ID V4AA66_LOTGI Unreviewed; 737 AA.
AC V4AA66;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Calpain catalytic domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=LOTGIDRAFT_104705 {ECO:0000313|EMBL:ESO93662.1};
OS Lottia gigantea (Giant owl limpet).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX NCBI_TaxID=225164 {ECO:0000313|EMBL:ESO93662.1, ECO:0000313|Proteomes:UP000030746};
RN [1] {ECO:0000313|EMBL:ESO93662.1, ECO:0000313|Proteomes:UP000030746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
CC -!- SIMILARITY: Belongs to the peptidase C2 family.
CC {ECO:0000256|ARBA:ARBA00007623}.
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DR EMBL; KB201890; ESO93662.1; -; Genomic_DNA.
DR RefSeq; XP_009055297.1; XM_009057049.1.
DR AlphaFoldDB; V4AA66; -.
DR STRING; 225164.V4AA66; -.
DR EnsemblMetazoa; LotgiT104705; LotgiP104705; LotgiG104705.
DR GeneID; 20229894; -.
DR KEGG; lgi:LOTGIDRAFT_104705; -.
DR CTD; 20229894; -.
DR HOGENOM; CLU_003001_1_0_1; -.
DR OMA; QIRHAYS; -.
DR OrthoDB; 142935at2759; -.
DR Proteomes; UP000030746; Unassembled WGS sequence.
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; 2.30.30.380; Zn-finger domain of Sec23/24; 1.
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; 1.
DR PRINTS; PR00704; CALPAIN.
DR SMART; SM00230; CysPc; 1.
DR SMART; SM00547; ZnF_RBZ; 2.
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; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
PE 3: Inferred from homology;
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}; Reference proteome {ECO:0000313|Proteomes:UP000030746};
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 63..92
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 137..444
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT REGION 22..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 202
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 365
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 385
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 737 AA; 83415 MW; 98CE742543A787EC CRC64;
MCTFENNAQD HKCHVCEFPK KGTVSKTTSD SSQNRENSRP ENGAVNKIRP KSEGDALTGA
KGNKNEWKCK RCTLLNSAGS ERCSVCESPR KPPSPSLPGT LSRQESSLME DLLKLEVEEA
LDRLECIRLF CKQNKEVFVD DSFPPAPKSL YVDHKSKLVA RNIQWLRPHE ITPYYQDEKS
LKWVIYRTPM PEDISQGILG DCWFLSSLAV LAERPELVER IILTKDYSYE GGYQVRLCKD
GMWTVVLIDD FLPCDQNGML VFSQAKRRQL WVPLIEKAMA KLHGCYEALV AGKCIEGLAT
LTGAPCESIN LQGDSTQGRV IEPDLIWAKL LSCRDLKFLM GASCGGGKMK TDFNHFQELG
LRSRHAYSIL DVQDVEGNKL LRLRNPWGRF SWKGDWSDKS SKWHTISSTV RNNLMIHGET
EGVFWISLDD LLKYFDSIDV CKIRPDWRET RIQGVFPRNA MEPMKIVKLT VFYTTELELG
LFQEGIRGNE STTLDLCLVV LREVKNTSTA AGRVVGGSKR ELKSFIGCNM MIEPGEYLVM
CLAFNHWTLG KLLSTYNSWE IEMLNIPSSS PLHHYVLSIH SSKAVMVDEI TTYRNRLYEH
ILPDAIIQLC IAHGHAQEIR DGVTLYNLMN GWAGGIFMVE NRLPQNYVQI WCECNDSSNV
VSTRGELETK DAVPALSRQI LMVLSHLERT QPYHLSRVIK NRLSTNQPGL GNWGSPVCNN
SPSLSPTIAL FHSPRPL
//
