NEM1_YEAST
ID NEM1_YEAST Reviewed; 446 AA.
AC P38757; D3DKU7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Nuclear envelope morphology protein 1;
DE EC=3.1.3.16;
GN Name=NEM1; OrderedLocusNames=YHR004C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION, IDENTIFICATION IN THE NEM1-SPO7 COMPLEX, AND SUBCELLULAR
RP LOCATION.
RX PubMed=9822591; DOI=10.1093/emboj/17.22.6449;
RA Siniossoglou S., Santos-Rosa H., Rappsilber J., Mann M., Hurt E.;
RT "A novel complex of membrane proteins required for formation of a spherical
RT nucleus.";
RL EMBO J. 17:6449-6464(1998).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP FUNCTION OF THE NEM1-SPO7 COMPLEX, AND MUTAGENESIS OF ASP-257.
RX PubMed=15889145; DOI=10.1038/sj.emboj.7600672;
RA Santos-Rosa H., Leung J., Grimsey N., Peak-Chew S., Siniossoglou S.;
RT "The yeast lipin Smp2 couples phospholipid biosynthesis to nuclear membrane
RT growth.";
RL EMBO J. 24:1931-1941(2005).
RN [7]
RP FUNCTION OF THE NEM1-SPO7 COMPLEX, AND DISRUPTION PHENOTYPE.
RX PubMed=29305265; DOI=10.1016/j.bbrc.2017.12.163;
RA Xu X., Okamoto K.;
RT "The Nem1-Spo7 protein phosphatase complex is required for efficient
RT mitophagy in yeast.";
RL Biochem. Biophys. Res. Commun. 496:51-57(2018).
CC -!- FUNCTION: Catalytic component of the NEM1-SPO7 complex which acts as a
CC phosphatase and dephosphorylates the phosphatidic acid phosphohydrolase
CC PAH1 (PubMed:15889145). Essential for the formation of a spherical
CC nucleus and meiotic division (PubMed:9822591). The NEM1-SPOo7 protein
CC phosphatase is required for efficient mitophagy under prolonged
CC respiration, as well as for reticulophagy and pexophagy
CC (PubMed:29305265). {ECO:0000269|PubMed:15889145,
CC ECO:0000269|PubMed:29305265, ECO:0000269|PubMed:9822591}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000269|PubMed:15889145};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC Evidence={ECO:0000269|PubMed:15889145};
CC -!- SUBUNIT: Component of the NEM1-SPO7 complex.
CC {ECO:0000269|PubMed:9822591}.
CC -!- INTERACTION:
CC P38757; P18410: SPO7; NbExp=3; IntAct=EBI-24435, EBI-17857;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:9822591}; Single-pass membrane protein
CC {ECO:0000269|PubMed:9822591}. Nucleus membrane
CC {ECO:0000269|PubMed:9822591}; Single-pass membrane protein
CC {ECO:0000269|PubMed:9822591}.
CC -!- DISRUPTION PHENOTYPE: Leads to inefficient mitochondrial sequestration
CC and degradation, as well as to defective reticulophagy and pexophagy
CC (PubMed:29305265). {ECO:0000269|PubMed:29305265}.
CC -!- MISCELLANEOUS: Present with 377 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the Dullard family. {ECO:0000305}.
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DR EMBL; U10555; AAB68431.1; -; Genomic_DNA.
DR EMBL; AY692950; AAT92969.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06691.1; -; Genomic_DNA.
DR PIR; S46802; S46802.
DR RefSeq; NP_011867.1; NM_001179134.1.
DR AlphaFoldDB; P38757; -.
DR SMR; P38757; -.
DR BioGRID; 36429; 312.
DR ComplexPortal; CPX-1787; Nem1-Spo7 phosphatase complex.
DR DIP; DIP-2440N; -.
DR IntAct; P38757; 4.
DR MINT; P38757; -.
DR STRING; 4932.YHR004C; -.
DR iPTMnet; P38757; -.
DR MaxQB; P38757; -.
DR PaxDb; P38757; -.
DR PRIDE; P38757; -.
DR EnsemblFungi; YHR004C_mRNA; YHR004C; YHR004C.
DR GeneID; 856393; -.
DR KEGG; sce:YHR004C; -.
DR SGD; S000001046; NEM1.
DR VEuPathDB; FungiDB:YHR004C; -.
DR eggNOG; KOG1605; Eukaryota.
DR GeneTree; ENSGT01040000240503; -.
DR HOGENOM; CLU_020262_5_2_1; -.
DR InParanoid; P38757; -.
DR OMA; YCDLFLS; -.
DR BioCyc; YEAST:G3O-31069-MON; -.
DR PRO; PR:P38757; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38757; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IDA:SGD.
DR GO; GO:0005811; C:lipid droplet; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0071595; C:Nem1-Spo7 phosphatase complex; IDA:ComplexPortal.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0140042; P:lipid droplet formation; IMP:SGD.
DR GO; GO:0071072; P:negative regulation of phospholipid biosynthetic process; IGI:SGD.
DR GO; GO:0006998; P:nuclear envelope organization; IDA:ComplexPortal.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; IMP:SGD.
DR GO; GO:1903740; P:positive regulation of phosphatidate phosphatase activity; IDA:SGD.
DR GO; GO:0008104; P:protein localization; IMP:SGD.
DR GO; GO:0071071; P:regulation of phospholipid biosynthetic process; IMP:SGD.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR011948; Dullard_phosphatase.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR02251; HIF-SF_euk; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Hydrolase; Membrane; Nucleus; Protein phosphatase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..446
FT /note="Nuclear envelope morphology protein 1"
FT /id="PRO_0000212579"
FT TRANSMEM 87..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 247..424
FT /note="FCP1 homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT REGION 53..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 257
FT /note="D->A: Abolishes phosphatase activity."
FT /evidence="ECO:0000269|PubMed:15889145"
SQ SEQUENCE 446 AA; 50642 MW; 4260748606E17062 CRC64;
MNALKYFSNH LITTKKQKKI NVEVTKNQDL LGPSKEVSNK YTSHSENDCV SEVDQQYDHS
SSHLKESDQN QERKNSVPKK PKALRSILIE KIASILWALL LFLPYYLIIK PLMSLWFVFT
FPLSVIERRV KHTDKRNRGS NASENELPVS SSNINDSSEK TNPKNCNLNT IPEAVEDDLN
ASDEIILQRD NVKGSLLRAQ SVKSRPRSYS KSELSLSNHS SSNTVFGTKR MGRFLFPKKL
IPKSVLNTQK KKKLVIDLDE TLIHSASRST THSNSSQGHL VEVKFGLSGI RTLYFIHKRP
YCDLFLTKVS KWYDLIIFTA SMKEYADPVI DWLESSFPSS FSKRYYRSDC VLRDGVGYIK
DLSIVKDSEE NGKGSSSSLD DVIIIDNSPV SYAMNVDNAI QVEGWISDPT DTDLLNLLPF
LEAMRYSTDV RNILALKHGE KAFNIN
