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Database: UniProt
Entry: H3CN15_TETNG
LinkDB: H3CN15_TETNG
Original site: H3CN15_TETNG 
ID   H3CN15_TETNG            Unreviewed;       640 AA.
AC   H3CN15;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Si:dkey-19b23.13 {ECO:0000313|Ensembl:ENSTNIP00000009646.1};
OS   Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS   nigroviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX   NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000009646.1, ECO:0000313|Proteomes:UP000007303};
RN   [1] {ECO:0000313|Proteomes:UP000007303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15496914; DOI=10.1038/nature03025;
RA   Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA   Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA   Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA   Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA   Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA   Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA   Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA   McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA   Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA   Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA   Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT   "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT   early vertebrate proto-karyotype.";
RL   Nature 431:946-957(2004).
RN   [2] {ECO:0000313|Ensembl:ENSTNIP00000009646.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase C2 family.
CC       {ECO:0000256|ARBA:ARBA00007623}.
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DR   AlphaFoldDB; H3CN15; -.
DR   STRING; 99883.ENSTNIP00000009646; -.
DR   Ensembl; ENSTNIT00000009821.1; ENSTNIP00000009646.1; ENSTNIG00000006853.1.
DR   GeneTree; ENSGT00940000156128; -.
DR   HOGENOM; CLU_010982_3_2_1; -.
DR   InParanoid; H3CN15; -.
DR   OMA; WQQMSRA; -.
DR   TreeFam; TF314748; -.
DR   Proteomes; UP000007303; Unassembled WGS sequence.
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   Gene3D; 2.60.120.380; -; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
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; IPR000169; Pept_cys_AS.
DR   InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR   PANTHER; PTHR10183; CALPAIN; 1.
DR   PANTHER; PTHR10183:SF405; CALPAIN-5; 1.
DR   Pfam; PF00168; C2; 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; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF49758; Calpain large subunit, middle domain (domain III); 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50203; CALPAIN_CAT; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00239};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU00239}; Reference proteome {ECO:0000313|Proteomes:UP000007303};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807, ECO:0000256|PROSITE-
KW   ProRule:PRU00239}.
FT   DOMAIN          26..340
FT                   /note="Calpain catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50203"
FT   DOMAIN          493..616
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   ACT_SITE        81
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        253
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        281
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00239"
SQ   SEQUENCE   640 AA;  72499 MW;  8F32A4C5E457472A CRC64;
     MPEPVHRFLG QKFHKLRRAC LHRGVLFKDP LFPATAQSLF YKREPPPGLT WKRPKEICKD
     PRLFLDGIST RDLHQGSLGN CWMVAAISCL ASEPSLWKKV IPDHAEQEWN PKRPDLYAGI
     FHFRFWRLGR WTDVVVDDRL PVSGDGVLLF CRSATPREFW SALLEKAYAK LNGCYEALEG
     GNTTEALIDF TGGVSEPLRL DGGALSARSH QRRALFQTLA KAHEHKALIT CSIRPAEGEA
     AESALGCGLV RGHAYGITAL RKVRLEERGS VARLFMVRMR NPWGTADWTG AWSQGSHEWQ
     RMSRSDREKM GLAVRDVGEF WMDFQDFCLY FTDVVVCRLV ERFLLRPRSH WREERLHGEW
     APAPAPDQTG RCGGCINHRD TFLHNPQFMF ELGGSEEEEV LICLQQEDRR IHRKHGGGEN
     LPIGFEVLKV EVNRSSRVQR VEEKAASSVY MDSRSVTLRA ALAPGRYVIL PTTFLPGATG
     RFLLRVFCHA PVRLRELRED LPPPWWFRCF LPQPAVVTTV HLRRASGLSS PKRPGSAPGV
     YAVVRCENHA VRSRVLRAEG NPEFNLRAIF YRRHPDAHIS IQLWARGLLR DLLLGGARLQ
     TAQPETRCSR VMDLRGGRSG AGLRGRVYVE TSSSVGLTDL
//
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