ID   MLF1_PONAB              Reviewed;         268 AA.
AC   Q5R4T3; Q5R7V0;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Myeloid leukemia factor 1;
DE   AltName: Full=Myelodysplasia-myeloid leukemia factor 1;
GN   Name=MLF1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in lineage commitment of primary hemopoietic
CC       progenitors by restricting erythroid formation and enhancing myeloid
CC       formation. Interferes with erythropoietin-induced erythroid terminal
CC       differentiation by preventing cells from exiting the cell cycle through
CC       suppression of CDKN1B/p27Kip1 levels. Suppresses COP1 activity via CSN3
CC       which activates p53 and induces cell cycle arrest. Binds DNA and
CC       affects the expression of a number of genes so may function as a
CC       transcription factor in the nucleus (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with CENPU. Also interacts with NRBP1/MADM,
CC       YWHAZ/14-3-3-zeta and HNRPUL2/MANP. NRBP1 recruits a serine kinase
CC       which phosphorylates both itself and MLF1. Phosphorylated MLF1 then
CC       binds to YWHAZ and is retained in the cytoplasm. Retained in the
CC       nucleus by binding to HNRPUL2. Binds to COPS3/CSN3 which is required
CC       for suppression of COP1 and activation of p53 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9QWV4}. Nucleus
CC       {ECO:0000250|UniProtKB:Q9QWV4}. Cell projection, cilium
CC       {ECO:0000250|UniProtKB:Q9QWV4}. Cytoplasm, cytoskeleton, cilium basal
CC       body {ECO:0000250|UniProtKB:Q9QWV4}. Note=Shuttles between the
CC       cytoplasm and nucleus. {ECO:0000250|UniProtKB:Q9QWV4}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5R4T3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5R4T3-2; Sequence=VSP_020021;
CC   -!- PTM: Phosphorylation is required for binding to YWHAZ. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MLF family. {ECO:0000305}.
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DR   EMBL; CR860009; CAH92160.1; -; mRNA.
DR   EMBL; CR861160; CAH93233.1; -; mRNA.
DR   RefSeq; NP_001127516.1; NM_001134044.1. [Q5R4T3-1]
DR   AlphaFoldDB; Q5R4T3; -.
DR   STRING; 9601.ENSPPYP00000015924; -.
DR   GeneID; 100174592; -.
DR   KEGG; pon:100174592; -.
DR   CTD; 4291; -.
DR   eggNOG; KOG4049; Eukaryota.
DR   InParanoid; Q5R4T3; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR   GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0002318; P:myeloid progenitor cell differentiation; ISS:UniProtKB.
DR   GO; GO:1902806; P:regulation of cell cycle G1/S phase transition; ISS:UniProtKB.
DR   GO; GO:0006351; P:transcription, DNA-templated; ISS:UniProtKB.
DR   InterPro; IPR019376; Myeloid_leukemia_factor.
DR   PANTHER; PTHR13105; PTHR13105; 1.
DR   Pfam; PF10248; Mlf1IP; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell cycle; Cell projection; Cytoplasm; Cytoskeleton;
KW   Developmental protein; Differentiation; DNA-binding; Nucleus;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..268
FT                   /note="Myeloid leukemia factor 1"
FT                   /id="PRO_0000247599"
FT   REGION          50..125
FT                   /note="Interaction with COPS3"
FT                   /evidence="ECO:0000250"
FT   REGION          208..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..261
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         6
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QWV4"
FT   MOD_RES         8
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P58340"
FT   MOD_RES         32
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P58340"
FT   VAR_SEQ         1..110
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_020021"
FT   CONFLICT        257
FT                   /note="H -> Y (in Ref. 1; CAH92160)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   268 AA;  30667 MW;  8A5304E519D1C757 CRC64;
     MFRMLSSSFE DDPFFSESIL AHRENMRQMM RSFTEPFGRD LLSISDGRGR VHNRRGHNDG
     EDSLTHTDVS SLQTVDQMVS NMRNYMQKLE RNFGQLSVDP NGHSFCSSSV MTYSKIGDEP
     PKVFQASTQT RRAPGGIKET RKAMRDSDSG LEKMAIGHHI HDRAHVIKKS KNKKTGDEEV
     NQEFINMNES DAHAFDEEWQ SEVLKYKPGR HNLENTRMRS VGHENPGSRE LKRREKPQQS
     PAIEHGRRSD VLGDKLHIKG SSVKSNKK