ID A0A0D9RK01_CHLSB Unreviewed; 1001 AA.
AC A0A0D9RK01;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Calpain 15 {ECO:0000313|Ensembl:ENSCSAP00000008940.1};
GN Name=CAPN15 {ECO:0000313|Ensembl:ENSCSAP00000008940.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000008940.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000008940.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000008940.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase C2 family.
CC {ECO:0000256|ARBA:ARBA00007623}.
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; AQIB01152163; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A0D9RK01; -.
DR STRING; 60711.ENSCSAP00000008940; -.
DR Ensembl; ENSCSAT00000010855.1; ENSCSAP00000008940.1; ENSCSAG00000012760.1.
DR eggNOG; KOG0045; Eukaryota.
DR GeneTree; ENSGT00940000158312; -.
DR OMA; GQLQCSI; -.
DR Proteomes; UP000029965; Chromosome 5.
DR Bgee; ENSCSAG00000012760; Expressed in adrenal cortex and 7 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; 4.
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:UP000029965};
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 68..97
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 208..237
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 403..434
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 477..506
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 552..858
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT REGION 179..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..298
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..329
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 617
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 782
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 802
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 1001 AA; 107859 MW; 9FA597F6DB6A809C CRC64;
MKGWCTGRRS LGERGAACVS PAACGRRGAE VLYSCQGLTL SISKPVIDGL QTQRYKCSHT
HSPGSMATAG EWSCARCTFL NPAGQRQCSI CEAPRHKPDL NHILRLSVEE QKWPCARCTF
RNFLGKEACE VCGFTPEPAP GAALLPVLNG VLPKPPAILG EPKGNCQEEA GPVRTAGLVA
TEPARGQHED KDEEEQEEQE EEEGAAEPRG GWACPRCTLH NTPVASSCSV CGGPRRLSLP
RIPPEALVVP EVVAPAGFHV VPAAPPPGLP GEGAEANPPA TSQGPAAEPE PPRVPPFSPF
SSTLQNNPVP RSRREVPPQL QPPVPEAAQP SPSAGCRGPP QGSGWAAAAR LAELLSGKRL
SVLEEEAMEG GSSRVEASSS TSGSDIIDLA GDTVRYTPAN PSSPDFTTWS CAKCTLRNPT
AAPRCSACGC SKLHGFQEHG EPPTHCPDCG VDKPGPCGRG CGRVSSTQKA TRVLPERPGQ
WSCPACTLLN APRAKHCAAC HTPQLLVTQR RGAAPLRRRE SMHVEQRRQT DEGEAKALWE
NIVAFCRENN VSFVDDSFPP GPESVGFPAG DSVQQRVRQW LRPQEINCSV FRDHRATWSV
FHTLRPSDIL QGLLGNCWFL SALAVLAERP DLVERVMVTR SLCAEGAYQV RLCKDGTWTT
VLVDDMLPCD EAGCLLFSQA QRKQLWVALI EKALAKLHGS YFALQAGRAI EGLATLTGAP
CESLALQVSS TNPREEPVDT DLIWAKMLSS KEAGFLMGAS CGGGNMKVDD SAYESLGLRP
RHAYSVLDVR DVQGTRLLRL RNPWGRFSWN GSWSDEWPHW PGHLRGELMP HGSSEGVFWM
EYGDFVRYFD SVDICKVHSD WQEARVQGCF PSSASAPVGV TALTVLERAS LEFALFQEGS
RRSDAVDSHL LDLCILVFRA TFGSGGHLSL GRLLAHSKRA VKKFVSCDVM LEPGEYAVVC
CAFNHWGPPP PGAPAPQGTC PLPQAHAPGP RGGLRLTRPS L
//
