the Cys-
CC rich subdomains may be required for proper folding of these regions and
CC for export from the endoplasmic reticulum during biosynthesis
CC (PubMed:14718370). {ECO:0000269|PubMed:14535999,
CC ECO:0000269|PubMed:14718370, ECO:0000269|PubMed:25939779}.
CC -!- PTM: Proteolytic cleavage in the C-terminal is initiated early in the
CC secretory pathway and does not involve a serine protease. The extent of
CC cleavage is increased in the acidic parts of the secretory pathway.
CC Cleavage generates a reactive group which could link the protein to a
CC primary amide. {ECO:0000269|PubMed:16787389}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA18431.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA18431.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAC15950.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA88307.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAH56330.1; Type=Frameshift; 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/MUC5ACID41460ch11p15.html";
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DR EMBL; FO680660; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FP326773; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KC800812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJ298317; CAC83674.1; -; mRNA.
DR EMBL; AJ298318; CAC83675.1; -; Genomic_DNA.
DR EMBL; AJ298319; CAC83676.1; -; Genomic_DNA.
DR EMBL; AF015521; AAC15950.1; ALT_FRAME; mRNA.
DR EMBL; X81649; CAA57309.1; -; mRNA.
DR EMBL; AJ001402; CAA04737.1; -; mRNA.
DR EMBL; AJ001403; CAA04738.1; -; Genomic_DNA.
DR EMBL; U06711; AAA18431.1; ALT_SEQ; mRNA.
DR EMBL; Z48314; CAA88307.1; ALT_FRAME; mRNA.
DR EMBL; BC033831; AAH33831.1; -; mRNA.
DR EMBL; AL833060; CAH56330.1; ALT_FRAME; mRNA.
DR CCDS; CCDS76369.1; -.
DR PIR; A33811; A33811.
DR PIR; JE0095; JE0095.
DR RefSeq; NP_001291288.1; NM_001304359.1.
DR PDB; 5AJN; X-ray; 1.67 A; P=4254-4268.
DR PDB; 5AJO; X-ray; 1.48 A; B=2528-2543.
DR PDB; 5AJP; X-ray; 1.65 A; B=2528-2543.
DR PDBsum; 5AJN; -.
DR PDBsum; 5AJO; -.
DR PDBsum; 5AJP; -.
DR SMR; P98088; -.
DR IntAct; P98088; 2.
DR STRING; 9606.ENSP00000485659; -.
DR ChEMBL; CHEMBL3713020; -.
DR MEROPS; I08.951; -.
DR GlyConnect; 375; 10 O-Linked glycans.
DR GlyGen; P98088; 63 sites, 17 O-linked glycans (1 site).
DR iPTMnet; P98088; -.
DR PhosphoSitePlus; P98088; -.
DR BioMuta; MUC5AC; -.
DR DMDM; 160370004; -.
DR jPOST; P98088; -.
DR MassIVE; P98088; -.
DR PaxDb; P98088; -.
DR PeptideAtlas; P98088; -.
DR PRIDE; P98088; -.
DR ProteomicsDB; 57789; -.
DR ABCD; P98088; 1 sequenced antibody.
DR Antibodypedia; 3457; 997 antibodies from 35 providers.
DR DNASU; 4586; -.
DR Ensembl; ENST00000621226.2; ENSP00000485659.1; ENSG00000215182.8.
DR Ensembl; ENST00000636567.1; ENSP00000490794.1; ENSG00000283158.1.
DR GeneID; 4586; -.
DR KEGG; hsa:4586; -.
DR MANE-Select; ENST00000621226.2; ENSP00000485659.1; NM_001304359.2; NP_001291288.1.
DR UCSC; uc031xcx.2; human.
DR CTD; 4586; -.
DR DisGeNET; 4586; -.
DR GeneCards; MUC5AC; -.
DR HGNC; HGNC:7515; MUC5AC.
DR HPA; ENSG00000215182; Tissue enriched (stomach).
DR MIM; 158373; gene.
DR neXtProt; NX_P98088; -.
DR OpenTargets; ENSG00000215182; -.
DR VEuPathDB; HostDB:ENSG00000215182; -.
DR eggNOG; KOG1216; Eukaryota.
DR GeneTree; ENSGT00940000156076; -.
DR HOGENOM; CLU_000076_3_1_1; -.
DR InParanoid; P98088; -.
DR OMA; GEESCVW; -.
DR OrthoDB; 12226at2759; -.
DR PathwayCommons; P98088; -.
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; P98088; -.
DR BioGRID-ORCS; 4586; 4 hits in 145 CRISPR screens.
DR GenomeRNAi; 4586; -.
DR Pharos; P98088; Tbio.
DR PRO; PR:P98088; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P98088; protein.
