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CAN15_MOUSE
ID   CAN15_MOUSE             Reviewed;        1095 AA.
AC   Q9JLG8; Q6PEE9;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Calpain-15;
DE            EC=3.4.22.-;
DE   AltName: Full=Small optic lobes homolog;
GN   Name=Capn15; Synonyms=Solh;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/cJ;
RX   PubMed=10708520; DOI=10.1006/geno.1999.6098;
RA   Kamei M., Webb G.C., Heydon K., Hendry I.A., Young I.G., Campbell H.D.;
RT   "Solh, the mouse homologue of the Drosophila melanogaster small optic lobes
RT   gene: organization, chromosomal mapping, and localization of gene product
RT   to the olfactory bulb.";
RL   Genomics 64:82-89(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Fetal brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=32885237; DOI=10.1093/hmg/ddaa198;
RA   Zha C., Farah C.A., Holt R.J., Ceroni F., Al-Abdi L., Thuriot F.,
RA   Khan A.O., Helaby R., Levesque S., Alkuraya F.S., Kraus A., Ragge N.K.,
RA   Sossin W.S.;
RT   "Biallelic variants in the small optic lobe calpain CAPN15 are associated
RT   with congenital eye anomalies, deafness and other neurodevelopmental
RT   deficits.";
RL   Hum. Mol. Genet. 29:3054-3063(2020).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9JLG8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9JLG8-2; Sequence=VSP_023363, VSP_023364, VSP_023365;
CC   -!- TISSUE SPECIFICITY: Highly expressed in the brain and eye during
CC       development (PubMed:32885237). Expressed in olfactory bulbs (at protein
CC       level) (PubMed:10708520). {ECO:0000269|PubMed:10708520,
CC       ECO:0000269|PubMed:32885237}.
CC   -!- DISRUPTION PHENOTYPE: Knockout animals show significantly reduced
CC       viability. Homozygous knockout mice also weigh significantly less than
CC       their wild-type or heterozygous littermates. These mice also display
CC       severe developmental eye defects, including anophthalmia,
CC       microphthalmia, and cataract, and the presence of these phenotypes is
CC       significantly increased compared to wild-type or heterozygous mice.
CC       {ECO:0000269|PubMed:32885237}.
CC   -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
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DR   EMBL; AF180445; AAF62871.1; -; Genomic_DNA.
DR   EMBL; BC058094; AAH58094.1; -; mRNA.
DR   CCDS; CCDS28540.1; -. [Q9JLG8-1]
DR   RefSeq; NP_056645.1; NM_015830.1. [Q9JLG8-1]
DR   AlphaFoldDB; Q9JLG8; -.
DR   SMR; Q9JLG8; -.
DR   BioGRID; 206132; 2.
DR   STRING; 10090.ENSMUSP00000039528; -.
DR   iPTMnet; Q9JLG8; -.
DR   PhosphoSitePlus; Q9JLG8; -.
DR   MaxQB; Q9JLG8; -.
DR   PaxDb; Q9JLG8; -.
DR   PRIDE; Q9JLG8; -.
DR   ProteomicsDB; 265522; -. [Q9JLG8-1]
DR   ProteomicsDB; 265523; -. [Q9JLG8-2]
DR   Antibodypedia; 22715; 76 antibodies from 15 providers.
DR   DNASU; 50817; -.
DR   Ensembl; ENSMUST00000041641; ENSMUSP00000039528; ENSMUSG00000037326. [Q9JLG8-1]
DR   Ensembl; ENSMUST00000212149; ENSMUSP00000148718; ENSMUSG00000037326. [Q9JLG8-1]
DR   GeneID; 50817; -.
DR   KEGG; mmu:50817; -.
DR   UCSC; uc008bcz.1; mouse. [Q9JLG8-1]
DR   CTD; 6650; -.
DR   MGI; MGI:1355075; Capn15.
DR   VEuPathDB; HostDB:ENSMUSG00000037326; -.
DR   eggNOG; KOG0045; Eukaryota.
DR   GeneTree; ENSGT00940000158312; -.
DR   HOGENOM; CLU_003001_0_0_1; -.
DR   InParanoid; Q9JLG8; -.
DR   OMA; HELMPHG; -.
DR   PhylomeDB; Q9JLG8; -.
DR   TreeFam; TF322245; -.
DR   Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR   BioGRID-ORCS; 50817; 7 hits in 73 CRISPR screens.
DR   ChiTaRS; Capn15; mouse.
DR   PRO; PR:Q9JLG8; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q9JLG8; protein.
DR   Bgee; ENSMUSG00000037326; Expressed in motor neuron and 249 other tissues.
DR   ExpressionAtlas; Q9JLG8; baseline and differential.
