MDM1_RAT
ID MDM1_RAT Reviewed; 719 AA.
AC Q5PQN4;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Nuclear protein MDM1;
GN Name=Mdm1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124; SER-127; SER-266;
RP SER-283 AND SER-286, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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=AAH87101.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BC087101; AAH87101.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001017459.2; NM_001017459.2.
DR AlphaFoldDB; Q5PQN4; -.
DR STRING; 10116.ENSRNOP00000041359; -.
DR iPTMnet; Q5PQN4; -.
DR PhosphoSitePlus; Q5PQN4; -.
DR PaxDb; Q5PQN4; -.
DR PRIDE; Q5PQN4; -.
DR Ensembl; ENSRNOT00000048765; ENSRNOP00000041359; ENSRNOG00000007286.
DR GeneID; 314859; -.
DR KEGG; rno:314859; -.
DR UCSC; RGD:1561092; rat.
DR CTD; 56890; -.
DR RGD; 1561092; Mdm1.
DR eggNOG; ENOG502QVRV; Eukaryota.
DR GeneTree; ENSGT00390000004106; -.
DR HOGENOM; CLU_023835_0_0_1; -.
DR InParanoid; Q5PQN4; -.
DR OMA; KVNTEYR; -.
DR OrthoDB; 350018at2759; -.
DR PhylomeDB; Q5PQN4; -.
DR TreeFam; TF331015; -.
DR PRO; PR:Q5PQN4; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000007286; Expressed in testis and 20 other tissues.
DR ExpressionAtlas; Q5PQN4; baseline and differential.
DR Genevisible; Q5PQN4; RN.
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:0097730; C:non-motile cilium; ISO:RGD.
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 GO; GO:0060041; P:retina development in camera-type eye; ISO:RGD.
DR InterPro; IPR029136; MDM1.
DR PANTHER; PTHR32078; PTHR32078; 1.
DR Pfam; PF15501; MDM1; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Microtubule; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..719
FT /note="Nuclear protein MDM1"
FT /id="PRO_0000299062"
FT REGION 78..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 339..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 192..198
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 235..241
FT /note="ST]-E-Y-X(3)-F motif 3; required for efficient
FT microtubule binding and stabilization"
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 94..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..488
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D067"
FT MOD_RES 565
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D067"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D067"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TC05"
SQ SEQUENCE 719 AA; 80698 MW; 322429903762FEE0 CRC64;
MPVRFKGLSE YQRNFLWKKS YLSESYNPSV GQKYTWAGLR SDQLGITKEP SFISKRRVPY
YDPQISKYLE WNGTVRENDA LAPPEPQIIR TPKPQEAEQR EDANHETVLP QEASRVPKRT
RSHSADSRAE GASDGVEKHQ DVTKNHSLVN ADVELRPSTK PLPESIEPRL DRHLRKKAGL
AVVPLNNALR NSEYQRQFVW KTCKETAPVC AANQVFRNKS QVIPQFQGNT FIHESEYKRN
FKGLTPVKEP KLREYLKGNS SFEILSPEKK ADEPLDLEVD MASEDSDQPI KKPAPWRHQR
LGKVNSEYRA KFLSPAQYLY KAGAWTRVKE SLSHQGSLNA MWYAEVKELR EKAESYRKRV
QGTHFSRDHL NQIMSDSNCC WDVSSVASSE GTISSNIQAL DLAGDLTSHR TLQKHPPTKL
EEKKVALAEQ PLENTIRSLE LPEAPTMARR KLAWDAAEGT QKEDTQEEPS GEEDGREARG
KDKQVCAGEL QKVDMQTSKA DGPTEGSETS SVSSGKGGRL PTPRLRELGI QRTHHDLTTP
AVGGAVLVSP AKAKPSALEQ RRRPSSQDGL ETLKKGITKK GKHRPLSLLT SPTAGMKTVD
PLPLRQDCDA NVLRVAEGTL PVLKNLDHQT NTPGQPSPCT LPYCHPSSRI QGRLRDPEFQ
HNIGKPRMNN TQLLPHGAFN DEDADRLSEI SARSAVSSLQ AFQTLARAQK RKENFWGKP
