CAN7_HUMAN
ID CAN7_HUMAN Reviewed; 813 AA.
AC Q9Y6W3;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Calpain-7;
DE EC=3.4.22.-;
DE AltName: Full=PalB homolog;
DE Short=PalBH;
GN Name=CAPN7; Synonyms=PALBH;
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].
RX PubMed=11342116; DOI=10.1016/s0167-4781(00)00256-6;
RA Futai E., Kubo T., Sorimachi H., Suzuki K., Maeda T.;
RT "Molecular cloning of PalBH, a mammalian homologue of the Aspergillus
RT atypical calpain PalB.";
RL Biochim. Biophys. Acta 1517:316-319(2001).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-95, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [3]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q9Y6W3; A0A087WVE9: ARNT2; NbExp=3; IntAct=EBI-1765641, EBI-12808086;
CC Q9Y6W3; Q9Y2T1: AXIN2; NbExp=3; IntAct=EBI-1765641, EBI-4400025;
CC Q9Y6W3; Q96MT8-3: CEP63; NbExp=3; IntAct=EBI-1765641, EBI-11522539;
CC Q9Y6W3; P56545-3: CTBP2; NbExp=3; IntAct=EBI-1765641, EBI-10171902;
CC Q9Y6W3; Q08379: GOLGA2; NbExp=3; IntAct=EBI-1765641, EBI-618309;
CC Q9Y6W3; Q13099: IFT88; NbExp=3; IntAct=EBI-1765641, EBI-347427;
CC Q9Y6W3; P53990: IST1; NbExp=6; IntAct=EBI-1765641, EBI-945994;
CC Q9Y6W3; Q9Y6D9: MAD1L1; NbExp=3; IntAct=EBI-1765641, EBI-742610;
CC Q9Y6W3; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-1765641, EBI-716006;
CC Q9Y6W3; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-1765641, EBI-1105153;
CC Q9Y6W3; Q14558: PRPSAP1; NbExp=3; IntAct=EBI-1765641, EBI-724449;
CC Q9Y6W3; Q13829: TNFAIP1; NbExp=3; IntAct=EBI-1765641, EBI-2505861;
CC Q9Y6W3; P14373: TRIM27; NbExp=3; IntAct=EBI-1765641, EBI-719493;
CC Q9Y6W3; Q8N720: ZNF655; NbExp=3; IntAct=EBI-1765641, EBI-625509;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
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DR EMBL; AB028639; BAA78730.1; -; mRNA.
DR CCDS; CCDS2624.1; -.
DR RefSeq; NP_055111.1; NM_014296.2.
DR PDB; 2QFE; X-ray; 1.45 A; A=684-813.
DR PDBsum; 2QFE; -.
DR AlphaFoldDB; Q9Y6W3; -.
DR SMR; Q9Y6W3; -.
DR BioGRID; 117033; 34.
DR IntAct; Q9Y6W3; 26.
DR MINT; Q9Y6W3; -.
DR STRING; 9606.ENSP00000253693; -.
DR MEROPS; C02.029; -.
DR GlyGen; Q9Y6W3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y6W3; -.
DR PhosphoSitePlus; Q9Y6W3; -.
DR BioMuta; CAPN7; -.
DR DMDM; 33112239; -.
DR EPD; Q9Y6W3; -.
DR jPOST; Q9Y6W3; -.
DR MassIVE; Q9Y6W3; -.
DR MaxQB; Q9Y6W3; -.
DR PaxDb; Q9Y6W3; -.
DR PeptideAtlas; Q9Y6W3; -.
DR PRIDE; Q9Y6W3; -.
DR ProteomicsDB; 86800; -.
DR Antibodypedia; 11065; 103 antibodies from 23 providers.
DR DNASU; 23473; -.
DR Ensembl; ENST00000253693.7; ENSP00000253693.2; ENSG00000131375.10.
DR GeneID; 23473; -.
DR KEGG; hsa:23473; -.
DR MANE-Select; ENST00000253693.7; ENSP00000253693.2; NM_014296.3; NP_055111.1.
DR UCSC; uc003bzn.4; human.
DR CTD; 23473; -.
DR DisGeNET; 23473; -.
DR GeneCards; CAPN7; -.
DR HGNC; HGNC:1484; CAPN7.
DR HPA; ENSG00000131375; Low tissue specificity.
DR MIM; 606400; gene.
DR neXtProt; NX_Q9Y6W3; -.
DR OpenTargets; ENSG00000131375; -.
DR PharmGKB; PA26064; -.
DR VEuPathDB; HostDB:ENSG00000131375; -.
DR eggNOG; KOG0045; Eukaryota.
DR GeneTree; ENSGT00940000155892; -.
DR HOGENOM; CLU_006770_2_0_1; -.
DR InParanoid; Q9Y6W3; -.
DR OMA; CSTFAPD; -.
DR OrthoDB; 343870at2759; -.
DR PhylomeDB; Q9Y6W3; -.
DR TreeFam; TF322245; -.
DR BRENDA; 3.4.22.B27; 2681.
DR PathwayCommons; Q9Y6W3; -.