DR Bgee; ENSG00000215182; Expressed in olfactory segment of nasal mucosa and 40 other tissues.
DR Genevisible; P98088; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR GO; GO:0070701; C:mucus layer; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005201; F:extracellular matrix structural constituent; TAS:UniProtKB.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IDA:UniProtKB.
DR InterPro; IPR006207; Cys_knot_C.
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 InterPro; IPR025155; WxxW_domain.
DR Pfam; PF08742; C8; 4.
DR Pfam; PF13330; Mucin2_WxxW; 9.
DR Pfam; PF01826; TIL; 2.
DR Pfam; PF00094; VWD; 4.
DR SMART; SM00832; C8; 4.
DR SMART; SM00041; CT; 1.
DR SMART; SM00214; VWC; 6.
DR SMART; SM00215; VWC_out; 2.
DR SMART; SM00216; VWD; 4.
DR SUPFAM; SSF57567; SSF57567; 4.
DR PROSITE; PS01185; CTCK_1; 1.
DR PROSITE; PS01225; CTCK_2; 1.
DR PROSITE; PS01208; VWFC_1; 2.
DR PROSITE; PS50184; VWFC_2; 2.
DR PROSITE; PS51233; VWFD; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..5654
FT /note="Mucin-5AC"
FT /evidence="ECO:0000255"
FT /id="PRO_0000158957"
FT DOMAIN 79..249
FT /note="VWFD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 338..394
FT /note="TIL 1"
FT /evidence="ECO:0000255"
FT DOMAIN 394..465
FT /note="VWFC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 432..607
FT /note="VWFD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 704..761
FT /note="TIL 2"
FT /evidence="ECO:0000255"
FT DOMAIN 818..863
FT /note="TIL 3"
FT /evidence="ECO:0000255"
FT DOMAIN 901..1072
FT /note="VWFD 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT REPEAT 1383..1481
FT /note="Cys-rich subdomain 1"
FT REPEAT 1577..1677
FT /note="Cys-rich subdomain 2"
FT REPEAT 1743..1847
FT /note="Cys-rich subdomain 3"
FT REPEAT 1950..2050
FT /note="Cys-rich subdomain 4"
FT REPEAT 2116..2220
FT /note="Cys-rich subdomain 5"
FT REPEAT 3222..3326
FT /note="Cys-rich subdomain 6"
FT REPEAT 3520..3660
FT /note="Cys-rich subdomain 7"
FT REPEAT 3953..4057
FT /note="Cys-rich subdomain 8"
FT REPEAT 4627..4731
FT /note="Cys-rich subdomain 9"
FT DOMAIN 4852..4918
FT /note="VWFC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 4919..5103
FT /note="VWFD 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 5276..5345
FT /note="VWFC 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 5381..5448
FT /note="VWFC 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 5532..5620
FT /note="CTCK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT REGION 27..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1336..1377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1383..4731
FT /note="9 X Cys-rich subdomain repeats"
FT REGION 1483..1575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1688..1733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1849..1948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2059..2110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2224..3214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2257..3200
FT /note="107 X 8 AA approximate tandem repeats of T-T-S-T-T-
FT S-A-P"
FT REGION 3329..3515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3363..3498
FT /note="17 X 8 AA approximate tandem repeats of T-T-S-T-T-S-
FT A-P"
FT REGION 3628..3951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3661..3931
FT /note="34 X 8 AA approximate tandem repeats of T-T-S-T-T-S-
FT A-P"
FT REGION 4060..4625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4093..4595
FT /note="58 X 8 AA approximate tandem repeats of T-T-S-T-T-S-
FT A-P"
FT REGION 4830..4849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 5622..5654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1336..1374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1483..1538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1548..1575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1849..1911
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1921..1948
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4835..4849
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 4926..4927
FT /note="Cleavage"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 524
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1389
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000305"
FT CARBOHYD 1584
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000305"
FT CARBOHYD 1749
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000305"
FT CARBOHYD 1957
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000305"
FT CARBOHYD 2122
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:14718370"
FT CARBOHYD 2395
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:25939779,
FT ECO:0007744|PDB:5AJO"
FT CARBOHYD 2405
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:25939779,
FT ECO:0007744|PDB:5AJO, ECO:0007744|PDB:5AJP"
FT CARBOHYD 2451
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:25939779,
FT ECO:0007744|PDB:5AJO"
FT CARBOHYD 2461
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:25939779,
FT ECO:0007744|PDB:5AJO, ECO:0007744|PDB:5AJP"
FT CARBOHYD 2531
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:25939779,
FT ECO:0007744|PDB:5AJO"
FT CARBOHYD 2541
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:25939779,
FT ECO:0007744|PDB:5AJO, ECO:0007744|PDB:5AJP"
FT CARBOHYD 2571
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:25939779,
FT ECO:0007744|PDB:5AJO"