DR   Genevisible; Q9JLG8; MM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   CDD; cd00044; CysPc; 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   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; SSF54001; 1.
DR   SUPFAM; SSF90209; SSF90209; 4.
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   1: Evidence at protein level;
KW   Alternative splicing; Hydrolase; Metal-binding; Phosphoprotein; Protease;
KW   Reference proteome; Repeat; Thiol protease; Zinc; Zinc-finger.
FT   CHAIN           1..1095
FT                   /note="Calpain-15"
FT                   /id="PRO_0000278771"
FT   DOMAIN          497..803
FT                   /note="Calpain catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT   ZN_FING         3..32
FT                   /note="RanBP2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT   ZN_FING         44..73
FT                   /note="RanBP2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT   ZN_FING         148..178
FT                   /note="RanBP2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT   ZN_FING         348..379
FT                   /note="RanBP2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT   ZN_FING         422..451
FT                   /note="RanBP2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT   REGION          96..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          204..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1074..1095
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..234
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..283
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        562
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        727
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        747
FT                   /evidence="ECO:0000250"
FT   MOD_RES         311
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75808"
FT   MOD_RES         345
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75808"
FT   MOD_RES         348
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75808"
FT   MOD_RES         1079
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75808"
FT   VAR_SEQ         921
FT                   /note="Q -> QGKGPSQMRPTPSFPTSEPQSPPTGKLLAPLSTPPT (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_023363"
FT   VAR_SEQ         978..1037
FT                   /note="GREGMTCYYLTHGWAGLIVVVENRHPKSYLHVQCDCTDSFNVVSTRGSLRTQ
FT                   DSVPPLHR -> VGGVLMGEGRGWATTSPGPPTLCLCPGSRGHDLLLPDSWLGGTHRGS
FT                   GEPAPQVLPACAM (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_023364"
FT   VAR_SEQ         1038..1095
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_023365"
SQ   SEQUENCE   1095 AA;  118719 MW;  081E1DFED2AE5D28 CRC64;
     MATVGEWSCA RCTFLNPAGQ RQCSICEAPR HKPDLDQILR LSVEEQKWPC ARCTFRNFLG
     KEACEVCGFT PEPVPGAPLL PIINGVLPKP PTILVEPKGS GKEEAGPVRT AGLVATEPAR
     GRPEGEEERE ERGEEEEKEQ EGEGERAEPG SGWACQRCTL HNTPVASSCS ACGGPRKLSL
     PRIPPEALVV PEVVAPTGFH VVPAPSQPVL PGEGAEADSP STSQGPTSTD QEPPRVPLFS
     PFSPTLQNNP VPRSRREVPP QLQPPVPEAV QSSASTSSKG PQQGPGRAAA GASRLAELLS
     GKELLPGKRL SVLEEEVPES SPARCESCSD VIDLAGDIVR YTPASPSSPD FTTWSCARCT
     LRNPTTAPRC SVCGGSKLHG FQEHSEPPTH CPDCGANKPG PCVGSCGRAP SAHKAVRLLP
     DRPGQWACPA CTLINTPRAK HCAACHTPQL LVTQCRGATP LRRRESMHVE KRRQTDEGEA
     KALWENIVAF CRENSVNFVD DSFPPGPASV GFPVGDSVQQ RVKQWLRPHE INCSVFRDHG
     TPWSVFHTLR PSDILQGLLG NCWFLSALAV LAERPDLVER VMVTRSLCAE GAYQVRLCKD
     GTWTTVLVDD MLPCDEAGFL LFSQAQRKQL WVALIEKALA KLHGSYFALQ AGRAIEGLAT
     LTGAPCESLA LQVSSTNPRE EPVDTDLIWA KMLSSKEAGF LMGASCGGGN MKVDDAAYES
     LGLRPRHAYS VLDVRDVQGS RLLRLRNPWG RFSWNGSWSD EWPHWPGHLR AELMPHGSSE
     GVFWMEYSDF IRYFDSVDIC KVHSDWQEAR VQGCFPSTAG GPVGVTALTV LERASLEFAL
     FQEGSRRSDS VDSHLLDLCI LVFRATFGTG GRLSLGRLLA HSKRAVKKFV NCDVMLEPGE
     YAVVCCAFNH WNPAPPGPPA QASSPSAGVP RGAPEPPGHV LAVYSSRLVM VEPVEAQPTT
     LADAIILLTE SRGERHEGRE GMTCYYLTHG WAGLIVVVEN RHPKSYLHVQ CDCTDSFNVV
     STRGSLRTQD SVPPLHRQVL VILSQLEGNA GFSITHRLAH RKAAQAFLSD WTASRGTHSP
     PLTPDVAGLH GPRPL
 
 
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