DEK1_MAIZE
ID DEK1_MAIZE Reviewed; 2159 AA.
AC Q8RVL1; B4FFL6;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 2.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Calpain-type cysteine protease DEK1;
DE EC=3.4.22.-;
DE AltName: Full=Phytocalpain DEK1;
DE AltName: Full=Protein DEFECTIVE KERNEL 1;
DE Short=ZmDEK1;
DE Flags: Precursor;
GN Name=DEK1;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, DISRUPTION PHENOTYPE,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. B73; TISSUE=Endosperm;
RX PubMed=11929961; DOI=10.1073/pnas.042098799;
RA Lid S.E., Gruis D., Jung R., Lorentzen J.A., Ananiev E., Chamberlin M.,
RA Niu X., Meeley R., Nichols S., Olsen O.-A.;
RT "The defective kernel 1 (dek1) gene required for aleurone cell development
RT in the endosperm of maize grains encodes a membrane protein of the calpain
RT gene superfamily.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:5460-5465(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=19965430; DOI=10.1126/science.1178534;
RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT "The B73 maize genome: complexity, diversity, and dynamics.";
RL Science 326:1112-1115(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=cv. B73;
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-1769, AND TISSUE
RP SPECIFICITY.
RX PubMed=12824178; DOI=10.1074/jbc.m300745200;
RA Wang C., Barry J.K., Min Z., Tordsen G., Rao A.G., Olsen O.A.;
RT "The calpain domain of the maize DEK1 protein contains the conserved
RT catalytic triad and functions as a cysteine proteinase.";
RL J. Biol. Chem. 278:34467-34474(2003).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=17933905; DOI=10.1105/tpc.106.048868;
RA Tian Q., Olsen L., Sun B., Lid S.E., Brown R.C., Lemmon B.E., Fosnes K.,
RA Gruis D.F., Opsahl-Sorteberg H.-G., Otegui M.S., Olsen O.-A.;
RT "Subcellular localization and functional domain studies of DEFECTIVE
RT KERNEL1 in maize and Arabidopsis suggest a model for aleurone cell fate
RT specification involving CRINKLY4 and SUPERNUMERARY ALEURONE LAYER1.";
RL Plant Cell 19:3127-3145(2007).
CC -!- FUNCTION: Essential protease involved in epiderm development. Required
CC for aleurone cell development in the endosperm probably by maintaining
CC and restricting the aleurone and embryonic epidermal L1 cell-layer
CC fates as well as meristems organization. Involved in the maintenance of
CC adaxial/abaxial axis information in developing leaves, probably by
CC regulating cell proliferation and expansion. Does not need calcium ions
CC to be active. {ECO:0000269|PubMed:11929961,
CC ECO:0000269|PubMed:12824178, ECO:0000269|PubMed:17933905}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Cell membrane {ECO:0000269|PubMed:17933905}; Multi-pass membrane
CC protein {ECO:0000269|PubMed:17933905}. Endosome membrane
CC {ECO:0000269|PubMed:17933905}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:17933905}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8RVL1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8RVL1-2; Sequence=VSP_047871;
CC -!- TISSUE SPECIFICITY: Expressed in most tissues at low levels ranging
CC from 30 to 55 ppm. Present in all endosperm cells at transcript level,
CC but confined to aleurones at protein level.
CC {ECO:0000269|PubMed:11929961, ECO:0000269|PubMed:12824178}.
CC -!- DEVELOPMENTAL STAGE: In endosperm, accumulates during early
CC developmental stages and declines near maturity. In embryos, levels
CC peak at middevelopment with highest expression in the embryonic axis.
CC Also present in young pericarp and immature ear tip and base.
CC {ECO:0000269|PubMed:11929961}.
CC -!- DOMAIN: The transmembrane regions are not required for calpain activity
CC but may play regulatory roles. {ECO:0000250}.
CC -!- PTM: Autocatalytic proteolytic cleavage leading to the production of
CC mainly cytoplasmic localized subproducts of about 85 and 120 kDa.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Loss of aleurone cells leading to white grains.
CC Embryos arrest at the juvenile globoid stage and are devoid of shoot
CC structures. {ECO:0000269|PubMed:11929961, ECO:0000269|PubMed:17933905}.
CC -!- MISCELLANEOUS: Although homology to other calpains is high within the
CC protease domain, the lack of calcium-binding sites suggests that this
CC protein is a protease that may not be activated by calcium ions.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
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DR EMBL; AY061806; AAL38189.1; -; mRNA.
DR EMBL; CM007647; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BT035904; ACF80909.1; -; mRNA.
DR RefSeq; NP_001105528.1; NM_001112058.1.
DR RefSeq; XP_008648830.1; XM_008650608.1.
DR AlphaFoldDB; Q8RVL1; -.
