ID   CAN6_RAT                Reviewed;         641 AA.
AC   O88501;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 119.
DE   RecName: Full=Calpain-6;
GN   Name=Capn6; Synonyms=Capa6;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Fischer;
RA   Shimizu T.;
RT   "Cellular genes modulated by a transactivator Tax of HTLV-1.";
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Microtubule-stabilizing protein that may be involved in the
CC       regulation of microtubule dynamics and cytoskeletal organization. May
CC       act as a regulator of RAC1 activity through interaction with ARHGEF2 to
CC       control lamellipodial formation and cell mobility. Does not seem to
CC       have protease activity as it has lost the active site residues (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts (via domain III) with microtubules. Interacts (via
CC       domain II) with ARHGEF2 (via the N-terminal zinc finger).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}.
CC       Cytoplasm, cytoskeleton, spindle {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
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DR   EMBL; AF067793; AAC19367.1; -; mRNA.
DR   RefSeq; NP_113996.1; NM_031808.1.
DR   AlphaFoldDB; O88501; -.
DR   SMR; O88501; -.
DR   STRING; 10116.ENSRNOP00000006638; -.
DR   MEROPS; C02.971; -.
DR   PaxDb; O88501; -.
DR   PRIDE; O88501; -.
DR   GeneID; 83685; -.
DR   KEGG; rno:83685; -.
DR   CTD; 827; -.
DR   RGD; 70960; Capn6.
DR   eggNOG; KOG0045; Eukaryota.
DR   InParanoid; O88501; -.
DR   OrthoDB; 704215at2759; -.
DR   PhylomeDB; O88501; -.
DR   Reactome; R-RNO-1474228; Degradation of the extracellular matrix.
DR   PRO; PR:O88501; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; ISO:RGD.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR   GO; GO:0005876; C:spindle microtubule; ISO:RGD.
DR   GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR   GO; GO:0001578; P:microtubule bundle formation; ISS:UniProtKB.
DR   GO; GO:0051493; P:regulation of cytoskeleton organization; ISS:UniProtKB.
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; 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.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; Microtubule; Reference proteome.
FT   CHAIN           1..641
FT                   /note="Calpain-6"
FT                   /id="PRO_0000207719"
FT   DOMAIN          26..343
FT                   /note="Calpain catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT   DOMAIN          498..621
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   REGION          344..495
FT                   /note="Domain III"
SQ   SEQUENCE   641 AA;  74560 MW;  3D9286F8B54369A6 CRC64;
     MGPPLKLFKN QKYQELKQDC MKDGRLFCDP TFLPENDSLF FNRLLPGKVV WKRPQDISDD
     PHLIVGNISN HQLIQGRLGN KAMISAFSCL AVQESHWTKA IPNHKEQEWD PRKPEKYAGI
     FRFRFWHFGE WTEVVIDDLL PTINGDLVFS FSTSMNEFWN ALLEKAYAKL LGCYEALDGL
     TITDIIMDFT GTLAEIIDMQ KGRYTDLVEE KYKLFGELYK TFTKGGLISC SIESPSQEEQ
     EVETDWGLLK GYTYTMTDIR KLRLGERLVE VFSTEKLYMV RLRNPLGRQE WSGPWSEISE
     EWQQLTVTDR KNLGLVMSDD GEFWMSLEDF CHNFHKLNVC RNVNNPVFGR KELESVVGCW
     TVDDDPLMNR SGGCYNNRDT FLQNPQYIFT VPEDGHKVIM SLQQKDLRTY RRMGRPDNYI
     IGFELFKVEM NRRFRLHHLY IQERAGTSTY IDTRTVFLSK YLKKGNYVLV PTMFQHGRTS
     EFLLRIFSEV PVQLRELTLD MPKMSCWNLA RGYPKVVTQI TVHSAEGLEK KYANETVNPY
     LTIKCGKEEV RSPVQKNTVH AIFDTQAIFY RRTTDIPIII QVWNSRKFCD QFLGQVTLDA
     DPSDCRDLKS LYLRKKGGPT AKVKQGHISF KVISSDDLTE L