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CAN5_HUMAN
ID   CAN5_HUMAN              Reviewed;         640 AA.
AC   O15484; O00263;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   12-FEB-2003, sequence version 2.
DT   03-AUG-2022, entry version 171.
DE   RecName: Full=Calpain-5;
DE            EC=3.4.22.-;
DE   AltName: Full=Calpain htra-3;
DE   AltName: Full=New calpain 3;
DE            Short=nCL-3;
GN   Name=CAPN5; Synonyms=NCL3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=9367857; DOI=10.1006/bbrc.1997.7571;
RA   Mugita N., Kimura Y., Ogawa M., Saya H., Nakao M.;
RT   "Identification of a novel, tissue-specific calpain htra-3; a human
RT   homologue of the Caenorhabditis elegans sex determination gene.";
RL   Biochem. Biophys. Res. Commun. 239:845-850(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pancreas;
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   NUCLEOTIDE SEQUENCE [MRNA] OF 1-633.
RC   TISSUE=Hippocampus;
RX   PubMed=9339374; DOI=10.1006/geno.1997.4870;
RA   Dear T.N., Matena K., Vingron M., Boehm T.;
RT   "A new subfamily of vertebrate calpains lacking a calmodulin-like domain:
RT   implications for calpain regulation and evolution.";
RL   Genomics 45:175-184(1997).
RN   [4]
RP   TISSUE SPECIFICITY, VARIANTS VRNI LEU-243 AND PRO-244, AND CHARACTERIZATION
RP   OF VARIANTS VRNI LEU-243 AND PRO-244.
RX   PubMed=23055945; DOI=10.1371/journal.pgen.1003001;
RA   Mahajan V.B., Skeie J.M., Bassuk A.G., Fingert J.H., Braun T.A.,
RA   Daggett H.T., Folk J.C., Sheffield V.C., Stone E.M.;
RT   "Calpain-5 mutations cause autoimmune uveitis, retinal neovascularization,
RT   and photoreceptor degeneration.";
RL   PLoS Genet. 8:E1003001-E1003001(2012).
CC   -!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease.
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in many tissues. Strong expression in the
CC       photoreceptor cells of the retina, with a punctate pattern of labeling
CC       over the nuclei and inner segments with less expression along the other
CC       segments and outer plexiform layer. {ECO:0000269|PubMed:23055945}.
CC   -!- DISEASE: Vitreoretinopathy, neovascular inflammatory (VRNI)
CC       [MIM:193235]: An autoimmune condition of the eye that sequentially
CC       mimics uveitis, retinitis pigmentosa, and proliferative diabetic
CC       retinopathy as it progresses to complete blindness. Patients present
CC       during the second or third decade of life with posterior uveitis and
CC       reduction of the electroretinogram b-wave. They become more symptomatic
CC       when cataracts, cystoid macular edema, and disk edema diminish visual
CC       acuity during the second stage. Severe vision loss begins during the
CC       third stage when proliferative retinal neovascularization and
CC       epiretinal membranes appear. There is an ongoing pigmentary retinal
CC       degeneration and peripheral visual field loss during all stages. In the
CC       fourth stage, proliferative vitreoretinopathy causes tractional retinal
CC       detachments at the macula and vitreous base. The fifth or end-stage
CC       disease is marked by phthisis. {ECO:0000269|PubMed:23055945}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
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DR   EMBL; U94346; AAC51869.1; -; mRNA.
DR   EMBL; BC018123; AAH18123.1; -; mRNA.
DR   EMBL; Y10552; CAA71584.1; -; mRNA.
DR   CCDS; CCDS8248.1; -.
DR   PIR; JC5772; JC5772.
DR   RefSeq; NP_004046.2; NM_004055.4.
DR   RefSeq; XP_016873712.1; XM_017018223.1.
DR   PDB; 6P3Q; X-ray; 2.80 A; A/B=1-343.
DR   PDBsum; 6P3Q; -.
DR   AlphaFoldDB; O15484; -.
DR   SMR; O15484; -.
DR   BioGRID; 107187; 13.
DR   IntAct; O15484; 5.
DR   STRING; 9606.ENSP00000278559; -.
DR   MEROPS; C02.011; -.
DR   iPTMnet; O15484; -.
DR   PhosphoSitePlus; O15484; -.
DR   SwissPalm; O15484; -.
DR   BioMuta; CAPN5; -.
DR   EPD; O15484; -.
DR   jPOST; O15484; -.
DR   MassIVE; O15484; -.
DR   MaxQB; O15484; -.
DR   PaxDb; O15484; -.
DR   PeptideAtlas; O15484; -.
DR   PRIDE; O15484; -.
DR   ProteomicsDB; 48688; -.
DR   Antibodypedia; 31220; 261 antibodies from 29 providers.
DR   DNASU; 726; -.
DR   Ensembl; ENST00000529629.5; ENSP00000432332.1; ENSG00000149260.18.