DR SMR; Q8RVL1; -.
DR STRING; 4577.GRMZM2G321753_P01; -.
DR MEROPS; C02.019; -.
DR PaxDb; Q8RVL1; -.
DR PRIDE; Q8RVL1; -.
DR GeneID; 542509; -.
DR KEGG; zma:542509; -.
DR MaizeGDB; 12148; -.
DR eggNOG; KOG0045; Eukaryota.
DR Proteomes; UP000007305; Chromosome 1.
DR ExpressionAtlas; Q8RVL1; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IMP:UniProtKB.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; ISS:UniProtKB.
DR GO; GO:0090628; P:plant epidermal cell fate specification; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:2000011; P:regulation of adaxial/abaxial pattern formation; ISS:UniProtKB.
DR GO; GO:0001558; P:regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:2000014; P:regulation of endosperm development; ISS:UniProtKB.
DR GO; GO:2000024; P:regulation of leaf development; ISS:UniProtKB.
DR GO; GO:0009934; P:regulation of meristem structural organization; ISS:UniProtKB.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IEA:EnsemblPlants.
DR GO; GO:0097264; P:self proteolysis; ISS:UniProtKB.
DR CDD; cd00044; CysPc; 1.
DR InterPro; IPR022682; Calpain_domain_III.
DR InterPro; IPR022683; Calpain_III.
DR InterPro; IPR036213; Calpain_III_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR Pfam; PF01067; Calpain_III; 1.
DR Pfam; PF00648; Peptidase_C2; 1.
DR SMART; SM00720; calpain_III; 1.
DR SMART; SM00230; CysPc; 1.
DR SUPFAM; SSF49758; SSF49758; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Developmental protein;
KW Endoplasmic reticulum; Endosome; Hydrolase; Membrane; Phosphoprotein;
KW Protease; Reference proteome; Repeat; Signal; Thiol protease;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..2159
FT /note="Calpain-type cysteine protease DEK1"
FT /id="PRO_0000423439"
FT PROPEP 34..?
FT /evidence="ECO:0000250"
FT /id="PRO_0000423440"
FT TOPO_DOM 34..70
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..95
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..127
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 149..164
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..236
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..264
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..294
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..320
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..623
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 624..644
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 645..660
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 661..681
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 682..694
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 695..715
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 716..719
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 720..740
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 741..770
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 771..791
FT /note="Helical; Name=13"
FT /evidence="ECO:0000255"
FT TOPO_DOM 792..822
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 823..843
FT /note="Helical; Name=14"
FT /evidence="ECO:0000255"
FT TOPO_DOM 844..853
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 854..874
FT /note="Helical; Name=15"
FT /evidence="ECO:0000255"
FT TOPO_DOM 875..887
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 888..908
FT /note="Helical; Name=16"
FT /evidence="ECO:0000255"
FT TOPO_DOM 909..921
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 922..942
FT /note="Helical; Name=17"
FT /evidence="ECO:0000255"
FT TOPO_DOM 943..946
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 947..967
FT /note="Helical; Name=18"
FT /evidence="ECO:0000255"
FT TOPO_DOM 968..981
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 982..1002
FT /note="Helical; Name=19"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1003..1016
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1017..1037
