MUC2_HUMAN
ID MUC2_HUMAN Reviewed; 5179 AA.
AC Q02817; Q14878;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Mucin-2;
DE Short=MUC-2;
DE AltName: Full=Intestinal mucin-2;
DE Flags: Precursor;
GN Name=MUC2; Synonyms=SMUC;
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].
RC TISSUE=Intestine;
RX PubMed=8300571; DOI=10.1016/s0021-9258(17)41965-x;
RA Gum J.R. Jr., Hicks J.W., Toribara N.W., Siddiki B., Kim Y.S.;
RT "Molecular cloning of human intestinal mucin (MUC2) cDNA. Identification of
RT the amino terminus and overall sequence similarity to prepro-von Willebrand
RT factor.";
RL J. Biol. Chem. 269:2440-2446(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 626-1895 AND 4196-5179.
RC TISSUE=Colon;
RX PubMed=1400449; DOI=10.1016/s0021-9258(19)36620-7;
RA Gum J.R. Jr., Hicks J.W., Toribara N.W., Rothe E.-M., Lagace R.E.,
RA Kim Y.S.;
RT "The human MUC2 intestinal mucin has cysteine-rich subdomains located both
RT upstream and downstream of its central repetitive region.";
RL J. Biol. Chem. 267:21375-21383(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1343-1895 AND 4176-4195.
RX PubMed=1885763; DOI=10.1172/jci115360;
RA Toribara N.W., Gum J.R. Jr., Culhane P.J., Lagace R.E., Hicks J.W.,
RA Petersen G.M., Kim Y.S.;
RT "MUC-2 human small intestinal mucin gene structure. Repeated arrays and
RT polymorphism.";
RL J. Clin. Invest. 88:1005-1013(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4075-4352.
RX PubMed=2703501; DOI=10.1016/s0021-9258(18)83373-7;
RA Gum J.R. Jr., Byrd J.C., Hicks J.W., Toribara N.W., Lamport D.T.A.,
RA Kim Y.S.;
RT "Molecular cloning of human intestinal mucin cDNAs. Sequence analysis and
RT evidence for genetic polymorphism.";
RL J. Biol. Chem. 264:6480-6487(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4487-4627.
RX PubMed=1550588; DOI=10.1016/0006-291x(92)90557-2;
RA Xu G., Huan L., Khatri I., Sajjan U.S., McCool D., Wang D., Jones C.,
RA Forstner G., Forstner J.;
RT "Human intestinal mucin-like protein (MLP) is homologous with rat MLP in
RT the C-terminal region, and is encoded by a gene on chromosome 11 p 15.5.";
RL Biochem. Biophys. Res. Commun. 183:821-828(1992).
RN [6]
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 [7]
RP SUBUNIT.
RX PubMed=12374796; DOI=10.1074/jbc.m208483200;
RA Godl K., Johansson M.E.V., Lidell M.E., Moergelin M., Karlsson H.,
RA Olson F.J., Gum J.R. Jr., Kim Y.S., Hansson G.C.;
RT "The N terminus of the MUC2 mucin forms trimers that are held together
RT within a trypsin-resistant core fragment.";
RL J. Biol. Chem. 277:47248-47256(2002).
RN [8]
RP AUTOCATALYTIC CLEAVAGE.
RX PubMed=12582180; DOI=10.1074/jbc.m210069200;
RA Lidell M.E., Johansson M.E.V., Hansson G.C.;
RT "An autocatalytic cleavage in the C terminus of the human MUC2 mucin occurs
RT at the low pH of the late secretory pathway.";
RL J. Biol. Chem. 278:13944-13951(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP SUBUNIT (MICROBIAL INFECTION).
RX PubMed=18327567; DOI=10.1007/s00203-008-0358-6;
RA Linden S.K., Bierne H., Sabet C., Png C.W., Florin T.H., McGuckin M.A.,
RA Cossart P.;
RT "Listeria monocytogenes internalins bind to the human intestinal mucin
RT MUC2.";
RL Arch. Microbiol. 190:101-104(2008).
RN [11]
RP INTERACTION WITH AGR2.
RX PubMed=19359471; DOI=10.1073/pnas.0808722106;
RA Park S.-W., Zhen G., Verhaeghe C., Nakagami Y., Nguyenvu L.T.,
RA Barczak A.J., Killeen N., Erle D.J.;
RT "The protein disulfide isomerase AGR2 is essential for production of
RT intestinal mucus.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:6950-6955(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND INTERACTION WITH FCGBP.
