MUC4_RAT
ID MUC4_RAT Reviewed; 2344 AA.
AC Q63661; Q63655; Q63657; Q63659; Q9JIC4;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 25-MAY-2022, entry version 111.
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=Pre-sialomucin complex;
DE Short=pSMC;
DE AltName: Full=Sialomucin complex;
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; Synonyms=Smc;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Fischer 344;
RX PubMed=8163496; DOI=10.1016/s0021-9258(17)32665-0;
RA Wu K., Fregien N., Carraway K.L.;
RT "Molecular cloning and sequencing of the mucin subunit of a heterodimeric,
RT bifunctional cell surface glycoprotein complex of ascites rat mammary
RT adenocarcinoma cells.";
RL J. Biol. Chem. 269:11950-11955(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-30.
RX PubMed=10880365; DOI=10.1042/0264-6021:3490641;
RA Price-Schiavi S.A., Perez A., Barco R., Carraway K.L.;
RT "Cloning and characterization of the 5' flanking region of the sialomucin
RT complex/rat Muc4 gene: promoter activity in cultured cells.";
RL Biochem. J. 349:641-649(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1601-2344, AND GLYCOSYLATION.
RC STRAIN=Fischer 344;
RX PubMed=1379596; DOI=10.1016/s0021-9258(18)42007-8;
RA Sheng Z., Wu K., Carraway K.L., Fregien N.;
RT "Molecular cloning of the transmembrane component of the 13762 mammary
RT adenocarcinoma sialomucin complex. A new member of the epidermal growth
RT factor superfamily.";
RL J. Biol. Chem. 267:16341-16346(1992).
RN [4]
RP SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=7440586; DOI=10.1016/s0021-9258(19)70243-9;
RA Sherblom A.P., Carraway K.L.;
RT "A complex of two cell surface glycoproteins from ascites mammary
RT adenocarcinoma cells.";
RL J. Biol. Chem. 255:12051-12059(1980).
RN [5]
RP POST-TRANSCRIPTIONAL REGULATION.
RX PubMed=9857062; DOI=10.1074/jbc.273.52.35228;
RA Price-Schiavi S.A., Carraway C.A., Fregien N., Carraway K.L.;
RT "Post-transcriptional regulation of a milk membrane protein, the sialomucin
RT complex (Ascites sialoglycoprotein (ASGP)-1/ASGP-2, rat muc4), by
RT transforming growth factor beta.";
RL J. Biol. Chem. 273:35228-35237(1998).
RN [6]
RP INTERACTION WITH ERBB2; ERBB3 AND NRG1, AND PHOSPHORYLATION OF ERBB2.
RX PubMed=12386815; DOI=10.1038/sj.onc.1205970;
RA Jepson S., Komatsu M., Haq B., Arango M.E., Huang D., Carraway C.A.,
RA Carraway K.L.;
RT "Muc4/sialomucin complex, the intramembrane ErbB2 ligand, induces specific
RT phosphorylation of ErbB2 and enhances expression of p27(kip), but does not
RT activate mitogen-activated kinase or protein kinaseB/Akt pathways.";
RL Oncogene 21:7524-7532(2002).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=15672420; DOI=10.1002/jcp.20277;
RA Zhang J., Perez A., Yasin M., Soto P., Rong M., Theodoropoulos G.,
RA Carothers Carraway C.A., Carraway K.L.;
RT "Presence of MUC4 in human milk and at the luminal surfaces of blood
RT vessels.";
RL J. Cell. Physiol. 204:166-177(2005).
RN [8]
RP INTERACTION WITH ERBB2 AND ERBB3.
RX PubMed=16624867; DOI=10.1091/mbc.e05-09-0895;
RA Ramsauer V.P., Pino V., Farooq A., Carothers Carraway C.A., Salas P.J.,
RA Carraway K.L.;
RT "Muc4-ErbB2 complex formation and signaling in polarized Caco-2 epithelial
RT cells indicate that Muc4 acts as an unorthodox ligand for ErbB2.";
RL Mol. Biol. Cell 17:2931-2941(2006).
CC -!- FUNCTION: Membrane-bound mucin, a family of highly glycosylated
CC proteins that constitute the major component of the mucus, the slimy
CC and viscous secretion covering epithelial surfaces. These glycoproteins
CC play important roles in the protection of the epithelium and are
CC implicated in epithelial renewal and differentiation. Regulates
CC cellular behavior through both anti-adhesive effects on cell-cell and
CC cell-extracellular matrix interactions and its ability to act as an
CC intramembrane ligand for ERBB2. Plays an important role in
CC proliferation and differentiation of epithelial cells by inducing
CC specific phosphorylation of ERBB2. In polarized epithelial cells,
CC segregates ERBB2 and other ERBB receptors and prevents ERBB2 from
CC acting as a coreceptor. The interaction with ERBB2 leads to enhanced
CC expression of CDKN1B. The formation of a MUC4-ERBB2-ERBB3-NRG1 complex
CC leads to down-regulation of CDKN1B, resulting in repression of
CC apoptosis and stimulation of proliferation. Its ability to promote
CC tumor growth may be mainly due to repression of apoptosis as opposed to
CC proliferation. {ECO:0000250|UniProtKB:Q99102}.
