ID A0A2D0S0V5_ICTPU Unreviewed; 1106 AA.
AC A0A2D0S0V5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 2.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Calpain-15 isoform X1 {ECO:0000313|RefSeq:XP_017336388.2};
GN Name=capn15 {ECO:0000313|RefSeq:XP_017336388.2};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017336388.2};
RN [1] {ECO:0000313|RefSeq:XP_017336388.2}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017336388.2};
RG RefSeq;
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_017336388.2; XM_017480899.3.
DR AlphaFoldDB; A0A2D0S0V5; -.
DR KEGG; ipu:108272449; -.
DR OrthoDB; 142935at2759; -.
DR Proteomes; UP000221080; Chromosome 1.
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; 2.
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; 2.
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; 2.
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; 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 70..100
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 108..138
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 184..216
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 389..420
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 438..468
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 513..819
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 40..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1080..1106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..273
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..310
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1095
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 578
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 743
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 763
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 1106 AA; 120920 MW; 9D5C6F1C36CAABCC CRC64;
MGSSASSLTT EAEPEHGFSR SSYPATPPVG WIRNSHSSPV WGSREHTHHH THHRPRSLSH
SRGSMMEAIV LGSDWSCVRC TFLNTAGSPR CSICEAPRNK PDLNRILRLS SCWTCPRCTL
TNHSASGACS VCGAPPNSTN GPTPSSSSPS ISEPITSNSE PKRQHVDEDL IKKSEPNGEV
GNTEVGVVSG WACPRCTLVN TPTAMSCSAC GGPRKLSLPK IPPEALVVPE VRTPVSGFPA
QNAGAVLIDL TEDSPPNPAP SQTPSPPPNN TNFLPPSLSS LQNNPVPRSR REVPPPTSPS
TGPASKPKPL PSSEPIKRLS VLEEEEPSPN HPAPPSWKCP GCSAPSGPSV SSAGRCDACR
GPRQGTGPSA DVIDVLGESV RFTPATPSSP DFTSWACSKC TLRNPTGSAH CSACGTSKLH
GFSEPFTKKT SHTPRGTGQG EKWACPACTL LNEVCVKHCV ACHTAQRYLR TRKVKALRRR
ESVHVEQRRK TDEGEAKELW ENIVSFCREN AVNFVDDSFP PGPRSVGFPE SDSVQQRIKK
WLRPHEINCN NFKDRGVKWS VFRTPRPSDI LQGLLGNCWF LSALAVLAER PELVERVMIT
RSICPEGAYQ VRLCKDGTWT TVLVDDMLPC DEYGYLLFSQ AQRRQLWVAL IEKALAKLHG
SYFALQAGRA IEGLATLTGA PCDSLNLQVN NTNPREEPID TDLIWAKMIS SKEAGFLMGA
SCGGGNMKVD DAVYESLGLR PRHAYSILDV RDVQGYRLLR LRNPWGRFSW NGSWSDEWPD
WPQHLRHELM AHGSSEGVFW MEYGDFIKYF DSVDICKIHS DWHEVRVQGS FPSRASGPIT
VSALTVLERT ALEFALFQEG SRRSDSADNH LLDLCIMVFR ASFSSGNKLT LGRLLAHSKR
AVKKFVGCDV MLEPGEYAVV CCAFNHWNSG GTPVSSPTAP PRACPDSPGF ILAIYSSRQV
MVEQVEATAT TLADAIILLT ENKGERHEGR EGMTCYYLTH GWAGLIVVVE NRHPKFHLHV
SCDCTDSFNV VSTRGSLKTI DSVPPLHRQV LVVLSQLEGN AGFSITHRLA HRKAAQANLG
DWTPTKATHS PQLTPDTEGL HKPRPL
//