RX PubMed=19432394; DOI=10.1021/pr9002504;
RA Johansson M.E.V., Thomsson K.A., Hansson G.C.;
RT "Proteomic analyses of the two mucus layers of the colon barrier reveal
RT that their main component, the Muc2 mucin, is strongly bound to the Fcgbp
RT protein.";
RL J. Proteome Res. 8:3549-3557(2009).
CC -!- FUNCTION: Coats the epithelia of the intestines, airways, and other
CC mucus membrane-containing organs. Thought to provide a protective,
CC lubricating barrier against particles and infectious agents at mucosal
CC surfaces. Major constituent of both the inner and outer mucus layers of
CC the colon and may play a role in excluding bacteria from the inner
CC mucus layer. {ECO:0000269|PubMed:19432394}.
CC -!- SUBUNIT: Homotrimer; disulfide-linked. Dimerizes in the endoplasmic
CC reticulum via its C-terminal region and polymerizes via its N-terminal
CC region by disulfide-linked trimerization. Interacts with FCGBP.
CC Interacts with AGR2; disulfide-linked. {ECO:0000269|PubMed:12374796,
CC ECO:0000269|PubMed:19359471, ECO:0000269|PubMed:19432394}.
CC -!- SUBUNIT: (Microbial infection) Interacts in vitro with L.monocytogenes
CC internalin proteins InlB, InlC and InlJ; for InlC binding is slightly
CC better at pH 5.5, (the pH of the intestine) than at pH 7.4.
CC {ECO:0000269|PubMed:18327567}.
CC -!- INTERACTION:
CC Q02817; O95994: AGR2; NbExp=2; IntAct=EBI-2105803, EBI-712648;
CC -!- SUBCELLULAR LOCATION: Secreted. Note=In the intestine, secreted into
CC the inner and outer mucus layers. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Colon, small intestine, colonic tumors, bronchus,
CC cervix and gall bladder.
CC -!- PTM: O-glycosylated.
CC -!- PTM: May undergo proteolytic cleavage in the outer mucus layer of the
CC colon, contributing to the expanded volume and loose nature of this
CC layer which allows for bacterial colonization in contrast to the inner
CC mucus layer which is dense and devoid of bacteria. {ECO:0000250}.
CC -!- PTM: At low pH of 6 and under, undergoes autocatalytic cleavage in
CC vitro in the N-terminal region of the fourth VWD domain. It is likely
CC that this also occurs in vivo and is triggered by the low pH of the
CC late secretory pathway.
CC -!- POLYMORPHISM: The number of repeats is highly polymorphic and varies
CC among different alleles.
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/MUC2ID41457ch11p15.html";
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DR EMBL; L21998; AAB95295.1; -; mRNA.
DR EMBL; M74027; AAA59875.1; -; Genomic_DNA.
DR EMBL; M94131; AAA59163.1; -; mRNA.
DR EMBL; M94132; AAA59164.1; -; mRNA.
DR PIR; A49963; A43932.
DR PDB; 6RBF; X-ray; 2.70 A; A/B/C/D=858-1259.
DR PDB; 6TM6; X-ray; 1.63 A; A=1301-1395.
DR PDB; 7A5O; EM; 2.95 A; A/B/C/D/E/F/G/H/I/J=21-1397.
DR PDBsum; 6RBF; -.
DR PDBsum; 6TM6; -.
DR PDBsum; 7A5O; -.
DR SMR; Q02817; -.
DR BioGRID; 110670; 3.
DR DIP; DIP-48824N; -.
DR IntAct; Q02817; 4.
DR DrugBank; DB01411; Pranlukast.
DR MEROPS; I08.951; -.
DR MEROPS; I08.954; -.
DR GlyConnect; 1519; 2 N-Linked glycans (3 sites), 27 O-Linked glycans.
DR GlyConnect; 373; 8 O-Linked glycans.
DR GlyGen; Q02817; 32 sites, 2 N-linked glycans (3 sites), 51 O-linked glycans (1 site).
DR iPTMnet; Q02817; -.
DR PhosphoSitePlus; Q02817; -.
DR SwissPalm; Q02817; -.
DR BioMuta; MUC2; -.
