ID W8BGV2_CERCA Unreviewed; 899 AA.
AC W8BGV2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Calpain-D {ECO:0000313|EMBL:JAB92486.1};
GN Name=CAND {ECO:0000313|EMBL:JAB92486.1};
OS Ceratitis capitata (Mediterranean fruit fly) (Tephritis capitata).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC Tephritidae; Ceratitis; Ceratitis.
OX NCBI_TaxID=7213 {ECO:0000313|EMBL:JAB92486.1};
RN [1] {ECO:0000313|EMBL:JAB92486.1}
RP NUCLEOTIDE SEQUENCE.
RA Geib S.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAB92486.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24495485; DOI=10.1186/1471-2164-15-98;
RA Calla B., Hall B., Hou S., Geib S.M.;
RT "A genomic perspective to assessing quality of mass-reared SIT flies used
RT in Mediterranean fruit fly (Ceratitis capitata) eradication in
RT California.";
RL BMC Genomics 15:98-98(2014).
CC -!- SIMILARITY: Belongs to the peptidase C2 family.
CC {ECO:0000256|ARBA:ARBA00007623}.
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DR EMBL; GAMC01014069; JAB92486.1; -; mRNA.
DR AlphaFoldDB; W8BGV2; -.
DR EnsemblMetazoa; XM_004536662.3; XP_004536719.1; LOC101457109.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00044; CysPc; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 1.
DR Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 2.
DR InterPro; IPR022684; Calpain_cysteine_protease.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR10183; CALPAIN; 1.
DR PANTHER; PTHR10183:SF382; CALPAIN-15; 1.
DR Pfam; PF00648; Peptidase_C2; 1.
DR Pfam; PF00641; zf-RanBP; 3.
DR PRINTS; PR00704; CALPAIN.
DR SMART; SM00230; CysPc; 1.
DR SMART; SM00547; ZnF_RBZ; 4.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 3.
DR PROSITE; PS50199; ZF_RANBP2_2; 3.
PE 2: Evidence at transcript level;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00239}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU00239};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807, ECO:0000256|PROSITE-
KW ProRule:PRU00239}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00322};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322}.
FT DOMAIN 59..88
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 99..129
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 236..265
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 319..626
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT REGION 172..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 384
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 550
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 570
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 899 AA; 100426 MW; 7CB5AA8DE7777F0C CRC64;
MLNNTRRTWT CSKCSYAYNR IWTDNCEICE SIRSQPTVEQ PSLITVTKSE NSITSAERIE
GKWTCKKCTL VNDPTSIACA VCGGSKLRSI CSVEDMTLRK GEFWTCNKCT LKNNLSTGIC
SACKSVRSLP IEPKRLQIKE INTEETVASH AADASSHFWQ PIAKTVNLQP SQIKVSRSPS
PREIQGSSGA IPKRHSTGGS ILTSNSGSVS TSVSPITALN DTTGQNRTNI VNSNTVSKMW
QCPACTYENC PASVVCDMCS SPRGLASSLN ESPLISAGKV TIDIRQESKL MENLRQIEEK
EALNKWKNII QYCSDNNELF VDDSFPPAPK SLYYNPTNSI PDGNPVVQWR RPHEISCEGG
TFPPWAVFRT PLPSDICQGV LGNCWLLSAL AVLAEREDLV KEVLVTKEIC LQGAYQVRLC
KDGKWITVLV DDLLPCDKRG HLVYSQAKRK QLWVPLIEKA VAKIHGCYEA LVSGRAIEGL
ATLTGAPCES IPLQASSLPM PSEDELDKDL IWAQLLSSRC VRFLMGASCG GGNMKVDEDE
YQRKGLRPRH AYSVLDVRDI QGHRLLKLRN PWGHYSWRGN WSDDSDLWTE DLREELMPHG
ASEGVFWISF EDVLNYFDCI DICKVRSGWN EVRLQDTLQP LCSISCVLLT VLEPTEAEFT
LFQEGQRNSE KSQRSQLDLC VVIFRTRSPV SPEIGRLVEH SKRQVRGFVG CHKMLERDIY
LLVCLAFNHW HTGIEEPHQY PQCVLAIHSS KRLLVEQITP SPHLLADAII SLTLSKGQRH
EGREGMTAYY LTKGWAGLVV MVENRHENKW IHVKCDCQES YNVVSTRGEL KTVDSVPPLQ
RQVIIVLTQL EGSGGFSIAH RLTHRLANSR GLHDWGPPGA THCPPIESVH GLHAPRLIT
//