CC -!- SUBUNIT: A heterodimeric complex, composed of a mucin-4 alpha chain and
CC a cysteine-rich transmembrane mucin-4 beta chain (PubMed:7440586).
CC Mucin-4 beta chain interacts with ERBB2 via the EGF-like domain 1. In
CC nonpolarized cells, associates with ERBB2 and ERBB3 (PubMed:12386815,
CC PubMed:16624867). {ECO:0000269|PubMed:12386815,
CC ECO:0000269|PubMed:16624867, ECO:0000269|PubMed:7440586}.
CC -!- SUBCELLULAR LOCATION: [Mucin-4 beta chain]: Cell membrane
CC {ECO:0000305|PubMed:7440586}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:7440586}.
CC -!- SUBCELLULAR LOCATION: [Mucin-4 alpha chain]: Secreted
CC {ECO:0000305|PubMed:7440586}. Note=Secreted by proteolytic processing.
CC {ECO:0000305|PubMed:7440586}.
CC -!- TISSUE SPECIFICITY: Expression is developmentally regulated in the
CC mammary gland, dramatically increases in the lactating gland compared
CC with the virgin mammary gland, while decreasing again during mammary
CC gland involution. Expressed in 13762 ascites cells. Overexpressed in
CC some aggressive mammary tumors. Overexpression seems to block cell-cell
CC and cell-matrix interactions to protect tumor cells from immune
CC surveillance, and to promote metastasis.
CC -!- DOMAIN: [Mucin-4 alpha chain]: Essentially composed of an array of
CC serine- and threonine-rich tandem repeats which is highly polymorphic,
CC the variable number of tandem repeats (VNTR) region.
CC {ECO:0000250|UniProtKB:Q99102}.
CC -!- PTM: Proteolytically cleaved into 2 subunits, mucin-4 alpha chain and
CC mucin-4 beta chain. {ECO:0000305|PubMed:7440586}.
CC -!- PTM: Mucin-4 alpha subunit is highly O-glycosylated.
CC {ECO:0000269|PubMed:1379596}.
CC -!- PTM: Mucin-4 beta subunit is predominantly N-glycosylated.
CC {ECO:0000269|PubMed:1379596}.
CC -!- POLYMORPHISM: The variable number of tandem repeats (VNTR) region, an
CC array of serine- and threonine-rich tandem repeats, is encoded by a
CC single exon (exon 2) which is highly polymorphic. {ECO:0000305}.
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DR EMBL; U06746; AAA85517.1; -; mRNA.
DR EMBL; U06748; AAA85519.1; -; mRNA.
DR EMBL; U06750; AAA85521.1; -; mRNA.
DR EMBL; U06752; AAA85523.1; -; mRNA.
DR EMBL; AF240632; AAF86958.1; -; Genomic_DNA.
DR PIR; A43353; A43353.
DR PIR; A53577; A53577.
DR AlphaFoldDB; Q63661; -.
DR GlyGen; Q63661; 27 sites.
DR UCSC; RGD:621331; rat.
DR RGD; 621331; Muc4.
DR InParanoid; Q63661; -.
DR Reactome; R-RNO-913709; O-linked glycosylation of mucins.
DR Reactome; R-RNO-977068; Termination of O-glycan biosynthesis.
DR PRO; PR:Q63661; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031528; C:microvillus membrane; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0005176; F:ErbB-2 class receptor binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:RGD.
DR GO; GO:0048565; P:digestive tract development; IEP:RGD.
DR GO; GO:0044849; P:estrous cycle; IEP:RGD.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; ISO:RGD.
DR GO; GO:0007595; P:lactation; IEP:RGD.
DR GO; GO:0030277; P:maintenance of gastrointestinal epithelium; ISO:RGD.
DR GO; GO:0030879; P:mammary gland development; IEP:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
DR GO; GO:0022408; P:negative regulation of cell-cell adhesion; IDA:RGD.
DR GO; GO:0001953; P:negative regulation of cell-matrix adhesion; IDA:RGD.
DR GO; GO:0002853; P:negative regulation of T cell mediated cytotoxicity directed against tumor cell target; IDA:RGD.
DR GO; GO:0031077; P:post-embryonic camera-type eye development; IEP:RGD.
