MISP_PONAB
ID MISP_PONAB Reviewed; 685 AA.
AC Q5RBH3;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Mitotic interactor and substrate of PLK1 {ECO:0000250|UniProtKB:Q8IVT2};
GN Name=MISP {ECO:0000250|UniProtKB:Q8IVT2};
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: Plays a role in mitotic spindle orientation and mitotic
CC progression. Regulates the distribution of dynactin at the cell cortex
CC in a PLK1-dependent manner, thus stabilizing cortical and astral
CC microtubule attachments required for proper mitotic spindle
CC positioning. May link microtubules to the actin cytospkeleton and focal
CC adhesions. May be required for directed cell migration and centrosome
CC orientation. May also be necessary for proper stacking of the Golgi
CC apparatus (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Associates with F-actin. Interacts with DCTN1; this
CC interaction regulates DCTN1 distribution at the cell cortex. Interacts
CC with PTK2/FAK and MAPRE1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000250}.
CC Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cell cortex
CC {ECO:0000250}. Note=Predominantly localizes to cortical actin
CC structures during interphase and mitosis. Present in retraction fibers,
CC which are formed at former adhesion sites during mitosis, and at
CC spicular membrane protrusions in re-attaching cytokinetic cells.
CC Partially colocalizes with cytoplasmic F-actin. Not detected at
CC microtubules at interphase, nor at spindle during mitosis (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated by CDK1 and PLK1. CDK1 is the priming kinase for
CC PLK1 phosphorylation. Phosphorylation by PLK1 is required for proper
CC spindle orientation at metaphase (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MISP family. {ECO:0000305}.
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DR EMBL; CR858675; CAH90887.1; -; mRNA.
DR RefSeq; NP_001125506.1; NM_001132034.1.
DR AlphaFoldDB; Q5RBH3; -.
DR SMR; Q5RBH3; -.
DR STRING; 9601.ENSPPYP00000010425; -.
DR GeneID; 100172415; -.
DR KEGG; pon:100172415; -.
DR CTD; 126353; -.
DR eggNOG; ENOG502RZZI; Eukaryota.
DR OrthoDB; 481627at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005884; C:actin filament; ISS:UniProtKB.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0031616; C:spindle pole centrosome; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0051660; P:establishment of centrosome localization; ISS:UniProtKB.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; ISS:UniProtKB.
DR GO; GO:0090307; P:mitotic spindle assembly; ISS:UniProtKB.
DR GO; GO:0051640; P:organelle localization; ISS:UniProtKB.
DR GO; GO:1904776; P:regulation of protein localization to cell cortex; ISS:UniProtKB.
DR InterPro; IPR029304; AKAP2_C.
DR InterPro; IPR042779; MISP/MISP3.
DR PANTHER; PTHR18839; PTHR18839; 2.
DR Pfam; PF15304; AKAP2_C; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; Cell cycle; Cell division; Cell junction; Coiled coil;
KW Cytoplasm; Cytoskeleton; Mitosis; Phosphoprotein; Reference proteome.
FT CHAIN 1..685
FT /note="Mitotic interactor and substrate of PLK1"
FT /id="PRO_0000079383"
FT REGION 155..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 551..575
FT /evidence="ECO:0000255"
FT COMPBIAS 356..373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 78
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q8IVT2"
FT MOD_RES 172
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q8IVT2"
FT MOD_RES 179
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IVT2"
FT MOD_RES 214
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q8IVT2"
FT MOD_RES 219
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IVT2"
FT MOD_RES 284
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q8IVT2"
FT MOD_RES 287
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q8IVT2"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IVT2"
FT MOD_RES 377
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q8IVT2"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IVT2"
FT MOD_RES 394
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q8IVT2"
FT MOD_RES 395
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q8IVT2"
FT MOD_RES 397
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q8IVT2"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IVT2"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IVT2"
FT MOD_RES 477
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q8IVT2"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IVT2"
FT MOD_RES 549
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IVT2"
FT MOD_RES 581
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q8IVT2"
FT MOD_RES 583
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IVT2"
FT MOD_RES 592
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q8IVT2"
FT MOD_RES 681
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IVT2"
SQ SEQUENCE 685 AA; 75892 MW; A3A99F4343396E81 CRC64;
MDRVTRYPIL GIPQAHRGTG LVLDGDTSYT YHLVCTGPEA SGWGQDEPQT WPTDYKAQQG
VLRQGVSYSV RAYPGQPSPR GLHLETGEDE GLKVYRLGAR DAHQGRPTWA VHPEDGEDEE
MKTYRLDAGD AVPRGLCDLE RERWAIIQGQ AVRKSGTVAT LQAAPDHGDP RTPGPPRSTP
LEENVVDREQ IDFLAARQQF LSLEQANKEV PHSSPARGTP AGPSPGVSQA PKAFNKPHLV
NGHVVPTKPQ GKGVFREENK VRAVPAWASV QVADDPGSLA PVESPGTPKE TPIEREIRLA
QEREADLREQ RGLRRAADHQ ELVEIPSRPL LTKVSLITAP RRERGRPSLY VQRDMVQETQ
REEDHRREGL HVGRASTPDW VSEDPQPGLR RALSSDSILS PDSILSPAPD ARAADPAPEV
RKVNRIPPDA YQPYLSPGTP QLEPSAFGAF SKPSGLSTVD TEAATSPKAT MSPRHLSESS
GKPMSTKQEP WKLPRGSPQA NRGVVRWEYF RLRPLQFRAP DEPQQAQVPH VWGWEVAGAP
ALRLQKSQSS DLLERERESV LRREREVAEE RRNALFPEVF SPTPDESCDQ NSRSSSQASG
ITGSYSVSES PFFSPIRLHS SLAWTVEDPV DSAPPGQRKK EQWYAGINPS DGINSEVLEA
IRVTRHKNTM AERWESRIYA SEEDD
