ID A0A1X7UEV1_AMPQE Unreviewed; 685 AA.
AC A0A1X7UEV1;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Calpain-3 {ECO:0008006|Google:ProtNLM};
GN Name=100632502 {ECO:0000313|EnsemblMetazoa:Aqu2.1.26016_001};
OS Amphimedon queenslandica (Sponge).
OC Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha;
OC Haplosclerida; Niphatidae; Amphimedon.
OX NCBI_TaxID=400682 {ECO:0000313|EnsemblMetazoa:Aqu2.1.26016_001, ECO:0000313|Proteomes:UP000007879};
RN [1] {ECO:0000313|Proteomes:UP000007879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20686567; DOI=10.1038/nature09201;
RA Srivastava M., Simakov O., Chapman J., Fahey B., Gauthier M.E., Mitros T.,
RA Richards G.S., Conaco C., Dacre M., Hellsten U., Larroux C., Putnam N.H.,
RA Stanke M., Adamska M., Darling A., Degnan S.M., Oakley T.H.,
RA Plachetzki D.C., Zhai Y., Adamski M., Calcino A., Cummins S.F.,
RA Goodstein D.M., Harris C., Jackson D.J., Leys S.P., Shu S., Woodcroft B.J.,
RA Vervoort M., Kosik K.S., Manning G., Degnan B.M., Rokhsar D.S.;
RT "The Amphimedon queenslandica genome and the evolution of animal
RT complexity.";
RL Nature 466:720-726(2010).
RN [2] {ECO:0000313|Proteomes:UP000007879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lucas S., Shapiro H., Lindquist E., Tice H., Dalin E., Glavina del Rio T.,
RA Bruce D., Barry K., Pitluck S., Srivastava M., Simakov O., Chapman J.,
RA Mitros T., Hellsten U., Putnam N.H., Fahey B., Gauthier M., Larroux C.,
RA Richards G.S., Stanke M., Adamska M., Darling A., Dacre M., Degnan S.M.,
RA Zhai Y., Adamski M., Calcino A., Cummins S.F., Goodstein D.M., Harris C.,
RA Shu S., Woodcroft B., Leys S.P., Manning G., Degnan B.M., Rokhsar D.S.;
RT "The genome of the haplosclerid demosponge Amphimedon queenslandica and the
RT evolution of animal complexity.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:Aqu2.1.26016_001}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (MAY-2017) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase C2 family.
CC {ECO:0000256|ARBA:ARBA00007623}.
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DR RefSeq; XP_003388253.1; XM_003388205.3.
DR AlphaFoldDB; A0A1X7UEV1; -.
DR STRING; 400682.A0A1X7UEV1; -.
DR EnsemblMetazoa; Aqu2.1.26016_001; Aqu2.1.26016_001; Aqu2.1.26016.
DR GeneID; 100632502; -.
DR KEGG; aqu:100632502; -.
DR eggNOG; KOG0045; Eukaryota.
DR InParanoid; A0A1X7UEV1; -.
DR OMA; RASCVAN; -.
DR OrthoDB; 142935at2759; -.
DR Proteomes; UP000007879; 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 Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 1.10.238.10; EF-hand; 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; IPR018247; EF_Hand_1_Ca_BS.
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 InterPro; IPR001751; S100/CaBP7/8-like_CS.
DR PANTHER; PTHR10183; CALPAIN; 1.
DR PANTHER; PTHR10183:SF426; CALPAIN CATALYTIC DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01067; Calpain_III; 1.
DR Pfam; PF13202; EF-hand_5; 2.
DR Pfam; PF00648; Peptidase_C2; 1.
DR PRINTS; PR00704; CALPAIN.
DR SMART; SM00720; calpain_III; 1.
DR SMART; SM00230; CysPc; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF49758; Calpain large subunit, middle domain (domain III); 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS00303; S100_CABP; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00239};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU00239}; Reference proteome {ECO:0000313|Proteomes:UP000007879};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807, ECO:0000256|PROSITE-
KW ProRule:PRU00239}.
FT DOMAIN 48..345
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT DOMAIN 588..623
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 103
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 260
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 284
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 685 AA; 77535 MW; BE173C61C65AABCC CRC64;
MADQSVQMKI SIPGKAPEEG QGTSDLGTRV PAQDYEKLRR DCIRRGKLFE DPYFPASDQS
LFYSQKFPVK VEWKRPKEIV SDPQMFTGGS SRFDVVQGML GDCWLVAAIA SLTQDKKLIN
KVIPQNQGWG KGYAGIFRFH FWHFGEWIDI VIDDRLPTYN GKLIFIHSTD ENEFWSALLE
KAYAKLYGGF EALKGGKTSE ALTDFTGGVV ETYDLKKCDA TLFDTITRNA TRSCLMSCSI
KIEGRDEVEA KLDSGLIKGH AYSVTGAKTL NMKGKVIKLL RIRNPWGQKE WNGDWSDNSP
SWNQISADKR KEILEGESAK EDGEFYMSYE DFLKHFTDFE VCSVTVSEMQ EDEKIKSWNS
IIINGEWSTV KGTAGGCRNY PTFVKNPQYI VNLTEDSDGD GKCSVLIALM QKHRRKQKKM
GVQDLCIGFS IYKSPGDGSL LTKQYVDYNY STGTSGSFTN AREVMKRFDL DPGKYVIVPC
SFKPGEEGDF LLRVFTESYS EEQSADQEDK PATDADPRIA KIRGLFTRIA GDDEEVDSEE
LQDLLTATMS KDLSSSVFGI DACRSMIAML DVNKNGTLNF EEFQTLLETI AKWKQMFYKF
DRDRSGTLEK PEVTAAIRSL GYNISGEGMN VLFNRFARKR KYMLIDDFSA CLSRVKIMTD
TFNRKSKNGS IQLNLDEYYK ITLDA
//
