NPL4_EMENI
ID NPL4_EMENI Reviewed; 652 AA.
AC Q5BGN5; C8VUA1;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Nuclear protein localization protein 4;
GN Name=npl4; ORFNames=AN0295;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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 -!- SEQUENCE CAUTION:
CC Sequence=EAA65701.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AACD01000006; EAA65701.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001308; CBF89782.1; -; Genomic_DNA.
DR RefSeq; XP_657899.1; XM_652807.1.
DR AlphaFoldDB; Q5BGN5; -.
DR SMR; Q5BGN5; -.
DR STRING; 162425.CADANIAP00002420; -.
DR EnsemblFungi; CBF89782; CBF89782; ANIA_00295.
DR EnsemblFungi; EAA65701; EAA65701; AN0295.2.
DR GeneID; 2876073; -.
DR KEGG; ani:AN0295.2; -.
DR eggNOG; KOG2834; Eukaryota.
DR HOGENOM; CLU_017172_0_0_1; -.
DR InParanoid; Q5BGN5; -.
DR OMA; KWSRTGR; -.
DR OrthoDB; 1106766at2759; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR Proteomes; UP000005890; 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..652
FT /note="Nuclear protein localization protein 4"
FT /id="PRO_0000339445"
FT DOMAIN 268..405
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 95..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..645
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 652 AA; 73085 MW; 9ACAA696AA670FB8 CRC64;
MTSRTIILRF ESRNGQFRLN VSPQDMFPSL ETKILEHLPP DTEPSSIKLS NKPIGAAGDE
RFLNTLDGVS FEQVGLRSGH GDKLYIGYQS KQDLQDGASN GTAAGSSARR LNGAPINQEI
TPTSRAQADR VASVTVKNPW DAVRQSALDD RLEKKDGKIH RSRDNKMCKH SAKGMCDYCM
PLEPYDPKYL AEKKIKHLSF HSYLRKINAA TNKPELKSSF MPPLSEPYYR VRTDCPSGHP
PWPEGICTKC QPSAISLQPQ EYRMVDHVEF STPDLINSLL DFWRKSGTQR LGYLYGTYEE
YDEVPLGIKA VVQAIYEPPQ VDEVDGVTLH EWENEKDVDE IARLCGLEKV GVIFTDLLDA
GRGDGSVLCK RHIDSYYLSS LEIAFASRLQ MQQPKATRWS RTGYFGSNFV TCVLSGDEEG
AITISSYQAS VAAVEMIRAD IIEPSAEPSV MLVQSEDDDT NKSRYIPEVF YRKINEYGVS
AQVNAKPAFP VEYLLVTLTH GFPTESKPLF IDSTYPIENR EVIGEGQEFH SLARKLVSHG
DPQKAIRAVS DFHLLCFLRT FSTFSKEEEA LLCRVATTQN PTDGLQLINT PGWATLVTIL
QDSGERPPKR PWLDPSHPVP QPGKRYSPSS RHESPRSESE QLAKRFKGAS LR
