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NPL4_SCLS1
ID   NPL4_SCLS1              Reviewed;         611 AA.
AC   A7EGK5;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Nuclear protein localization protein 4;
GN   Name=npl4; ORFNames=SS1G_04446;
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS   (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1;
RX   PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476625; EDO01971.1; -; Genomic_DNA.
DR   RefSeq; XP_001594639.1; XM_001594589.1.
DR   AlphaFoldDB; A7EGK5; -.
DR   SMR; A7EGK5; -.
DR   STRING; 665079.A7EGK5; -.
DR   EnsemblFungi; EDO01971; EDO01971; SS1G_04446.
DR   GeneID; 5490811; -.
DR   KEGG; ssl:SS1G_04446; -.
DR   VEuPathDB; FungiDB:sscle_02g016730; -.
DR   eggNOG; KOG2834; Eukaryota.
DR   HOGENOM; CLU_017172_0_0_1; -.
DR   InParanoid; A7EGK5; -.
DR   OMA; KWSRTGR; -.
DR   Proteomes; UP000001312; Unassembled WGS sequence.
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..611
FT                   /note="Nuclear protein localization protein 4"
FT                   /id="PRO_0000339455"
FT   DOMAIN          267..404
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   REGION          89..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   611 AA;  67728 MW;  012E1A1964C97CFF CRC64;
     MLLRFRGPDG TVRIAVEANE TFGQLGDKLL KLLPENLDPR TLTLSNAPSG GEVKLLMEIA
     RAKVSQIGLK NGDMVFINYK LLDNLPNGNS TTSTSTTHSS HLTSSTNRLN GSAVLPESIP
     VNVPAQAVTS PSEKIKNPWE VVQQSDLDNR LDKKDGKIPR KRDTKMCRHG EKGMCDYCMP
     LEPFNAQYLA EKKIKNLSFH SYLRKINSAT NKPELGSSFM PPLTEPYYRV KKNCPSGHPQ
     WPEGICTKCQ PSAITLQPQE FRMVDHVEFA QASLVENLLV FWRSTGAQRF GYLYGRYEEY
     TEVPLGVKAV VEAIYEPPQV DELDGITLNK WESEKDVDEM ARLCGMERVG VIWTDLLDSG
     AGDGTVICKR HIDSYYLSSL EIAFAARLQA KHPKPTKWSD TGKFGSNFVT CVVTADETGG
     IAISAYQVSN TAVEMVRADI VEPSADPAVM IVRSEGDDDS DTSARYIPEV FYRKINEYGR
     SVQENAKPSF PVEYLLVTLT HGFPSDPKPA FMAKNSFTIE NRLVIGQEQD IKDVGKQLGL
     DKNGQLTQSS DGVLAVSDFH LLCYIYSMGI LSKEEMALLC RVATQHDLAD GYQLIATPGW
     ANFLAILQST G
 
 
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