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Protein

Calpain-5

Gene

CAPN5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Broad endopeptidase specificity.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei81By similarity1
Active sitei252By similarity1
Active sitei284By similarity1

GO - Molecular functioni

  • calcium-dependent cysteine-type endopeptidase activity Source: ProtInc

GO - Biological processi

  • signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

BioCyciZFISH:ENSG00000149260-MONOMER.
BRENDAi3.4.22.B25. 2681.
ReactomeiR-HSA-1474228. Degradation of the extracellular matrix.

Protein family/group databases

MEROPSiC02.011.

Names & Taxonomyi

Protein namesi
Recommended name:
Calpain-5 (EC:3.4.22.-)
Alternative name(s):
Calpain htra-3
New calpain 3
Short name:
nCL-3
Gene namesi
Name:CAPN5
Synonyms:NCL3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:1482. CAPN5.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • cytoplasm Source: GO_Central
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Vitreoretinopathy, neovascular inflammatory (VRNI)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autoimmune condition of the eye that sequentially mimics uveitis, retinitis pigmentosa, and proliferative diabetic retinopathy as it progresses to complete blindness. Patients present during the second or third decade of life with posterior uveitis and reduction of the electroretinogram b-wave. They become more symptomatic when cataracts, cystoid macular edema, and disk edema diminish visual acuity during the second stage. Severe vision loss begins during the third stage when proliferative retinal neovascularization and epiretinal membranes appear. There is an ongoing pigmentary retinal degeneration and peripheral visual field loss during all stages. In the fourth stage, proliferative vitreoretinopathy causes tractional retinal detachments at the macula and vitreous base. The fifth or end-stage disease is marked by phthisis.
See also OMIM:193235
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_069277243R → L in VRNI; largely mislocalized to the cytoplasm whereas the wild-type protein is localized near the cell surface. 1 PublicationCorresponds to variant rs397514601dbSNPEnsembl.1
Natural variantiVAR_069278244L → P in VRNI; largely mislocalized to the cytoplasm whereas the wild-type protein is localized near the cell surface. 1 PublicationCorresponds to variant rs397514602dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi726.
MalaCardsiCAPN5.
MIMi193235. phenotype.
OpenTargetsiENSG00000149260.
Orphaneti329211. Autosomal dominant neovascular inflammatory vitreoretinopathy.
PharmGKBiPA26062.

Polymorphism and mutation databases

BioMutaiCAPN5.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002077131 – 640Calpain-5Add BLAST640

Proteomic databases

EPDiO15484.
MaxQBiO15484.
PaxDbiO15484.
PeptideAtlasiO15484.
PRIDEiO15484.

PTM databases

iPTMnetiO15484.
PhosphoSitePlusiO15484.
SwissPalmiO15484.

Expressioni

Tissue specificityi

Expressed in many tissues. Strong expression in the photoreceptor cells of the retina, with a punctate pattern of labeling over the nuclei and inner segments with less expression along the other segments and outer plexiform layer.1 Publication

Gene expression databases

BgeeiENSG00000149260.
CleanExiHS_CAPN5.
ExpressionAtlasiO15484. baseline and differential.
GenevisibleiO15484. HS.

Organism-specific databases

HPAiCAB033237.
HPA060614.

Interactioni

Protein-protein interaction databases

BioGridi107187. 3 interactors.
IntActiO15484. 1 interactor.
STRINGi9606.ENSP00000278559.

Structurei

3D structure databases

ProteinModelPortaliO15484.
SMRiO15484.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini26 – 343Calpain catalyticPROSITE-ProRule annotationAdd BLAST318
Domaini518 – 619C2Add BLAST102

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni344 – 496Domain IIIAdd BLAST153

Sequence similaritiesi

Belongs to the peptidase C2 family.Curated
Contains 1 C2 domain.Curated
Contains 1 calpain catalytic domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0045. Eukaryota.
ENOG410XP0B. LUCA.
GeneTreeiENSGT00760000118971.
HOGENOMiHOG000232036.
HOVERGENiHBG001095.
InParanoidiO15484.
KOiK08574.
PhylomeDBiO15484.
TreeFamiTF314748.