DR DMDM; 2506877; -.
DR CPTAC; CPTAC-1497; -.
DR EPD; Q02817; -.
DR jPOST; Q02817; -.
DR MassIVE; Q02817; -.
DR PaxDb; Q02817; -.
DR PeptideAtlas; Q02817; -.
DR PRIDE; Q02817; -.
DR ProteomicsDB; 58127; -.
DR GeneCards; MUC2; -.
DR HGNC; HGNC:7512; MUC2.
DR MIM; 158370; gene.
DR neXtProt; NX_Q02817; -.
DR PharmGKB; PA31316; -.
DR InParanoid; Q02817; -.
DR OrthoDB; 12226at2759; -.
DR PathwayCommons; Q02817; -.
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; Q02817; -.
DR SIGNOR; Q02817; -.
DR ChiTaRS; MUC2; human.
DR GeneWiki; MUC2; -.
DR Pharos; Q02817; Tdark.
DR PRO; PR:Q02817; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q02817; protein.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
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:0070702; C:inner mucus layer; ISS:UniProtKB.
DR GO; GO:0070703; C:outer mucus layer; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030277; P:maintenance of gastrointestinal epithelium; IMP:UniProtKB.
DR InterPro; IPR006207; Cys_knot_C.
DR InterPro; IPR028580; MUC2.
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 PANTHER; PTHR11339:SF261; PTHR11339:SF261; 5.
DR Pfam; PF08742; C8; 4.
DR Pfam; PF13330; Mucin2_WxxW; 2.
DR Pfam; PF01826; TIL; 1.
DR Pfam; PF00094; VWD; 4.
DR SMART; SM00832; C8; 4.
DR SMART; SM00041; CT; 1.
DR SMART; SM00214; VWC; 3.
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; Autocatalytic cleavage; Disulfide bond; Glycoprotein;
KW Phosphoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..5179
FT /note="Mucin-2"
FT /id="PRO_0000019281"
FT DOMAIN 35..207
FT /note="VWFD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 295..351
FT /note="TIL"
FT DOMAIN 389..564
FT /note="VWFD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 858..1028
FT /note="VWFD 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT REPEAT 1401..1416
FT /note="1"
FT REPEAT 1417..1432
FT /note="2"
FT REPEAT 1433..1448
FT /note="3"
FT REPEAT 1449..1464
FT /note="4"
FT REPEAT 1465..1471
FT /note="5"
FT REPEAT 1472..1478
FT /note="6"
FT REPEAT 1479..1494
FT /note="7A"
FT REPEAT 1495..1517
FT /note="7B"
FT REPEAT 1518..1533
FT /note="8A"
FT REPEAT 1534..1556
FT /note="8B"
FT REPEAT 1557..1572
FT /note="9A"
FT REPEAT 1573..1596
FT /note="9B"
FT REPEAT 1597..1612
FT /note="10A"
FT REPEAT 1613..1635
FT /note="10B"
FT REPEAT 1636..1651
FT /note="11A"
FT REPEAT 1652..1675
FT /note="11B"
FT REPEAT 1676..1683
FT /note="12"
FT REPEAT 1684..1699
FT /note="13"
FT REPEAT 1700..1715
FT /note="14"
FT REPEAT 1716..1731
FT /note="15"
FT REPEAT 1732..1747
FT /note="16"
FT DOMAIN 4479..4662
FT /note="VWFD 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 4815..4886
FT /note="VWFC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 4924..4991
FT /note="VWFC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 5075..5160
FT /note="CTCK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT REGION 1399..1773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1401..1747
FT /note="Approximate repeats"
FT REGION 1885..4320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4382..4414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4660..4685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1401..1698
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1699..1717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1718..1744
