ID S4RHT9_PETMA Unreviewed; 1077 AA.
AC S4RHT9;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Calpain 15 {ECO:0000313|Ensembl:ENSPMAP00000004771.1};
GN Name=CAPN15 {ECO:0000313|Ensembl:ENSPMAP00000004771.1};
OS Petromyzon marinus (Sea lamprey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX NCBI_TaxID=7757 {ECO:0000313|Ensembl:ENSPMAP00000004771.1, ECO:0000313|Proteomes:UP000245300};
RN [1] {ECO:0000313|Ensembl:ENSPMAP00000004771.1}
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 AlphaFoldDB; S4RHT9; -.
DR STRING; 7757.ENSPMAP00000004771; -.
DR Ensembl; ENSPMAT00000004790.1; ENSPMAP00000004771.1; ENSPMAG00000004340.1.
DR GeneTree; ENSGT00940000158312; -.
DR OMA; GQLQCSI; -.
DR Proteomes; UP000245300; 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; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 4.
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:UP000245300};
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 3..32
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 151..180
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 348..373
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 380..411
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 411..440
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 485..789
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT REGION 96..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1042..1077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 549
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 713
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 733
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 1077 AA; 117766 MW; 7E1AED6F91647EFB CRC64;
MGSSGQWSCK RCTLLNPEGL SRCSICESPR MECNLENILR LSNGLSVNSG SLVAVEKTLN
CQACGGQQNA HTVTHCQACQ NSRTLFSTAS ELAQVARTSE KEAQPPEQKT DVSRDTADGI
CGMQTDTLPE NNNTVLPSLG TGLPSVASEI PKTTWVCRCC TLENNIADKA CNACGAPEKV
SLPIISPTVS EINVAVPNVI NPHSRQDAHP YPESVPIAGN VGEAERESPT PVLTAEGGEV
VSTSRSFDSE SPVERPALVR RFDVLPEPQP KGVRREEPAK QCTPEGSKPP KLFVSASNSS
GGKVSGNRNR PNSVAANDVP RSSEAIGSTA NLIKHKHTSS PSPHFLVWTC SQCTLVNSLK
NLECAACKAS KLQGLQQPPS VGKTGWICKQ CTYHNKAIDT VCAICQSDRS NPGAWVCSVC
TLHNDVKDKV CEACSNPKLK PQMKSMHKLQ RRESININAQ RNSDEKTAEE LRENIVQASK
ETGVNFVDDS FVPGKKSLGS NLESSIVQRV AHWLRPTQIT CAPHETTIPW VVFRTPRPSD
ILQGLLGNCW FLSALAVLAE RPQLVERVMV TRQICPEGAY QVRLCKDGVW QTVLVDDMLP
CDDNRCLLFS QAQRKQLWVP LIEKALAKLH GSYNALQAGR TIEGLATLTG APCESVQLQP
SPICPSEPID TDLIWAKLLS SKEAGFLMGA SCGGGNMKAD ETEYDRVGLR PRHAYSILDV
RDIEGHRLMR LRNPWGRFSW NGPWSDNSPE WTPQLRTELM AHGNSEGVFW MNYDDFKRYY
ESVDICKTHP DWNEVRLPGT FPVSHGRPIS ATLVSVFYHT EVDLTLFQEG ARRGDDVEGN
ILDLCIVIYQ VTTDKKEKMC LEKVIVHSQR AVKKFVSCSS MLAPGQYAII CLAFNHWQTA
GPTSPNSPTG GAGMLLPSLL YYILAVHSSK PVFVEQLVLP PSVLASAVIN LAVSKGQCHE
AREGMSCYYL TQGWAGLIVV VENRHPDRYL QVVCDCSDSF NVVSTRGGLK TADSVPPLNR
QVLLILSQLE ANSGFSVTHR LQHRKAGSPG LGDWGPRGHN HEPQLGPGLG LHSPRPL
//
