ID   CAN7_PIG                Reviewed;         813 AA.
AC   A0FKG7;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Calpain-7;
DE            EC=3.4.22.-;
GN   Name=CAPN7;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Yang X.Q., Yu H., Guo L.J., Liu D.;
RT   "The cloning and sequence analysis of pig CAPN7.";
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
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; EF026106; ABK20170.1; -; mRNA.
DR   RefSeq; NP_001090912.1; NM_001097443.1.
DR   AlphaFoldDB; A0FKG7; -.
DR   SMR; A0FKG7; -.
DR   STRING; 9823.ENSSSCP00000021370; -.
DR   MEROPS; C02.029; -.
DR   PaxDb; A0FKG7; -.
DR   PRIDE; A0FKG7; -.
DR   GeneID; 100037936; -.
DR   KEGG; ssc:100037936; -.
DR   CTD; 23473; -.
DR   eggNOG; KOG0045; Eukaryota.
DR   InParanoid; A0FKG7; -.
DR   OrthoDB; 343870at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
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:0006508; P:proteolysis; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Acetylation; Hydrolase; Nucleus; Phosphoprotein; Protease;
KW   Reference proteome; Repeat; Thiol protease.
FT   CHAIN           1..813
FT                   /note="Calpain-7"
FT                   /id="PRO_0000270513"
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:0000250|UniProtKB:Q9Y6W3"
FT   MOD_RES         95
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y6W3"
SQ   SEQUENCE   813 AA;  92370 MW;  386EF90B19B16256 CRC64;
     MDAAALERDA VQFARLAVQR DHEGRYSGAV FYYKEAAQAL IYAEMAGSSL EHIQEKINEY
     LERVQALHSA VQSKSADPLK SKHQLDLERA HLLVTQAFDE DEKGNVEDAI ELYTEAVDLC
     LKTSYETADK TLQNKLKQLA RQALDRAEAL SEPLTKPLCK VKATNIKPKP PPTRTHFPLG
     TNPFQEGPQP FISPQSCDAQ GQRYTAEEIE VLRTTSKING IEYVPFMNID LRERFAYPMP
     FCDRCGKLPL SPKQKAMFSK WVRPEDLTNN PTMIYTVSSF SIKQTIVSDC SFVASLAISA
     AYERRFTKKL ITSIIYPQNK DGESEYNPCG KYMVKLHLNG VPRKVIIDDQ LPVDHKGELL
     CSYSNNKSEL WVSLIEKAYM KVMGGYDFPG SNSNIDLHAL TGWIPERIAM HSDSQTFSKD
     NSFRMLYQRF HKGDVLITAS TGVMTEAEGE KWGLVPTHAY AVLDIREFKG LRFIQLKNPW
     SHLRWKGRYS ENDVKNWTPE LQKYLNFDPR TPQKIDNGIF WISWDDLCQY YDVIYLSWNP
     GLLKESTCIH STWDAKQGPV KDAYSLANNP QYKLEVQCPQ GGAAVWVLLS RHITDKDDFA
     NNREFITMVV YKTDGKKVYY PADPPPYIDG IRINSPHYLT KIKLTTPGTH TFTLVVSQYE
     KQNTIHYTVR VYSACSFTFS KIPSPYTVSK QINGKWSGQS AGGCGNFQET HKNNPIYQFH
     IEKSGPLLIE LRGPRQYSVG FEVVTVSVVG DPGPHGFQRK SSGDYRCGFC YLELESIPAG
     IYNIIPSTFL PKQEGPFFLD FNSVIPIKTT QLQ