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1745..1759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1885..4271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4279..4320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4382..4413
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 4486..4487
FT /note="Cleavage; by autolysis; in vitro"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 670
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 770
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 894
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1787
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1820
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4502
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4616
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4627
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4752
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4787
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4881
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4888
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4955
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4970
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 5019
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 5038
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 5069
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 37..169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 59..206
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 391..528
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 413..563
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 435..443
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 860..992
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 882..1027
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 891..989
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 909..916
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 4481..4622
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 4503..4661
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 4527..4535
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 5075..5122
FT /evidence="ECO:0000250"
FT DISULFID 5089..5136
FT /evidence="ECO:0000250"
FT DISULFID 5098..5152
FT /evidence="ECO:0000250"
FT DISULFID 5102..5154
FT /evidence="ECO:0000250"
FT DISULFID ?..5159
FT /evidence="ECO:0000250"
FT VARIANT 58
FT /note="L -> P (in dbSNP:rs2856111)"
FT /id="VAR_056582"
FT VARIANT 116
FT /note="V -> M (in dbSNP:rs11825977)"
FT /id="VAR_056583"
FT VARIANT 832
FT /note="G -> S (in dbSNP:rs11245936)"
FT /id="VAR_056584"
FT VARIANT 1619
FT /note="S -> R (in dbSNP:rs11245947)"
FT /id="VAR_059531"
FT VARIANT 1689
FT /note="P -> L (in dbSNP:rs11245949)"
FT /id="VAR_059532"
FT VARIANT 1768
FT /note="P -> H (in dbSNP:rs34493663)"
FT /id="VAR_061487"
FT VARIANT 2154
FT /note="I -> T (in dbSNP:rs6421972)"
FT /id="VAR_059533"
FT VARIANT 2524
FT /note="T -> P (in dbSNP:rs7480563)"
FT /id="VAR_059534"
FT VARIANT 2524
FT /note="T -> S (in dbSNP:rs7480563)"
FT /id="VAR_059535"
FT VARIANT 2653
FT /note="Q -> L (in dbSNP:rs7126405)"
FT /id="VAR_059536"
FT VARIANT 2653
FT /note="Q -> P (in dbSNP:rs7126405)"
FT /id="VAR_059537"
FT CONFLICT 1351
FT /note="H -> L (in Ref. 3; AAA59875)"
FT /evidence="ECO:0000305"
FT CONFLICT 1412
FT /note="T -> S (in Ref. 3; AAA59875)"
FT /evidence="ECO:0000305"
FT CONFLICT 1449
FT /note="L -> P (in Ref. 3; AAA59875)"
FT /evidence="ECO:0000305"
FT CONFLICT 1504
FT /note="M -> T (in Ref. 3; AAA59875)"
FT /evidence="ECO:0000305"
