MUP4_CAEEL
ID MUP4_CAEEL Reviewed; 2104 AA.
AC Q21281; Q964N4;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 4.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Transmembrane matrix receptor MUP-4 {ECO:0000312|EMBL:AAK69172.1};
DE AltName: Full=Muscle-positioning protein 4;
DE Flags: Precursor;
GN Name=mup-4 {ECO:0000312|EMBL:CCD63613.1, ECO:0000312|WormBase:K07D8.1};
GN ORFNames=K07D8.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAK69172.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=11470827; DOI=10.1083/jcb.200007075;
RA Hong L., Elbl T., Ward J., Franzini-Armstrong C., Rybicka K.K.,
RA Gatewood B.K., Baillie D.L., Bucher E.A.;
RT "MUP-4 is a novel transmembrane protein with functions in epithelial cell
RT adhesion in Caenorhabditis elegans.";
RL J. Cell Biol. 154:403-414(2001).
RN [2] {ECO:0000312|EMBL:CCD63613.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CCD63613.1};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9136009; DOI=10.1093/genetics/146.1.165;
RA Gatewood B.K., Bucher E.A.;
RT "The mup-4 locus in Caenorhabditis elegans is essential for hypodermal
RT integrity, organismal morphogenesis and embryonic body wall muscle
RT position.";
RL Genetics 146:165-183(1997).
CC -!- FUNCTION: Required for junctional attachments between hypodermis and
CC muscle, and between the apical epithelial surface and the cuticular
CC matrix. Essential for enclosure of the embryo by the hypodermis,
CC hypodermal integrity, embryo elongation, and maintenance of hypodermal
CC morphology in fully elongated embryos. {ECO:0000269|PubMed:11470827,
CC ECO:0000269|PubMed:9136009}.
CC -!- SUBCELLULAR LOCATION: Cell junction, hemidesmosome
CC {ECO:0000269|PubMed:11470827}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:11470827}. Cell membrane {ECO:0000255}; Single-pass
CC membrane protein {ECO:0000255}. Note=Detected in intermediate filaments
CC and hemidesmosomes. {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Abundant at hypodermal cell-matrix junctions
CC overlying muscle of threefold embryos. Expression continues in body
CC wall muscle in larvae and adults and is also detected in other regions
CC where cells show mechanical attachment to the hypodermis including the
CC inner surface of the pharynx, overlying anal and intestinal muscles,
CC overlying vulval and uterine sex muscles, male tail muscle attachment
CC zones and the six mechanosensory neurons (at protein level).
CC {ECO:0000269|PubMed:11470827}.
CC -!- DEVELOPMENTAL STAGE: Expression detected in embryo, larva and adult.
CC {ECO:0000269|PubMed:11470827}.
CC -!- DISRUPTION PHENOTYPE: Arrested embryonic development either at bean or
CC twofold stages with failure of hypodermis to enclose the embryo or at
CC threefold stage with defects in hypodermal cell organization and muscle
CC cell positioning. When disrupted in larvae, causes paralysis and
CC displacement of muscles. {ECO:0000269|PubMed:11470827,
CC ECO:0000269|PubMed:9136009}.
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DR EMBL; AF289202; AAK69172.1; -; mRNA.
DR EMBL; FO080425; CCD63613.1; -; Genomic_DNA.
DR RefSeq; NP_498645.1; NM_066244.6.
DR AlphaFoldDB; Q21281; -.
DR SMR; Q21281; -.
DR BioGRID; 41268; 12.
DR DIP; DIP-26346N; -.
DR IntAct; Q21281; 2.
DR STRING; 6239.K07D8.1; -.
DR EPD; Q21281; -.
DR PaxDb; Q21281; -.
DR PeptideAtlas; Q21281; -.
DR PRIDE; Q21281; -.
DR EnsemblMetazoa; K07D8.1.1; K07D8.1.1; WBGene00003497.
DR GeneID; 176060; -.
DR KEGG; cel:CELE_K07D8.1; -.
DR UCSC; K07D8.1.1; c. elegans.
DR CTD; 176060; -.
DR WormBase; K07D8.1; CE29511; WBGene00003497; mup-4.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000167387; -.
DR HOGENOM; CLU_000420_0_0_1; -.
