MDM1_CHICK
ID MDM1_CHICK Reviewed; 691 AA.
AC Q5ZMW6;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Nuclear protein MDM1;
GN Name=MDM1; ORFNames=RCJMB04_1a5;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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}.
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DR EMBL; AJ719268; CAG30927.1; -; mRNA.
DR RefSeq; NP_001025913.1; NM_001030742.1.
DR AlphaFoldDB; Q5ZMW6; -.
DR STRING; 9031.ENSGALP00000016111; -.
DR PaxDb; Q5ZMW6; -.
DR GeneID; 417839; -.
DR KEGG; gga:417839; -.
DR CTD; 56890; -.
DR VEuPathDB; HostDB:geneid_417839; -.
DR eggNOG; ENOG502QVRV; Eukaryota.
DR InParanoid; Q5ZMW6; -.
DR PhylomeDB; Q5ZMW6; -.
DR PRO; PR:Q5ZMW6; -.
DR Proteomes; UP000000539; 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 GO; GO:0060041; P:retina development in camera-type eye; IBA:GO_Central.
DR InterPro; IPR029136; MDM1.
DR PANTHER; PTHR32078; PTHR32078; 2.
DR Pfam; PF15501; MDM1; 2.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Microtubule; Nucleus;
KW Reference proteome; Repeat.
FT CHAIN 1..691
FT /note="Nuclear protein MDM1"
FT /id="PRO_0000299063"
FT REGION 87..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 411..445
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 184..190
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 259..265
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 COMPBIAS 90..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..249
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 691 AA; 77350 MW; 14E75C3DB0A0F9A0 CRC64;
MPVRFRGLSE YKRNFRWKTP ELCSPSQEQK SPWAGLRSDQ LGITREPNFI SKRRVPYHNP
QISKSFEWTG DCDSDDPVET EALKTAESLA EHSNDVNQEN TETPEGPRLP PKVRSHSSDS
GVETALALAG NSMKKTPPVA PPNQKEAFVS PKKEAEKVNN GLHRVLQRKG GMNTPHLSTF
PRNSEYQSQF VWKSPHEKSP ILAAEEALYN TKREELIQKP AEDASKQEKS EQKHPKRKNK
QHISQKPLSL HTHRGKMNTE YRSKFLSPAQ YFYKDGAWSR IRSKVPNQAS QNPLNSMWYM
EVRELRARAK AYRQRIEGTH FSRYHLNQLL SDNNSLWDVS SNSSSEEGIS NDIRALDLAG
VSEKETAPRP KMLQQPGSRE QSHQDDTEKK GLSDAPTVPV KRRLVWGEQE GTAEKDSQQL
REEEEKENEQ AAVVTQNLEK NNEGINEDNR IEGENTCLPN SPAAVSESSS VSSEPGGRLP
TPKLRALGRA QRTHHDLTTP AVGGAVLVSP PKFKSSTSQQ RMRSLGTDPS SVGQGAREAS
QRRSFRPGAK LKAVSLLTSP PAGLGTVDPL PLRQDQWHPN GVSGETVAIN SAYQERSSTP
PVLKSTKNRP MPCWSPSPRI QGTLKDPEFQ HNGNVGNPKM GSFQLPLQER NYNNEDDRLS
QISARSAASS SLASQILERA QKRKEDFWGK T
