NED1_SCHPO
ID NED1_SCHPO Reviewed; 656 AA.
AC Q9UUJ6;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Nuclear elongation and deformation protein 1;
GN Name=ned1; ORFNames=SPAC1952.13;
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 [GENOMIC DNA], FUNCTION, INTERACTION WITH DIS3; PIM1
RP AND NUP189, PHOSPHORYLATION, AND MUTAGENESIS OF GLY-80 AND GLY-402.
RX PubMed=12376568; DOI=10.1242/jcs.00135;
RA Tange Y., Hirata A., Niwa O.;
RT "An evolutionarily conserved fission yeast protein, Ned1, implicated in
RT normal nuclear morphology and chromosome stability, interacts with Dis3,
RT Pim1/RCC1 and an essential nucleoporin.";
RL J. Cell Sci. 115:4375-4385(2002).
RN [2]
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-103; THR-106;
RP SER-107; SER-159; SER-286; SER-318; SER-321 AND SER-587, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: May have a role in the maintenance of the nuclear envelope
CC structure and in minichromosome stability.
CC {ECO:0000269|PubMed:12376568}.
CC -!- SUBUNIT: Interacts with dis3, pim1 and nup189.
CC {ECO:0000269|PubMed:12376568}.
CC -!- SIMILARITY: Belongs to the lipin family. {ECO:0000305}.
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DR EMBL; CU329670; CAB52577.1; -; Genomic_DNA.
DR PIR; T37941; T37941.
DR RefSeq; NP_594815.1; NM_001020244.2.
DR AlphaFoldDB; Q9UUJ6; -.
DR BioGRID; 278743; 8.
DR STRING; 4896.SPAC1952.13.1; -.
DR iPTMnet; Q9UUJ6; -.
DR MaxQB; Q9UUJ6; -.
DR PaxDb; Q9UUJ6; -.
DR PRIDE; Q9UUJ6; -.
DR EnsemblFungi; SPAC1952.13.1; SPAC1952.13.1:pep; SPAC1952.13.
DR GeneID; 2542274; -.
DR KEGG; spo:SPAC1952.13; -.
DR PomBase; SPAC1952.13; ned1.
DR VEuPathDB; FungiDB:SPAC1952.13; -.
DR eggNOG; KOG2116; Eukaryota.
DR HOGENOM; CLU_002546_3_0_1; -.
DR InParanoid; Q9UUJ6; -.
DR OMA; TWSSINP; -.
DR PhylomeDB; Q9UUJ6; -.
DR Reactome; R-SPO-1483191; Synthesis of PC.
DR Reactome; R-SPO-1483213; Synthesis of PE.
DR Reactome; R-SPO-4419969; Depolymerisation of the Nuclear Lamina.
DR Reactome; R-SPO-75109; Triglyceride biosynthesis.
DR PRO; PR:Q9UUJ6; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; ISM:PomBase.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; ISO:PomBase.
DR GO; GO:0044255; P:cellular lipid metabolic process; IBA:GO_Central.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IMP:PomBase.
DR GO; GO:0009062; P:fatty acid catabolic process; IBA:GO_Central.
DR GO; GO:0019915; P:lipid storage; IMP:PomBase.
DR GO; GO:0071763; P:nuclear membrane organization; IMP:PomBase.
DR GO; GO:0019432; P:triglyceride biosynthetic process; ISO:PomBase.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR026058; LIPIN.
DR InterPro; IPR007651; Lipin_N.
DR InterPro; IPR013209; LNS2.
DR InterPro; IPR031315; LNS2/PITP.
DR PANTHER; PTHR12181; PTHR12181; 2.
DR Pfam; PF04571; Lipin_N; 1.
DR Pfam; PF08235; LNS2; 1.
DR SMART; SM00775; LNS2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..656
FT /note="Nuclear elongation and deformation protein 1"
FT /id="PRO_0000209886"
FT REGION 99..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..656
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 106
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 80
FT /note="G->A: No interaction with dis3; 10-fold increase in
FT minichromosome loss."
FT /evidence="ECO:0000269|PubMed:12376568"
FT MUTAGEN 402
FT /note="G->D: 10-fold increase in minichromosome loss."
FT /evidence="ECO:0000269|PubMed:12376568"
SQ SEQUENCE 656 AA; 73352 MW; 2A90382C341C6E61 CRC64;
MQYVGRAFDS VTKTWNAINP STLSGAIDVI VVEQEDKTLA CSPFHVRFGK FSLLLPSDKK
VEFSVNGQLT GFNMKLGDGG EAFFVFATEN AVPRELQTSP IVSPTTSPKQ TPSINVTEPQ
DLELDKVSQD HEKDQSNTYL MEDGYEFPLT RDLIRRSKSD ADQTPPTGFK HLRHSSCLEM
AGSDRTPSMP ATTLADLRLL QKAKELGKRL SGKELPTRVG DNGDVMLDMT GYKSSAANIN
IAELARETFK DEFPMIEKLL REDEEGNLWF HASEDAKKFA EVYGHSPPAS PSRTPASPKS
DSALMDEDSD LSRRHSLSEQ SLSPVSESYP QYAKTLRLTS DQLRSLNLKP GKNELSFGVN
GGKAICTANL FFWKHNDPVV ISDIDGTITK SDALGHMFTL IGKDWTHAGV AKLYTDITNN
GYKIMYLTSR SVGQADSTRH YLRNIEQNGY SLPDGPVILS PDRTMAALHR EVILRKPEVF
KMACLRDLCN IFALPVPRTP FYAGFGNRIT DAISYNHVRV PPTRIFTINS AGEVHIELLQ
RSGHRSSYVY MNELVDHFFP PIEVSTRDEV SSFTDVNFWR SPLLELSDEE EDDTNKSTSK
SPKTPKNTKF GYQEFEGIDE EDAQDYSPSP LIKSFNELMF EGEEDEEGEE DVENAV
