ID H2U5V3_TAKRU Unreviewed; 697 AA.
AC H2U5V3;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Calpain-2 catalytic subunit {ECO:0000256|ARBA:ARBA00014052};
DE EC=3.4.22.53 {ECO:0000256|ARBA:ARBA00012481};
DE AltName: Full=Calcium-activated neutral proteinase 2 {ECO:0000256|ARBA:ARBA00031308};
DE AltName: Full=Calpain M-type {ECO:0000256|ARBA:ARBA00032449};
DE AltName: Full=Calpain-2 large subunit {ECO:0000256|ARBA:ARBA00032544};
DE AltName: Full=Millimolar-calpain {ECO:0000256|ARBA:ARBA00030109};
GN Name=LOC101076595 {ECO:0000313|Ensembl:ENSTRUP00000032319.2};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000032319.2, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000032319.2, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000032319.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Broad endopeptidase specificity.; EC=3.4.22.53;
CC Evidence={ECO:0000256|ARBA:ARBA00001223};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC -!- SIMILARITY: Belongs to the peptidase C2 family.
CC {ECO:0000256|ARBA:ARBA00007623}.
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DR RefSeq; XP_003972258.1; XM_003972209.2.
DR AlphaFoldDB; H2U5V3; -.
DR STRING; 31033.ENSTRUP00000032320; -.
DR Ensembl; ENSTRUT00000032443.3; ENSTRUP00000032319.2; ENSTRUG00000012768.3.
DR GeneID; 101076595; -.
DR KEGG; tru:101076595; -.
DR eggNOG; KOG0045; Eukaryota.
DR GeneTree; ENSGT00940000154784; -.
DR OrthoDB; 142935at2759; -.
DR TreeFam; TF314748; -.
DR Proteomes; UP000005226; Chromosome 17.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00214; Calpain_III; 1.
DR CDD; cd00044; CysPc; 1.
DR CDD; cd16189; EFh_PEF_CAPN1_like; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
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; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR PANTHER; PTHR10183; CALPAIN; 1.
DR PANTHER; PTHR10183:SF268; CALPAIN-2 CATALYTIC SUBUNIT; 1.
DR Pfam; PF01067; Calpain_III; 1.
DR Pfam; PF00648; Peptidase_C2; 1.
DR PRINTS; PR00704; CALPAIN.
DR SMART; SM00720; calpain_III; 1.
DR SMART; SM00230; CysPc; 1.
DR SUPFAM; SSF49758; Calpain large subunit, middle domain (domain III); 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00239}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU00239}; Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807, ECO:0000256|PROSITE-
KW ProRule:PRU00239}.
FT DOMAIN 45..341
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT DOMAIN 599..634
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT ACT_SITE 105
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 262
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 286
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 697 AA; 78303 MW; 6A4F1DBF9F0FF55C CRC64;
MSGVASTLAK KRALAAGFGT NANAVPYLNQ NFAALRAECL SARKLFCDPA FPAAPEALGF
KELGRSSYKV RGVTWKRPAE LVSNPEFIMG GATRTDICQG ALGDCWLLAA IASLTLNEYV
MARVVPSDQG FGDDYAGIFH FQFWQFGEWV DVVIDDRLPV KDNELMFVHS AEGREFWSAL
LEKAYAKVNG CYEALSGGST TEGFEDFTGG IAENYDLRQP PSNLFQIVKK ALEAGALLGC
SIDITSAADS EAVTRQKLVK GHAYSLTGAV EVNYRGRQEK LVRMRNPWGQ VEWTGAWSDG
SSEWNYMQGD CPHANAEDGE FWMSFSDFLR HYSRIEVCTL TPDTILDDSV KHWSVSKFDG
TWRKGSTAGG CRNHPYTFWM NPQFVINLQE EDDDPDDGEE GCSFVVGLIQ KNRRKLRKQG
EDMHTIGFAI YEVPEQFKGQ REVHLDKNFF LSHAQTARSE TFINLREVCS RFKLPPGEYL
IVPSTFEPHQ NGDFCIRVFS EKQTDTQPCD DPINADLDDE TVSDEDVDAG FRGLFTKLAG
NDMEISAVEL QTIMNKIVGK RSDIKTNGFS METCRVMVNL MDDSGNGKLG LGEFATLWKK
IQRYLSIYKK NDIDNSGTMS TPEMRVAFKD AGFTLNNTIY QLLVARYSDP NMTIDFDNFV
GCLMRLEMMF RIFKKLDVQN SGLIELNFQQ WVNFSMV
//
