NPL4_SCHPO
ID NPL4_SCHPO Reviewed; 572 AA.
AC Q9P780;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Nuclear protein localization protein 4;
GN Name=npl4; ORFNames=SPBC1711.10c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP REVISION OF GENE MODEL.
RX PubMed=21270388; DOI=10.1534/genetics.110.123497;
RA Bitton D.A., Wood V., Scutt P.J., Grallert A., Yates T., Smith D.L.,
RA Hagan I.M., Miller C.J.;
RT "Augmented annotation of the Schizosaccharomyces pombe genome reveals
RT additional genes required for growth and viability.";
RL Genetics 187:1207-1217(2011).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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; CU329671; CAB88240.2; -; Genomic_DNA.
DR RefSeq; NP_595883.2; NM_001021789.2.
DR AlphaFoldDB; Q9P780; -.
DR SMR; Q9P780; -.
DR BioGRID; 276371; 3.
DR STRING; 4896.SPBC1711.10c.1; -.
DR iPTMnet; Q9P780; -.
DR MaxQB; Q9P780; -.
DR PaxDb; Q9P780; -.
DR EnsemblFungi; SPBC1711.10c.1; SPBC1711.10c.1:pep; SPBC1711.10c.
DR GeneID; 2539821; -.
DR KEGG; spo:SPBC1711.10c; -.
DR PomBase; SPBC1711.10c; npl4.
DR VEuPathDB; FungiDB:SPBC1711.10c; -.
DR eggNOG; KOG2834; Eukaryota.
DR HOGENOM; CLU_017172_0_0_1; -.
DR InParanoid; Q9P780; -.
DR OMA; KWSRTGR; -.
DR Reactome; R-SPO-110320; Translesion Synthesis by POLH.
DR Reactome; R-SPO-8951664; Neddylation.
DR Reactome; R-SPO-9755511; KEAP1-NFE2L2 pathway.
DR PRO; PR:Q9P780; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0036266; C:Cdc48p-Npl4p-Vms1p AAA ATPase complex; ISO:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000836; C:Hrd1p ubiquitin ligase complex; ISO:PomBase.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1990112; C:RQC complex; ISO:PomBase.
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:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; ISO:PomBase.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISO:PomBase.
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; 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..572
FT /note="Nuclear protein localization protein 4"
FT /id="PRO_0000339454"
FT DOMAIN 242..379
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 87..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 572 AA; 63619 MW; 5382928D32FA6ED6 CRC64;
MILRFRSKRG MARAEFQPTD TLAMLSAKIL SDILKNDYSP ENVSLCQNES DQGVIFSNLN
DQTLQDAGLT HGQMLYLRLG TPNSDIASSN NEPALTVTGA PKQVSTPDVS EKKPSMPVIQ
DPIDDSLEKE DGLIRRSMTS LCRHGPKGMC DYCSPLEPYD ESYRQENKIK HLSFHAYLRK
INSNVNKYAS SQSFIPPLEE PSFTVKEKCP SGHPPWPAGI CTKCQPSTVM LNLQPFRVID
HIEFASPGIV DSFLNKWRQS GFQRIGYTYG HFEQYNNVPL GIKGVIEAIY EPPQVSEADG
VTLEEWADEA LVEQVATACG LRRIGIIFTD LTDDGSNSGK VLCKRHSDSY FLSSLEVYNS
ANFQTKFKNP CKWSRSGYFG SKFVTSVISG NLNGEIEVMS YQVSNIGTAL YQADLIQPSV
DPDRMLVKKE DQTRYVPDVL YRYTDKYGKQ VSENAKPAFP VSFLLVTLTD GFPEKPDPLF
SNNDTSIITT LESTDETGRL RQLAKLFDHN AIANGSLSNF SVLLAIAKLS ILGKDDLAAL
ASYATAPTEE NEKNLNSRES YQTLLAILYS SL
