ID A0A2K5KH91_CERAT Unreviewed; 1153 AA.
AC A0A2K5KH91;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Calpain 15 {ECO:0000313|Ensembl:ENSCATP00000000056.1};
GN Name=CAPN15 {ECO:0000313|Ensembl:ENSCATP00000000056.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000000056.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000000056.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase C2 family.
CC {ECO:0000256|ARBA:ARBA00007623}.
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DR AlphaFoldDB; A0A2K5KH91; -.
DR STRING; 9531.ENSCATP00000000056; -.
DR Ensembl; ENSCATT00000000259.1; ENSCATP00000000056.1; ENSCATG00000000186.1.
DR GeneTree; ENSGT00940000158312; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000000186; Expressed in skeletal muscle tissue and 10 other cell types or tissues.
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; 2.
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; 3.
DR PRINTS; PR00704; CALPAIN.
DR SMART; SM00230; CysPc; 1.
DR SMART; SM00547; ZnF_RBZ; 5.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 4.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 5.
DR PROSITE; PS50199; ZF_RANBP2_2; 4.
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:UP000233060};
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 71..100
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 210..239
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 405..436
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 479..508
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 554..860
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 973..992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1131..1153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..300
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..331
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 619
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 784
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 804
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 1153 AA; 124207 MW; B12E797B798DF195 CRC64;
MGSSASSLAA ETESDHSFPR GPPYPGPPAA AGWCRSGPGG PIWGGALVSR QHQPPRPRAR
SHTHSPGSMA TAGEWSCARC TFLNPAGQRQ CSICEAPRHK PDLNHILRLS VEEQKWPCAR
CTFRNFLGKE ACEVCGFTPE PAPGAALLPV LNGVLPKPPA ILGEPKGNCQ EEAGPVRTAG
LVATEPARGQ HKDKDEEEQE EQEEEGAAEP RGGWACPRCT LHNTPVASSC SVCGGPRRLS
LPRIPPEALV VPEVVAPAGF HVVPAAPPPG LPAEGAEANP PATSQGPAAE PEPPRVPPFS
PFSSTLQNNP VPRSRREVPP QLQPPVPEAA QPSPSASCRG PPQGSGWAAA ARLAELLSGR
RLSVLEEEAM EGGSSRVEAS SSTSGSDVID LAGDTVRYTP ASPSSPDFTT WSCAKCTLRN
PTAAPRCSAC GCSKLHGFQE HGEPPTHCPD CGADKPCPCG RGCGRVSSTQ KATRVLPERP
GQWACPACTL LNAPRAKHCA ACHTPQLLVT QRRGAAPLRR RESMHVEQRR QTDEGEAKAL
WENIVAFCRE NNVSFVDDSF PPGPESVGFP AGDSVQQRVR QWLRPQEINC SVFRDHRTTW
SVFHTLRPSD ILQGLLGNCW FLSALAVLAE RPDLVERVMV TRSLCAEGAY QVRLCKDGTW
TTVLVDDMLP CDEAGCLLFS QAQRKQLWVA LIEKALAKLH GSYFALQAGR AIEGLATLTG
APCESLALQV SSTNPREEPV DTDLIWAKML SSKEAGFLMG ASCGGGNMKV DDSAYESLGL
RPRHAYSVLD VRDVQGTRLL RLRNPWGRFS WNGSWSDEWP HWPGHLRGEL MPHGSSEGVF
WMEYGDFVRY FDSVDICKVH SDWQEARVQG CFPSSASAPV GVTALTVLER ASLEFALFQE
GSRRSDAVDS HLLDLCILVF RATFGSGGHL SLGRLLAHSK RAVKKFVSCD VMLEPGEYAV
VCCAFNHWGP PPPGAPAPQA SSPSAGVPRA SPEPPGHVLA VYSSRLVMVE PVEAQPTTLA
DAIILLTESR GERHEGREGM TCYYLTHGWA GLIVVVENRH PKAYLHVQCD CTDSFNVVST
RGSLRTQDSV PPLHRQVLVI LSQLEGNAGF SITHRLAHRK AAQAFLSDWT ASKGTHSPPL
TPEVAGLHGP RPL
//