FT CARBOHYD 2581
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:25939779,
FT ECO:0007744|PDB:5AJO, ECO:0007744|PDB:5AJP"
FT CARBOHYD 2699
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:25939779,
FT ECO:0007744|PDB:5AJO"
FT CARBOHYD 2709
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:25939779,
FT ECO:0007744|PDB:5AJO, ECO:0007744|PDB:5AJP"
FT CARBOHYD 2883
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:25939779,
FT ECO:0007744|PDB:5AJO"
FT CARBOHYD 2893
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:25939779,
FT ECO:0007744|PDB:5AJO, ECO:0007744|PDB:5AJP"
FT CARBOHYD 2979
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:25939779,
FT ECO:0007744|PDB:5AJO"
FT CARBOHYD 2989
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:25939779,
FT ECO:0007744|PDB:5AJO, ECO:0007744|PDB:5AJP"
FT CARBOHYD 3067
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:25939779,
FT ECO:0007744|PDB:5AJO"
FT CARBOHYD 3077
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:25939779,
FT ECO:0007744|PDB:5AJO, ECO:0007744|PDB:5AJP"
FT CARBOHYD 3228
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000305"
FT CARBOHYD 3526
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000305"
FT CARBOHYD 3774
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3959
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000305"
FT CARBOHYD 4224
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:25939779,
FT ECO:0007744|PDB:5AJO"
FT CARBOHYD 4234
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:25939779,
FT ECO:0007744|PDB:5AJO, ECO:0007744|PDB:5AJP"
FT CARBOHYD 4296
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:25939779,
FT ECO:0007744|PDB:5AJO"
FT CARBOHYD 4306
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:25939779,
FT ECO:0007744|PDB:5AJO, ECO:0007744|PDB:5AJP"
FT CARBOHYD 4320
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:25939779,
FT ECO:0007744|PDB:5AJO"
FT CARBOHYD 4330
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:25939779,
FT ECO:0007744|PDB:5AJO, ECO:0007744|PDB:5AJP"
FT CARBOHYD 4376
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:25939779,
FT ECO:0007744|PDB:5AJO"
FT CARBOHYD 4386
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:25939779,
FT ECO:0007744|PDB:5AJO, ECO:0007744|PDB:5AJP"
FT CARBOHYD 4440
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:25939779,
FT ECO:0007744|PDB:5AJO"
FT CARBOHYD 4450
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:25939779,
FT ECO:0007744|PDB:5AJO, ECO:0007744|PDB:5AJP"
FT CARBOHYD 4480
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:25939779,
FT ECO:0007744|PDB:5AJO"
FT CARBOHYD 4490
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:25939779,
FT ECO:0007744|PDB:5AJO, ECO:0007744|PDB:5AJP"
FT CARBOHYD 4512
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:25939779,
FT ECO:0007744|PDB:5AJO"
FT CARBOHYD 4522
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:25939779,
FT ECO:0007744|PDB:5AJO, ECO:0007744|PDB:5AJP"
FT CARBOHYD 4568
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:25939779,
FT ECO:0007744|PDB:5AJO"
FT CARBOHYD 4578
FT /note="O-linked (GalNAc) threonine"
FT /evidence="ECO:0000269|PubMed:25939779,
FT ECO:0007744|PDB:5AJO, ECO:0007744|PDB:5AJP"
FT CARBOHYD 4633
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000305"
FT CARBOHYD 4869
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4942
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 5057
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 5093
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 5236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 5347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 5377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 5386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 5455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 5528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 5591
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 81..211
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 103..248
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 434..571
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 456..606
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 478..486
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 903..1036
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 925..1071
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 934..1033
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 953..960
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 4921..5063
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 4943..5102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 4967..4975
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 5532..5582
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT DISULFID 5546..5596
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT DISULFID 5557..5612
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT DISULFID 5561..5614
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT VARIANT 5521
FT /note="P -> L (in dbSNP:rs1132436)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9620876"
FT /id="VAR_036832"
FT MUTAGEN 2122
FT /note="W->A: No binding to mannose-specific lectin. Loss of
FT secretion from the endoplasmic reticulum."
FT /evidence="ECO:0000269|PubMed:14718370"
FT MUTAGEN 4926
FT /note="D->A,E: Abolishes cleavage."
