ID G3UN93_LOXAF Unreviewed; 1045 AA.
AC G3UN93;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Calpain 15 {ECO:0000313|Ensembl:ENSLAFP00000029302.1};
GN Name=CAPN15 {ECO:0000313|Ensembl:ENSLAFP00000029302.1};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000029302.1, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000029302.1, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000029302.1,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000029302.1}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000029302.1};
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; G3UN93; -.
DR STRING; 9785.ENSLAFP00000029302; -.
DR Ensembl; ENSLAFT00000025787.1; ENSLAFP00000029302.1; ENSLAFG00000029213.1.
DR eggNOG; KOG0045; Eukaryota.
DR GeneTree; ENSGT00940000158312; -.
DR HOGENOM; CLU_003001_0_0_1; -.
DR InParanoid; G3UN93; -.
DR OMA; GQLQCSI; -.
DR TreeFam; TF322245; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
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; 1.
DR Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 2.
DR InterPro; IPR022684; Calpain_cysteine_protease.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
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; 3.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 3.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 3.
DR PROSITE; PS50199; ZF_RANBP2_2; 3.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00239};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU00239};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW Thiol protease {ECO:0000256|PROSITE-ProRule:PRU00239};
KW 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 44..73
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 129..158
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 440..747
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT REGION 183..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1024..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 506
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 671
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 691
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 1045 AA; 113354 MW; D2E9647F3EF82C6C CRC64;
MAAVREWSCT RCTFLNPAGQ RQCAICEAPR QKPDLDQILR LSVEEQKWPC PRCTFRNFLG
KEACEVCGFA PDPAPGAPLA PIINGALPTT PAVLAEPRGS CQKETGPVQT AGRAAVEPAG
WCPKEVVTEP GAWACPRCTL HNTPVASSCS ACGGPRRLSL PRIPPEALVV PEVVAPARFH
AGLTPPPPGL PGDSTEATPV SASQGVPTAN QEPLRRRESV LVEKRRLTDE GEAKALWEHI
VAFCREVSSW GQKGGRGVMG AEGGTGRHRV VGGGSGWWAW AWPASHPPVT TSGHRCWRVG
VGAGDMEALG RARVRASNFT LSCGRHWPCS SPSTLRSQGR PAAPTHHIPL LARVPDLGPT
SWERTWVACL GYLPDSSGMG AVLSPGPTPS HTTKQACLGP ALDGGCGIQP PLADTSASGV
PVLHRVSWRP VGLCSVNGVN FVDDSFPPGP ASVGFPEGDG VQQRVRQWLR PHEINCSVFK
DPSPVQWSVF CRLRPSDILQ GLLGNCRFLS ALAVLAERPD LVERVMVTRD LCPEGAYQVR
LCKDGTWTTV LVDDMLPCDE GGYLLFSQAQ RKQLWVALIE KALAKLHGSY FALQAGRAIE
GLATLTGAPC ESLLLQVSST NPREEPVDTD LIWAKMLSSK EAGFLMGASC GGGNMKVDDA
AYESLGLRPR HAYSILDVRE VQGSRLLRLR NPWGRFSWNG SWSDEWPHWP GHLRGELVPL
SSGEGVFWME YSDFIRYFDS VDICKARSDW QEVRVQGCFP RSASRPVGVT TLTVLERTSL
DFALFQEGSR RSDAGDSHLL DLCILVFRAN FGRGGRLCLG RLLAHSKRAV KKFVNCDVML
EPGEYAVVCC AFNHWGTSPT ATQGNWAPGQ APSSMSGSLR YTPEPPGHVL AVYSSRLVMV
EPVEAQPTTL ADAIILLTES QGERHEQGRE GMTCYYLTHG WAGLIVVVEN RHPRSYLHVQ
CDCTDSFNVV STRGSLRTHD SVPPLHRQVL VILSQLEGNA GFSITHRLAH RKAAQAFLND
WTATKGTHSP PLTPEVAGLH GPRPL
//
