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CPLA_DICDI
ID   CPLA_DICDI              Reviewed;         649 AA.
AC   Q8MUF9; Q55BR8;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Putative calpain-like cysteine protease A;
DE            EC=3.4.22.-;
DE   Contains:
DE     RecName: Full=Putative processed calpain-like cysteine protease A;
DE   Flags: Precursor;
GN   Name=cplA; Synonyms=cpl; ORFNames=DDB_G0269200;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 4-15 AND 193-199, FUNCTION,
RP   SUBCELLULAR LOCATION, SUBUNIT, AND AUTOCATALYTIC CLEAVAGE.
RC   STRAIN=AX3;
RX   PubMed=12578394; DOI=10.1021/bi026461+;
RA   Huang X., Czerwinski E., Mellgren R.L.;
RT   "Purification and properties of the Dictyostelium calpain-like protein,
RT   Cpl.";
RL   Biochemistry 42:1789-1795(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Has a weak caseinolytic activity.
CC       {ECO:0000269|PubMed:12578394}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12578394}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12578394}.
CC   -!- PTM: Undergoes autolytic cleavage between Pro-192 and Ala-193.
CC   -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
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DR   EMBL; AF525418; AAM91927.1; -; mRNA.
DR   EMBL; AAFI02000005; EAL71950.1; -; Genomic_DNA.
DR   RefSeq; XP_646763.1; XM_641671.1.
DR   AlphaFoldDB; Q8MUF9; -.
DR   SMR; Q8MUF9; -.
DR   STRING; 44689.DDB0191171; -.
DR   PaxDb; Q8MUF9; -.
DR   PRIDE; Q8MUF9; -.
DR   EnsemblProtists; EAL71950; EAL71950; DDB_G0269200.
DR   GeneID; 8617736; -.
DR   KEGG; ddi:DDB_G0269200; -.
DR   dictyBase; DDB_G0269200; cplA.
DR   eggNOG; ENOG502SS2N; Eukaryota.
DR   HOGENOM; CLU_422394_0_0_1; -.
DR   InParanoid; Q8MUF9; -.
DR   OMA; TMASDNI; -.
DR   Reactome; R-DDI-6798695; Neutrophil degranulation.
DR   PRO; PR:Q8MUF9; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IDA:dictyBase.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   Gene3D; 2.60.40.150; -; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR022684; Calpain_cysteine_protease.
DR   InterPro; IPR022682; Calpain_domain_III.
DR   InterPro; IPR022683; Calpain_III.
DR   InterPro; IPR036213; Calpain_III_sf.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF01067; Calpain_III; 2.
DR   PRINTS; PR00704; CALPAIN.
DR   SMART; SM00720; calpain_III; 2.
DR   SUPFAM; SSF49562; SSF49562; 1.
DR   SUPFAM; SSF49758; SSF49758; 3.
DR   PROSITE; PS50004; C2; 1.
PE   1: Evidence at protein level;
KW   Autocatalytic cleavage; Cytoplasm; Direct protein sequencing; Hydrolase;
KW   Protease; Reference proteome; Repeat; Thiol protease.
FT   PROPEP          1..3
FT                   /evidence="ECO:0000269|PubMed:12578394"
FT                   /id="PRO_0000327882"
FT   CHAIN           4..649
FT                   /note="Putative calpain-like cysteine protease A"
FT                   /id="PRO_0000327883"
FT   CHAIN           193..649
FT                   /note="Putative processed calpain-like cysteine protease A"
FT                   /id="PRO_0000327884"
FT   DOMAIN          15..123
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          124..193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          458..489
FT                   /note="Domain III 1"
FT   REGION          498..633
FT                   /note="Domain III 2"
FT   COMPBIAS        137..157
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        158..175
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            192..193
FT                   /note="Cleavage; by autolysis"
SQ   SEQUENCE   649 AA;  72623 MW;  1D1691E255288570 CRC64;
     MLTTESPTTT TTTTTTTTSS PSSDIRDKFI FGNLEVKVKE VKGCQLHFLN VKCELALKKT
     EIKTKPLANH TFFDVFSFRV SAATSELEIE AWKKNFLFKD KMTGSLTIPI NDLLHANGEA
     KWYPLSNKKP RSSRVKKENI TNSNNKDNNT ASPSSPDEAQ EKGDEDQHHS ADESPAEETS
     PTTGRPRSVS MPAKKVKAAP EICLEIKFVL NEPPKEVLKG IVLDGVWNSE NNFGSLINNP
     HWIKCTQYLL SIKDEITPIT LKLRQPEGTD QRCSFFVINY DPFYNGSKKV ILDTTNDIKK
     VSSFNSPIPA TSVDCKIDLE PGQYCIIPYA ESFAFSGTYK FNLDSEKLDN CEFYALPKSQ
     EQAWNEITVD GLWTTATNGG GDINILGWTK NPQYSFTLTK KSRACVLLSQ DDNDKSVGFY
     VIKQLDAGKR AIEFREQVGK TESFKFSCST GCTLTLDEGT YIVIPSTYDH GIEGAFHLTL
     FTDDKNATFQ PLTNAFQEVE QVKGTWVGKS AGGSPNQPTF FNNPQFHLKV PASDKDEVIA
     VQLIQDSTIA DEGIGFIVLS RDSHSEPLTA QDFQNEMVFT KTSNWEKRND IVCRLHVKPE
     SPREFTIIPS TFDPSVNRSF KLQVYSDVSI SLDEIEQKDE SSDSEQNDD
 
 
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