FT /evidence="ECO:0000269|PubMed:16787389"
FT CONFLICT 25
FT /note="G -> S (in Ref. 3; AAC15950)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="S -> R (in Ref. 3; AAC15950)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="D -> E (in Ref. 2; CAC83674 and 3; AAC15950)"
FT /evidence="ECO:0000305"
FT CONFLICT 432
FT /note="G -> D (in Ref. 2; CAC83674)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="L -> P (in Ref. 2; CAC83674)"
FT /evidence="ECO:0000305"
FT CONFLICT 658
FT /note="M -> V (in Ref. 2; CAC83674)"
FT /evidence="ECO:0000305"
FT CONFLICT 702
FT /note="T -> I (in Ref. 3; AAC15950)"
FT /evidence="ECO:0000305"
FT CONFLICT 716
FT /note="T -> A (in Ref. 3; AAC15950)"
FT /evidence="ECO:0000305"
FT CONFLICT 817..818
FT /note="GD -> RG (in Ref. 3; AAC15950)"
FT /evidence="ECO:0000305"
FT CONFLICT 869
FT /note="E -> K (in Ref. 3; AAC15950)"
FT /evidence="ECO:0000305"
FT CONFLICT 978
FT /note="G -> R (in Ref. 3; AAC15950)"
FT /evidence="ECO:0000305"
FT CONFLICT 996
FT /note="R -> Q (in Ref. 2; CAC83674)"
FT /evidence="ECO:0000305"
FT CONFLICT 1141
FT /note="A -> R (in Ref. 4; CAA57309)"
FT /evidence="ECO:0000305"
FT CONFLICT 1151..1155
FT /note="LCVSW -> TCVCL (in Ref. 4; CAA57309)"
FT /evidence="ECO:0000305"
FT CONFLICT 1154..1155
FT /note="SW -> CL (in Ref. 2; CAC83674)"
FT /evidence="ECO:0000305"
FT CONFLICT 1480
FT /note="P -> A (in Ref. 4; CAA57309)"
FT /evidence="ECO:0000305"
FT CONFLICT 1683
FT /note="L -> P (in Ref. 4; CAA57309)"
FT /evidence="ECO:0000305"
FT CONFLICT 1738
FT /note="L -> P (in Ref. 4; CAA57309)"
FT /evidence="ECO:0000305"
FT CONFLICT 1790
FT /note="L -> V (in Ref. 2; CAC83674 and 4; CAA57309)"
FT /evidence="ECO:0000305"
FT CONFLICT 1803
FT /note="E -> N (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1874
FT /note="T -> I (in Ref. 2; CAC83674)"
FT /evidence="ECO:0000305"
FT CONFLICT 2008..2009
FT /note="AD -> GR (in Ref. 2; CAC83674)"
FT /evidence="ECO:0000305"
FT CONFLICT 2176
FT /note="E -> N (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 2207
FT /note="Y -> I (in Ref. 2; CAC83674)"
FT /evidence="ECO:0000305"
FT CONFLICT 2238
FT /note="T -> I (in Ref. 2; CAC83674)"
FT /evidence="ECO:0000305"
FT CONFLICT 2289..4237
FT /note="Missing (in Ref. 2; CAC83674)"
FT /evidence="ECO:0000305"
FT CONFLICT 3047
FT /note="S -> T (in Ref. 2; CAC83675)"
FT /evidence="ECO:0000305"
FT CONFLICT 3088
FT /note="A -> S (in Ref. 2; CAC83676)"
FT /evidence="ECO:0000305"
FT CONFLICT 3095..3096
FT /note="AP -> PL (in Ref. 2; CAC83676)"
FT /evidence="ECO:0000305"
FT CONFLICT 3105
