ID   NUR1_YEAS7              Reviewed;         484 AA.
AC   A6ZXN8;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Nuclear rim protein 1;
GN   Name=NUR1; ORFNames=SCY_0826;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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; AAFW02000145; EDN60268.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZXN8; -.
DR   EnsemblFungi; EDN60268; EDN60268; SCY_0826.
DR   HOGENOM; CLU_033252_1_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
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_0000409034"
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..458
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;  56805 MW;  E4ED0E4D18A0918D 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
     QEYEDKHIMA RINQCSNIDT LSSAMGTRSK TPRIFTTHSL CGEEIREVYN YEKREFEALP
     KMTESVPGSR ETRIKDYGGI SQVSDNQSHP IGFHYSPRMS PYYRDKVLDN NLAQSSSNEN
     LEKGGAFLPN QDQNRPSKSL SPLRKTPLSA RQKRFEGSEF NVLNKNDINS ILRSPKKKKN
     YHKR