ID   NUR1_YEAS1              Reviewed;         484 AA.
AC   B3LGY4;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=Nuclear rim protein 1;
GN   Name=NUR1; ORFNames=SCRG_00586;
OS   Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=285006;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM11-1a;
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA   Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA   Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA   Kruglyak L.;
RT   "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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; CH408043; EDV08363.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3LGY4; -.
DR   EnsemblFungi; EDV08363; EDV08363; SCRG_00586.
DR   HOGENOM; CLU_033252_1_0_1; -.
DR   Proteomes; UP000008335; 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_0000409032"
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;  56821 MW;  E4EB6FAD18AE2B8D CRC64;
     MGSNDLINEA YDDSEVVGEE RESKSAWMKR WYQLLTSPLD LQLVINEKLE MINWDAYAKS
     LAKPLGNFLT ILFFIIRLLQ DNLIKPNYYK LNVKSGAFDL SKSNKLKEFD YLWEISSSFQ
     NSNQFYAFQS WYFVTLRFLN NLFRFTIFIL LSLNLYVSCK FMFGYFKTYN LFHLKKEFNS
     PNLTKHNLKD LSKEYYEDIY KQSLWSMLKH FFRGSRDDGP HVNQNEDEIF 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