GenomeNet

Database: UniProt
Entry: Q80Z19
LinkDB: Q80Z19
Original site: Q80Z19 
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   08-MAY-2019, entry version 111.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RP   GLYCOSYLATION.
RC   STRAIN=129 {ECO:0000312|EMBL:AAD01593.1};
RC   TISSUE=Colon {ECO:0000312|EMBL:AAD01593.1};
RX   PubMed=9886986;
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
RT   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
RT   project: 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RT   devoid 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,
RP   AND 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
RT   reveal that their main component, the Muc2 mucin, is strongly bound to
RT   the Fcgbp protein.";
RL   J. Proteome Res. 8:3549-3557(2009).
CC   -!- FUNCTION: Coats the epithelia of the intestines, airways, and
CC       other mucus membrane-containing organs. Thought to provide a
CC       protective, lubricating barrier against particles and infectious
CC       agents at mucosal surfaces. Major constituent of both the inner
CC       and outer mucus layers of the colon and may play a role in
CC       excluding bacteria from the inner mucus layer.
CC       {ECO:0000250|UniProtKB:Q02817, ECO:0000269|PubMed:18806221,
CC       ECO:0000269|PubMed:19432394}.
CC   -!- SUBUNIT: Homotrimer; disulfide-linked. Dimerizes in the
CC       endoplasmic reticulum via its C-terminal region and polymerizes
CC       via its N-terminal region by disulfide-linked trimerization (By
CC       similarity). Interacts with FCGBP. Interacts with AGR2; disulfide-
CC       linked (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18806221,
CC       ECO:0000269|PubMed:19432394}. Note=In the intestine, secreted into
CC       the inner and outer mucus layers.
CC   -!- TISSUE SPECIFICITY: Highly expressed in goblet cells of the colon
CC       with lower levels in the small intestine and no expression in the
CC       stomach (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
CC       the colon, contributing to the expanded volume and loose nature of
CC       this layer which allows for bacterial colonization in contrast to
CC       the inner 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
CC       low pH of the late secretory pathway.
CC       {ECO:0000250|UniProtKB:Q02817}.
CC   -!- DISRUPTION PHENOTYPE: Aberrant intestinal crypt morphology and
CC       altered cell maturation and migration. Frequent development of
CC       adenomas in the small intestine which progress to invasive
CC       adenocarcinomas, as well as rectal tumors. Absence of inner and
CC       outer mucus layers in the colon so that bacteria are in direct
CC       contact with the colon epithelium and enter into the cells and
CC       crypts in contrast to wild-type animals which are devoid of
CC       bacteria in the inner mucus layer. {ECO:0000269|PubMed:11872843,
CC       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/";
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   SMR; Q80Z19; -.
DR   STRING; 10090.ENSMUSP00000141128; -.
DR   MEROPS; I08.954; -.
DR   SwissPalm; Q80Z19; -.
DR   MaxQB; Q80Z19; -.
DR   PaxDb; Q80Z19; -.
DR   PeptideAtlas; Q80Z19; -.
DR   PRIDE; Q80Z19; -.
DR   UCSC; uc029wpp.2; mouse.
DR   MGI; MGI:1339364; Muc2.
DR   HOGENOM; HOG000203111; -.
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   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR   GO; GO:0070702; C:inner mucus layer; IDA:UniProtKB.
DR   GO; GO:0070703; C:outer mucus layer; IDA:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR   GO; GO:0002064; P: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; 2.
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; Complete proteome; Disulfide bond;
KW   Glycoprotein; Phosphoprotein; Reference proteome; Repeat; Secreted;
KW   Signal.
FT   SIGNAL        1     20       {ECO:0000255}.
FT   CHAIN        21   2680       Mucin-2. {ECO:0000255}.
FT                                /FTId=PRO_0000378062.
FT   DOMAIN       33    238       VWFD 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00580}.
FT   DOMAIN      295    351       TIL. {ECO:0000255}.
FT   DOMAIN      388    601       VWFD 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00580}.
FT   DOMAIN      857   1062       VWFD 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00580}.
FT   DOMAIN     1985   2197       VWFD 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00580}.
FT   DOMAIN     2315   2386       VWFC 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00220}.
FT   DOMAIN     2424   2491       VWFC 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00220}.
FT   DOMAIN     2575   2660       CTCK. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00039}.
FT   COMPBIAS   1257   1913       Thr-rich. {ECO:0000255}.
FT   MOD_RES      21     21       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q02817}.
FT   CARBOHYD    667    667       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1227   1227       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1849   1849       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     56     64       {ECO:0000255}.
FT   DISULFID   2575   2622       {ECO:0000255}.
FT   DISULFID   2589   2636       {ECO:0000255}.
FT   DISULFID   2598   2652       {ECO:0000255}.
FT   DISULFID   2602   2654       {ECO:0000255}.
FT   DISULFID      ?   2659       {ECO:0000255}.
FT   CONFLICT    301    301       E -> G (in Ref. 2; AAD01593).
FT                                {ECO:0000305}.
FT   CONFLICT   2120   2120       V -> G (in Ref. 3; AAH30862/AAH36168).
FT                                {ECO:0000305}.
FT   CONFLICT   2398   2398       T -> P (in Ref. 3; AAH36168).
FT                                {ECO:0000305}.
FT   NON_CONS   1442   1443       {ECO:0000305}.
FT   NON_CONS   1758   1759       {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
//
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