DR InParanoid; Q21281; -.
DR OMA; HGDCIHD; -.
DR OrthoDB; 1174178at2759; -.
DR PhylomeDB; Q21281; -.
DR PRO; PR:Q21281; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00003497; Expressed in larva and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030056; C:hemidesmosome; IDA:WormBase.
DR GO; GO:0098733; C:hemidesmosome associated protein complex; IDA:WormBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR006150; Cys_repeat_1.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR024731; EGF_dom.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR000082; SEA_dom.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF07645; EGF_CA; 7.
DR Pfam; PF12661; hEGF; 3.
DR Pfam; PF00092; VWA; 1.
DR SMART; SM00181; EGF; 27.
DR SMART; SM00179; EGF_CA; 19.
DR SMART; SM00200; SEA; 2.
DR SMART; SM00327; VWA; 1.
DR SMART; SM00289; WR1; 3.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 13.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 21.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS50024; SEA; 2.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Cell junction; Cell membrane; Cytoplasm;
KW Cytoskeleton; Developmental protein; Disulfide bond; EGF-like domain;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..2104
FT /note="Transmembrane matrix receptor MUP-4"
FT /evidence="ECO:0000255"
FT /id="PRO_0000423668"
FT TOPO_DOM 16..1860
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1861..1881
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1882..2104
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 71..110
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 122..163
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 175..213
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 220..265
FT /note="WR1"
FT /evidence="ECO:0000255"
FT DOMAIN 278..315
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 327..360
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 377..416
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 437..612
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 728..772
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 819..857
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 869..907
FT /note="EGF-like 9; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 919..958
FT /note="EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 968..1007
FT /note="EGF-like 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1016..1058
FT /note="EGF-like 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1071..1110
FT /note="EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1121..1160
FT /note="EGF-like 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1169..1208
FT /note="EGF-like 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1215..1254
FT /note="EGF-like 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1322..1444
FT /note="SEA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT DOMAIN 1495..1620
FT /note="SEA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT DOMAIN 1622..1658
FT /note="EGF-like 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1669..1705
FT /note="EGF-like 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1717..1754
FT /note="EGF-like 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1772..1810
FT /note="EGF-like 20; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1817..1853
FT /note="EGF-like 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 2031..2104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2031..2053
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2057..2071
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2079..2096
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 494
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 556
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 879
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1037
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1576
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1730
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1782
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1838
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 75..89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 83..98
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 126..142
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 136..151
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 179..192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 186..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 282..294
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 288..303
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 331..344
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 338..353
