ID A0A3Q3AP90_KRYMA Unreviewed; 1149 AA.
AC A0A3Q3AP90;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Calpain 15 {ECO:0000313|Ensembl:ENSKMAP00000018663.1};
GN Name=CAPN15 {ECO:0000313|Ensembl:ENSKMAP00000018663.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000018663.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000018663.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase C2 family.
CC {ECO:0000256|ARBA:ARBA00007623}.
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DR RefSeq; XP_017273815.1; XM_017418326.1.
DR RefSeq; XP_017273816.1; XM_017418327.1.
DR Ensembl; ENSKMAT00000018905.1; ENSKMAP00000018646.1; ENSKMAG00000013861.1.
DR Ensembl; ENSKMAT00000018923.1; ENSKMAP00000018663.1; ENSKMAG00000013861.1.
DR GeneID; 108237120; -.
DR CTD; 6650; -.
DR GeneTree; ENSGT00940000158312; -.
DR OrthoDB; 142935at2759; -.
DR Proteomes; UP000264800; Unplaced.
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; 3.
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; 6.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 2.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 6.
DR PROSITE; PS50199; ZF_RANBP2_2; 5.
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:UP000264800};
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 6..35
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 137..169
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 320..351
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 374..403
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 472..501
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 547..853
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT REGION 193..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1123..1149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..287
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1123..1137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 612
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 777
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 797
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 1149 AA; 125024 MW; 89752ED40724938F CRC64;
MAAAVRGSEW SCGRCTFLNT GAAPRCSICE APRQKPDLNQ ILRLSSTEEH RWACPRCTLN
NPQGSGACSV CGFGSSSGTN TSPTTTIAVT VNGLPPAANE PLTPTTIPTV VLEPNGQLPA
KEEVLRRSES NGEVAGPEGQ NSGWACSRCT LHNTPVAMSC SACGGPRKLS LPKIPPEALV
VPEVRTPVLG FPVPTAGSAP LLIDLTDDST TTPPCDPQES PNVSSQALSS PFASFPSLQN
NPVPRSRREV PPPGRPQNPG TNTPSPTSPS TAIVPPQPGP QRPAKPKHAQ PQEPLYPSKR
LSILEEEDTP HHPVTPHLAS SAVPTWKCPS CSLPNPNGSS KCEACRSSQA GADLIDLVGC
ETVRFTPASP SSPDFSTWAC SKCTLRNPTG AHKCSACGSS KLHGFQEQQP PLARCCTHCG
LPTGSSTASC SCTPSSSGHK TRKQARGFPP SSSAVASSVS SSSSASPSFQ EKVGQWSCPA
CTLLNDIKAK NCAACHTPQQ YLTLRKVVKP LKRRESMHVE ARRRNDEGEA KELWENIVSF
CRENSVNFVD DSFPPGPRSV GFPEGDSVQQ RIKKWLRPHE INCSNFKDRG VKWSVFRTPR
PSDILQGLLG NCWFLSALAV LAERPELVER VMITRTICPE GAYQVRLCKD GTWTTVLVDD
MLPCDDYGYL LFSQAQRKQL WVALIEKALA KLHGSYFALQ AGRAIEGLAT LTGAPCDSLM
LQVSSTNPRE EPIDTDLIWA KMLSSKEAGF LMGASCGGGN MKVDDAIYES LGLRPRHAYS
ILDVRDVQGY RLLRLRNPWG RFSWNGNWSD EWTDWPQHLR RELMAHGSSE GVFWMEYTDF
IKYFDSVDIC KIHSDWQEVR LQGCFPSKAS GPITVTALTV LERTALEFAL FQEGSRRSDT
ADSHLLDLCI MVFRASFGSG NKLTLGRLLA HSKRAVKKFV GCDVMLEPGE YAVVCCAFNH
WQMNVSMAGG PPTPISSPTS GTGRRPSQDF PGYILAIYSS RQVMVEQVEA TSTTLADAII
LLTENKGERH EGREGMTCYY LTHGWAGLIV VVENRHPKYY LHVSCDCTDS FNVVSTRGSL
KTIDSVPPLH RQVLVVLSQL EGNAGFSITH RLAHRKAAQA SLGDWTPTKS THSPQLTPDI
DGLHRPRPL
//