DR Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR SignaLink; Q9Y6W3; -.
DR BioGRID-ORCS; 23473; 7 hits in 1077 CRISPR screens.
DR ChiTaRS; CAPN7; human.
DR EvolutionaryTrace; Q9Y6W3; -.
DR GenomeRNAi; 23473; -.
DR Pharos; Q9Y6W3; Tbio.
DR PRO; PR:Q9Y6W3; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9Y6W3; protein.
DR Bgee; ENSG00000131375; Expressed in secondary oocyte and 197 other tissues.
DR ExpressionAtlas; Q9Y6W3; baseline and differential.
DR Genevisible; Q9Y6W3; HS.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0090541; F:MIT domain binding; IPI:UniProtKB.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0097264; P:self proteolysis; IDA:UniProtKB.
DR CDD; cd00044; CysPc; 1.
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; IPR007330; MIT_dom.
DR InterPro; IPR036181; MIT_dom_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR Pfam; PF01067; Calpain_III; 1.
DR Pfam; PF04212; MIT; 2.
DR Pfam; PF00648; Peptidase_C2; 1.
DR PRINTS; PR00704; CALPAIN.
DR SMART; SM00720; calpain_III; 1.
DR SMART; SM00230; CysPc; 1.
DR SMART; SM00745; MIT; 2.
DR SUPFAM; SSF116846; SSF116846; 2.
DR SUPFAM; SSF49758; SSF49758; 2.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Hydrolase; Nucleus; Phosphoprotein; Protease;
KW Reference proteome; Repeat; Thiol protease.
FT CHAIN 1..813
FT /note="Calpain-7"
FT /id="PRO_0000207720"
FT DOMAIN 232..540
FT /note="Calpain catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT REGION 541..701
FT /note="Domain III"
FT REGION 702..813
FT /note="Domain N"
FT ACT_SITE 290
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT ACT_SITE 458
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT ACT_SITE 478
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 95
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT STRAND 688..696
FT /evidence="ECO:0007829|PDB:2QFE"
FT HELIX 698..700
FT /evidence="ECO:0007829|PDB:2QFE"
FT TURN 708..710
FT /evidence="ECO:0007829|PDB:2QFE"
FT HELIX 711..713
FT /evidence="ECO:0007829|PDB:2QFE"
FT STRAND 717..723
FT /evidence="ECO:0007829|PDB:2QFE"
FT STRAND 725..732
FT /evidence="ECO:0007829|PDB:2QFE"
FT STRAND 737..747
FT /evidence="ECO:0007829|PDB:2QFE"
FT STRAND 758..761
FT /evidence="ECO:0007829|PDB:2QFE"
FT STRAND 766..777
FT /evidence="ECO:0007829|PDB:2QFE"
FT STRAND 779..790
FT /evidence="ECO:0007829|PDB:2QFE"
FT STRAND 795..805
FT /evidence="ECO:0007829|PDB:2QFE"
FT STRAND 808..811
FT /evidence="ECO:0007829|PDB:2QFE"
SQ SEQUENCE 813 AA; 92652 MW; 814769611360D281 CRC64;
MDATALERDA VQFARLAVQR DHEGRYSEAV FYYKEAAQAL IYAEMAGSSL ENIQEKITEY
LERVQALHSA VQSKSADPLK SKHQLDLERA HFLVTQAFDE DEKENVEDAI ELYTEAVDLC
LKTSYETADK VLQNKLKQLA RQALDRAEAL SEPLTKPVGK ISSTSVKPKP PPVRAHFPLG
ANPFLERPQS FISPQSCDAQ GQRYTAEEIE VLRTTSKING IEYVPFMNVD LRERFAYPMP
FCDRWGKLPL SPKQKTTFSK WVRPEDLTNN PTMIYTVSSF SIKQTIVSDC SFVASLAISA
AYERRFNKKL ITGIIYPQNK DGEPEYNPCG KYMVKLHLNG VPRKVIIDDQ LPVDHKGELL
CSYSNNKSEL WVSLIEKAYM KVMGGYDFPG SNSNIDLHAL TGWIPERIAM HSDSQTFSKD
NSFRMLYQRF HKGDVLITAS TGMMTEAEGE KWGLVPTHAY AVLDIREFKG LRFIQLKNPW
SHLRWKGRYS ENDVKNWTPE LQKYLNFDPR TAQKIDNGIF WISWDDLCQY YDVIYLSWNP
GLFKESTCIH STWDAKQGPV KDAYSLANNP QYKLEVQCPQ GGAAVWVLLS RHITDKDDFA
NNREFITMVV YKTDGKKVYY PADPPPYIDG IRINSPHYLT KIKLTTPGTH TFTLVVSQYE
KQNTIHYTVR VYSACSFTFS KIPSPYTLSK RINGKWSGQS AGGCGNFQET HKNNPIYQFH
IEKTGPLLIE LRGPRQYSVG FEVVTVSTLG DPGPHGFLRK SSGDYRCGFC YLELENIPSG
IFNIIPSTFL PKQEGPFFLD FNSIIPIKIT QLQ
