MDM1_PONAB
ID MDM1_PONAB Reviewed; 724 AA.
AC Q5RC32;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Nuclear protein MDM1;
GN Name=MDM1;
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].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Microtubule-binding protein that negatively regulates
CC centriole duplication. Binds to and stabilizes microtubules.
CC {ECO:0000250|UniProtKB:Q8TC05}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8TC05}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q8TC05}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:Q8TC05}. Note=Localizes to the centriole lumen.
CC {ECO:0000250|UniProtKB:Q8TC05}.
CC -!- SIMILARITY: Belongs to the MDM1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH90678.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CR858450; CAH90678.1; ALT_INIT; mRNA.
DR RefSeq; NP_001125370.1; NM_001131898.2.
DR RefSeq; XP_009246276.1; XM_009248001.1.
DR AlphaFoldDB; Q5RC32; -.
DR STRING; 9601.ENSPPYP00000005410; -.
DR PRIDE; Q5RC32; -.
DR GeneID; 100172273; -.
DR KEGG; pon:100172273; -.
DR CTD; 56890; -.
DR eggNOG; ENOG502QVRV; Eukaryota.
DR HOGENOM; CLU_023835_0_0_1; -.
DR InParanoid; Q5RC32; -.
DR OrthoDB; 350018at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0046600; P:negative regulation of centriole replication; ISS:UniProtKB.
DR InterPro; IPR029136; MDM1.
DR PANTHER; PTHR32078; PTHR32078; 1.
DR Pfam; PF15501; MDM1; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Microtubule; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..724
FT /note="Nuclear protein MDM1"
FT /id="PRO_0000299061"
FT REGION 79..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 340..364
FT /evidence="ECO:0000255"
FT MOTIF 9..15
FT /note="ST]-E-Y-X(3)-F motif 1; required for efficient
FT microtubule binding and stabilization"
FT /evidence="ECO:0000250|UniProtKB:Q8TC05"
FT MOTIF 189..195
FT /note="ST]-E-Y-X(3)-F motif 2; required for efficient
FT microtubule binding and stabilization"
FT /evidence="ECO:0000250|UniProtKB:Q8TC05"
FT MOTIF 232..238
FT /note="ST]-E-Y-X(3)-F motif 3; required for efficient
FT microtubule binding"
FT /evidence="ECO:0000250|UniProtKB:Q8TC05"
FT MOTIF 306..312
FT /note="ST]-E-Y-X(3)-F motif 4; required for efficient
FT microtubule binding and stabilization"
FT /evidence="ECO:0000250|UniProtKB:Q8TC05"
FT COMPBIAS 91..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..647
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TC05"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D067"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D067"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TC05"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TC05"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D067"
FT MOD_RES 570
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D067"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TC05"
FT MOD_RES 658
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TC05"
SQ SEQUENCE 724 AA; 81888 MW; 7258F7366731900A CRC64;
MPVRFKGLSE YQRNFLWKKS YLSESCNSSV GRKYPWAGLR SDQLGITKEP SFISKRRVPY
HDPQISKSLE WNGAISESNV VASPEPEAPE TPKSQEAEQK DVTQERVHSL EASRVPKRTR
SHSADSRAEG ASDVENNEGV TNHTPVNENV ELEHSTKVLS ENVDNGLDRL LRKKAGLTVV
PSYNALRNSE YQRQFVWKTS KETAPAFSAN QVFHNKSQFV PPFKGNSIIH ETEYKRNFKG
LSPVKEPKLR NDLRENRNLE TVSPEKKSNK IDDPLKLEAE MELKDLHQPK KKLAPWKHQR
LGKVNSEYRA KFLSPAQYLY KAGAWTRVKG NMPNQGSLNA MWYAEVKELR EKAEFYRKRV
QGTHFSRDHL NQILSDSNCC WDVSSTTSSE GTISSNIRAL DLAGDPTSHK TLQKCPSTEP
EEKGNIVEEQ PQKNTTEKLG VSAPTIPVRR RLAWDTENTS EDVQKQPREK EEEDDDEEEG
DRKTGKQAVR GEQEKLDVHE KSKADKMKEG SDSSVSSEKG GRLPTPKLRE LGGIQRTHHD
LTTPAVGGAV LVSPSKMKPP APEQRKRMTS QDCLETSKND FTKKESHAVS LLTSPAAGIK
TVDPLPLRED SEDNIPKFAE ATLPVSKIPE YPTNPPGQSP SPPHVPSYWY PSRRIQGSLR
DPEFQHNVRK ARMNNLRLPQ HEAFNDEDED RLSEISARSA ASSLRAFQTL ARAKKRKENF
WGIT