FT CONFLICT 4076..4083
FT /note="TGTQTPTT -> NGLQAPTP (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 4087
FT /note="T -> S (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 4130..4131
FT /note="TP -> VL (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 4138
FT /note="V -> M (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 4146..4152
FT /note="GTQTPTT -> STKSTTV (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 4163
FT /note="P -> A (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 4175..4176
FT /note="TT -> MI (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 4179
FT /note="T -> S (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 4192..4194
FT /note="GTQ -> TGS (in Ref. 4)"
FT /evidence="ECO:0000305"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:7A5O"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 132..139
FT /evidence="ECO:0007829|PDB:7A5O"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 143..151
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:7A5O"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:7A5O"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:7A5O"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:7A5O"
FT HELIX 190..195
FT /evidence="ECO:0007829|PDB:7A5O"
FT HELIX 222..229
FT /evidence="ECO:0007829|PDB:7A5O"
FT HELIX 232..237
FT /evidence="ECO:0007829|PDB:7A5O"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:7A5O"
FT HELIX 244..255
FT /evidence="ECO:0007829|PDB:7A5O"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:7A5O"
FT HELIX 268..278
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 300..305
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:7A5O"
FT HELIX 317..320
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 326..330
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 339..342
FT /evidence="ECO:0007829|PDB:7A5O"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 353..357
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 369..375
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 377..384
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 389..394
FT /evidence="ECO:0007829|PDB:7A5O"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 398..401
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 404..407
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 413..425
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 427..434
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 442..451
FT /evidence="ECO:0007829|PDB:7A5O"
FT TURN 452..455
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 456..461
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 466..472
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 480..485
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 487..505
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 507..509
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 511..516
FT /evidence="ECO:0007829|PDB:7A5O"
FT HELIX 518..520
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 524..526
FT /evidence="ECO:0007829|PDB:7A5O"
FT TURN 536..539
FT /evidence="ECO:0007829|PDB:7A5O"
FT HELIX 550..553
FT /evidence="ECO:0007829|PDB:7A5O"
FT HELIX 554..556
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 557..560
FT /evidence="ECO:0007829|PDB:7A5O"
FT HELIX 573..576
FT /evidence="ECO:0007829|PDB:7A5O"
FT HELIX 580..588
FT /evidence="ECO:0007829|PDB:7A5O"
FT HELIX 589..591
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 594..596