FT /note="Helical; Name=20"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1038..1060
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1061..1081
FT /note="Helical; Name=21"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1082..2159
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1417..1609
FT /note="Calpain catalytic 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT DOMAIN 1703..2005
FT /note="Calpain catalytic 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT REGION 365..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1769
FT /evidence="ECO:0000250"
FT ACT_SITE 1927
FT /evidence="ECO:0000250"
FT ACT_SITE 1947
FT /evidence="ECO:0000250"
FT MOD_RES 1371
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 1376
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 1665
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..1877
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11929961,
FT ECO:0000303|PubMed:19936069"
FT /id="VSP_047871"
FT MUTAGEN 1769
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12824178"
FT CONFLICT 92
FT /note="M -> L (in Ref. 1; AAL38189)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="E -> K (in Ref. 1; AAL38189)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="C -> G (in Ref. 1; AAL38189)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="M -> T (in Ref. 1; AAL38189)"
FT /evidence="ECO:0000305"
FT CONFLICT 469
FT /note="I -> T (in Ref. 1; AAL38189)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2159 AA; 239106 MW; 041D8974E4BA0AA5 CRC64;
MEGEGHHGVV LACSICGFLF AVLSPFSFWV LWAVNWRPWR LYSWIYARKW PTYVQGPQLS
TLCSLLTLCA WLVVISPIAV LLVWGSVLIA LMERNIIGLA VIMAGVALLL SFYSIMLWWR
TQWQSSEAVA YLLLLAVCLL CAYDFCAIYV TAGASASELN SPSGFFFGVS VISLAINMLF
ICKILFNVSG FDVDEYVRRS YKFAYSDCVE VAPVSCSPEP PDPSELYMTK SSRVKHLGLL
YISSLLVLVG YSILYGLTSK EARWLGALTS VAVVILDWNL GLCSFRFELL KSRMIVLFVA
GTSRAFLVSF GVHYWYLGHC ISYAFVASVL LSAAVSSWLS ISNPSVARID ALRSTVIKLR
EGFRRKGQNS SSNSSEGCGS SVKRSSGSVE AGQNGNAMDS MYRSNSQSDG VNWSSIPFDR
SNSCQEGRSS DKNIDSARAS LAHRSNSCLS AVQDSETAVV SVDRHGDPIT SLVCSSSGLE
SHGCEPSGSA TTSGNQQLLD LNLAAIFQDR LNDPRISSML KKNGGLGDVE LANLLQDKGL
DPNFSYMLKD KVMDPRILAL LQRSSLDADR EHQDDVDVTA TDSDRLDTTI ANQISLSEEL
RRSGLEKWLN ISRLIFHHLA GSPIRAFIVF TVMFIIETAT VAIYRPETIK VINATHEQFE
FGFSILLLSP VVCSIMAFIW SLRAEEMLMT SKPQKYGFIA WLLSTCVGLF LSFLSKSSVI
LGLSLTVPLM VACLSFAVPI WIRNGYSFWI PGREFANREN VSQAPGEKER ALFVITIAVF
TASIIGLGAI VSAKPLDALG YKGWDADKNS SYSPYATSMY LGWALSSTIA VITTGLIPIV
AWFATYRFSP SSAICVGLFA TVLVSFCGAS YWGVVNSRED GVPLKADFLA ALLPLLCIPA
FFSLFTGLYK WKDDDWKISR GVYLFVGMGM LLLFGAVAAV IVTIRPWTVG VACLVAILFL
VFVIGVIHYW TSNNFYLTRT QMLLVCSIAF LLALAAFLMG LFHGKPFVGA SIGYFSFIFL
LTGRALTVLL SPPIVVYSPR VLPVYVYDAH ADSAKNVSYA FLILYGIALA TEVWGVIASL
IMNPPFVGAG VSATTLVIAF SFAVSRPCLT LKMMEDAVHF LSKDTVVQAM SRSANKTRNA
ISGTYSAPQR SASSAALLVG DPALTLDRAG NFVLPRADVM KLRDRLRNEE IAAGSFLCGV
KDCLLICPQS LSNIDYRRNM CAHARILALE EAIDTEWVYM WDKFGGYLLL LLGLTAKAEQ
IQDEVRLRLF LDSIGLSDLS AKEIKKWMPE DRRQFELIQE SYIREKEMEE EALMQRREEE
GKGRERRRAL LEREERKWKE LEISLLSSIP NTGSRDAAAM AAAVRAVGGD SALEDSFARD
RVSSIANHIR KAQLARRAEQ TGIPGTICIL DDEPRSTGRH CGELDLCLCQ SQKVTLSIAV
MVQPVSGPVC LFGSEFQKVC WEILVAGSEQ GMEAGQVGLR LVTKGERMTT VAKEWNIGAS
SIADGRWHLV TVTLDADLGE ATSFIDGVYD GYQNGLPLPT DNGIWEPGTD IWVGARPPMD
LDAFGRSDSE GSDSKMQIMD AFLWGRCLSE DEVTVLHTAM SPAEYGFFDL APGDAWHGSY
SARVDDWESE EAYELYDQGD VEWDGQYSSG RKRPVHDAVA IDLDSFARRP RKPRFETRDE
VNQRMLSVER AVRDALIAKG ERNFTDQEFP PEDRSLFVDP MNPPLKLQVV SEWMRPSDIA
KDISISCQPC LFSGSVNSSD VCQGRLGDCW FLSAVAVLTE MSRISEVIIT PEYNDEGIYT
VRFCIQGEWV AVVVDDWIPC ESPGKPAFAT SRKQNELWVS ILEKAYAKLH GSYEALEGGL
VQDALVDLTG GAGEEIDMRS PQAQLDLASG RLWSQLLHFK QEGFLLGAGS PSGSDAHISS
SGIVQGHAYS ILQVREVDGH KLIQIRNPWA NEVEWNGPWS DSSPEWTERM KHKLMHVPQS
KNGVFWMSWQ DFQIHFRSIY VCRVYPPEMR YSVHGQWRGY NAGGCQDYDS WHQNPQYRLR
VTGRDALYPV HVFITLTQGV GFSRKTNGFR NYQSSHDSSM FYIGMRILKT QGCRAAYNIY
MHESAGGTDY VNSREISCEL VLDPYPKGYT IVPTTIHPGE EAPFVLSVFS KASIRLEAV