Family and domain databases

CDDicd04046. C2_Calpain. 1 hit.
cd00214. Calpain_III. 1 hit.
cd00044. CysPc. 1 hit.
Gene3Di2.60.40.150. 1 hit.
InterProiIPR033884. C2_Calpain.
IPR000008. C2_dom.
IPR033883. C2_III.
IPR022684. Calpain_cysteine_protease.
IPR022682. Calpain_domain_III.
IPR022683. Calpain_III.
IPR000169. Pept_cys_AS.
IPR001300. Peptidase_C2_calpain_cat.
[Graphical view]
PfamiPF01067. Calpain_III. 1 hit.
PF00648. Peptidase_C2. 1 hit.
[Graphical view]
PRINTSiPR00704. CALPAIN.
SMARTiSM00239. C2. 1 hit.
SM00720. calpain_III. 1 hit.
SM00230. CysPc. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF49758. SSF49758. 1 hit.
PROSITEiPS50203. CALPAIN_CAT. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O15484-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFSCVKPYED QNYSALRRDC RRRKVLFEDP LFPATDDSLY YKGTPGPAVR
60 70 80 90 100
WKRPKGICED PRLFVDGISS HDLHQGQVGN CWFVAACSSL ASRESLWQKV
110 120 130 140 150
IPDWKEQEWD PEKPNAYAGI FHFHFWRFGE WVDVVIDDRL PTVNNQLIYC
160 170 180 190 200
HSNSRNEFWC ALVEKAYAKL AGCYQALDGG NTADALVDFT GGVSEPIDLT
210 220 230 240 250
EGDFANDETK RNQLFERMLK VHSRGGLISA SIKAVTAADM EARLACGLVK
260 270 280 290 300
GHAYAVTDVR KVRLGHGLLA FFKSEKLDMI RLRNPWGERE WNGPWSDTSE
310 320 330 340 350
EWQKVSKSER EKMGVTVQDD GEFWMTFEDV CRYFTDIIKC RVINTSHLSI
360 370 380 390 400
HKTWEEARLH GAWTLHEDPR QNRGGGCINH KDTFFQNPQY IFEVKKPEDE
410 420 430 440 450
VLICIQQRPK RSTRREGKGE NLAIGFDIYK VEENRQYRMH SLQHKAASSI
460 470 480 490 500
YINSRSVFLR TDQPEGRYVI IPTTFEPGHT GEFLLRVFTD VPSNCRELRL
510 520 530 540 550
DEPPHTCWSS LCGYPQLVTQ VHVLGAAGLK DSPTGANSYV IIKCEGDKVR
560 570 580 590 600
SAVQKGTSTP EYNVKGIFYR KKLSQPITVQ VWNHRVLKDE FLGQVHLKAD
610 620 630 640
PDNLQALHTL HLRDRNSRQP SNLPGTVAVH ILSSTSLMAV
Length:640
Mass (Da):73,169
Last modified:February 12, 2003 - v2
Checksum:i7A3A9A1A920410BC
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti18R → Q in AAC51869 (PubMed:9367857).Curated1
Sequence conflicti51W → R in CAA71584 (PubMed:9339374).Curated1
Sequence conflicti112 – 115EKPN → RKAQ in AAC51869 (PubMed:9367857).Curated4
Sequence conflicti128 – 131FGEW → LGM in AAC51869 (PubMed:9367857).Curated4
Sequence conflicti138D → E in AAC51869 (PubMed:9367857).Curated1
Sequence conflicti502E → K in AAC51869 (PubMed:9367857).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_069277243R → L in VRNI; largely mislocalized to the cytoplasm whereas the wild-type protein is localized near the cell surface. 1 PublicationCorresponds to variant rs397514601dbSNPEnsembl.1
Natural variantiVAR_069278244L → P in VRNI; largely mislocalized to the cytoplasm whereas the wild-type protein is localized near the cell surface. 1 PublicationCorresponds to variant rs397514602dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U94346 mRNA. Translation: AAC51869.1.
BC018123 mRNA. Translation: AAH18123.1.
Y10552 mRNA. Translation: CAA71584.1.
CCDSiCCDS8248.1.
PIRiJC5772.
RefSeqiNP_004046.2. NM_004055.4.
UniGeneiHs.248153.