FT /evidence="ECO:0007829|PDB:7A5O"
FT HELIX 599..601
FT /evidence="ECO:0007829|PDB:7A5O"
FT TURN 602..604
FT /evidence="ECO:0007829|PDB:7A5O"
FT TURN 607..609
FT /evidence="ECO:0007829|PDB:7A5O"
FT HELIX 610..620
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 621..623
FT /evidence="ECO:0007829|PDB:7A5O"
FT HELIX 624..635
FT /evidence="ECO:0007829|PDB:7A5O"
FT HELIX 637..640
FT /evidence="ECO:0007829|PDB:7A5O"
FT TURN 641..643
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 651..654
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 656..658
FT /evidence="ECO:0007829|PDB:7A5O"
FT HELIX 678..683
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 684..687
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 702..704
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 708..711
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 744..747
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 784..786
FT /evidence="ECO:0007829|PDB:7A5O"
FT TURN 787..789
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 810..813
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 822..824
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 827..829
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 834..837
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 840..844
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 846..849
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 858..863
FT /evidence="ECO:0007829|PDB:6RBF"
FT TURN 864..866
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 867..869
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 875..877
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 881..889
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 899..908
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 910..913
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 915..924
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 927..932
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 935..940
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 943..945
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 949..954
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 957..962
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 965..970
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 972..974
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 976..980
FT /evidence="ECO:0007829|PDB:6RBF"
FT HELIX 982..984
FT /evidence="ECO:0007829|PDB:6RBF"
FT HELIX 999..1001
FT /evidence="ECO:0007829|PDB:7A5O"
FT HELIX 1014..1020
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 1022..1024
FT /evidence="ECO:0007829|PDB:6RBF"
FT HELIX 1036..1039
FT /evidence="ECO:0007829|PDB:6RBF"
FT HELIX 1041..1043
FT /evidence="ECO:0007829|PDB:6RBF"
FT HELIX 1044..1051
FT /evidence="ECO:0007829|PDB:6RBF"
FT HELIX 1052..1055
FT /evidence="ECO:0007829|PDB:6RBF"
FT HELIX 1057..1059
FT /evidence="ECO:0007829|PDB:6RBF"
FT HELIX 1062..1065
FT /evidence="ECO:0007829|PDB:6RBF"
FT HELIX 1069..1081
FT /evidence="ECO:0007829|PDB:6RBF"
FT HELIX 1087..1105
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 1114..1117
FT /evidence="ECO:0007829|PDB:6RBF"
FT HELIX 1121..1124
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 1133..1135
FT /evidence="ECO:0007829|PDB:6RBF"
FT HELIX 1145..1149
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 1162..1164
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 1173..1175
