ID   LIN9_MACFA              Reviewed;         542 AA.
AC   Q4R8N2;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Protein lin-9 homolog;
GN   Name=LIN9; ORFNames=QtsA-12009;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as a tumor suppressor. Inhibits DNA synthesis. Its
CC       ability to inhibit oncogenic transformation is mediated through its
CC       association with RB1. Plays a role in the expression of genes required
CC       for the G1/S transition (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the DREAM complex (also named LINC complex) at
CC       least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2,
CC       RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in quiescent
CC       cells where it represses cell cycle-dependent genes. It dissociates in
CC       S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds
CC       to MYBL2. Interacts with RB1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. Note=Found in
CC       perinucleolar structures. Associated with chromatin. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the lin-9 family. {ECO:0000305}.
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DR   EMBL; AB168419; BAE00540.1; -; mRNA.
DR   RefSeq; NP_001306385.1; NM_001319456.1.
DR   AlphaFoldDB; Q4R8N2; -.
DR   STRING; 9541.XP_005541067.1; -.
DR   PRIDE; Q4R8N2; -.
DR   GeneID; 101925602; -.
DR   CTD; 286826; -.
DR   eggNOG; KOG1019; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0017053; C:transcription repressor complex; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   InterPro; IPR033471; DIRP.
DR   InterPro; IPR010561; LIN-9/ALY1.
DR   InterPro; IPR045831; LIN9_C.
DR   PANTHER; PTHR21689; PTHR21689; 2.
DR   Pfam; PF06584; DIRP; 1.
DR   Pfam; PF19438; LIN9_C; 1.
DR   SMART; SM01135; DIRP; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cell cycle; Coiled coil; DNA synthesis; Isopeptide bond;
KW   Nucleus; Phosphoprotein; Reference proteome; Tumor suppressor;
KW   Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q5TKA1"
FT   CHAIN           2..542
FT                   /note="Protein lin-9 homolog"
FT                   /id="PRO_0000249547"
FT   REGION          2..296
FT                   /note="Sufficient for interaction with RB1"
FT                   /evidence="ECO:0000250"
FT   COILED          355..413
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5TKA1"
FT   MOD_RES         65
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5TKA1"
FT   MOD_RES         95
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8C735"
FT   MOD_RES         96
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5TKA1"
FT   MOD_RES         304
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5TKA1"
FT   MOD_RES         309
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5TKA1"
FT   MOD_RES         321
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5TKA1"
FT   CROSSLNK        21
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q5TKA1"
SQ   SEQUENCE   542 AA;  61960 MW;  078C3A6EAD382D71 CRC64;
     MAELDQLPDE SSSAKALVSL KEGSLSNTWN EKYSSLQKTP VWKGRNTSPA VEMPFRNSKR
     SRLFSDEDDR QINTRSPKRN QRVAMVPQKF TATMSTPDKK ASQKIGFRLR NLLKLPKAHK
     WCIYEWFYSN IDKPLFEGDN DFCVCLKESF PNLKTRKLTR VEWGKIRRLM GKPRRCSSAF
     FEEERSALKQ KRQKIRLLQQ RKVADVSQFK DLPDEIPLPL VIGTKVTARL RGVHDGLFTG
     QIDAVDTLNA TYRVTFDRTG LGTHTIPDYE VLSNEPHETM PIAAFGQKQR PSRFFMTPPR
     LHYTPPLQSP IMDNDPLLGQ SPWRSKISGS DTETLGGFPV EFLIQVTRLS KILMIKKEHI
     KKLREMNTDA EKLKSYSMPI SIEFQRRYAT IVLELEQLNK DLNKVLHKVQ QYCYELAPDQ
     GLQPADQPTD MRRRCEEEAQ EIVRHANSST GQPCVENENL TDLISRLTAI LLQIKCLAEG
     GDLNSFEFKS LTDSLNDIKS TIDASNISCF QNNVEIHVAH IQSGLSQMGN LHAFAANNTN
     RD