CAN_SCHMA
ID CAN_SCHMA Reviewed; 758 AA.
AC P27730;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Calpain;
DE EC=3.4.22.-;
DE AltName: Full=Calcium-activated neutral proteinase;
DE Short=CANP;
OS Schistosoma mansoni (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6183;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1775175; DOI=10.1016/0166-6851(91)90078-k;
RA Karcz S.R., Podesta R.B., Siddiqui A.A., Dekaban G.A., Strejan G.H.,
RA Clarke M.W.;
RT "Molecular cloning and sequence analysis of a calcium-activated neutral
RT protease (calpain) from Schistosoma mansoni.";
RL Mol. Biochem. Parasitol. 49:333-336(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Puerto Rican;
RX PubMed=1869543; DOI=10.1016/s0021-9258(18)98590-x;
RA Andresen K., Tom T.D., Strand M.;
RT "Characterization of cDNA clones encoding a novel calcium-activated neutral
RT proteinase from Schistosoma mansoni.";
RL J. Biol. Chem. 266:15085-15090(1991).
CC -!- FUNCTION: Calpains are calcium-activated non-lysosomal thiol-proteases.
CC -!- ACTIVITY REGULATION: Activated by free cytoplasmic calcium.
CC -!- DEVELOPMENTAL STAGE: In sporocysts and adult worms.
CC -!- MISCELLANEOUS: This protein binds calcium.
CC -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M74233; AAA29857.1; -; mRNA.
DR EMBL; M67499; AAA29858.1; -; mRNA.
DR PIR; A39343; A39343.
DR AlphaFoldDB; P27730; -.
DR SMR; P27730; -.
DR STRING; 6183.Smp_157500.1; -.
DR MEROPS; C02.023; -.
DR PRIDE; P27730; -.
DR eggNOG; KOG0045; Eukaryota.
DR HOGENOM; CLU_244471_0_0_1; -.
DR Proteomes; UP000008854; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00214; Calpain_III; 1.
DR CDD; cd00044; CysPc; 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; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
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 PRINTS; PR00704; CALPAIN.
DR SMART; SM00720; calpain_III; 1.
DR SMART; SM00230; CysPc; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF49758; SSF49758; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 2: Evidence at transcript level;
KW Calcium; Hydrolase; Metal-binding; Protease; Reference proteome; Repeat;
KW Thiol protease.
FT CHAIN 1..758
FT /note="Calpain"
FT /id="PRO_0000207735"
FT DOMAIN 99..397
FT /note="Calpain catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT DOMAIN 658..693
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 694..729
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 398..562
FT /note="Domain III"
FT REGION 563..582
FT /note="Linker"
FT REGION 583..757
FT /note="Domain IV"
FT ACT_SITE 154
FT /evidence="ECO:0000250"
FT ACT_SITE 313
FT /evidence="ECO:0000250"
FT ACT_SITE 337
FT /evidence="ECO:0000250"
FT BINDING 641
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 643
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 645
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 647
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 652
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 671
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 673
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 675
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 677
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 682
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="H -> L (in Ref. 2; AAA29858)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="R -> L (in Ref. 2; AAA29858)"
FT /evidence="ECO:0000305"
FT CONFLICT 385..387
FT /note="VTC -> CYL (in Ref. 2; AAA29858)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="S -> N (in Ref. 2; AAA29858)"
FT /evidence="ECO:0000305"
FT CONFLICT 755
FT /note="S -> R (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 757
FT /note="Y -> D (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 758 AA; 86863 MW; 9F5E0C98B6B2AF19 CRC64;
MGRIQIVYSP DENVSGRTNR PGKEVVDPRT GRIIKVKRET PDDYLNVLKP IKGPKRMEFN
PYLPKTLTPK GYAKFKLMMN VASKQYETLV KRLKTERTLW EDPDFPANDK AIGNLPDFRE
RIEWKRPHEI NPNAKFFAGG ASRFDIEQGA LGDCWLLAVV ASISGYPQLF DQVVPKDQEL
KGPEYVGVVR FRFWRFGHWV EVLIDDRLPV RQGRNTLVFM HSNDPTEFWS ALLEKAYAKL
NGCYAHLSGG SQSEAMEDLT GGICLSLELN QKERPSDLID QLKIYAQRCC LMGCSIDSSV
MEQKMDNGLI GSHAYSLTGV YPVNYRGRTQ WLMRLRNPWG DSHEWKGAWC DGSPQWREIS
EQEKKNINLS FTADGEFWMS YEDFVTCFSR VEVCHLGLES LEYNQNFHGK RRLDEAIFSG
QWQRNVNAGG CINNRTTYWT SPQFRITVED PDPDDDDNKC SVLIGLMQTD IRKKVGADFQ
PIGFMVYNAP DDLNTLLSRA QLLTRSPIAK SQFINTREVT AQFRVPPGSY VVIPSTFDPN
IEVNFILRVF SQTSITEQEL DEDNTNQGLP DDVIEALKLE DTLLDEDQEI EQKFLAIRDP
KTNAINAVKL GELLNNSTLQ DIPNFQGFNK ELCRSMVASV DNNLTGHVEL NEFMDLWIQA
KGWKHIFIKH DVDQSGYFSA YEFREALNDA GYHVSNRLIN AIINRYQDPG TDKISFEDFM
LCMVRLKTAF ETIEAHPKNI EGTSLFSAED YLRFSVYI