FT /evidence="ECO:0007829|PDB:6RBF"
FT TURN 1176..1179
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 1180..1182
FT /evidence="ECO:0007829|PDB:6RBF"
FT HELIX 1184..1186
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 1189..1193
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 1205..1213
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 1219..1223
FT /evidence="ECO:0007829|PDB:6RBF"
FT STRAND 1301..1305
FT /evidence="ECO:0007829|PDB:6TM6"
FT STRAND 1316..1324
FT /evidence="ECO:0007829|PDB:6TM6"
FT TURN 1327..1329
FT /evidence="ECO:0007829|PDB:6TM6"
FT STRAND 1334..1343
FT /evidence="ECO:0007829|PDB:6TM6"
FT HELIX 1348..1351
FT /evidence="ECO:0007829|PDB:6TM6"
FT STRAND 1356..1358
FT /evidence="ECO:0007829|PDB:6TM6"
FT TURN 1359..1361
FT /evidence="ECO:0007829|PDB:6TM6"
FT STRAND 1362..1366
FT /evidence="ECO:0007829|PDB:6TM6"
FT HELIX 1367..1369
FT /evidence="ECO:0007829|PDB:6TM6"
FT TURN 1371..1373
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 1374..1376
FT /evidence="ECO:0007829|PDB:7A5O"
FT STRAND 1382..1391
FT /evidence="ECO:0007829|PDB:6TM6"
FT HELIX 1392..1394
FT /evidence="ECO:0007829|PDB:6TM6"
SQ SEQUENCE 5179 AA; 540300 MW; 85CD7571FB9A5663 CRC64;
MGLPLARLAA VCLALSLAGG SELQTEGRTR YHGRNVCSTW GNFHYKTFDG DVFRFPGLCD
YNFASDCRGS YKEFAVHLKR GPGQAEAPAG VESILLTIKD DTIYLTRHLA VLNGAVVSTP
HYSPGLLIEK SDAYTKVYSR AGLTLMWNRE DALMLELDTK FRNHTCGLCG DYNGLQSYSE
FLSDGVLFSP LEFGNMQKIN QPDVVCEDPE EEVAPASCSE HRAECERLLT AEAFADCQDL
VPLEPYLRAC QQDRCRCPGG DTCVCSTVAE FSRQCSHAGG RPGNWRTATL CPKTCPGNLV
YLESGSPCMD TCSHLEVSSL CEEHRMDGCF CPEGTVYDDI GDSGCVPVSQ CHCRLHGHLY
TPGQEITNDC EQCVCNAGRW VCKDLPCPGT CALEGGSHIT TFDGKTYTFH GDCYYVLAKG
DHNDSYALLG ELAPCGSTDK QTCLKTVVLL ADKKKNAVVF KSDGSVLLNQ LQVNLPHVTA
SFSVFRPSSY HIMVSMAIGV RLQVQLAPVM QLFVTLDQAS QGQVQGLCGN FNGLEGDDFK
TASGLVEATG AGFANTWKAQ STCHDKLDWL DDPCSLNIES ANYAEHWCSL LKKTETPFGR
CHSAVDPAEY YKRCKYDTCN CQNNEDCLCA ALSSYARACT AKGVMLWGWR EHVCNKDVGS
CPNSQVFLYN LTTCQQTCRS LSEADSHCLE GFAPVDGCGC PDHTFLDEKG RCVPLAKCSC
YHRGLYLEAG DVVVRQEERC VCRDGRLHCR QIRLIGQSCT APKIHMDCSN LTALATSKPR
ALSCQTLAAG YYHTECVSGC VCPDGLMDDG RGGCVVEKEC PCVHNNDLYS SGAKIKVDCN
TCTCKRGRWV CTQAVCHGTC SIYGSGHYIT FDGKYYDFDG HCSYVAVQDY CGQNSSLGSF
SIITENVPCG TTGVTCSKAI KIFMGRTELK LEDKHRVVIQ RDEGHHVAYT TREVGQYLVV
ESSTGIIVIW DKRTTVFIKL APSYKGTVCG LCGNFDHRSN NDFTTRDHMV VSSELDFGNS
WKEAPTCPDV STNPEPCSLN PHRRSWAEKQ CSILKSSVFS ICHSKVDPKP FYEACVHDSC
SCDTGGDCEC FCSAVASYAQ ECTKEGACVF WRTPDLCPIF CDYYNPPHEC EWHYEPCGNR
SFETCRTING IHSNISVSYL EGCYPRCPKD RPIYEEDLKK CVTADKCGCY VEDTHYPPGA
SVPTEETCKS CVCTNSSQVV CRPEEGKILN QTQDGAFCYW EICGPNGTVE KHFNICSITT
RPSTLTTFTT ITLPTTPTSF TTTTTTTTPT SSTVLSTTPK LCCLWSDWIN EDHPSSGSDD
GDREPFDGVC GAPEDIECRS VKDPHLSLEQ HGQKVQCDVS VGFICKNEDQ FGNGPFGLCY
DYKIRVNCCW PMDKCITTPS PPTTTPSPPP TTTTTLPPTT TPSPPTTTTT TPPPTTTPSP
PITTTTTPLP TTTPSPPIST TTTPPPTTTP SPPTTTPSPP TTTPSPPTTT TTTPPPTTTP
SPPMTTPITP PASTTTLPPT TTPSPPTTTT TTPPPTTTPS PPTTTPITPP TSTTTLPPTT
TPSPPPTTTT TPPPTTTPSP PTTTTPSPPT ITTTTPPPTT TPSPPTTTTT TPPPTTTPSP
PTTTPITPPT STTTLPPTTT PSPPPTTTTT PPPTTTPSPP TTTTPSPPIT TTTTPPPTTT
PSSPITTTPS PPTTTMTTPS PTTTPSSPIT TTTTPSSTTT PSPPPTTMTT PSPTTTPSPP
TTTMTTLPPT TTSSPLTTTP LPPSITPPTF SPFSTTTPTT PCVPLCNWTG WLDSGKPNFH
KPGGDTELIG DVCGPGWAAN ISCRATMYPD VPIGQLGQTV VCDVSVGLIC KNEDQKPGGV
IPMAFCLNYE INVQCCECVT QPTTMTTTTT ENPTPPTTTP ITTTTTVTPT PTPTGTQTPT
TTPITTTTTV TPTPTPTGTQ TPTTTPITTT TTVTPTPTPT GTQTPTTTPI TTTTTVTPTP
TPTGTQTPTT TPITTTTTVT PTPTPTGTQT PTTTPITTTT TVTPTPTPTG TQTPTTTPIT
