ID   NUR1_YEAS8              Reviewed;         484 AA.
AC   C8Z6L4;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=Nuclear rim protein 1;
GN   Name=NUR1; ORFNames=EC1118_1D0_1354g;
OS   Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's
OS   yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=643680;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lalvin EC1118 / Prise de mousse;
RX   PubMed=19805302; DOI=10.1073/pnas.0904673106;
RA   Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., Cambon B.,
RA   Legras J.-L., Wincker P., Casaregola S., Dequin S.;
RT   "Eukaryote-to-eukaryote gene transfer events revealed by the genome
RT   sequence of the wine yeast Saccharomyces cerevisiae EC1118.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:16333-16338(2009).
CC   -!- FUNCTION: Member of a perinuclear network that controls recombination
CC       at multiple loci to maintain genome stability. Required for rDNA repeat
CC       stability (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with CSM1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NUR1 family. {ECO:0000305}.
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DR   EMBL; FN393063; CAY78419.1; -; Genomic_DNA.
DR   AlphaFoldDB; C8Z6L4; -.
DR   EnsemblFungi; CAY78419; CAY78419; EC1118_1D0_1354g.
DR   HOGENOM; CLU_033252_1_0_1; -.
DR   Proteomes; UP000000286; Chromosome IV, Scaffold EC1118_1D0.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR018819; Nur1/Mug154.
DR   PANTHER; PTHR28293; PTHR28293; 1.
DR   Pfam; PF10332; DUF2418; 1.
PE   3: Inferred from homology;
KW   Membrane; Nucleus; Phosphoprotein; Transmembrane; Transmembrane helix.
FT   CHAIN           1..484
FT                   /note="Nuclear rim protein 1"
FT                   /id="PRO_0000409035"
FT   TRANSMEM        145..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        252..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          416..457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..446
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         3
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12066"
FT   MOD_RES         417
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12066"
FT   MOD_RES         474
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12066"
SQ   SEQUENCE   484 AA;  56833 MW;  AC05FF8F519D2DD0 CRC64;
     MGSNDLINEA YDDSEVVGEE RESKSAWMKR WYQLLTSPLD LQLVINEKLE MINWDAYAKS
     LAKPLGNFLT ILFFIIRLLQ DNLIKPNYYK LNVKSGAFDL SKSNKLKEFD YLWEISSSFQ
     NSNQFYAFQS WYFVTLRFLN NLFRFTIFIL LSLNLYVSCK FMFGYFKTYN LFHLKKEFNS
     PNLTKHNLKD LSKEYYEDIY KQSLWSMLKH FFRGSRDDGP HVNQNEVEIF FQLRKWIPTN
     FMINLFVSFS PTAIVFLSFS DVSFTSAIAI VFHQYILDYI ITKRFQRSVD DDLILSSAAL
     QEYEDKHIMV RINQCSNIDT LSSAMGTRSK TPRIFTTHSL CGEEIREVYN YEKREFEALP
     KMTESVPGSR ETRIKDYGGI SQVSDNQSHP IGFHYSPRMS PYYRDKVLDN NLAQSSSNEN
     LEKGGAFLPN QDQNRPSKSL SPLRKTPLSA RQKRFEGSEF NVLNKNDINS ILRSPKKKKN
     YHKR