MUC2_MOUSE
ID MUC2_MOUSE Reviewed; 2680 AA.
AC Q80Z19; Q0P637; Q80Z17; Q8K0Q1; Q9CVG8; Q9Z2U5;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Mucin-2 {ECO:0000303|PubMed:9886986};
DE Short=MUC-2 {ECO:0000303|PubMed:9886986};
DE AltName: Full=Colonic mucin {ECO:0000303|PubMed:9886986};
DE Short=MCM {ECO:0000303|PubMed:9886986};
DE AltName: Full=Secreted gel-forming mucin {ECO:0000312|EMBL:CAD54414.1};
DE Flags: Precursor; Fragments;
GN Name=Muc2 {ECO:0000312|MGI:MGI:1339364};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAD54414.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1442 AND 1759-2680, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:CAD54414.1};
RX PubMed=14984930; DOI=10.1016/j.bbaexp.2004.01.001;
RA Escande F., Porchet N., Bernigaud A., Petitprez D., Aubert J.-P.,
RA Buisine M.-P.;
RT "The mouse secreted gel-forming mucin gene cluster.";
RL Biochim. Biophys. Acta 1676:240-250(2004).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAD01593.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-301, TISSUE SPECIFICITY, AND GLYCOSYLATION.
RC STRAIN=129 {ECO:0000312|EMBL:AAD01593.1};
RC TISSUE=Colon {ECO:0000312|EMBL:AAD01593.1};
RX PubMed=9886986; DOI=10.1152/ajpgi.1999.276.1.g115;
RA van Klinken B.J.-W., Einerhand A.W.C., Duits L.A., Makkink M.K.,
RA Tytgat K.M.A.J., Renes I.B., Verburg M., Bueller H.A., Dekker J.;
RT "Gastrointestinal expression and partial cDNA cloning of murine Muc2.";
RL Am. J. Physiol. 276:G115-G124(1999).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH30862.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1443-1758 AND 1795-2680.
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH30862.1};
RC TISSUE=Colon {ECO:0000312|EMBL:AAH30862.1};
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 [4] {ECO:0000305, ECO:0000312|EMBL:BAB25557.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2199-2680.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB25557.1};
RC TISSUE=Small intestine {ECO:0000312|EMBL:BAB25557.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=11872843; DOI=10.1126/science.1069094;
RA Velcich A., Yang W., Heyer J., Fragale A., Nicholas C., Viani S.,
RA Kucherlapati R., Lipkin M., Yang K., Augenlicht L.;
RT "Colorectal cancer in mice genetically deficient in the mucin Muc2.";
RL Science 295:1726-1729(2002).
RN [6] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=18806221; DOI=10.1073/pnas.0803124105;
RA Johansson M.E.V., Phillipson M., Petersson J., Velcich A., Holm L.,
RA Hansson G.C.;
RT "The inner of the two Muc2 mucin-dependent mucus layers in colon is devoid
RT of bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:15064-15069(2008).
RN [7] {ECO:0000305}
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH FCGBP, AND
RP SUBCELLULAR LOCATION.
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:0000250|UniProtKB:Q02817,
CC ECO:0000269|PubMed:18806221, 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 (By similarity). Interacts
CC with FCGBP. Interacts with AGR2; disulfide-linked (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18806221,
CC ECO:0000269|PubMed:19432394}. Note=In the intestine, secreted into the
CC inner and outer mucus layers.
CC -!- TISSUE SPECIFICITY: Highly expressed in goblet cells of the colon with
CC lower levels in the small intestine and no expression in the stomach
CC (at protein level). {ECO:0000269|PubMed:14984930,
CC ECO:0000269|PubMed:9886986}.
CC -!- PTM: O-glycosylated. {ECO:0000269|PubMed:9886986}.
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.
CC {ECO:0000269|PubMed:18806221}.
CC -!- PTM: May undergo autocatalytic cleavage in vivo triggered by the low pH
CC of the late secretory pathway. {ECO:0000250|UniProtKB:Q02817}.
CC -!- DISRUPTION PHENOTYPE: Aberrant intestinal crypt morphology and altered
CC cell maturation and migration. Frequent development of adenomas in the
CC small intestine which progress to invasive adenocarcinomas, as well as
CC rectal tumors. Absence of inner and outer mucus layers in the colon so
CC that bacteria are in direct contact with the colon epithelium and enter
CC into the cells and crypts in contrast to wild-type animals which are
CC devoid of bacteria in the inner mucus layer.
CC {ECO:0000269|PubMed:11872843, ECO:0000269|PubMed:18806221}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH30862.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Mucin database;
CC URL="http://www.medkem.gu.se/mucinbiology/databases/";
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DR EMBL; AJ511872; CAD54414.1; -; Genomic_DNA.
DR EMBL; AJ511873; CAD54416.1; -; Genomic_DNA.
DR EMBL; AJ511874; CAD54416.1; JOINED; Genomic_DNA.
DR EMBL; AF016695; AAD01593.1; -; mRNA.