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 355..359
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 381..395
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 389..404
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 732..746
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 740..756
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 758..771
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 823..836
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 830..845
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 873..886
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 880..895
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 923..937
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 931..946
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 972..985
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 979..995
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1020..1034
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1028..1046
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1075..1089
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1083..1098
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1125..1139
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1133..1148
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1173..1187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1181..1196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1219..1233
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1227..1242
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1626..1637
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1631..1646
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1673..1687
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1681..1696
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1721..1733
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1727..1742
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1776..1789
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1783..1798
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1821..1830
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1824..1841
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1843..1852
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CONFLICT 919
FT /note="L -> P (in Ref. 1; AAK69172)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2104 AA; 230054 MW; C98CD462CC434F8B CRC64;
MRWVPLVLLP LIASAATTYQ HRQTYSSLQC RVNDPLSCNQ AKSEVCVFVN GQYRCECPVG
VSRLADGRCL VVNECARPSL NACHKDAQCV DLAEGYTCRC NSGFADTSPD KVNKPGRQCQ
KTTNECGAKQ TYGVDCDENA ACVDTPEGFQ CVCQPGYADV STSISKLPGR KCVESVNECT
NGEADCSNNA DCFDRADGYE CKCRPGFVDA SPNVDKYPGR VCNKPKAPEY YGQQSRQPQC
SEGSGCGPNE ECRFNTAGEK VCQCRRGSVQ QSNGVCKVFS QCEQANECDR NAFCSNTYDG
PKCQCKDGFL DVSPDPVRLP GRKCQQVRNE CADGSHDCSH QAACQDTPTG YICSCNSNCI
DVSSRYNLPP GRKCSVAANQ CSDKSLNSCD ENADCVQLPD GYTCKCFAGY VDVSSNANLP
PGRVCTLSTA CPAQPTDLVF LIDGSGSIGS YVFQTEVLRF LAEFTELFDI APQKTRVSVV
QYSDQIRHEF GLDNYSDRKS LQNAIRNIEY LTGLTRTGAA IEHVANEAFS ERRGARPVGQ
VSRVAIVITD GRSQDNVTRP SDNARRQDIQ LFAVGVTNHV LDAELEEISG SKDRTFHVSG
FEDLNTRLRS AIQRVACPHQ NNEDTYNKGP CDPSNHNGCD RSLNQVCQQK NGKFVCACPA
GFDIHPVTKV CGGDICNPEI ATSCPDPEIC EKTPFGNWRC TCPADLGWRD RLTGVCKIGE
KPVQTSESND ECSPNDVHSC PANSKCEKGA GGEFICKCDA GFQRNGRTNK CEAPGTCDPR
MPDSCDARKK EKCLPDGRGA FACMCDRHHK RHPVTDICLI DECAAGVADC DPNAKCTDTD
ESYICTCNEG FLDKSPEQNK KPGRVCSKQR NECLDGTHNC SMNADCIDLP DGFLCRCKED
FVDISPNPNA FGGIDCRALV NECLITGGHN CHEHAICIDT RDSYKCQCKE GYVDHDELRN
PGRTCKKLNQ ICESGKHECD KNARCVEKGA NDYECVCNAG FIDKSPLTHR PGRKCVEPIC
SDDSKHDCHS AAICEENDSV PEKYTCKCRD GYLDVGAVMG GGKSGRECKE LVNECLSASL
NSCDAAATCI DLDDGYTCKC PLGSKDESPV PKLPGRSCKG LVNECNIPHL NNCSHFATCI
DLEEGYECKC KPEYHDQKPE QPGTECKFII NECLAENLND CSPNAMCIDK IDGYDCKCKA
PFQDEMPSNP GRICRFDECA DPKDNDCDKH ALCIDTDDSY TCQCKEGFFD EISDPKKPGR
VCIGLVIEPQ NQSEDPTTPD PNTIKCGNGL CHLDLGEVCV GGATCSCRPG ESRDNEKEKC
VPTTSIPLVV RVMEYDGEPI QYRTDYSKPD TQAHIEIVDA VKKSVGKIIG KTDVAPRFVT
TDVNYITNPK VQNSEWDKGL LGNVSVHLAG KEEVDKCRFY EQFAEIVREM GGRVDRIKLS
DDADLDPCKK EEEKKGIPCG NTFCSIELGE ECIAGKICGC PKGQKRKDAN SPCRAVESWN
LPLYVIRDGH EKITYSPSLS NPLNDDHKDL VSRFESGVAQ SYDKTPLKGA FVTAEVNEIE
NPESRKKSWD TGILYNFTSH FVKGSVAEPA SVFTDLIDYI QKRNDFEVGK SKLFISPEQL
NPFSNCYHSD CHPDAICKEV GKGYTCTCPD GFRDLNPSRP GRNCLSYRGV NECEKPELNE
CSPHARCIDL DYLYKCECIR PYVNSAVGDA LPGSVCSIDY CQDVNYCPLN STCVNVDEQA
RCDCKPGFVD LRKSGHLSEA GLGESICRRQ SDIDECALGL HNCSAAAICI DKKIGYECQC
QEGYEDGNPS QPGRICAASL CGLCNGHGDC IHDALSSNVT CACLDGYTGQ FCETAPSNLP
LILMTLLALL FLLLTLLCCL YMCARCRCFG ARGRSEGSAS GQEILGSDYY TIPRAKLARP
LYGDEMGDDH AGALAAYLDD GASISSDGSI EEIERRVTTD VTTREVRTTT VRDDDGNIIS
QSQTISHGNP HETDTEQYGM ISSDHYKTSA SEAMDAAMST SASGAAYNQS SGAMMSSASG
HKSAYNQGYA SDSEDSDAGH AVYDRTTRTN QSHDFEPGAD PRTGTERSKR EFVTTTKAEE
VNYF
