NEM1_SCHPO
ID NEM1_SCHPO Reviewed; 476 AA.
AC O59718;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Nuclear envelope morphology protein 1;
DE EC=3.1.3.16;
GN Name=nem1; ORFNames=SPBC3B8.10c;
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 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: Catalytic component of the nem1-spo7 complex which acts as a
CC phosphatase and may be required for proper nuclear membrane morphology.
CC {ECO:0000250}.
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 -!- 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 -!- SUBUNIT: Component of the nem1-spo7 complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16823372}; Single-pass membrane protein
CC {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000250}; Single-
CC pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Dullard family. {ECO:0000305}.
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DR EMBL; CU329671; CAA18299.1; -; Genomic_DNA.
DR PIR; T40330; T40330.
DR RefSeq; NP_596404.1; NM_001022323.2.
DR AlphaFoldDB; O59718; -.
DR SMR; O59718; -.
DR BioGRID; 277536; 97.
DR STRING; 4896.SPBC3B8.10c.1; -.
DR iPTMnet; O59718; -.
DR MaxQB; O59718; -.
DR PaxDb; O59718; -.
DR PRIDE; O59718; -.
DR EnsemblFungi; SPBC3B8.10c.1; SPBC3B8.10c.1:pep; SPBC3B8.10c.
DR GeneID; 2541021; -.
DR KEGG; spo:SPBC3B8.10c; -.
DR PomBase; SPBC3B8.10c; nem1.
DR VEuPathDB; FungiDB:SPBC3B8.10c; -.
DR eggNOG; KOG1605; Eukaryota.
DR HOGENOM; CLU_020262_7_0_1; -.
DR InParanoid; O59718; -.
DR OMA; HKENAIP; -.
DR PhylomeDB; O59718; -.
DR Reactome; R-SPO-4419969; Depolymerisation of the Nuclear Lamina.
DR PRO; PR:O59718; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; ISO:PomBase.
DR GO; GO:0071595; C:Nem1-Spo7 phosphatase complex; ISO:PomBase.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IBA:GO_Central.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0019915; P:lipid storage; IMP:PomBase.
DR GO; GO:0101026; P:mitotic nuclear membrane biogenesis; IMP:PomBase.
DR GO; GO:0071072; P:negative regulation of phospholipid biosynthetic process; ISO:PomBase.
DR GO; GO:0071763; P:nuclear membrane organization; IMP:PomBase.
DR GO; GO:0023052; P:signaling; NAS:PomBase.
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 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane; Nucleus;
KW Protein phosphatase; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..476
FT /note="Nuclear envelope morphology protein 1"
FT /id="PRO_0000315975"
FT TRANSMEM 123..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 299..460
FT /note="FCP1 homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT REGION 47..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 476 AA; 54598 MW; 012BBD6EF067090F CRC64;
MNSIARLSDE INKAILATPL DDDEADKEKL ANARGRASSA TLRHYNRRRS SYSASSLSSL
SSKPTEKEVP TRNEKPKHAN IMRVVVYWIR VFLKRIYTFF VHSARVFLYH FLNEEKEFTL
ASFFWGLCRF VFFPVLLSYK RREMLPPQPS VRRPRFYSSY SYPSSHQDPA YSSFKRHRSS
NSYSSSSNGN HVRFQPSIAE EEISFNSFSN SLNSEEDVCV SPMKPKEVSL MGKANSNRSG
HSHQPQSTQF SPPANDNISK LPSSFTIVND PLKSPSSSRL RIRNITLCAD KIPRPLLNSK
LPRKTLVLDL DETLIHSVSR GSRTTSGQPI EVHVPGEHPI LYYIHKRPHL DYFLSNVSQW
FRLILFTASV QPYADPIIDY LERDKKIFAK RYYRQHCALV DSSFVKDISI CNIHLSRIMI
IDNSPASYNA HKENAIPIEG WISDPSDVDL LNLLSFLHAL QYVHDVRDLL GLRLAK