TTTTVTPTPT PTGTQTPTTT PITTTTTVTP TPTPTGTQTP TTTPITTTTT VTPTPTPTGT
QTPTTTPITT TTTVTPTPTP TGTQTPTTTP ITTTTTVTPT PTPTGTQTPT TTPITTTTTV
TPTPTPTGTQ TPTTTPITTT TTVTPTPTPT GTQTPTTTPI TTTTTVTPTP TPTGTQTPTT
TPITTTTTVT PTPTPTGTQT PTTTPITTTT TVTPTPTPTG TQTPTTTPIT TTTTVTPTPT
PTGTQTPTTT PITTTTTVTP TPTPTGTQTP TTTPITTTTT VTPTPTPTGT QTPTTTPITT
TTTVTPTPTP TGTQTPTTTP ITTTTTVTPT PTPTGTQTPT TTPITTTTTV TPTPTPTGTQ
TPTTTPITTT TTVTPTPTPT GTQTPTTTPI TTTTTVTPTP TPTGTQTPTT TPITTTTTVT
PTPTPTGTQT PTTTPITTTT TVTPTPTPTG TQTPTTTPIT TTTTVTPTPT PTGTQTPTTT
PITTTTTVTP TPTPTGTQTP TTTPITTTTT VTPTPTPTGT QTPTTTPITT TTTVTPTPTP
TGTQTPTTTP ITTTTTVTPT PTPTGTQTPT TTPITTTTTV TPTPTPTGTQ TPTTTPITTT
TTVTPTPTPT GTQTPTTTPI TTTTTVTPTP TPTGTQTPTT TPITTTTTVT PTPTPTGTQT
PTTTPITTTT TVTPTPTPTG TQTPTTTPIT TTTTVTPTPT PTGTQTPTTT PITTTTTVTP
TPTPTGTQTP TTTPITTTTT VTPTPTPTGT QTPTTTPITT TTTVTPTPTP TGTQTPTTTP
ITTTTTVTPT PTPTGTQTPT TTPITTTTTV TPTPTPTGTQ TPTTTPITTT TTVTPTPTPT
GTQTPTTTPI TTTTTVTPTP TPTGTQTPTT TPITTTTTVT PTPTPTGTQT PTTTPITTTT
TVTPTPTPTG TQTPTTTPIT TTTTVTPTPT PTGTQTPTTT PITTTTTVTP TPTPTGTQTP
TTTPITTTTT VTPTPTPTGT QTPTTTPITT TTTVTPTPTP TGTQTPTTTP ITTTTTVTPT
PTPTGTQTPT TTPITTTTTV TPTPTPTGTQ TPTTTPITTT TTVTPTPTPT GTQTPTTTPI
TTTTTVTPTP TPTGTQTPTT TPITTTTTVT PTPTPTGTQT PTTTPITTTT TVTPTPTPTG
TQTPTTTPIT TTTTVTPTPT PTGTQTPTTT PITTTTTVTP TPTPTGTQTP TTTPITTTTT
VTPTPTPTGT QTPTTTPITT TTTVTPTPTP TGTQTPTTTP ITTTTTVTPT PTPTGTQTPT
TTPITTTTTV TPTPTPTGTQ TPTTTPITTT TTVTPTPTPT GTQTPTTTPI TTTTTVTPTP
TPTGTQTPTT TPITTTTTVT PTPTPTGTQT PTTTPITTTT TVTPTPTPTG TQTPTTTPIT
TTTTVTPTPT PTGTQTPTTT PITTTTTVTP TPTPTGTQTP TTTPITTTTT VTPTPTPTGT
QTPTTTPITT TTTVTPTPTP TGTQTPTTTP ITTTTTVTPT PTPTGTQTPT TTPITTTTTV
TPTPTPTGTQ TPTTTPITTT TTVTPTPTPT GTQTPTTTPI TTTTTVTPTP TPTGTQTPTT
TPITTTTTVT PTPTPTGTQT PTTTPITTTT TVTPTPTPTG TQTPTTTPIT TTTTVTPTPT
PTGTQTPTTT PITTTTTVTP TPTPTGTQTP TTTPITTTTT VTPTPTPTGT QTPTTTPITT
TTTVTPTPTP TGTQTPTTTP ITTTTTVTPT PTPTGTQTPT TTPITTTTTV TPTPTPTGTQ
TPTTTPITTT TTVTPTPTPT GTQTPTTTPI TTTTTVTPTP TPTGTQTPTT TPITTTTTVT
PTPTPTGTQT PTTTPITTTT TVTPTPTPTG TQTPTTTPIT TTTTVTPTPT PTGTQTPTTT
PITTTTTVTP TPTPTGTQTP TTTPITTTTT VTPTPTPTGT QTPTTTPITT TTTVTPTPTP
TGTQTPTTTP ITTTTTVTPT PTPTGTQTPT TTPITTTTTV TPTPTPTGTQ TPTTTPITTT
TTVTPTPTPT GTQTPTTTPI TTTTTVTPTP TPTGTQTPTT TPITTTTTVT PTPTPTGTQT
PTTTPITTTT TVTPTPTPTG TQTPTTTPIT TTTTVTPTPT PTGTQTPTTT PITTTTTVTP
TPTPTGTQTP TTTPITTTTT VTPTPTPTGT QTPTTTPITT TTTVTPTPTP TGTQTGPPTH
TSTAPIAELT TSNPPPESST PQTSRSTSSP LTESTTLLST LPPAIEMTST APPSTPTAPT
TTSGGHTLSP PPSTTTSPPG TPTRGTTTGS SSAPTPSTVQ TTTTSAWTPT PTPLSTPSII
RTTGLRPYPS SVLICCVLND TYYAPGEEVY NGTYGDTCYF VNCSLSCTLE FYNWSCPSTP
SPTPTPSKST PTPSKPSSTP SKPTPGTKPP ECPDFDPPRQ ENETWWLCDC FMATCKYNNT
VEIVKVECEP PPMPTCSNGL QPVRVEDPDG CCWHWECDCY CTGWGDPHYV TFDGLYYSYQ
GNCTYVLVEE ISPSVDNFGV YIDNYHCDPN DKVSCPRTLI VRHETQEVLI KTVHMMPMQV
QVQVNRQAVA LPYKKYGLEV YQSGINYVVD IPELGVLVSY NGLSFSVRLP YHRFGNNTKG
QCGTCTNTTS DDCILPSGEI VSNCEAAADQ WLVNDPSKPH CPHSSSTTKR PAVTVPGGGK
TTPHKDCTPS PLCQLIKDSL FAQCHALVPP QHYYDACVFD SCFMPGSSLE CASLQAYAAL
CAQQNICLDW RNHTHGACLV ECPSHREYQA CGPAEEPTCK SSSSQQNNTV LVEGCFCPEG
TMNYAPGFDV CVKTCGCVGP DNVPREFGEH FEFDCKNCVC LEGGSGIICQ PKRCSQKPVT
HCVEDGTYLA TEVNPADTCC NITVCKCNTS LCKEKPSVCP LGFEVKSKMV PGRCCPFYWC
ESKGVCVHGN AEYQPGSPVY SSKCQDCVCT DKVDNNTLLN VIACTHVPCN TSCSPGFELM
EAPGECCKKC EQTHCIIKRP DNQHVILKPG DFKSDPKNNC TFFSCVKIHN QLISSVSNIT
CPNFDASICI PGSITFMPNG CCKTCTPRNE TRVPCSTVPV TTEVSYAGCT KTVLMNHCSG
SCGTFVMYSA KAQALDHSCS CCKEEKTSQR EVVLSCPNGG SLTHTYTHIE SCQCQDTVCG
LPTGTSRRAR RSPRHLGSG