DR EMBL; BC024540; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC030862; AAH30862.1; ALT_INIT; mRNA.
DR EMBL; BC036168; AAH36168.1; -; mRNA.
DR EMBL; AK008250; BAB25557.1; -; mRNA.
DR AlphaFoldDB; Q80Z19; -.
DR SMR; Q80Z19; -.
DR STRING; 10090.ENSMUSP00000141128; -.
DR MEROPS; I08.954; -.
DR GlyGen; Q80Z19; 3 sites.
DR SwissPalm; Q80Z19; -.
DR jPOST; Q80Z19; -.
DR MaxQB; Q80Z19; -.
DR PaxDb; Q80Z19; -.
DR PeptideAtlas; Q80Z19; -.
DR PRIDE; Q80Z19; -.
DR ProteomicsDB; 291459; -.
DR UCSC; uc029wpp.2; mouse.
DR MGI; MGI:1339364; Muc2.
DR eggNOG; KOG1216; Eukaryota.
DR InParanoid; Q80Z19; -.
DR TreeFam; TF337106; -.
DR Reactome; R-MMU-913709; O-linked glycosylation of mucins.
DR Reactome; R-MMU-977068; Termination of O-glycan biosynthesis.
DR ChiTaRS; Muc2; mouse.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q80Z19; protein.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0070702; C:inner mucus layer; IDA:UniProtKB.
DR GO; GO:0070701; C:mucus layer; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0070703; C:outer mucus layer; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0002068; P:glandular epithelial cell development; IMP:MGI.
DR GO; GO:0030277; P:maintenance of gastrointestinal epithelium; ISO:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; IMP:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:MGI.
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; 4.
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; 4.
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 Autocatalytic cleavage; Disulfide bond; Glycoprotein; Phosphoprotein;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..2680
FT /note="Mucin-2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000378062"
FT DOMAIN 32..205
FT /note="VWFD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 295..351
FT /note="TIL"
FT /evidence="ECO:0000255"
FT DOMAIN 387..562
FT /note="VWFD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 856..1025
FT /note="VWFD 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 1984..2167
FT /note="VWFD 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 2315..2386
FT /note="VWFC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 2424..2491
FT /note="VWFC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 2575..2660
FT /note="CTCK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT REGION 1394..1500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1609..1810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1868..1910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1880..1910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02817"
FT CARBOHYD 667
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1849
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34..166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 56..204
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 389..526
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 411..561
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 433..441
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 858..989
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 880..1024
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 889..986
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 906..913
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1986..2127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 2008..2166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 2032..2040
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 2575..2622
FT /evidence="ECO:0000255"
