ID E7FAX5_DANRE Unreviewed; 1122 AA.
AC E7FAX5; A0A8M1RRB5;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Calpain 15 {ECO:0000313|Ensembl:ENSDARP00000080000};
DE SubName: Full=Calpain-15 isoform X2 {ECO:0000313|RefSeq:XP_002663893.2};
GN Name=capn15 {ECO:0000313|Ensembl:ENSDARP00000080000,
GN ECO:0000313|RefSeq:XP_002663893.2,
GN ECO:0000313|ZFIN:ZDB-GENE-140106-70};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000080000};
RN [1] {ECO:0000313|Ensembl:ENSDARP00000080000}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000080000};
RG Ensembl;
RL Submitted (JUL-2011) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSDARP00000080000, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000080000};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3] {ECO:0000313|RefSeq:XP_002663893.2}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_002663893.2};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase C2 family.
CC {ECO:0000256|ARBA:ARBA00007623}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CABZ01056607; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01056608; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FO905001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_002663893.2; XM_002663847.6.
DR PaxDb; 7955-ENSDARP00000080000; -.
DR Ensembl; ENSDART00000085565; ENSDARP00000080000; ENSDARG00000060600.
DR Ensembl; ENSDART00000085565.6; ENSDARP00000080000.4; ENSDARG00000060600.6.
DR GeneID; 100330198; -.
DR KEGG; dre:100330198; -.
DR AGR; ZFIN:ZDB-GENE-140106-70; -.
DR CTD; 6650; -.
DR ZFIN; ZDB-GENE-140106-70; capn15.
DR eggNOG; KOG0045; Eukaryota.
DR HOGENOM; CLU_003001_0_0_1; -.
DR OrthoDB; 142935at2759; -.
DR PhylomeDB; E7FAX5; -.
DR TreeFam; TF322245; -.
DR Proteomes; UP000000437; Chromosome 24.
DR Bgee; ENSDARG00000060600; Expressed in early embryo and 20 other cell types or tissues.
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; 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; 5.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 3.
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; 4.
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:UP000000437};
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 45..74
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 161..192
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 380..409
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 449..479
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 525..831
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1096..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..134
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..252
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..300
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 590
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 755
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 775
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 1122 AA; 122385 MW; 0A5C5160CC8FD37E CRC64;
MANSGPQKGK LKGQIKEEEK LGPSKGLPVL HNHSHSPGSM EAVVRNSDWS CGRCTFLNSS
GSMRCSICEA PRQKPDLNHI LRLSSAEEPR WSCPRCTLTN HHGLGSCSVC GAAPVTPNGP
LPPKQTPPTP IDLASSPEPK GQVANGESQC IESNGEVPMS GQGSSEWACP RCTLVNTPVA
LSCSACGGPR KLSLPKIPPE ALVVPEVRTP VAGFPTQTAG ASAPLLIDLT EDSPPQAPSE
TPSPPPVPFL PPSLSSLQNN PVPRSRREVP PPGRPPNPGP SPTSPSSCPP TKPKPLPPSG
NYPVKRLSVL EEEEPNNPTP PVTSPPSWKC PGCSAPTAPP SSSAGRCDAC RGSRPGSGGD
VIDVLGESVR FTPASPSSPD FSSWACSKCT LRNPTGAGHC TACGSSKLHG FSEPSSCSSC
SRKQPHSHPR AFTSTSSSSS ISSPSAQDKS VCQWTCPACT LLNEGRMKHC AACHTPQQYL
NLRKTGKPLK RRESMHVEAR RRTDEGEAKE LWENIVSFCR ENAVNFVDDS FPPGPRSVGF
PENDSVQQRI KKWLRPHEIN CNNFKDRGVK WSVFRTPRPS DILQGLLGNC WFLSALAVLA
ERPELVERVM ITRSICQEGA YQVRLCKDGM WTTVLVDDML PCDEYGFLLF SQAQRRQLWV
ALIEKALAKL HGSYFALQAG RAIEGLATLT GAPCESLMLQ VSSTNPREEP IDTDLIWAKM
LSSKEAGFLM GASCGGGNMK VDDAVYESLG LRPRHAYSIL DVRDVQGYRL LRLRNPWGRF
SWNGSWSDEW SDWPQHLRHE LMAHGSSEGV FWMEYGDFIK YFDSVDICKI HPDWQEVRLQ
GCFPCRASKP VTVTALTVLE RTALEFALFQ EGSRRSDTAD SHLLDLCIMV FRASFSNGNK
LVLGRLLAHS KRAVKKFVGC DVMLEPGEYA VVCCAFNHWQ MDLSGASTPV SSPTNARRPS
QDFPGYILAI YSSRQVMVEQ VEATSTTLAD AIILLTENKG ERHEGREGMT CYYLTHGWAG
LIVVVENRHP KYYLHVSCDC TDSFNVVSTR GSLKTIDSVP PLHRQVLVVL SQLEGNAGFS
ITHRLAHRKA AQASLGDWTS SKATHSPQLT PDTDGLHRPR PL
//