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Database: UniProt
Entry: Q8JZM8
LinkDB: Q8JZM8
Original site: Q8JZM8 
ID   MUC4_MOUSE              Reviewed;        3443 AA.
AC   Q8JZM8; Q4VAA3; Q9ERB8; Q9QXG0; Q9WV36;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   13-FEB-2019, entry version 94.
DE   RecName: Full=Mucin-4;
DE            Short=MUC-4;
DE   AltName: Full=Ascites sialoglycoprotein;
DE            Short=ASGP;
DE   AltName: Full=Pancreatic adenocarcinoma mucin;
DE   AltName: Full=Testis mucin;
DE   Contains:
DE     RecName: Full=Mucin-4 alpha chain;
DE     AltName: Full=Ascites sialoglycoprotein 1;
DE              Short=ASGP-1;
DE   Contains:
DE     RecName: Full=Mucin-4 beta chain;
DE     AltName: Full=Ascites sialoglycoprotein 2;
DE              Short=ASGP-2;
DE   Flags: Precursor;
GN   Name=Muc4;
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]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=129/SvJ;
RX   PubMed=12084055; DOI=10.1046/j.1432-1033.2002.02988.x;
RA   Desseyn J.-L., Clavereau I., Laine A.;
RT   "Cloning, chromosomal localization and characterization of the murine
RT   mucin gene orthologous to human MUC4.";
RL   Eur. J. Biochem. 269:3150-3159(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-231.
RC   STRAIN=CD-1;
RA   Bartman A.E., Shekels L.L., Anway R.E., Gipson I.K., Moccia R.,
RA   Ho S.B.;
RT   "Identification and structure of a mouse homolog to the human MUC4
RT   gene.";
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3076-3443.
RC   STRAIN=FVB/N; 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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3181-3351.
RX   PubMed=12107190; DOI=10.1074/jbc.M206395200;
RA   Lee C.G., Homer R.J., Cohn L., Link H., Jung S., Craft J.E.,
RA   Graham B.S., Johnson T.R., Elias J.A.;
RT   "Transgenic overexpression of interleukin (IL)-10 in the lung causes
RT   mucus metaplasia, tissue inflammation, and airway remodeling via IL-
RT   13-dependent and -independent pathways.";
RL   J. Biol. Chem. 277:35466-35474(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3343-3443.
RC   STRAIN=CF-1; TISSUE=Uterine horn luminal epithelium;
RA   DeSouza M.M., Carson D.D., Harris M.N., Julian J.;
RT   "Cloning and expression analysis of mouse ascites sialoglycoprotein-2
RT   (ASGP-2)/Mucin 4 (Muc4).";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May play a role in tumor progression. Ability to promote
CC       tumor growth may be mainly due to repression of apoptosis as
CC       opposed to proliferation. Has anti-adhesive properties. Seems to
CC       alter cellular behavior through both anti-adhesive effects on
CC       cell-cell and cell-extracellular matrix interactions and in its
CC       ability to act as an intramembrane ligand for ERBB2. Plays an
CC       important role in cell proliferation and differentiation of
CC       epithelial cells by inducing specific phosphorylation of ERBB2.
CC       The MUC4-ERBB2 complex causes site-specific phosphorylation of the
CC       ERBB2 'Tyr-1248'. In polarized epithelial cells segregates ERBB2
CC       and other ERBB receptors and prevents ERBB2 from acting as a
CC       coreceptor. The interaction with ERBB2 leads to enhanced
CC       expression of CDKN1B. The formation of a MUC4-ERBB2-ERBB3-NRG1
CC       complex leads to down-regulation of CDKN1B, resulting in
CC       repression of apoptosis and stimulation of proliferation (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: A heterodimeric complex, composed of a mucin-4 alpha
CC       chain and a cysteine-rich transmembrane mucin-4 beta chain. Mucin-
CC       4 beta chain interacts with ERBB2 via the EGF-like domain 1. In
CC       nonpolarized cells, associates with ERBB2 and ERBB3 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein.
CC       Secreted. Note=Secreted by proteolytic processing. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in trachea, duodenum and intestine.
CC       Lower expression in stomach, salivary glands, liver, gallbladder,
CC       and kidney. {ECO:0000269|PubMed:12084055}.
CC   -!- PTM: Proteolytically cleaved into 2 chains, mucin-4 alpha chain
CC       and mucin-4 beta chain. {ECO:0000250}.