DR   Ensembl; ENST00000531028.2; ENSP00000467244.2; ENSG00000149260.18.
DR   Ensembl; ENST00000648180.1; ENSP00000498132.1; ENSG00000149260.18.
DR   GeneID; 726; -.
DR   KEGG; hsa:726; -.
DR   MANE-Select; ENST00000648180.1; ENSP00000498132.1; NM_004055.5; NP_004046.2.
DR   UCSC; uc001oxx.4; human.
DR   CTD; 726; -.
DR   DisGeNET; 726; -.
DR   GeneCards; CAPN5; -.
DR   HGNC; HGNC:1482; CAPN5.
DR   HPA; ENSG00000149260; Tissue enhanced (intestine).
DR   MalaCards; CAPN5; -.
DR   MIM; 193235; phenotype.
DR   MIM; 602537; gene.
DR   neXtProt; NX_O15484; -.
DR   OpenTargets; ENSG00000149260; -.
DR   Orphanet; 329211; Autosomal dominant neovascular inflammatory vitreoretinopathy.
DR   PharmGKB; PA26062; -.
DR   VEuPathDB; HostDB:ENSG00000149260; -.
DR   eggNOG; KOG0045; Eukaryota.
DR   GeneTree; ENSGT00940000156536; -.
DR   HOGENOM; CLU_010982_3_2_1; -.
DR   InParanoid; O15484; -.
DR   OrthoDB; 704215at2759; -.
DR   PhylomeDB; O15484; -.
DR   TreeFam; TF314748; -.
DR   BRENDA; 3.4.22.B25; 2681.
DR   PathwayCommons; O15484; -.
DR   Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR   SignaLink; O15484; -.
DR   BioGRID-ORCS; 726; 14 hits in 1073 CRISPR screens.
DR   ChiTaRS; CAPN5; human.
DR   GeneWiki; CAPN5; -.
DR   GenomeRNAi; 726; -.
DR   Pharos; O15484; Tbio.
DR   PRO; PR:O15484; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; O15484; protein.
DR   Bgee; ENSG00000149260; Expressed in mucosa of transverse colon and 146 other tissues.
DR   ExpressionAtlas; O15484; baseline and differential.
DR   Genevisible; O15484; HS.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR   GO; GO:0045202; C:synapse; IEA:Ensembl.
DR   GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   CDD; cd04046; C2_Calpain; 1.
DR   CDD; cd00214; Calpain_III; 1.
DR   CDD; cd00044; CysPc; 1.
DR   Gene3D; 2.60.40.150; -; 1.
DR   InterPro; IPR033884; C2_Calpain.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR033883; C2_III.
DR   InterPro; IPR022684; Calpain_cysteine_protease.
DR   InterPro; IPR022682; Calpain_domain_III.
DR   InterPro; IPR022683; Calpain_III.
DR   InterPro; IPR036213; Calpain_III_sf.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF01067; Calpain_III; 1.
DR   Pfam; PF00648; Peptidase_C2; 1.
DR   PRINTS; PR00704; CALPAIN.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00720; calpain_III; 1.
DR   SMART; SM00230; CysPc; 1.
DR   SUPFAM; SSF49562; SSF49562; 1.
DR   SUPFAM; SSF49758; SSF49758; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50203; CALPAIN_CAT; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Disease variant; Hydrolase; Protease; Reference proteome;
KW   Thiol protease.
FT   CHAIN           1..640
FT                   /note="Calpain-5"
FT                   /id="PRO_0000207713"
FT   DOMAIN          26..343
FT                   /note="Calpain catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT   DOMAIN          499..614
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   REGION          344..496
FT                   /note="Domain III"
FT   ACT_SITE        81
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        252
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        284
FT                   /evidence="ECO:0000250"
FT   VARIANT         243
FT                   /note="R -> L (in VRNI; largely mislocalized to the
FT                   cytoplasm whereas the wild-type protein is localized near
FT                   the cell surface; dbSNP:rs397514601)"
FT                   /evidence="ECO:0000269|PubMed:23055945"
FT                   /id="VAR_069277"
FT   VARIANT         244
FT                   /note="L -> P (in VRNI; largely mislocalized to the
FT                   cytoplasm whereas the wild-type protein is localized near
FT                   the cell surface; dbSNP:rs397514602)"
FT                   /evidence="ECO:0000269|PubMed:23055945"
FT                   /id="VAR_069278"
FT   CONFLICT        18
FT                   /note="R -> Q (in Ref. 1; AAC51869)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        51