FT /note="T -> I (in Ref. 2; CAC83676)"
FT /evidence="ECO:0000305"
FT CONFLICT 3107..4287
FT /note="Missing (in Ref. 2; CAC83676)"
FT /evidence="ECO:0000305"
FT CONFLICT 3234
FT /note="I -> V (in Ref. 2; CAC83675)"
FT /evidence="ECO:0000305"
FT CONFLICT 3481
FT /note="G -> S (in Ref. 2; CAC83675)"
FT /evidence="ECO:0000305"
FT CONFLICT 3562
FT /note="E -> Q (in Ref. 2; CAC83675)"
FT /evidence="ECO:0000305"
FT CONFLICT 3580
FT /note="E -> N (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 3636..3644
FT /note="TPSGRATSP -> PLVGEPPAQ (in Ref. 2; CAC83675)"
FT /evidence="ECO:0000305"
FT CONFLICT 3817
FT /note="S -> P (in Ref. 2; CAC83675)"
FT /evidence="ECO:0000305"
FT CONFLICT 4244
FT /note="A -> V (in Ref. 2; CAC83674)"
FT /evidence="ECO:0000305"
FT CONFLICT 4250..4254
FT /note="TSGPG -> ISGPK (in Ref. 2; CAC83674)"
FT /evidence="ECO:0000305"
FT CONFLICT 4262
FT /note="S -> T (in Ref. 2; CAC83674)"
FT /evidence="ECO:0000305"
FT CONFLICT 4265
FT /note="T -> I (in Ref. 2; CAC83675)"
FT /evidence="ECO:0000305"
FT CONFLICT 4274
FT /note="T -> I (in Ref. 2; CAC83674)"
FT /evidence="ECO:0000305"
FT CONFLICT 4280..4284
FT /note="RTTSA -> STTSV (in Ref. 2; CAC83674)"
FT /evidence="ECO:0000305"
FT CONFLICT 4286..4373
FT /note="Missing (in Ref. 2; CAC83674)"
FT /evidence="ECO:0000305"
FT CONFLICT 4290
FT /note="T -> P (in Ref. 2; CAC83676)"
FT /evidence="ECO:0000305"
FT CONFLICT 4314..4473
FT /note="Missing (in Ref. 2; CAC83676)"
FT /evidence="ECO:0000305"
FT CONFLICT 4381
FT /note="P -> L (in Ref. 2; CAC83674)"
FT /evidence="ECO:0000305"
FT CONFLICT 4398..4400
FT /note="TAS -> PAG (in Ref. 2; CAC83674)"
FT /evidence="ECO:0000305"
FT CONFLICT 4407
FT /note="S -> N (in Ref. 2; CAC83674)"
FT /evidence="ECO:0000305"
FT CONFLICT 4418
FT /note="T -> I (in Ref. 2; CAC83674)"
FT /evidence="ECO:0000305"
FT CONFLICT 4421..4484
FT /note="Missing (in Ref. 2; CAC83674)"
FT /evidence="ECO:0000305"
FT CONFLICT 4489
FT /note="T -> I (in Ref. 2; CAC83674)"
FT /evidence="ECO:0000305"
FT CONFLICT 4501..4503
FT /note="STA -> PTS (in Ref. 2; CAC83674)"
FT /evidence="ECO:0000305"
FT CONFLICT 4521
FT /note="T -> I (in Ref. 2; CAC83674)"
FT /evidence="ECO:0000305"
FT CONFLICT 4533..4572
FT /note="Missing (in Ref. 2; CAC83674)"
FT /evidence="ECO:0000305"
FT CONFLICT 4588
FT /note="G -> A (in Ref. 2; CAC83674)"
FT /evidence="ECO:0000305"
FT CONFLICT 4614..4615
FT /note="VS -> HE (in Ref. 7; AAA18431)"
FT /evidence="ECO:0000305"
FT CONFLICT 4827
FT /note="P -> R (in Ref. 8; CAA88307)"
FT /evidence="ECO:0000305"
FT CONFLICT 4884
FT /note="R -> S (in Ref. 6; CAA04737/CAA04738 and 8;
