ID M5W795_PRUPE Unreviewed; 2160 AA.
AC M5W795;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Calpain catalytic domain-containing protein {ECO:0000259|PROSITE:PS50203};
GN ORFNames=PRUPE_6G003300 {ECO:0000313|EMBL:ONH98985.1};
OS Prunus persica (Peach) (Amygdalus persica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=3760 {ECO:0000313|EMBL:ONH98985.1, ECO:0000313|Proteomes:UP000006882};
RN [1] {ECO:0000313|EMBL:ONH98985.1, ECO:0000313|Proteomes:UP000006882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX PubMed=23525075; DOI=10.1038/ng.2586;
RA Verde I., Abbott A.G., Scalabrin S., Jung S., Shu S., Marroni F.,
RA Zhebentyayeva T., Dettori M.T., Grimwood J., Cattonaro F., Zuccolo A.,
RA Rossini L., Jenkins J., Vendramin E., Meisel L.A., Decroocq V.,
RA Sosinski B., Prochnik S., Mitros T., Policriti A., Cipriani G., Dondini L.,
RA Ficklin S., Goodstein D.M., Xuan P., Del Fabbro C., Aramini V., Copetti D.,
RA Gonzalez S., Horner D.S., Falchi R., Lucas S., Mica E., Maldonado J.,
RA Lazzari B., Bielenberg D., Pirona R., Miculan M., Barakat A., Testolin R.,
RA Stella A., Tartarini S., Tonutti P., Arus P., Orellana A., Wells C.,
RA Main D., Vizzotto G., Silva H., Salamini F., Schmutz J., Morgante M.,
RA Rokhsar D.S.;
RT "The high-quality draft genome of peach (Prunus persica) identifies unique
RT patterns of genetic diversity, domestication and genome evolution.";
RL Nat. Genet. 45:487-494(2013).
RN [2] {ECO:0000313|EMBL:ONH98985.1}
RP NUCLEOTIDE SEQUENCE.
RA Verde I., Jenkins J., Dondini L., Micali S., Pagliarani G., Vendramin E.,
RA Paris R., Aramini V., Gazza L., Rossini L., Bassi D., Troggio M., Shu S.,
RA Grimwood J.H., Tartarini S., Dettori M.T., Schmutz J.;
RT "WGS assembly of Prunus persica.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase C2 family.
CC {ECO:0000256|ARBA:ARBA00007623}.
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DR EMBL; CM007656; ONH98985.1; -; Genomic_DNA.
DR EMBL; CM007656; ONH98986.1; -; Genomic_DNA.
DR RefSeq; XP_007208412.1; XM_007208350.1.
DR RefSeq; XP_007208413.1; XM_007208351.1.
DR STRING; 3760.M5W795; -.
DR EnsemblPlants; ONH98985; ONH98985; PRUPE_6G003300.
DR EnsemblPlants; ONH98986; ONH98986; PRUPE_6G003300.
DR GeneID; 18775568; -.
DR Gramene; ONH98985; ONH98985; PRUPE_6G003300.
DR Gramene; ONH98986; ONH98986; PRUPE_6G003300.
DR KEGG; pper:18775568; -.
DR eggNOG; KOG0045; Eukaryota.
DR HOGENOM; CLU_001987_0_0_1; -.
DR OMA; IYVCRIY; -.
DR OrthoDB; 142935at2759; -.
DR Proteomes; UP000006882; Chromosome g6.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:2000011; P:regulation of adaxial/abaxial pattern formation; IEA:EnsemblPlants.
DR GO; GO:2000024; P:regulation of leaf development; IEA:EnsemblPlants.
DR GO; GO:0009934; P:regulation of meristem structural organization; IEA:EnsemblPlants.
DR CDD; cd00214; Calpain_III; 1.
DR CDD; cd00044; CysPc; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR033883; C2_III.
DR InterPro; IPR022684; Calpain_cysteine_protease.
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 PANTHER; PTHR10183; CALPAIN; 1.
DR PANTHER; PTHR10183:SF379; CALPAIN-A-RELATED; 1.
DR Pfam; PF01067; Calpain_III; 1.
DR Pfam; PF00648; Peptidase_C2; 1.
DR PRINTS; PR00704; CALPAIN.
DR SMART; SM00720; calpain_III; 1.
DR SMART; SM00230; CysPc; 1.