CC   -!- PTM: Mucin-4 alpha chain is highly O-glycosylated.
CC   -!- PTM: Mucin-4 beta chain is predominantly N-glycosylated.
CC       {ECO:0000250}.
DR   EMBL; AF441786; AAM66254.1; -; mRNA.
DR   EMBL; AF520422; AAM66746.1; -; Genomic_DNA.
DR   EMBL; AF520421; AAM66746.1; JOINED; Genomic_DNA.
DR   EMBL; AY007202; AAG02256.1; -; mRNA.
DR   EMBL; BC096477; AAH96477.1; -; mRNA.
DR   EMBL; AF218819; AAF25480.1; -; mRNA.
DR   EMBL; AF161256; AAD43349.1; -; mRNA.
DR   UniGene; Mm.214599; -.
DR   ProteinModelPortal; Q8JZM8; -.
DR   jPOST; Q8JZM8; -.
DR   MaxQB; Q8JZM8; -.
DR   PeptideAtlas; Q8JZM8; -.
DR   PRIDE; Q8JZM8; -.
DR   MGI; MGI:2153525; Muc4.
DR   HOVERGEN; HBG081997; -.
DR   InParanoid; Q8JZM8; -.
DR   PhylomeDB; Q8JZM8; -.
DR   ChiTaRS; Muc4; mouse.
DR   PRO; PR:Q8JZM8; -.
DR   Proteomes; UP000000589; Unplaced.
DR   GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031528; C:microvillus membrane; ISO:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0005176; F:ErbB-2 class receptor binding; ISO:MGI.
DR   GO; GO:0030197; F:extracellular matrix constituent, lubricant activity; IEA:InterPro.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR   GO; GO:0010669; P:epithelial structure maintenance; IEA:InterPro.
DR   GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR   GO; GO:0022408; P:negative regulation of cell-cell adhesion; ISO:MGI.
DR   GO; GO:0001953; P:negative regulation of cell-matrix adhesion; ISO:MGI.
DR   GO; GO:0002853; P:negative regulation of T cell mediated cytotoxicity directed against tumor cell target; ISO:MGI.
DR   GO; GO:0010469; P:regulation of signaling receptor activity; ISO:MGI.
DR   InterPro; IPR005533; AMOP_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR039898; Mucin_4.
DR   InterPro; IPR003886; NIDO_dom.
DR   InterPro; IPR001846; VWF_type-D.
DR   PANTHER; PTHR42668; PTHR42668; 11.
DR   Pfam; PF06119; NIDO; 1.
DR   Pfam; PF00094; VWD; 1.
DR   SMART; SM00723; AMOP; 1.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00539; NIDO; 1.
DR   SMART; SM00216; VWD; 1.
DR   PROSITE; PS50856; AMOP; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS51220; NIDO; 1.
DR   PROSITE; PS51233; VWFD; 1.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Complete proteome; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Membrane; Reference proteome; Repeat; Secreted; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     28       {ECO:0000255}.
FT   CHAIN        29   3443       Mucin-4.
FT                                /FTId=PRO_0000274227.
FT   CHAIN        29   2718       Mucin-4 alpha chain.
FT                                /FTId=PRO_0000274228.
FT   CHAIN      2719   3443       Mucin-4 beta chain.
FT                                /FTId=PRO_0000274229.
FT   TRANSMEM   3405   3425       Helical. {ECO:0000255}.
FT   REPEAT       93    213       1.
FT   REPEAT      333    454       2.
FT   REPEAT      455    580       3.
FT   REPEAT      581    685       4.
FT   REPEAT      686    786       5.
FT   REPEAT      787    994       6.
FT   REPEAT      995   1273       7.
FT   REPEAT     1274   1399       8.
FT   REPEAT     1400   1525       9.
FT   REPEAT     1526   1651       10.
FT   REPEAT     1652   1775       11.
FT   REPEAT     1776   1899       12.
FT   REPEAT     1900   2025       13.
FT   REPEAT     2026   2151       14.
FT   DOMAIN     2431   2586       NIDO. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00570}.
FT   DOMAIN     2587   2699       AMOP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00347}.
FT   DOMAIN     2712   2946       VWFD. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00580}.
FT   DOMAIN     3146   3185       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     3355   3394       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   COMPBIAS     29   2338       Thr-rich.