FT                   /note="W -> R (in Ref. 3; CAA71584)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        112..115
FT                   /note="EKPN -> RKAQ (in Ref. 1; AAC51869)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        128..131
FT                   /note="FGEW -> LGM (in Ref. 1; AAC51869)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        138
FT                   /note="D -> E (in Ref. 1; AAC51869)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        502
FT                   /note="E -> K (in Ref. 1; AAC51869)"
FT                   /evidence="ECO:0000305"
FT   HELIX           8..10
FT                   /evidence="ECO:0007829|PDB:6P3Q"
FT   HELIX           13..23
FT                   /evidence="ECO:0007829|PDB:6P3Q"
FT   STRAND          30..32
FT                   /evidence="ECO:0007829|PDB:6P3Q"
FT   TURN            36..39
FT                   /evidence="ECO:0007829|PDB:6P3Q"
FT   HELIX           54..57
FT                   /evidence="ECO:0007829|PDB:6P3Q"
FT   STRAND          58..60
FT                   /evidence="ECO:0007829|PDB:6P3Q"
FT   HELIX           81..92
FT                   /evidence="ECO:0007829|PDB:6P3Q"
FT   HELIX           94..100
FT                   /evidence="ECO:0007829|PDB:6P3Q"
FT   HELIX           104..107
FT                   /evidence="ECO:0007829|PDB:6P3Q"
FT   STRAND          111..113
FT                   /evidence="ECO:0007829|PDB:6P3Q"
FT   HELIX           114..116
FT                   /evidence="ECO:0007829|PDB:6P3Q"
FT   STRAND          119..127
FT                   /evidence="ECO:0007829|PDB:6P3Q"
FT   STRAND          130..137
FT                   /evidence="ECO:0007829|PDB:6P3Q"
FT   STRAND          142..154
FT                   /evidence="ECO:0007829|PDB:6P3Q"
FT   HELIX           159..171
FT                   /evidence="ECO:0007829|PDB:6P3Q"
FT   HELIX           174..179
FT                   /evidence="ECO:0007829|PDB:6P3Q"
FT   HELIX           182..190
FT                   /evidence="ECO:0007829|PDB:6P3Q"
FT   STRAND          191..198
FT                   /evidence="ECO:0007829|PDB:6P3Q"
FT   HELIX           199..202
FT                   /evidence="ECO:0007829|PDB:6P3Q"
FT   HELIX           204..206
FT                   /evidence="ECO:0007829|PDB:6P3Q"
FT   HELIX           209..223
FT                   /evidence="ECO:0007829|PDB:6P3Q"
FT   STRAND          227..231
FT                   /evidence="ECO:0007829|PDB:6P3Q"
FT   HELIX           237..239
FT                   /evidence="ECO:0007829|PDB:6P3Q"
FT   STRAND          253..263
FT                   /evidence="ECO:0007829|PDB:6P3Q"
FT   HELIX           269..272
FT                   /evidence="ECO:0007829|PDB:6P3Q"
FT   STRAND          275..283
FT                   /evidence="ECO:0007829|PDB:6P3Q"
FT   HELIX           300..303
FT                   /evidence="ECO:0007829|PDB:6P3Q"
FT   HELIX           307..313
FT                   /evidence="ECO:0007829|PDB:6P3Q"
FT   STRAND          322..326
FT                   /evidence="ECO:0007829|PDB:6P3Q"
FT   HELIX           327..333
FT                   /evidence="ECO:0007829|PDB:6P3Q"
FT   STRAND          335..341
FT                   /evidence="ECO:0007829|PDB:6P3Q"
SQ   SEQUENCE   640 AA;  73169 MW;  7A3A9A1A920410BC CRC64;
     MFSCVKPYED QNYSALRRDC RRRKVLFEDP LFPATDDSLY YKGTPGPAVR WKRPKGICED
     PRLFVDGISS HDLHQGQVGN CWFVAACSSL ASRESLWQKV IPDWKEQEWD PEKPNAYAGI
     FHFHFWRFGE WVDVVIDDRL PTVNNQLIYC HSNSRNEFWC ALVEKAYAKL AGCYQALDGG
     NTADALVDFT GGVSEPIDLT EGDFANDETK RNQLFERMLK VHSRGGLISA SIKAVTAADM
     EARLACGLVK GHAYAVTDVR KVRLGHGLLA FFKSEKLDMI RLRNPWGERE WNGPWSDTSE
     EWQKVSKSER EKMGVTVQDD GEFWMTFEDV CRYFTDIIKC RVINTSHLSI HKTWEEARLH
     GAWTLHEDPR QNRGGGCINH KDTFFQNPQY IFEVKKPEDE VLICIQQRPK RSTRREGKGE
     NLAIGFDIYK VEENRQYRMH SLQHKAASSI YINSRSVFLR TDQPEGRYVI IPTTFEPGHT
     GEFLLRVFTD VPSNCRELRL DEPPHTCWSS LCGYPQLVTQ VHVLGAAGLK DSPTGANSYV
     IIKCEGDKVR SAVQKGTSTP EYNVKGIFYR KKLSQPITVQ VWNHRVLKDE FLGQVHLKAD
     PDNLQALHTL HLRDRNSRQP SNLPGTVAVH ILSSTSLMAV
 
 
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