ID A0A3B3CE49_ORYME Unreviewed; 1206 AA.
AC A0A3B3CE49;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Calpain-15-like {ECO:0000313|Ensembl:ENSOMEP00000016201.1};
GN Name=CAPN15 {ECO:0000313|Ensembl:ENSOMEP00000016201.1};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000016201.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000016201.1}
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; A0A3B3CE49; -.
DR STRING; 30732.ENSOMEP00000016201; -.
DR PaxDb; 30732-ENSOMEP00000016201; -.
DR Ensembl; ENSOMET00000034311.1; ENSOMEP00000016201.1; ENSOMEG00000017877.1.
DR GeneTree; ENSGT00940000158312; -.
DR OrthoDB; 142935at2759; -.
DR Proteomes; UP000261560; 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; 4.
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; 6.
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};
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 72..101
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 202..235
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 381..410
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 432..461
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 529..558
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 604..910
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1181..1206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..350
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 669
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 834
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 854
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 1206 AA; 131176 MW; 9283E18D1217FB80 CRC64;
MGSSASSLAA ETESDHGFPS TPFSSSPPVG WLRNSHSSPV WGGTFITRQQ HPLPHRERSH
SHSPGSMAAA VRSSEWSCGR CTFLNAGAAP RCSICEAPRQ KPDLNKILRL SSGEEHRWAC
PRCTLNNPQE SGACSICGFG PSSDARNPPN TSLAVTPNGF QPSSEEPSAP TITSTVLLEP
HGQKPAKEEG LRPPESNGEV GDLGGLHSGW ACPRCTLHNT PMAMSCSACG GPRKLSLPKI
PPEALVVPEV HTPVQGFPVH TAGSAPLLID LTDDSPPPSS SDPQESPQGS SKTLSSPFTP
FSSLQNNPVP RSRREVPPPG RPAANTPSPT SPSTAVVPPQ PGPQQPSKPK HAQPQEPSYP
KKRLSILEEE EGQHHPQSSS AASTWKCPSC SLPNPGSSSK CEACRSSRAG SDLIDLVGET
VRFTPASPSS PDFSTWACSK CTLRNPTGAP KCSACGSSKL HGFQEQQPLL PRCCTNCGLP
SGPGTASCSC TPSSGHKARK QARGYPSSSS AVVPSGSSAF SSPSSLQEKV GQWSCPACTL
LNDIKAKNCA ACHTAQQYLT LRKVVKPLKR RESMHVEARR RNDEGEAKEL WENIVSFCRE
NSVNFVDDSF PPGPRSVGFP EGDSVQQRIK KWLRPHEINC SNFKDRSVKW SVFRTPRPSD
ILQGLLGNCW FLSALAVLAE RPELVERVMI TRTICHEGAY QIRLCKDGTW TTVLVDDMLP
CDEYGYLLFS QAQRKQLWVA LIEKALAKLH GSYFALQAGR AIEGLATLTG APCDSLMLQV
SSTNPREEPI DTDLIWAKML SSKEAGFLMG ASCGGGNMKV DDTVYESLGL RPRHAYSILD
VRDVQGYRLL RLRNPWGRFS WNGSWSDEWT DWPQHLRHEL MAHGSSEGVF WMEYSDFIKY
FDSVDICKIH SDWQEVRLQG CFPSKASGPV TVTALTVLER TALEFALFQE GSRRSDTADS
HLLDLCIMVF RASFGSGNKL TLGRLLAHSK RAVKKFVGCD VMLEPGEYAV VCCAFNHWQM
NVSGTGGPPT PISSPTSGAA RRPTQDFPGY ILAIYSSRQV MVEQVEATAT TLADAIILLT
ENKGERHEGR EGMTCYYLTH GWAGLIVVVE NRHPKYYLHV SCDCTDSFNV VSTRGSLKTI
DSVPPLHRQV LVVLSQLEGN AGFSITHRLA HRKAAQASLG DWTPTKATHS PQLTPDIDGL
HRPRPL
//