FT CAA88307)"
FT /evidence="ECO:0000305"
FT CONFLICT 4886
FT /note="R -> P (in Ref. 7; AAA18431)"
FT /evidence="ECO:0000305"
FT CONFLICT 4899
FT /note="G -> A (in Ref. 7; AAA18431)"
FT /evidence="ECO:0000305"
FT CONFLICT 4946..4947
FT /note="VL -> AW (in Ref. 7; AAA18431)"
FT /evidence="ECO:0000305"
FT CONFLICT 5013
FT /note="G -> A (in Ref. 8; CAA88307)"
FT /evidence="ECO:0000305"
FT CONFLICT 5081..5084
FT /note="VVAS -> HASA (in Ref. 10; AAH33831)"
FT /evidence="ECO:0000305"
FT CONFLICT 5148
FT /note="Q -> H (in Ref. 8; CAA88307 and 7; AAA18431)"
FT /evidence="ECO:0000305"
FT CONFLICT 5209..5210
FT /note="GH -> RD (in Ref. 7; AAA18431)"
FT /evidence="ECO:0000305"
FT CONFLICT 5245
FT /note="P -> R (in Ref. 6; CAA04737/CAA04738 and 7;
FT AAA18431)"
FT /evidence="ECO:0000305"
FT CONFLICT 5264
FT /note="S -> T (in Ref. 6; CAA04737/CAA04738)"
FT /evidence="ECO:0000305"
FT CONFLICT 5356
FT /note="G -> R (in Ref. 7; AAA18431)"
FT /evidence="ECO:0000305"
FT CONFLICT 5363
FT /note="A -> R (in Ref. 7; AAA18431)"
FT /evidence="ECO:0000305"
FT CONFLICT 5433
FT /note="G -> R (in Ref. 7; AAA18431)"
FT /evidence="ECO:0000305"
FT CONFLICT 5441
FT /note="G -> A (in Ref. 7; AAA18431)"
FT /evidence="ECO:0000305"
FT CONFLICT 5546
FT /note="C -> S (in Ref. 7; AAA18431)"
FT /evidence="ECO:0000305"
FT CONFLICT 5622
FT /note="P -> A (in Ref. 7; AAA18431)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 5654 AA; 585570 MW; 13217A8257E8E2DE CRC64;
MSVGRRKLAL LWALALALAC TRHTGHAQDG SSESSYKHHP ALSPIARGPS GVPLRGATVF
PSLRTIPVVR ASNPAHNGRV CSTWGSFHYK TFDGDVFRFP GLCNYVFSEH CGAAYEDFNI
QLRRSQESAA PTLSRVLMKV DGVVIQLTKG SVLVNGHPVL LPFSQSGVLI QQSSSYTKVE
ARLGLVLMWN HDDSLLLELD TKYANKTCGL CGDFNGMPVV SELLSHNTKL TPMEFGNLQK
MDDPTDQCQD PVPEPPRNCS TGFGICEELL HGQLFSGCVA LVDVGSYLEA CRQDLCFCED
TDLLSCVCHT LAEYSRQCTH AGGLPQDWRG PDFCPQKCPN NMQYHECRSP CADTCSNQEH
SRACEDHCVA GCFCPEGTVL DDIGQTGCVP VSKCACVYNG AAYAPGATYS TDCTNCTCSG
GRWSCQEVPC PGTCSVLGGA HFSTFDGKQY TVHGDCSYVL TKPCDSSAFT VLAELRRCGL
TDSETCLKSV TLSLDGAQTV VVIKASGEVF LNQIYTQLPI SAANVTIFRP STFFIIAQTS
LGLQLNLQLV PTMQLFMQLA PKLRGQTCGL CGNFNSIQAD DFRTLSGVVE ATAAAFFNTF
KTQAACPNIR NSFEDPCSLS VENEKYAQHW CSQLTDADGP FGRCHAAVKP GTYYSNCMFD
TCNCERSEDC LCAALSSYVH ACAAKGVQLG GWRDGVCTKP MTTCPKSMTY HYHVSTCQPT
CRSLSEGDIT CSVGFIPVDG CICPKGTFLD DTGKCVQASN CPCYHRGSMI PNGESVHDSG
AICTCTHGKL SCIGGQAPAP VCAAPMVFFD CRNATPGDTG AGCQKSCHTL DMTCYSPQCV
PGCVCPDGLV ADGEGGCITA EDCPCVHNEA SYRAGQTIRV GCNTCTCDSR MWRCTDDPCL
ATCAVYGDGH YLTFDGQSYS FNGDCEYTLV QNHCGGKDST QDSFRVVTEN VPCGTTGTTC
SKAIKIFLGG FELKLSHGKV EVIGTDESQE VPYTIRQMGI YLVVDTDIGL VLLWDKKTSI
