PRC1_MOUSE
ID PRC1_MOUSE Reviewed; 603 AA.
AC Q99K43; E9QPF0; Q8CE25;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Protein regulator of cytokinesis 1 {ECO:0000312|MGI:MGI:1858961};
GN Name=Prc1 {ECO:0000312|MGI:MGI:1858961};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAH05475.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II {ECO:0000312|EMBL:AAH05475.1};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH05475.1};
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 [3] {ECO:0000305, ECO:0000312|EMBL:BAC26320.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-484.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC26320.1};
RC TISSUE=Skin {ECO:0000312|EMBL:BAC26320.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4] {ECO:0000305}
RP DEVELOPMENTAL STAGE.
RX PubMed=10727870; DOI=10.1016/s0925-4773(00)00243-4;
RA Tarabykin V., Britanova O., Fradkov A., Voss A., Katz L.S., Lukyanov S.,
RA Gruss P.;
RT "Expression of PTTG and prc1 genes during telencephalic neurogenesis.";
RL Mech. Dev. 92:301-304(2000).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Key regulator of cytokinesis that cross-links antiparrallel
CC microtubules at an average distance of 35 nM. Essential for controlling
CC the spatiotemporal formation of the midzone and successful cytokinesis.
CC Required for KIF14 localization to the central spindle and midbody.
CC Required to recruit PLK1 to the spindle. Stimulates PLK1
CC phosphorylation of RACGAP1 to allow recruitment of ECT2 to the central
CC spindle. Acts as an oncogene for promoting bladder cancer cells
CC proliferation, apoptosis inhibition and carcinogenic progression.
CC {ECO:0000250|UniProtKB:O43663}.
CC -!- SUBUNIT: Homodimer. Interacts with the C-terminal Rho-GAP domain and
CC the basic region of RACGAP1. The interaction with RACGAP1 inhibits its
CC GAP activity towards CDC42 in vitro, which may be required for
CC maintaining normal spindle morphology. Interacts (via N-terminus) with
CC the C-terminus of CENPE (via C-terminus); the interaction occurs during
CC late mitosis. Interacts (via N-terminus) with KIF4A (via C-terminus);
CC the interaction is required for the progression of mitosis. Interacts
CC (via N-terminus) with KIF23 (via C-terminus); the interaction occurs
CC during late mitosis. Interacts with KIF14 and KIF20A. Interacts with
CC PLK1. Interacts with KIF20B. {ECO:0000250|UniProtKB:O43663}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43663}. Cytoplasm
CC {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}.
CC Midbody {ECO:0000250|UniProtKB:O43663}. Note=Colocalized with KIF20B in
CC the nucleus of bladder carcinoma cells at the interphase. Colocalized
CC with KIF20B in bladder carcinoma cells at prophase, metaphase, early
CC anaphase, at the midzone in late anaphase and at the contractile ring
CC in telophase. Predominantly localized to the nucleus of interphase
CC cells. During mitosis becomes associated with the mitotic spindle
CC poles, and localizes with the cell midbody during cytokinesis. Co-
CC localizes with PRC1 in early mitosis and at the spindle midzone from
CC anaphase B to telophase. {ECO:0000250|UniProtKB:O43663}.
CC -!- DEVELOPMENTAL STAGE: During the stages 11.5-13.5 dpc it is expressed in
CC most embryonic tissues. Within the telencephalon, it is predominantly
CC expressed inside the ventricular zone where expression reaches its peak
CC at 15.5 dpc and starts to decrease by 18.5 dpc. Expression is also
CC observed in mitotically active cells outside the telencephalon, but not
CC in adult brain. {ECO:0000269|PubMed:10727870}.
CC -!- DOMAIN: Microtubule binding occurs via a basic patch in the central
CC spectrin-like domain and requires also the unstructured C-terminal
CC domain. {ECO:0000250}.