FT   COMPBIAS     37   2337       Ser-rich.
FT   COMPBIAS   2773   3120       Ser/Thr-rich.
FT   SITE       2718   2719       Cleavage.
FT   CARBOHYD     98     98       O-linked (GalNAc...) threonine.
FT                                {ECO:0000255}.
FT   CARBOHYD    188    188       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    241    241       O-linked (GalNAc...) threonine.
FT                                {ECO:0000255}.
FT   CARBOHYD    278    278       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    286    286       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    311    311       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    385    385       O-linked (GalNAc...) threonine.
FT                                {ECO:0000255}.
FT   CARBOHYD    465    465       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    517    517       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    550    550       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    627    627       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    756    756       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    793    793       O-linked (GalNAc...) threonine.
FT                                {ECO:0000255}.
FT   CARBOHYD    797    797       O-linked (GalNAc...) threonine.
FT                                {ECO:0000255}.
FT   CARBOHYD    833    833       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    907    907       O-linked (GalNAc...) threonine.
FT                                {ECO:0000255}.
FT   CARBOHYD    920    920       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    964    964       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1046   1046       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1114   1114       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1243   1243       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1320   1320       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1369   1369       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1382   1382       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1495   1495       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1621   1621       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1745   1745       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1869   1869       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1995   1995       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2077   2077       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2121   2121       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2728   2728       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2746   2746       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2774   2774       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2800   2800       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2817   2817       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2826   2826       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2861   2861       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2882   2882       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2889   2889       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2905   2905       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2931   2931       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2958   2958       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2976   2976       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2987   2987       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3027   3027       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3052   3052       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3075   3075       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3082   3082       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3130   3130       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3147   3147       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3213   3213       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3220   3220       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3326   3326       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID   3150   3161       {ECO:0000250}.
FT   DISULFID   3155   3173       {ECO:0000250}.
FT   DISULFID   3175   3184       {ECO:0000250}.
FT   DISULFID   3358   3369       {ECO:0000250}.
FT   DISULFID   3363   3378       {ECO:0000250}.
FT   DISULFID   3380   3393       {ECO:0000250}.
FT   CONFLICT     24     24       P -> PE (in Ref. 2; AAG02256).
FT                                {ECO:0000305}.
FT   CONFLICT     36     36       M -> V (in Ref. 2; AAG02256).
FT                                {ECO:0000305}.
FT   CONFLICT    139    139       S -> R (in Ref. 2; AAG02256).
FT                                {ECO:0000305}.
FT   CONFLICT    156    156       E -> D (in Ref. 2; AAG02256).
FT                                {ECO:0000305}.
FT   CONFLICT    203    203       R -> S (in Ref. 2; AAG02256).
FT                                {ECO:0000305}.
FT   CONFLICT    225    225       S -> L (in Ref. 2; AAG02256).
FT                                {ECO:0000305}.
FT   CONFLICT   3094   3094       G -> A (in Ref. 3; AAH96477).
FT                                {ECO:0000305}.
FT   CONFLICT   3162   3162       G -> D (in Ref. 3; AAH96477).
FT                                {ECO:0000305}.
FT   CONFLICT   3180   3180       A -> T (in Ref. 3; AAH96477).
FT                                {ECO:0000305}.
FT   CONFLICT   3181   3181       D -> G (in Ref. 4; AAF25480).
FT                                {ECO:0000305}.
FT   CONFLICT   3197   3197       T -> M (in Ref. 4; AAF25480).
FT                                {ECO:0000305}.
FT   CONFLICT   3205   3205       M -> V (in Ref. 3; AAH96477 and 4;
FT                                AAF25480). {ECO:0000305}.
FT   CONFLICT   3225   3225       N -> Y (in Ref. 3; AAH96477).
FT                                {ECO:0000305}.
FT   CONFLICT   3322   3322       Q -> K (in Ref. 3; AAH96477).
FT                                {ECO:0000305}.
FT   CONFLICT   3384   3384       T -> I (in Ref. 3; AAH96477 and 5;
FT                                AAD43349). {ECO:0000305}.
FT   CONFLICT   3391   3391       K -> E (in Ref. 3; AAH96477 and 5;
FT                                AAD43349). {ECO:0000305}.
FT   CONFLICT   3432   3432       M -> K (in Ref. 3; AAH96477 and 5;
FT                                AAD43349). {ECO:0000305}.