FINLSPEFKG RVCGLCGNFD DIAVNDFATR SRSVVGDVLE FGNSWKLSPS CPDALAPKDP
CTANPFRKSW AQKQCSILHG PTFAACHAHV EPARYYEACV NDACACDSGG DCECFCTAVA
AYAQACHEVG LCVSWRTPSI CPLFCDYYNP EGQCEWHYQP CGVPCLRTCR NPRGDCLRDV
RGLEGCYPKC PPEAPIFDED KMQCVATCPT PPLPPRCHVH GKSYRPGAVV PSDKNCQSCL
CTERGVECTY KAEACVCTYN GQRFHPGDVI YHTTDGTGGC ISARCGANGT IERRVYPCSP
TTPVPPTTFS FSTPPLVVSS THTPSNGPSS AHTGPPSSAW PTTAGTSPRT RLPTASASLP
PVCGEKCLWS PWMDVSRPGR GTDSGDFDTL ENLRAHGYRV CESPRSVECR AEDAPGVPLR
ALGQRVQCSP DVGLTCRNRE QASGLCYNYQ IRVQCCTPLP CSTSSSPAQT TPPTTSKTTE
TRASGSSAPS STPGTVSLST ARTTPAPGTA TSVKKTFSTP SPPPVPATST SSMSTTAPGT
SVVSSKPTPT EPSTSSCLQE LCTWTEWIDG SYPAPGINGG DFDTFQNLRD EGYTFCESPR
SVQCRAESFP NTPLADLGQD VICSHTEGLI CLNKNQLPPI CYNYEIRIQC CETVNVCRDI
TRLPKTVATT RPTPHPTGAQ TQTTFTTHMP SASTEQPTAT SRGGPTATSV TQGTHTTLVT
RNCHPRCTWT KWFDVDFPSP GPHGGDKETY NNIIRSGEKI CRRPEEITRL QCRAKSHPEV
SIEHLGQVVQ CSREEGLVCR NQDQQGPFKM CLNYEVRVLC CETPRGCHMT STPGSTSSSP
AQTTPSTTSK TTETQASGSS APSSTPGTVS LSTARTTPAP GTATSVKKTF STPSPPPVPA
TSTSSMSTTA PGTSVVSSKP TPTEPSTSSC LQELCTWTEW IDGSYPAPGI NGGDFDTFQN
LRDEGYTFCE SPRSVQCRAE SFPNTPLADL GQDVICSHTE GLICLNKNQL PPICYNYEIR
IQCCETVNVC RDITRPPKTV ATTRPTPHPT GAQTQTTFTT HMPSASTEQP TATSRGGPTA
TSVTQGTHTT PVTRNCHPRC TWTTWFDVDF PSPGPHGGDK ETYNNIIRSG EKICRRPEEI
TRLQCRAKSH PEVSIEHLGQ VVQCSREEGL VCRNQDQQGP FKMCLNYEVR VLCCETPKGC
PVTSTPVTAP STPSGRATSP TQSTSSWQKS RTTTLVTTST TSTPQTSTTY AHTTSTTSAP
TARTTSAPTT RTTSASPAST TSGPGNTPSP VPTTSTISAP TTSITSAPTT STTSAPTSST
TSGPGTTPSP VPTTSITSAP TTSTTSAPTT STTSARTSST TSATTTSRIS GPETTPSPVP
TTSTTSATTT STTSAPTTST TSAPTSSTTS SPQTSTTSAP TTSTTSGPGT TPSPVPTTST
TSAPTTRTTS APKSSTTSAA TTSTTSGPET TPRPVPTTST TSSPTTSTTS APTTSTTSAS
TTSTTSGAGT TPSPVPTTST TSAPTTSTTS APISSTTSAT TTSTTSGPGT TPSPVPTTST
TSAPTTSTTS GPGTTPSAVP TTSITSAPTT STNSAPISST TSATTTSRIS GPETTPSPVP
TASTTSASTT STTSGPGTTP SPVPTTSTIS VPTTSTTSAS TTSTTSASTT STTSGPGTTP
SPVPTTSTTS APTTSTTSAP TTSTISAPTT STTSATTTST TSAPTPRRTS APTTSTISAS
TTSTTSATTT STTSATTTST ISAPTTSTTL SPTTSTTSTT ITSTTSAPIS STTSTPQTST
TSAPTTSTTS GPGTTSSPVP TTSTTSAPTT STTSAPTTRT TSVPTSSTTS TATTSTTSGP
GTTPSPVPTT STTSAPTTRT TSAPTTSTTS APTTSTTSAP TSSTTSATTT STISVPTTST
TSVPGTTPSP VPTTSTISVP TTSTTSASTT STTSGPGTTP SPVPTTSTTS APTTSTTSAP
TTSTISAPTT STPSAPTTST TLAPTTSTTS APTTSTTSTP TSSTTSSPQT STTSASTTSI
TSGPGTTPSP VPTTSTTSAP TTSTTSAATT STISAPTTST TSAPTTSTTS ASTASKTSGL
GTTPSPIPTT STTSPPTTST TSASTASKTS GPGTTPSPVP TTSTIFAPRT STTSASTTST
TPGPGTTPSP VPTTSTASVS KTSTSHVSIS KTTHSQPVTR DCHLRCTWTK WFDIDFPSPG
PHGGDKETYN NIIRSGEKIC RRPEEITRLQ CRAESHPEVS IEHLGQVVQC SREEGLVCRN
