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NPL4_CANGA
ID   NPL4_CANGA              Reviewed;         580 AA.
AC   Q6FJI2;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Nuclear protein localization protein 4;
GN   Name=NPL4; OrderedLocusNames=CAGL0M06105g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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: Involved in the import of nuclear-targeted proteins into the
CC       nucleus and the export of poly(A) RNA out of the nucleus. Has a role in
CC       the endoplasmic reticulum-associated degradation (ERAD) pathway (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}.
CC       Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}. Note=Localizes mainly at the nuclear periphery and
CC       the endoplasmic reticulum membrane. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NPL4 family. {ECO:0000305}.
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DR   EMBL; CR380959; CAG62588.1; -; Genomic_DNA.
DR   RefSeq; XP_449612.1; XM_449612.1.
DR   AlphaFoldDB; Q6FJI2; -.
DR   SMR; Q6FJI2; -.
DR   STRING; 5478.XP_449612.1; -.
DR   PRIDE; Q6FJI2; -.
DR   EnsemblFungi; CAG62588; CAG62588; CAGL0M06105g.
DR   GeneID; 2891660; -.
DR   KEGG; cgr:CAGL0M06105g; -.
DR   CGD; CAL0137323; CAGL0M06105g.
DR   VEuPathDB; FungiDB:CAGL0M06105g; -.
DR   eggNOG; KOG2834; Eukaryota.
DR   HOGENOM; CLU_017172_0_0_1; -.
DR   InParanoid; Q6FJI2; -.
DR   OMA; KWSRTGR; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0036266; C:Cdc48p-Npl4p-Vms1p AAA ATPase complex; IEA:EnsemblFungi.
DR   GO; GO:0000837; C:Doa10p ubiquitin ligase complex; IEA:EnsemblFungi.
DR   GO; GO:0000839; C:Hrd1p ubiquitin ligase ERAD-L complex; IEA:EnsemblFungi.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030894; C:replisome; IEA:EnsemblFungi.
DR   GO; GO:1990112; C:RQC complex; IEA:EnsemblFungi.
DR   GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; IEA:EnsemblFungi.
DR   GO; GO:0071629; P:cytoplasm protein quality control by the ubiquitin-proteasome system; IEA:EnsemblFungi.
DR   GO; GO:0006274; P:DNA replication termination; IEA:EnsemblFungi.
DR   GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0072671; P:mitochondria-associated ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0051228; P:mitotic spindle disassembly; IEA:EnsemblFungi.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0051974; P:negative regulation of telomerase activity; IEA:EnsemblFungi.
DR   GO; GO:0070651; P:nonfunctional rRNA decay; IEA:EnsemblFungi.
DR   GO; GO:1900182; P:positive regulation of protein localization to nucleus; IEA:EnsemblFungi.
DR   GO; GO:0072665; P:protein localization to vacuole; IEA:EnsemblFungi.
DR   GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IEA:EnsemblFungi.
DR   GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:EnsemblFungi.
DR   CDD; cd08061; MPN_NPL4; 1.
DR   InterPro; IPR037518; MPN.
DR   InterPro; IPR016563; Npl4.
DR   InterPro; IPR007717; NPL4_C.
DR   InterPro; IPR024682; Npl4_Ub-like_dom.
DR   InterPro; IPR007716; NPL4_Zn-bd_put.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR12710; PTHR12710; 1.
DR   Pfam; PF05021; NPL4; 1.
DR   Pfam; PF11543; UN_NPL4; 1.
DR   Pfam; PF05020; zf-NPL4; 1.
DR   PIRSF; PIRSF010052; Polyub_prc_Npl4; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS50249; MPN; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Endoplasmic reticulum; Membrane; mRNA transport; Nucleus;
KW   Protein transport; Reference proteome; Translocation; Transport.
FT   CHAIN           1..580
FT                   /note="Nuclear protein localization protein 4"
FT                   /id="PRO_0000339440"
FT   DOMAIN          238..378
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   REGION          86..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..108
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   580 AA;  65349 MW;  197DADFBE42E2B88 CRC64;
     MIIRFRSPVG MHRVRCEGSE TLGQVLPQLQ TILNEHGITP RAIELGKEAN GKDKTNVESL
     LEKTIEALGF RHGDIVYVHY QVDSSETKGS ANDNNGSVAV NIPNNLVPGK SQKADELEVD
     KELEKLDGLI PRQKTKLCKH GDRGMCEYCS PLPPWDANYA NENNIKHISF HAYLKKLNES
     TNKRESGSSY IAPLSQPNFK INKHCTNGHE PWPKGICSKC QPSAITLQQQ EFRMVDHVEF
     QSSELINQFI EFWRASGTQR FAYLYGKYEK YDATPLGIKA CVHAIYEPPQ HDEQDGITMD
     MEQVTQELNT IDLLAKEMGL LRVGMIFSDL TDAGNGDGTV LCKRHKDSFF LSSLETIMAA
     QHQTRHPNVS KFSEQGIFSS KFVTCVVSGN LKEEIDIASY QVSIDAEALV SADMIGGSTH
     PSMAYINDTT EDRYVPEIFY MKKNEYGLTV KENAKPAFPV DYLIVSLTHG FPKDEDTTTQ
     LFNSVTGFPW SNRQAMGYSQ DYHELKRYLH STAASGNFND LHDKLANFHL LLYIHSLQIL
     SQEEWELLVK GALSQDYQEP LYKLSASPGW QTLLMIIESA
 
 
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