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NPL4_CRYNJ
ID   NPL4_CRYNJ              Reviewed;         693 AA.
AC   P0CP30; Q55VJ9; Q5KKN9;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Nuclear protein localization protein 4;
GN   Name=NPL4; OrderedLocusNames=CNC02370;
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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; AE017343; AAW42211.1; -; Genomic_DNA.
DR   RefSeq; XP_569518.1; XM_569518.1.
DR   AlphaFoldDB; P0CP30; -.
DR   SMR; P0CP30; -.
DR   STRING; 5207.AAW42211; -.
DR   PaxDb; P0CP30; -.
DR   EnsemblFungi; AAW42211; AAW42211; CNC02370.
DR   GeneID; 3256137; -.
DR   KEGG; cne:CNC02370; -.
DR   VEuPathDB; FungiDB:CNC02370; -.
DR   eggNOG; KOG2834; Eukaryota.
DR   HOGENOM; CLU_017172_1_0_1; -.
DR   InParanoid; P0CP30; -.
DR   OMA; KWSRTGR; -.
DR   OrthoDB; 1106766at2759; -.
DR   Proteomes; UP000002149; Chromosome 3.
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:0005634; C:nucleus; IBA:GO_Central.
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:0043130; F:ubiquitin binding; IBA:GO_Central.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
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   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   CDD; cd08061; MPN_NPL4; 1.
DR   InterPro; IPR037518; MPN.
DR   InterPro; IPR016563; Npl4.
DR   InterPro; IPR007717; NPL4_C.
DR   InterPro; IPR007716; NPL4_Zn-bd_put.
DR   PANTHER; PTHR12710; PTHR12710; 1.
DR   Pfam; PF05021; NPL4; 1.
DR   Pfam; PF05020; zf-NPL4; 1.
DR   PIRSF; PIRSF010052; Polyub_prc_Npl4; 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..693
FT                   /note="Nuclear protein localization protein 4"
FT                   /id="PRO_0000339443"
FT   DOMAIN          259..399
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   REGION          85..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          613..665
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..120
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        613..632
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   693 AA;  75103 MW;  5532ECBFEA134A03 CRC64;
     MLLRIRSPAG TARLTVQPET TGEDFAEAIL NTIPAADPQP DPATLALSNQ PGAAGESVPF
     HALSGRTVGD MGFSHGDLLF LSYKPRAADP DSHPAMQATA PHPQPAQPDP SHPKTHTDPP
     MPNTIPLRDL SSVQEPEIDQ YWEKQTGKIE RKRDPAFCRH GDKAMCDYCM PLEPYDPKFQ
     SEHQIKHLSY HAYLRKLLSS RPPTASSATD LPPLSPTSLS VITPCPTGAH PSFPDGICST
     CQPSAVTLQS QPFRMVDHIE FASPSIIEGL LSAWRRTGTQ RIAFLIGRED KYEKVPMGIK
     VIVEAVWEPK QEGELDGLTV ETPWSDESRV QEIAKWCDKG LSVVGMIYTD LTPSPDDITK
     TLYKRHAQSY TASSLEMLLS AAYQLSHPLS TRMSPTGHYS SRFVTCCLTG DKDGGVDILA
     WQASEHAEAM VKAGIVEASV DPAVVRVRKP GEGEYVPEVF YSYKNEYGLQ VKMPAKPTFP
     VEYLYVNITH GFPLAPSPLF LSNAFPTENR PGLHDQSMQV VITQLAAILK TSDAEIGDAG
     TWPGRIKKDV EKWLSDWHLV TFLCMQGLFS LKEQQILCRA ATAHAHPNDT HALEELFASG
     GWQTLLTIVD SEASANARSN PPPTSSFNNL GIDSPAFAGP STESSAPPSG PDSVGAGAGA
     GAGGGRERVC PHCTFVNEHG GSDCEICGLP LDG
 
 
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