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PALB_YARLI
ID   PALB_YARLI              Reviewed;         795 AA.
AC   Q9HFC8; Q6C929;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Calpain-like protease palB/RIM13;
DE            EC=3.4.22.-;
DE   AltName: Full=Cysteine protease RIM13;
GN   Name=RIM13; OrderedLocusNames=YALI0D14740g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=11861549; DOI=10.1093/genetics/160.2.417;
RA   Gonzalez-Lopez C.I., Szabo R., Blanchin-Roland S., Gaillardin C.;
RT   "Genetic control of extracellular protease synthesis in the yeast Yarrowia
RT   lipolytica.";
RL   Genetics 160:417-427(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Required for the proteolytic cleavage of the transcription
CC       factor RIM101 in response to alkaline ambient pH.
CC       {ECO:0000269|PubMed:11861549}.
CC   -!- SIMILARITY: Belongs to the peptidase C2 family. PalB/RIM13 subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-12 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAG81021.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ277150; CAC14603.1; -; Genomic_DNA.
DR   EMBL; CR382130; CAG81021.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_502833.1; XM_502833.1.
DR   AlphaFoldDB; Q9HFC8; -.
DR   STRING; 4952.CAG81021; -.
DR   GeneID; 2910310; -.
DR   KEGG; yli:YALI0D14740g; -.
DR   InParanoid; Q9HFC8; -.
DR   Proteomes; UP000001300; Chromosome D.
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; 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; PF00648; Peptidase_C2; 1.
DR   SMART; SM00720; calpain_III; 1.
DR   SMART; SM00230; CysPc; 1.
DR   SUPFAM; SSF49758; SSF49758; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS50203; CALPAIN_CAT; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Protease; Reference proteome; Thiol protease.
FT   CHAIN           1..795
FT                   /note="Calpain-like protease palB/RIM13"
FT                   /id="PRO_0000207745"
FT   DOMAIN          89..408
FT                   /note="Calpain catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        158
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        326
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        362
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
SQ   SEQUENCE   795 AA;  89799 MW;  B29D4B04526227DC CRC64;
     MSLPEEIYTS AMLAIACNDD KKAQEILVSL LQTYPDLVDY AKSISPATGK LVLRQAKRSM
     DAYDSIKKGG SVLSLAEKIV YLSSRTNYGY ALPWEYATPV SALKKSDDLY VDATDGGLRQ
     SQHRDVSWLR IPHVFASSDA VFTWSGFETL YQDGLENCSF VASLLSIGVM EKRCNYSLLK
     EALLDKSSNH HLGTPPSSGR YDIKLFINGC DRRITIDDRF PIREPSLPNM YLRSYTNPTL
     VWPALLEKAF MKVLDGYDYA GSHAGGDTFV LCKWFPEFVS LTSYHDTNGL WRYIYDSWLQ
     GDVLLCLGTG SFSREEADYK GLLGEHDYAV LELREIQDGC NTAHILRIRD PLLFGPFSNP
     KNPLVEESNR LAKLVDGKNV DMASRGEIWM DFNQATREYQ SLYLNWRPER FFCRLEQHFF
     WKTSDIMDFQ MCGSFVQNPQ YTITNNGTKT ATGKLVLLRH TQGRETDAKS FCCIHLFEGA
     TRVVLQETSH AVYKGKLMNL HYYTVSLTLK PGESTTAVMA CSGMTDSEPM YRFSLFLYAN
     NPLTMSKPTA PLAYSQIFKG KWSEDQAGGN WAKPMYIHNP QFLLTVNEHC DQLYIYLTSS
     SRQPIAAQLF WGSKSLKEYK ESAIETSSGK YKTGSTHLKT RNIDAGSNLI LIISTFDSAP
     QTDYNIRVFS SGNFSLTQLA RHTAGKFTKS HKSKFYNSCS EQVEFSVQQS TQHLSLAARM
     IKTRPFIRLT IREAQSNTVV ATTNTFSDSI YGVHLDGVRV SRGLVYLAVI EKMEHSNNEP
     YVMEFAADTL VTLGH
 
 
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