Genome annotation databases

EnsembliENST00000278559; ENSP00000278559; ENSG00000149260.
ENST00000529629; ENSP00000432332; ENSG00000149260.
GeneIDi726.
KEGGihsa:726.
UCSCiuc001oxx.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U94346 mRNA. Translation: AAC51869.1.
BC018123 mRNA. Translation: AAH18123.1.
Y10552 mRNA. Translation: CAA71584.1.
CCDSiCCDS8248.1.
PIRiJC5772.
RefSeqiNP_004046.2. NM_004055.4.
UniGeneiHs.248153.

3D structure databases

ProteinModelPortaliO15484.
SMRiO15484.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107187. 3 interactors.
IntActiO15484. 1 interactor.
STRINGi9606.ENSP00000278559.

Protein family/group databases

MEROPSiC02.011.

PTM databases

iPTMnetiO15484.
PhosphoSitePlusiO15484.
SwissPalmiO15484.

Polymorphism and mutation databases

BioMutaiCAPN5.

Proteomic databases

EPDiO15484.
MaxQBiO15484.
PaxDbiO15484.
PeptideAtlasiO15484.
PRIDEiO15484.

Protocols and materials databases

DNASUi726.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000278559; ENSP00000278559; ENSG00000149260.
ENST00000529629; ENSP00000432332; ENSG00000149260.
GeneIDi726.
KEGGihsa:726.
UCSCiuc001oxx.4. human.

Organism-specific databases

CTDi726.
DisGeNETi726.
GeneCardsiCAPN5.
HGNCiHGNC:1482. CAPN5.
HPAiCAB033237.
HPA060614.
MalaCardsiCAPN5.
MIMi193235. phenotype.
602537. gene.
neXtProtiNX_O15484.
OpenTargetsiENSG00000149260.
Orphaneti329211. Autosomal dominant neovascular inflammatory vitreoretinopathy.
PharmGKBiPA26062.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0045. Eukaryota.
ENOG410XP0B. LUCA.
GeneTreeiENSGT00760000118971.
HOGENOMiHOG000232036.
HOVERGENiHBG001095.
InParanoidiO15484.
KOiK08574.
PhylomeDBiO15484.
TreeFamiTF314748.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000149260-MONOMER.
BRENDAi3.4.22.B25. 2681.
ReactomeiR-HSA-1474228. Degradation of the extracellular matrix.

Miscellaneous databases

ChiTaRSiCAPN5. human.
GeneWikiiCAPN5.
GenomeRNAii726.
PROiO15484.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000149260.
CleanExiHS_CAPN5.
ExpressionAtlasiO15484. baseline and differential.
GenevisibleiO15484. HS.

Family and domain databases

CDDicd04046. C2_Calpain. 1 hit.
cd00214. Calpain_III. 1 hit.
cd00044. CysPc. 1 hit.
Gene3Di2.60.40.150. 1 hit.
InterProiIPR033884. C2_Calpain.
IPR000008. C2_dom.
IPR033883. C2_III.
IPR022684. Calpain_cysteine_protease.
IPR022682. Calpain_domain_III.
IPR022683. Calpain_III.
IPR000169. Pept_cys_AS.
IPR001300. Peptidase_C2_calpain_cat.
[Graphical view]
PfamiPF01067. Calpain_III. 1 hit.
PF00648. Peptidase_C2. 1 hit.
[Graphical view]
PRINTSiPR00704. CALPAIN.
SMARTiSM00239. C2. 1 hit.
SM00720. calpain_III. 1 hit.
SM00230. CysPc. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF49758. SSF49758. 1 hit.
PROSITEiPS50203. CALPAIN_CAT. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCAN5_HUMAN
AccessioniPrimary (citable) accession number: O15484
Secondary accession number(s): O00263
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: February 12, 2003
Last modified: November 30, 2016
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.