FT DISULFID 2589..2636
FT /evidence="ECO:0000255"
FT DISULFID 2598..2652
FT /evidence="ECO:0000255"
FT DISULFID 2602..2654
FT /evidence="ECO:0000255"
FT DISULFID ?..2659
FT /evidence="ECO:0000255"
FT CONFLICT 301
FT /note="E -> G (in Ref. 2; AAD01593)"
FT /evidence="ECO:0000305"
FT CONFLICT 2120
FT /note="V -> G (in Ref. 3; AAH30862/AAH36168)"
FT /evidence="ECO:0000305"
FT CONFLICT 2398
FT /note="T -> P (in Ref. 3; AAH36168)"
FT /evidence="ECO:0000305"
FT NON_CONS 1442..1443
FT /evidence="ECO:0000305"
FT NON_CONS 1758..1759
FT /evidence="ECO:0000305"
SQ SEQUENCE 2680 AA; 293436 MW; D67D8664AAB15933 CRC64;
MGLPLARLVA ACLVLALAKG SELQKEARSR NHVCSTWGDF HYKTFDGDVY RFPGLCDYNF
ASDCRDSYKE FAVHLKRGLG EAGGHSQIES ILITIKDDTI YLTHKLAVVN GAMVSTPHYS
SGLLIEKNDA YTKVYSRAGL SLMWNREDAL MVELDSRFQN HTCGLCGDFN GMQTNYEFLS
EEGIQFSAIE FGNMQKINKP EVQCEDPEAV QEPESCSEHR AECERLLTSA AFEDCQTRVP
VESYVRACMH DRCQCPKGGA CECSTLAEFS RQCSHAGGRP ENWRTASLCP KKCPNNMVYL
ESSSPCVDTC SHLEVSSLCE EHYMDGCFCP EGTVYDDITG SGCIPVSQCH CKLHGHLYMP
GQEFTNDCEQ CVCNAGRWVC KDLPCPETCA LEGGSHITTF DGKKFTFHGD CYYVLTKSEH
NDSYALLGEL ASCGSTDKQT CLKTVVLLTD DKKNVVAFKS GGSVLLNEME VTLPHVAASF
SIFQPSSYHI VVNTKFGLRL QIQLLPVMQL FVTLDQAAQG QVQGLCGNFN GLESDDFMTS
GGMVEATGAG FANTWKAQSS CHDKLDWLDD PCSLNIETNY AEHWCSLLKR SETPFARCHL
AVDPTEYYKR CKYDTCNCQN NEDCMCAALS SYARACAAKG VMLWGWRERV CNKDVHACPS
SQIFMYNLTT CQQTCRSLSE GDSHCLKGFA PVEGCGCPDH TFMDEKGRCV PLAKCSCYHH
GLYLEAGDVI LRQEERCICR NGRLQCTQVK LIGHTCQYPK ILVDCNNLTA LAVRKPRPTS
CQTLVAGYYH TECISGCVCP DGLLDDGRGG CVEEDKCPCI HNKDLYSSGE SIKLDCNNTC
TCQKGRWECT RYACHSTCSI YGSGHYITFD GKHYDFDGHC SYVAVQDYCG QNSTGSFSII
TENVPCGTTG VTCSKAIKIF IGGTELKLVD KHRVVKQLEE GHHVPYITRE VGQYLVVEAS
SGIIVIWDKK TTIFIKLDPS YKGTVCGLCG NFDDQTKNDF TTRDHMVVTS ELDFGNSWKE
ASTCPDVSHN PDPCSLNPHR RSWAEKQCSI IKSRVFKVCH SKVDPTVFYE ACVHDSCSCD
TGGDCDCFCS AVASYAQECT KAEACVFWRT PDLCPIFCDY YNPPDECEWH YEPCGNRSFE
TCRTLNGIHS NISVSYLEGC YPRCPEDRPI YDEDLKKCVT GDKCGCYIED TRYPPGGSVP
TDEICKSCTC TNTSKIECHP DEGKILNMTQ DGIFCYWEFC GPNGTVGQHF NICGSSTAIP
STTTSFTTIS TPISTTPIST TITTTTVTMT TEQVPCCFWS DWINKYHPTK ENGGDRETFT
HVCSAPEDIE CRAATDPKLS WEELGQKVQC NVSTGLICNN EDQYGIGEFE LCYDYEIRVN
CCYPMEYCTP STISPTTSTT TLSTTPPTSS PTTLPTSSPV TSSATLPTTS SITSTISPTT
SPSTATQTIS VTTSQTSSSA TPPNSSPTSS ATTSPTTSSG TSTATSPSTS PTTSSTFTTP
PSTTCIDDCK WTGWLDSGKP TYDIKSGDFE LIKGVCEPHW EVQNISCRAV MHSNIPLDQL
GQIVVCNKEV GLVCKNEDQE IGGIIPMRMC LNYEINVYCC NPICFTSTPS STTTETPTTT
STTKTSILTS TTTQTPSPSP TTTVTPTPAP TTTQIPTSTS TTTQTTTPTP ITETSTPTST
ISQTPSPAST TTVTPATTST TTETSTSTST TTQTTSPTPT VTETSTPRST TTQTPSPVPT
TTVTSTPTPT IGETTTPKRP PSTSTPTSFT VPTETTTQTR PLSTTPTTLE TTRTSSWGTF
SSTSPITSPS TVWTHTETQV TCCVLNEMFY GPGELVYNST HGGTCFYVNC SLDCHLQFFN
WSCPSTPSTP TPSTPTPTPS QTTTPSTTSS KSTPSTPQST SPKSTLSTPT KTTPYGCPDF
DPPRQVNETW WLCNCTMAIC NHDNVVEIVP LKCDPPPMPT CANGLKPVRV PDADNCCWHW
ECDCYCTGWG DPHFVTFDGL YYSYQGNCTY VLVEEITPTV DNFGVYIDNY HCDANDKVSC
PRTLIVRHET QEVQIKTVRM MPIEVEVQVN KQLVALPYKK YGLEVYESGI NIVVNISRLE
AKISYNGLSF SIRLPYKLFV NNTKGQCGTC TNNTADDCIL PSGKIISDCE IAADEWLVND
PSKPHCPHKG LTTKRPATTT PGLSLNNCTV SPVCHLIMDS LFSQCHAFVP PKHYYEACLF
DSCYVPGSNM ECASVQAYAT LCAKEGVCID WRNHTQGVCS VKCPPHKQYQ ACGPEEEPTC
QPSSSQNSTL LVEGCFCPEG TTKFAPGYDV CVKTCGCVGP DNVPREFGEH FEFDCKDCVC
REGGSGIVCQ PKKCSGGNQT TCEEDGTYLV VETNPDDKCC NITSCKCDTK RCKAERPTCL
LGFEVKTEIV PGKCCPVYSC VPKGVCVHQN AEYQPGSPVY SNKCQDCVCT NILDNSTQLN
VISCTHVPCN ISCSSGFELV DVPGECCKKC QQTHCIIEGP KQQYIILKPG EIHKNPSNKC
TFFSCMKINN QLISSVSNIT CPDFNPSDCV SGSITYMPNG CCKTCIPQNQ TRVPCSAVSV
MKEISYNGCT KNISMNYCFG SCGTFAMYSA QVQGLDHRCS CCKEEKTSVR SVTLECPDGS
ELSHTYTHIE SCLCQDTVCG LPQAQQVRTR RSSPRFLGRK