SQ   SEQUENCE   3443 AA;  365216 MW;  88CC32D3226F632B CRC64;
     MRGPHWRVPW LCLSCLYSCL LLLPDALATT STQTPMSLSS STRTSQMSSQ ASTSSTSSDR
     RTSKTEQTST RDTPSSITTV SQSHHTTSME TSKPQTTTTT EVTTSTPSAS SRDQIQTETS
     SQRTISPDGT TTSHAPSISS SAPSTTHMLT TTSSTESTSV DSGHTTAITT QGLTPATAQV
     SLTPSSQNMS TVSTPITSTL TQRQHTGSKQ TSSKSQVNIV TSTLSTSTSD STPAQTMSQV
     TSSSDKRTKP STSGVSSTSL TTTEVLTQTS STDSAPGNTT LRITQNSTTH TTKVSTTSTP
     QKLSPVSTLI NSSQKMSTLP QNQHTESMDT SRQPQTTTTT EVTTSTPSAS SLHQIQTETN
     SQKTISPGET TTSHAPNMRS SPPKTSQILT TMPSTKSTSV DTKQTKAITT KVSTPDTTQV
     SMTPSSQKLP THSTSTQELT SSYSQHIQSK GTSSKSQTTT NTKVNTSTPS ASSRDKIQTE
     TSSQRTNSPG EKRTSHGPSM SSSAPSTTHM LSTTSSNQST SVDTGQTTSV TAQGSTPAIT
     QTSLTPSSQN MSTVSTPITS TQILSTLPQS QHTGSMGTSS NPQTTTSPVV TTSTPSGTSG
     DQIQTETSSQ RTISPGKTTI SHAPNINSSA PSTTHMLSTT SSTQSTSGDT RHITAGRTQG
     STPATTQTSL TPSSPXXXXX XXXXXETETS SQRTISPGET TTSHAPIMSS SPPSSTHMLS
     TASSTEITSV DTRHTTAIMT QGSTPATTQV SPSSQNMSTV SAPITSTHIL STLSQSQHTG
     SKGTSSNPQT TTTPVVTTST PSASSRDQIQ TETSSQRTIS PGKTTTSHVP NMNSSAPSTT
     HILSTTSSIQ STSGDTRHTT AVRTQGSTPA TTQVSLTPSS QXXXXXXXXX XETETSSLRT
     ISPDGTTTSH ASSMSSSSPN TTHLLFTTSS TESTSVDTGH STVITTHGST LATTQVSLTP
     SSQNMSTVSA PITSSQILST LRQSQHTGSK GTSSNHQTTT TPVVTTSTPS AASRDQIQTE
     TSSLRTISPD GTTTSHASSM SSSSPNTTHL LITTSSTEST SVDTGHSTVI TTHGSTLATT
     XXXXXXXXXX ETETSSQRTI SPGKTTTSHV PNMNSSAPST THISSTTSSI QSTSGDTRHT
     TAVRTQGSTP ATTQVSLTPS SQXXXXXXXX XXETETSSQR TISLGETTTS HAPIMSSSPP
     SSTHMLSTAS STEITSVDTG HTTAIMTQGS TPATIQVSPS SQNMSTVSAP ITSTHILSTL
     PKSQHTGSKG TSSNPQTTTT PVVTTSTPSA SSRDQIQTET SSQRTISPGK TTTSHVPNMN
     SSAPSTTHIL STTSSTQSTS GDTRHTTAVR TQGPTPATTQ VSLAPSSQNM STLSAPITSP
     QNFSTLPQNQ HTGSMGTSSN PQSTTIPEVT TSTLSASSRD QVQTETSSQR TIPPGETTTS
     HASSLSSSGP STTNMLTRTS STQITSGDTR HTTAIVTQGS TPATTQTSLT PSSQNMSTVS
     APITSSQILS TLRQSQHTGS KGTSSNHQTT TTPVVTTSTP SATSRDQIQT ETSSLRTISP
     GETTTSHASS LSSSGPSTTN MLTRTSSTQI TSGDTRHTTA IVTQGSTPAT TQTSLTPSSR
     NMSTVSTPIT STHKLSTLPQ RQHTGSKGTS SNPQTTTTPE MTTSTPSATS HDLIETETSS
     QRTISPGETT TSYAPIMSSS APSTTHMLST TSSTRSTSVD TRHTTTLMTQ GSTPATTQVS
