ID   MLF1_BOVIN              Reviewed;         270 AA.
AC   Q32KY3;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Myeloid leukemia factor 1;
DE   AltName: Full=Myelodysplasia-myeloid leukemia factor 1;
GN   Name=MLF1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) 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   -!- 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; BC109859; AAI09860.1; -; mRNA.
DR   RefSeq; NP_001033247.1; NM_001038158.2.
DR   AlphaFoldDB; Q32KY3; -.
DR   STRING; 9913.ENSBTAP00000005403; -.
DR   PaxDb; Q32KY3; -.
DR   Ensembl; ENSBTAT00000005403; ENSBTAP00000005403; ENSBTAG00000004126.
DR   GeneID; 533379; -.
DR   KEGG; bta:533379; -.
DR   CTD; 4291; -.
DR   VEuPathDB; HostDB:ENSBTAG00000004126; -.
DR   eggNOG; KOG4049; Eukaryota.
DR   GeneTree; ENSGT00390000005023; -.
DR   HOGENOM; CLU_063313_0_1_1; -.
DR   InParanoid; Q32KY3; -.
DR   OrthoDB; 1471165at2759; -.
DR   TreeFam; TF317561; -.
DR   Proteomes; UP000009136; Chromosome 1.
DR   Bgee; ENSBTAG00000004126; Expressed in semen and 105 other tissues.
DR   ExpressionAtlas; Q32KY3; baseline and differential.
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:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
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   Cell cycle; Cell projection; Cytoplasm; Cytoskeleton;
KW   Developmental protein; Differentiation; DNA-binding; Nucleus;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..270
FT                   /note="Myeloid leukemia factor 1"
FT                   /id="PRO_0000247598"
FT   REGION          50..125
FT                   /note="Interaction with COPS3"
FT                   /evidence="ECO:0000250"
FT   REGION          127..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          221..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        225..247
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   MOD_RES         34
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P58340"
SQ   SEQUENCE   270 AA;  31227 MW;  A584162BEFFD612B CRC64;
     MFGMLSSSFE DDPFFSDSFI AHRESMRQMM RSFSEPFGRD MLSISDRRGR ARNRMGHEDE
     ENSLTHTDVS PFQAMDRMML NMRNSMQELQ RNFGHLSMDP NGHSFSSSSV MTYSKVGDEP
     PKVFQASTQT RRAPGGIKET RKALRDSDSG LEKMAVGHHL HDRAHVIKKS KNNKTGDEEV
     NQEFINMNEC DAHAFDDEWQ NEILKYQPRG QWRNLDNSRM RSVAHENSGS RELKRREKHH
     QSPAIEHGRR SNVFVDKLNI KGSPVKINKK