ETT1_SCHPO
ID ETT1_SCHPO Reviewed; 393 AA.
AC Q9USJ7; Q9UTV3; Q9UU19;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Negative regulator of ofd1;
GN Name=nro1; ORFNames=SPCC4B3.07;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 142-348, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15116432; DOI=10.1002/yea.1115;
RA Chen X.Q., Du X., Liu J., Balasubramanian M.K., Balasundaram D.;
RT "Identification of genes encoding putative nucleoporins and transport
RT factors in the fission yeast Schizosaccharomyces pombe: a deletion
RT analysis.";
RL Yeast 21:495-509(2004).
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).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH OFD1.
RX PubMed=19158663; DOI=10.1038/emboj.2008.271;
RA Lee C.Y., Stewart E.V., Hughes B.T., Espenshade P.J.;
RT "Oxygen-dependent binding of Nro1 to the prolyl hydroxylase Ofd1 regulates
RT SREBP degradation in yeast.";
RL EMBO J. 28:135-143(2009).
CC -!- FUNCTION: Required for correct translation termination (By similarity).
CC Positive regulator of the stability of the N-terminal transcription
CC factor domain (Sre1N) of sre1 which is released from the membrane and
CC enters the nucleus to activate hypoxic gene expression. Acts also as a
CC direct inhibitor of ofd1. Functions probably by inhibiting the ability
CC of the ofd1 to accelerate Sre1N degradation in absence of oxygen.
CC {ECO:0000250, ECO:0000269|PubMed:15116432,
CC ECO:0000269|PubMed:19158663}.
CC -!- SUBUNIT: Interacts with ofd1. {ECO:0000269|PubMed:19158663}.
CC -!- INTERACTION:
CC Q9USJ7; Q11120: ofd1; NbExp=11; IntAct=EBI-8549032, EBI-8549003;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- SIMILARITY: Belongs to the ETT1 family. {ECO:0000305}.
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DR EMBL; CU329672; CAB60681.1; -; Genomic_DNA.
DR EMBL; AB027975; BAA87279.1; -; Genomic_DNA.
DR EMBL; AB027866; BAA87170.1; -; Genomic_DNA.
DR PIR; T50441; T50441.
DR RefSeq; NP_588083.1; NM_001023075.2.
DR PDB; 3MSV; X-ray; 2.18 A; A/B=1-393.
DR PDB; 3QTM; X-ray; 2.15 A; A/B=56-393.
DR PDB; 3QTN; X-ray; 3.50 A; B=56-393.
DR PDBsum; 3MSV; -.
DR PDBsum; 3QTM; -.
DR PDBsum; 3QTN; -.
DR AlphaFoldDB; Q9USJ7; -.
DR SMR; Q9USJ7; -.
DR BioGRID; 276001; 25.
DR DIP; DIP-57178N; -.
DR IntAct; Q9USJ7; 16.
DR MINT; Q9USJ7; -.
DR STRING; 4896.SPCC4B3.07.1; -.
DR iPTMnet; Q9USJ7; -.
DR MaxQB; Q9USJ7; -.
DR PaxDb; Q9USJ7; -.
DR PRIDE; Q9USJ7; -.
DR EnsemblFungi; SPCC4B3.07.1; SPCC4B3.07.1:pep; SPCC4B3.07.
DR GeneID; 2539438; -.
DR KEGG; spo:SPCC4B3.07; -.
DR PomBase; SPCC4B3.07; nro1.
DR VEuPathDB; FungiDB:SPCC4B3.07; -.
DR HOGENOM; CLU_710101_0_0_1; -.
DR InParanoid; Q9USJ7; -.
DR OMA; WGLYEMS; -.
DR EvolutionaryTrace; Q9USJ7; -.
DR PRO; PR:Q9USJ7; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0071456; P:cellular response to hypoxia; IDA:PomBase.
DR GO; GO:1900039; P:positive regulation of cellular response to hypoxia; IC:GOC-OWL.
DR GO; GO:0043388; P:positive regulation of DNA binding; IMP:PomBase.
DR GO; GO:2000640; P:positive regulation of SREBP signaling pathway; IMP:PomBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:PomBase.
DR GO; GO:0006606; P:protein import into nucleus; IMP:PomBase.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0032933; P:SREBP signaling pathway; IGI:PomBase.
DR GO; GO:0006415; P:translational termination; IBA:GO_Central.
DR InterPro; IPR024318; Nro1/ETT1.
DR PANTHER; PTHR28290; PTHR28290; 1.
DR Pfam; PF12753; Nro1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Translation regulation.
FT CHAIN 1..393
FT /note="Negative regulator of ofd1"
FT /id="PRO_0000116807"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 142..146
FT /note="NTEES -> IPKNP (in Ref. 2)"
FT /evidence="ECO:0000305"
FT HELIX 14..32
FT /evidence="ECO:0007829|PDB:3MSV"
FT HELIX 62..81
FT /evidence="ECO:0007829|PDB:3QTM"
FT HELIX 85..105
FT /evidence="ECO:0007829|PDB:3QTM"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:3QTM"
FT HELIX 114..129
FT /evidence="ECO:0007829|PDB:3QTM"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:3QTM"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:3QTM"
FT HELIX 144..157
FT /evidence="ECO:0007829|PDB:3QTM"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:3QTM"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:3QTM"
FT HELIX 166..189
FT /evidence="ECO:0007829|PDB:3QTM"
FT TURN 191..195
FT /evidence="ECO:0007829|PDB:3QTM"
FT HELIX 198..217
FT /evidence="ECO:0007829|PDB:3QTM"
FT TURN 229..234
FT /evidence="ECO:0007829|PDB:3QTM"
FT HELIX 235..244
FT /evidence="ECO:0007829|PDB:3QTM"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:3QTM"
FT HELIX 251..267
FT /evidence="ECO:0007829|PDB:3QTM"
FT HELIX 276..301
FT /evidence="ECO:0007829|PDB:3QTM"
FT HELIX 309..332
FT /evidence="ECO:0007829|PDB:3QTM"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:3QTM"
FT HELIX 339..352
FT /evidence="ECO:0007829|PDB:3QTM"
FT HELIX 356..375
FT /evidence="ECO:0007829|PDB:3QTM"
FT HELIX 382..390
FT /evidence="ECO:0007829|PDB:3QTM"
SQ SEQUENCE 393 AA; 44450 MW; 081D5A027088DDDC CRC64;
MIGRRPQGLR AAASLKKQQQ LEKQKQEASY ELSGNSSPSK ENGSENVDNG EMEDETMLVY
TEEDNISQLW GLYEMSREKL ENDDIDASVS LVFGTIHEAD RILRNTEDIS TLPKDFHAAY
SSALLAVSEL FEIAQKRLKE TNTEESYIDA AIERAQLGLD APGNESRLFL ALARAYLEKV
RVLVWRHDNE ESLANIPVTQ LVNPYIEKAI QYLRPLAQDS TEYFDALTPD SLRPLYILSS
YLFQFGDQFS EAFLLDVCSI ITALWLKSVV DPNTPAYYKL IAQEAVLNNY TTFAEYYMDL
LDNSESNVDD LINKASSWLN NSVDTWNVIY TLDKSPERLL KLADIKMDLA QIVQDEASQD
NYLKEACNAI KEAQGSGVEL SPDYVEFVEA YSA