DR SUPFAM; SSF49758; Calpain large subunit, middle domain (domain III); 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00239};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU00239};
KW Reference proteome {ECO:0000313|Proteomes:UP000006882};
KW Thiol protease {ECO:0000256|PROSITE-ProRule:PRU00239};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 67..89
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 130..151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 163..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 238..257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 263..286
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..314
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 624..642
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 662..682
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 694..712
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 718..740
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 769..789
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 818..841
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 848..870
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 886..907
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 919..941
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 947..968
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 980..1000
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1012..1034
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1055..1074
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1080..1102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1704..2006
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT REGION 363..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1770
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 1928
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 1948
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 2160 AA; 239392 MW; 6F03399C9CE11E40 CRC64;
MEGDERHVLL ACVISGTLFS VLGSASFSIL WLVNWRPWRI YSWIFARKWP DIFHGPQLDI
VCGFLSLSAW ILVISPVLVL IIWGSWLVII LDRHIIGLAV IMAGTALLLA FYSIMLWWRT
QWQSSRAVAI LLLLAVALLC AYELCAVYVT AGSKASQRYS PSGFFFGVSA IALAINMLFI
CRMVFNGNGL DVDEYVRKAY KFAYSDCIEV GPVACLPEPP DPNELYPRQS SRASHLGLLY
LGSLVVLLVY SILYGLTAKE SRWLGAITSS AVIILDWNMG ACLYGFQLLQ SRVAALFVAG
TSRIFLICFG VHYWYLGHCI SYAVVASVLL GASVSRHLSV TNPLAARRDA LQSTVIRLRE
GFRKKEQNSS SSSSDGCGSS MKRSSSVEVG CLGNVVEASN RSTAQCTVDA NNWTNVLLRT
ASSHEGINSD KSIDSGRPSL ALRSSSCRSV IQEPEVGTSC TDKNFDHNNT LAVCSSSGLE
SQGCESSASN SANQQTLDLN LAFALQERLN DPRITSMLKK RARQGDLELV NLLQDKGLDP
NFAMMLKEKS LDPTILALLQ RSSLDADRDH RDNTDITIVD SNSVDNALPN QISLSEELRL
HGLEKWLQLS RLLLHHVVGT PERAWVLFSF VFILETIAVA IFRPKTIKII NATHQQFEFG
FAVLLLSPVV CSIMAFLQSL KAEEMTMTSK PRKYGFVAWL LSTSVGLLLS FLSKSSVLLG
LSLTVPFMVA CLSVAIPIWI RNGYQFWVPQ LQCAGPAGNH QIRGTKEGVI LVLSTTLFAA
SVLALGAIVS AKPLDDLGYK GWTGEQKSFT SPYASSVYIG WAMASAIALM VTGILPIVSW
FATYRFSLSS AVCVGIFTVV LVTFCGASYM EVVKSRDDQV PTSGDFLAAL LPLICSPALL
SLCSGLHKWK DDDWRLSRGV YIFVTIGLLL LLGAISAVIV VVKPWTIGVA FLLVLLMIVL
AIGAIHHWAS NNFYLTRTQM FFVCFLAFLL ALAAFLVGWF EDKPFVGASV GYFLFLFLLA
GRALTVLLSP PIVVYSPRVL PVYVYDAHAD CGKNVSAAFL VLYGIALATE GWGVVASLKI
FPPFAGASVS AITLVVAFGF AFSRPCLTLK MMEDAVHFLS KETVVQAIAR SATKTRNALS
GTYSAPQRSA SSAALLVGDP TVMRDRAGNF VLPRADVMKL RDRLRNEELV AGSFFCRKRY
GRTFRHEPTN DVDHRREMCA HARILALEEA IDTEWVYMWD KFGGYLLLLL GLTAKAERVQ
DEVRLRLFLD SIGFADLSAK KIKKWMPEDR RQFEIIQESY IREKEMEEEL LMQRREEEGK
GKERRKALLE KEERKWKEIE ASLISSIPNA GSREAAAMAA AVRAVGGDSV LDDSFARERV
SSIARRIRTA QLARRALQTG ISGAVCVLDD EPTTSGRHCG QIDPTICQSQ KISFSVAVMI
QPVSGPVCLF GTEFQKQICW EILVAGSEQG IEAGQVGLRL ITKGDRQTTV AKEWSISATS
IADGRWHLVT MTIDADLGEA TCYLDGGFDG YQTGLPLHVG NTIWEQGTEV WVGVRPPTDM
DAFGRSDSEG AESKMHIMDV FLWGRCLTED DIAALHSAIG STDSNMIDFP EDNWQWADSP
SRVDEWDSDP ADVDLYDRDD VDWDGQYSSG RKRRSERDGV LVDVDSFARR FRKPRMETRE
EINQRMLSVE LAVKEALSAR GEIHFTDQEF PPNDQSLFVD PENPPLKLQV VSEWVRPAEI
VKDSRLDAHP CLFSGTANPS DVCQGRLGDC WFLSAVAVLT EVSRISEVII TPEYNEEGIY
TVRFCIQGEW VPVVVDDWIP CESPGKPAFA TSRKGNELWV SLLEKAYAKL HGSYEALEGG
LVQDALVDLT GGAGEEIDMR SAQAQIDLAS GRLWSQLLRF KQEGFLLGAG SPSGSDVHVS
SSGIVQGHAY SLLQVREVDG YKLIQIRNPW ANEVEWNGPW SDSSPEWTDR MKHKLKHVPQ
SKDGIFWMSW QDFQIHFRSI YVCRIYPPEM RYSVHGQWRG YSAGGCQDYE TWHQNPQFRL
RATGPDAALP IHVFITLTQG VSFSRTVAGF RNYQSSHDSM MFYIGMRILK TRGRRAAYNI
YLHESVGGTD YVNSREISCE MVLDPDPKGY TIVPTTIHPG EEAPFVLSVF TKASITLEAL
//
