ID   NPL4_CANAL              Reviewed;         598 AA.
AC   Q5AA50; A0A1D8PDQ6; Q5AAD8;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Nuclear protein localization protein 4;
GN   Name=NPL4; OrderedLocusNames=CAALFM_C106110CA;
GN   ORFNames=CaO19.2434, CaO19.9970;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP017623; AOW26275.1; -; Genomic_DNA.
DR   RefSeq; XP_718457.1; XM_713364.1.
DR   AlphaFoldDB; Q5AA50; -.
DR   SMR; Q5AA50; -.
DR   STRING; 237561.Q5AA50; -.
DR   GeneID; 3639820; -.
DR   KEGG; cal:CAALFM_C106110CA; -.
DR   CGD; CAL0000200595; NPL4.
DR   VEuPathDB; FungiDB:C1_06110C_A; -.
DR   eggNOG; KOG2834; Eukaryota.
DR   HOGENOM; CLU_017172_0_0_1; -.
DR   InParanoid; Q5AA50; -.
DR   OrthoDB; 1106766at2759; -.
DR   PRO; PR:Q5AA50; -.
DR   Proteomes; UP000000559; Chromosome 1.
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   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR12710; PTHR12710; 1.
DR   Pfam; PF05021; 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..598
FT                   /note="Nuclear protein localization protein 4"
FT                   /id="PRO_0000339439"
FT   DOMAIN          264..403
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   REGION          99..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   598 AA;  67354 MW;  8E373A45B36D0FC2 CRC64;
     MSSIILRFRS KDGMFRITTD SSSNFTLVLE QLIEKLSQSG NNGNGNGNNN KIDLQSLTIA
     NKPQDKGKSS YEFQNQTVNE LGLKNGDMLY VNYESVTNDS GPTTTATNTT TNTASGNTIP
     ITGPVPSIPI NSVVTSHGPL KVEELPIDQE LDKEDGLITR PLSSMCRHGP KGMCEYCSPL
     PPWDENYRKD HAIKHISFHA YLKQQLEKLK SSGGSYFPPL DPVDYSIDLT CNQGHKPYPN
     GICSKCQPSP ITLQLQKFRM VDHLEFADSF ILNDFINVWR VSGVQRFGYL YGRYAKSEKT
     PLGIKAIVET IIEPPQHDEL DGITLLDWDQ QEEKMVDQVA NKFGLYKVGI IFTDLTDAGT
     KNGKVLCKRH KDSYFLTNLE IIMAAKFQLK YPNISKYSTA KNNGQFSSKF VTCVISGGLN
     GEIEPRSYQV STSAEALVKA DIITGCTQPS QIYVNESNNH RYVPDIQYSK INKYGLEVKS
     NAKPTFPGEF LLVSLTDSFP LQPTPIFTNS YVIENREFLG DENHDIQSLK TLHNYLKSNN
     DQIFNFHFIL HLIKTHILND QEIDLLIEYI KSKNLEDYLK LVESNGWMTL MTILEQSV