     PSSKNMSTVS TPITSTHKLS TLPQSQHTGS KGTSSNPQTT TTPEVTTSTP SATTRDQIQT
     ESSSQRTISP GETTTSHAPS MSSLAPSTTH MLSTTSSSQS TSGDTGHTTA VRTQGSTPAT
     TQVSLSSQNI STVSTPMTST HKLSTLPQSQ HTGSMGTSSN PQTTTTPEVT TSTPSATSYD
     QIQTETSFQR TISPGETTTS HAPSMSNSAP SSTHKLSTAS STEITSVDTR HTIAITTEGS
     TLANTQTSLT PSSQNMSTVS APITSSQILS TLRQSQHTGS KGTSSNHQTT TTPVVTTSTP
     SATSRDQIQT ETSSLRTISP DGTTTSHASS MSSSSPNTTH LLITTSSTES TSVDTGHSTV
     ITTHGSTLAT TQVSLTPSSQ NMSTVSMPST SSQELTSLPQ RQHTGSMETS SQPQNITPTV
     VTTSTLLSFS RGSTELQTMS WGTSSSGTIT TLSTPVRNTS PASTSGILTS TLTTSGNTGY
     TGVTRSLGVI TSRVTSTSLP GKSTVVHSTP AQPLSAHSQS HQTYGTGTPS TSQISILPDV
     TSEKHVASSP GPTVTESFSH VSSSSGLTTK TDNDRNTAVS ATSSTLTSPS PTTASRSTVP
     LPSLLPDQGI SLFPYGSEVG DQNLFARTVD FNSPIFKILI GFPLGSSLRD SFYVTDNGQI
     IFPESDYDVF SYPNPPQRGF TGRERVAMVA PFWADADFSS SRGAIFYQEY VTFYNGHHQL
     IREVETLIND FTSSWGYRAK WTLKVTWVNV PAYTAQESFG TNTYQAILST DGSRSYALFL
     YQNSGMRWDV TQEPYNRVLM GFSSGDGYFE NSPLTFRPAM EKYRPDRFLN SKLGIRGLQV
     YRLHGEERPN YRLKCLRWLE SQPQQPSWGW SSVSCPCSWQ QGQRDFRFRP INPGWWDRQL
     CSFSSGRGGV CCSYGAWGEF REGWRMHSPW QFDEEQEAQN WCCQWNDKPS FCVWYQLRRP
     RVSCAGYRPP RPAWTFGDPH ITTLDNANFT FNGLGDFLLV QAQDRNSSFL LEGRTAQTGT
     AKATNFIAFA AQYNTSSLKS PITVQWFLEP SDKIRVVYNN QTVAFNTRDT EVLPIFNTTG
     VLLTQNGSQV SANFDGTVTI SVIARSNILH ASSSLSEEYR NHTEGLLGVW NDNPEDDFRM
     PNGSTIPSNS SEETLFFYGM TWHVNGTGLL GIRADPLPTK FTPIFLSQLL NQSASGEDLA
     SGCKGDRKCM FDILATGNRT IGQSTNSILN EFQHMNDTLN QYPPSINCSS KIQAYKGQTV
     TTEITSNSKD ATLSLSKKCS GFQLFENGSL QWTPTSPEAC TLEILARDVR TNLSWVLQPK
     TVACFCSKEE QCLYNETSKE GNSSLEVTSC KCDGDTFGRL CERFKDPCDE PCFPNVNCIP
     GKGCEACPPN TTGDGRHCAA LEDSCPNRSC PVNYCYNNGH CGISEAPGCQ PTCTCPPAFA
     DNRCFLAGNS FTPTISTELP LRTIMLSLRE DENASAADVN ASVANILENL DMRAFFSNSL
     VELIRTSPGA QPSSKSIHHW KVTSHFKYRP RGPLIHYLNN QLIGAVMEAF LLQARQERQK
     RSGEARKDVH FFPISRADVQ DQMALNLSML EEYFTCDGYK GYHLVYSPQD GVTCVSPCSE
     GYCHNGGQCK HLPDGPQCSC ASFTIYTSSG KHCEHLSVKL GAFYGILFGT LGALLLLGIL
     AFMIFHFCGC SMNKFSYPLD SEL
//
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