DR GO; GO:0010469; P:regulation of signaling receptor activity; IDA:RGD.
DR GO; GO:0046677; P:response to antibiotic; IEP:RGD.
DR GO; GO:0034097; P:response to cytokine; IEP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0009725; P:response to hormone; IEP:RGD.
DR GO; GO:0032570; P:response to progesterone; IEP:RGD.
DR GO; GO:0033189; P:response to vitamin A; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR003886; NIDO_dom.
DR InterPro; IPR001846; VWF_type-D.
DR Pfam; PF06119; NIDO; 1.
DR Pfam; PF00094; VWD; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00539; NIDO; 1.
DR SMART; SM00216; VWD; 1.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS51220; NIDO; 1.
DR PROSITE; PS51233; VWFD; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Disulfide bond; EGF-like domain;
KW Glycoprotein; Membrane; Reference proteome; Repeat; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..2344
FT /note="Mucin-4"
FT /id="PRO_0000274230"
FT CHAIN 31..1615
FT /note="Mucin-4 alpha chain"
FT /evidence="ECO:0000305|PubMed:7440586"
FT /id="PRO_0000274231"
FT CHAIN 1616..2344
FT /note="Mucin-4 beta chain"
FT /evidence="ECO:0000305|PubMed:7440586"
FT /id="PRO_0000274232"
FT TRANSMEM 2173..2193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2301..2321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1332..1492
FT /note="NIDO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00570"
FT DOMAIN 1609..1804
FT /note="VWFD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 2047..2086
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2256..2295
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 32..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..1006
FT /note="Variable number of tandem repeats (VNTR)"
FT /evidence="ECO:0000305"
FT REGION 773..1036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1072..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1171..1197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1233..1269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1574..1597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1233..1266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1582..1597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 1616..1617
FT /note="Cleavage"
FT /evidence="ECO:0000305|PubMed:7440586"
FT CARBOHYD 133
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 392
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 470
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 479
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1644
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1660
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1672
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1689
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1698
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1704
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1715
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1724
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1759
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1780
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 1829
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1874
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1926
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1951
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1974
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1981
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2029
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2048
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 2051..2062
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2056..2074
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2076..2085
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2259..2270
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2264..2279
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2281..2294
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CONFLICT 81