QDQQGPFKMC LNYEVRVLCC ETPKGCPVTS TPVTAPSTPS GRATSPTQST SSWQKSRTTT
LVTTSTTSTP QTSTTSAPTT STTSAPTTST TSAPTTSTTS TPQTSISSAP TSSTTSAPTS
STISARTTSI ISAPTTSTTS SPTTSTTSAT TTSTTSAPTS STTSTPQTSK TSAATSSTTS
GSGTTPSPVT TTSTASVSKT STSHVSVSKT THSQPVTRDC HPRCTWTKWF DVDFPSPGPH
GGDKETYNNI IRSGEKICRR PEEITRLQCR AKSHPEVSIE HLGQVVQCSR EEGLVCRNQD
QQGPFKMCLN YEVRVLCCET PKGCPVTSTS VTAPSTPSGR ATSPTQSTSS WQKSRTTTLV
TSSITSTTQT STTSAPTTST TPASIPSTTS APTTSTTSAP TTSTTSAPTT STTSTPQTTT
SSAPTSSTTS APTTSTISAP TTSTISAPTT STTSAPTAST TSAPTSTSSA PTTNTTSAPT
TSTTSAPITS TISAPTTSTT STPQTSTISS PTTSTTSTPQ TSTTSSPTTS TTSAPTTSTT
SAPTTSTTST PQTSISSAPT SSTTSAPTAS TISAPTTSTT SFHTTSTTSP PTSSTSSTPQ
TSKTSAATSS TTSGSGTTPS PVPTTSTASV SKTSTSHVSV SKTTHSQPVT RDCHPRCTWT
KWFDVDFPSP GPHGGDKETY NNIIRSGEKI CRRPEEITRL QCRAESHPEV SIEHLGQVVQ
CSREEGLVCR NQDQQGPFKM CLNYEVRVLC CETPKGCPVT STPVTAPSTP SGRATSPTQS
TSSWQKSRTT TLVTTSTTST PQTSTTSAPT TSTIPASTPS TTSAPTTSTT SAPTTSTTSA
PTHRTTSGPT TSTTLAPTTS TTSAPTTSTN SAPTTSTISA STTSTISAPT TSTISSPTSS
TTSTPQTSKT SAATSSTTSG SGTTPSPVPT TSTTSASTTS TTSAPTTSTT SGPGTTPSPV
PSTSTTSAAT TSTTSAPTTR TTSAPTSSMT SGPGTTPSPV PTTSTTSAPT TSTTSGPGTT
PSPVPTTSTT SAPITSTTSG PGSTPSPVPT TSTTSAPTTS TTSASTASTT SGPGTTPSPV
PTTSTTSAPT TRTTSASTAS TTSGPGSTPS PVPTTSTTSA PTTRTTPAST ASTTSGPGTT
PSPVPTTSTT SASTTSTISL PTTSTTSAPI TSMTSGPGTT PSPVPTTSTT SAPTTSTTSA
STASTTSGPG TTPSPVPTTS TTSAPTTSTT SASTASTTSG PGTSLSPVPT TSTTSAPTTS
TTSGPGTTPS PVPTTSTTSA PTTSTTSGPG TTPSPVPTTS TTPVSKTSTS HLSVSKTTHS
QPVTSDCHPL CAWTKWFDVD FPSPGPHGGD KETYNNIIRS GEKICRRPEE ITRLQCRAES
HPEVNIEHLG QVVQCSREEG LVCRNQDQQG PFKMCLNYEV RVLCCETPRG CPVTSVTPYG
TSPTNALYPS LSTSMVSASV ASTSVASSSV ASSSVAYSTQ TCFCNVADRL YPAGSTIYRH
RDLAGHCYYA LCSQDCQVVR GVDSDCPSTT LPPAPATSPS ISTSEPVTEL GCPNAVPPRK
KGETWATPNC SEATCEGNNV ISLRPRTCPR VEKPTCANGY PAVKVADQDG CCHHYQCQCV
CSGWGDPHYI TFDGTYYTFL DNCTYVLVQQ IVPVYGHFRV LVDNYFCGAE DGLSCPRSII
LEYHQDRVVL TRKPVHGVMT NEIIFNNKVV SPGFRKNGIV VSRIGVKMYA TIPELGVQVM
FSGLIFSVEV PFSKFANNTE GQCGTCTNDR KDECRTPRGT VVASCSEMSG LWNVSIPDQP
ACHRPHPTPT TVGPTTVGST TVGPTTVGST TVGPTTPPAP CLPSPICQLI LSKVFEPCHT
VIPPLLFYEG CVFDRCHMTD LDVVCSSLEL YAALCASHDI CIDWRGRTGH MCPFTCPADK
VYQPCGPSNP SYCYGNDSAS LGALPEAGPI TEGCFCPEGM TLFSTSAQVC VPTGCPRCLG
PHGEPVKVGH TVGMDCQECT CEAATWTLTC RPKLCPLPPA CPLPGFVPVP AAPQAGQCCP
QYSCACNTSR CPAPVGCPEG ARAIPTYQEG ACCPVQNCSW TVCSINGTLY QPGAVVSSSL
CETCRCELPG GPPSDAFVVS CETQICNTHC PVGFEYQEQS GQCCGTCVQV ACVTNTSKSP
AHLFYPGETW SDAGNHCVTH QCEKHQDGLV VVTTKKACPP LSCSLDEARM SKDGCCRFCP
PPPPPYQNQS TCAVYHRSLI IQQQGCSSSE PVRLAYCRGN CGDSSSMYSL EGNTVEHRCQ
CCQELRTSLR NVTLHCTDGS SRAFSYTEVE ECGCMGRRCP APGDTQHSEE AEPEPSQEAE
SGSWERGVPV SPMH