FT /note="I -> L (in Ref. 1; AAA85519/AAA85521)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="S -> G (in Ref. 1; AAA85519/AAA85521)"
FT /evidence="ECO:0000305"
FT CONFLICT 103..104
FT /note="GT -> RN (in Ref. 1; AAA85519/AAA85521)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="T -> A (in Ref. 1; AAA85521)"
FT /evidence="ECO:0000305"
FT CONFLICT 126..127
FT /note="QT -> RA (in Ref. 1; AAA85521)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="T -> A (in Ref. 1; AAA85519)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="T -> A (in Ref. 1; AAA85521)"
FT /evidence="ECO:0000305"
FT CONFLICT 141..143
FT /note="RES -> ER (in Ref. 1; AAA85519)"
FT /evidence="ECO:0000305"
FT CONFLICT 150..485
FT /note="Missing (in Ref. 1; AAA85519)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="T -> M (in Ref. 1; AAA85521)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="M -> T (in Ref. 1; AAA85521)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="T -> V (in Ref. 1; AAA85521)"
FT /evidence="ECO:0000305"
FT CONFLICT 490
FT /note="G -> V (in Ref. 1; AAA85519)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="T -> K (in Ref. 1; AAA85519)"
FT /evidence="ECO:0000305"
FT CONFLICT 501..502
FT /note="VT -> IS (in Ref. 1; AAA85519)"
FT /evidence="ECO:0000305"
FT CONFLICT 505
FT /note="D -> G (in Ref. 1; AAA85519)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2344 AA; 248041 MW; 0182776F4FDE997F CRC64;
MRGPHGVSWR VPWLCLSCLC SCLLLLPVNT STTSAPKTST ALPSSTNPSQ MTSQVSNPTA
SSYRMTKNTG QASPMVTSSS ITTLPQSQHT GSMKTTRNPQ TTGTTEVTTT LSASSSDQVQ
VETTSQTTLS PDTTTTSHAP RESSSPPSTS VILTTTASTE GTSGDTGHTM AVTTQGSTPA
TTEISVTPST QKMSPVSTFS TSTQEITTLS QSQHTGGMKT TRNPQTTGTT EVTTTLSASS
SDHPTSSPES TPGNTAPRTT ETSTTTTTKV LMTSLQQKLP TGSTLGTSTQ ELTTLPQSQH
TGIMKTTSRT QTTTPTEVTT RTLSASSSDH RQAETSSQTT LSPDTTTTSH APRESSPPST
SVILTHGHRE GTSGDTGHTM AVTTQGSTPA TTEISVTPST QKMSPVSTFS TSTQEITTLS
QSQHTGGMKT TRNPQRTTPT EVTTSTLSAS SSDQVQVETT SRATLSPDTT TTSHAPSVSS
SSPSPPSTEG TSVDTGLTTA VTTQDSTPAT TQGSLTSSSQ TLSTVSPLST STQETSTQEL
TSSQSQHTGS MKTTHNPQTT RNTEVTTTLS ASSSDQVQVE TTSQTTLSDA TTTSHAPRES
SSPPSTSDIL TTMASTEGTS GDTGHTMAVT TQGSTPATTE ISVTPSTQKM SPVSTFSTST
QEITTLSQSQ HTGGMKTTRN PQTTGTTEVT TTLSASSSDQ VQAETSSQTT LSPDTTTTSH
APRESSSPPS TSDMLTTTAS TEGTSGDTGH TTAVTTQGSI PATTQLSTTF ASQKMSTVST
PTTSSIQELS TLPQSQHTGS MEISSRPQTT SVTSTLSSSP SGSTPVQTRS VTSSSDERTN
PTSSGVSNTS PATTEVLTPT SSPESTPGNT APRTTETSTT TTTKVLMTSL QQKLPTGSTL
GTSTPTEVTT TLSASSSDQV QVETTSQTTL SPDATTTSHA PRESSSPPST SVILTTMAST
EGTSGDTGHT TAVTDQGSTP ATTEISVTPS TQKMSTVSTL VTSTQELTSS QSQRTGSMGT
SSKPQATTPT EVTTSTLSSF SRGSLFSARN CCLQTKKPPL PAVVCLPDPS SVPSLMHSSK
PQATTPTEVT TSTLSSFSRG STQTQTVSWE TSSSGKITAP STSSRRTPSV ATSDIFTTTD
STSGNAGHTL LTGSHSVITS RVASTTLGRL STVAHRQSTQ RSSTHSQSYL TESMGASSTS
ETSLLTEATT ETSLCLFTWT HCDRDLLSWT SSSGLTTKTD NDRSTALSAT SLTLPAPSTS
TASRSTVPPA PLPPDQGISL FQIGFPLGSL CGIPSILQIT VRSFSPSQTT MSSPTPTHLK
EASQEGSVCH SGHSGVMLIS LAPGEPYFRT TTSHFTMSST SLIRKVESLI NEFTSDWSFK
PSDTEVTWVN VPAYPAQGRT LGANTYQAIL STDGSRSYAL FLYQSGGMRW DVTQGLYNRV
LMGFSSGDGY FENSPLIFRP AVEKYRPDRF LTPNYGSGDS RSTGYTGRCG PTTGSSVCSG
WKVSLSSPAG AGTRFPALAP GSRDFGSGSS TQVCGAGSYA ASLRAGRVLY VWHLGEFREG
WRMHSPWQFD EDEGRHRTGL AAGTTSPLSA SSTSSGGPEL VVLGTRPPRP AWTFGDPHIT
TLDNAKYTFN GLGYFLLVQA QDRNSSFLLE GRTAQTDSAN ATNFIAFAAQ YNTSSLKSPI
TVQWFLEPND TIRVVHNNQT VAFNTSDTED LPVFNATGVL LIQNGSQVSA NFDGTVTISV
IALSNILHAS SSLSEEYRNH TKGLLGVWND NPEDDFRMPN GSTIPSNTSE ETLFHYGMTS
ETNGIGLLGV RTDPLPSEFT PIFLSQLWNK SGAGEDLISG CNEDAQCKFD ILATGNRDIG
QSTNSILRTF RHVNGTLNQY PPPIHYSSKI QAYKGREQWP LRSPATLRMS YSASPTSAVA
FELFENGSLH VDTNIPRRTY LEILARDVKT NLSSVLQPET VACFCSKEEQ CLYNETSKEG
NSSTEVTSCK CDGNSFGRLC EHSKDLCTEP CFPNVDCIPG KGCQACPPNM TGDGRHCVAV
EISEFCQNHS CPVNYCYNHG HCDISGPPDC QPTCTCAPAF TGNRCFLAGN NFTPIIYKEL
PLRTITLSLR EDENASNADV NASVANVLEN LDMRAFLSNS LVELIRTSPG APVLGKPIHH
WKVVSHFKYR PRGPLIHYLN NQLISAVMEA FLLQARQERR KRSGEARKNV RFFPISRADV
QDGMALNLSM LDEYFTCDGY KGYHLVYSPQ DGVTCVSPCS EGYCHNGGQC KHLPDGPQCT
CATFSIYTSW GERCEHLSVK LGAFFGILFG ALGALLLLAI LACVVFHFCG CSMNKFSYPL
DSEL