CC -!- PTM: Phosphorylation by CDK1 in early mitosis holds PRC1 in an inactive
CC monomeric state, during the metaphase to anaphase transition, PRC1 is
CC dephosphorylated, promoting interaction with KIF4A, which then
CC translocates PRC1 along mitotic spindles to the plus ends of
CC antiparallel interdigitating microtubules. Dephosphorylation also
CC promotes MT-bundling activity by allowing dimerization. Phosphorylation
CC by CDK1 prevents PLK1-binding: upon degradation of CDK1 at anaphase and
CC dephosphorylation, it is then phosphorylated by PLK1, leading to
CC cytokinesis (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MAP65/ASE1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC26320.1; Type=Miscellaneous discrepancy; Note=Probable intron retention.; Evidence={ECO:0000305};
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DR EMBL; AC109232; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC136740; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005475; AAH05475.1; -; mRNA.
DR EMBL; AK029140; BAC26320.1; ALT_SEQ; mRNA.
DR CCDS; CCDS71985.1; -.
DR RefSeq; NP_001272926.1; NM_001285997.1.
DR AlphaFoldDB; Q99K43; -.
DR SMR; Q99K43; -.
DR BioGRID; 231410; 3.
DR IntAct; Q99K43; 4.
DR STRING; 10090.ENSMUSP00000129675; -.
DR iPTMnet; Q99K43; -.
DR PhosphoSitePlus; Q99K43; -.
DR EPD; Q99K43; -.
DR MaxQB; Q99K43; -.
DR PaxDb; Q99K43; -.
DR PRIDE; Q99K43; -.
DR ProteomicsDB; 291858; -.
DR Antibodypedia; 28979; 269 antibodies from 36 providers.
DR Ensembl; ENSMUST00000047558; ENSMUSP00000043379; ENSMUSG00000038943.
DR GeneID; 233406; -.
DR KEGG; mmu:233406; -.
DR UCSC; uc009iaf.3; mouse.
DR CTD; 9055; -.
DR MGI; MGI:1858961; Prc1.
DR VEuPathDB; HostDB:ENSMUSG00000038943; -.
DR eggNOG; KOG4302; Eukaryota.
DR GeneTree; ENSGT00390000009453; -.
DR InParanoid; Q99K43; -.
DR OrthoDB; 272248at2759; -.
DR Reactome; R-MMU-5625900; RHO GTPases activate CIT.
DR BioGRID-ORCS; 233406; 25 hits in 73 CRISPR screens.
DR ChiTaRS; Prc1; mouse.
DR PRO; PR:Q99K43; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q99K43; protein.
DR Bgee; ENSMUSG00000038943; Expressed in primary oocyte and 220 other tissues.
DR ExpressionAtlas; Q99K43; baseline and differential.
DR Genevisible; Q99K43; MM.
DR GO; GO:0070938; C:contractile ring; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:1990023; C:mitotic spindle midzone; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019894; F:kinesin binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0001578; P:microtubule bundle formation; ISO:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0051256; P:mitotic spindle midzone assembly; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0032465; P:regulation of cytokinesis; ISS:UniProtKB.
DR InterPro; IPR007145; MAP65_Ase1_PRC1.
DR InterPro; IPR032921; PRC1.
DR PANTHER; PTHR19321; PTHR19321; 1.
DR PANTHER; PTHR19321:SF1; PTHR19321:SF1; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton;
KW Microtubule; Nucleus; Oncogene; Phosphoprotein; Reference proteome.
FT CHAIN 1..603
FT /note="Protein regulator of cytokinesis 1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000229738"
FT REGION 1..341
FT /note="Dimerization"
FT /evidence="ECO:0000250"
FT REGION 342..466
FT /note="Spectrin-fold"
FT /evidence="ECO:0000250"
FT REGION 447..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..603
FT /note="Unstructured, Arg/Lys rich"
FT /evidence="ECO:0000250"
FT REGION 583..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 34..65
FT /evidence="ECO:0000255"
FT COILED 96..136
FT /evidence="ECO:0000255"
FT COILED 211..246
FT /evidence="ECO:0000255"
FT COILED 272..304
FT /evidence="ECO:0000255"
FT COILED 383..463
FT /evidence="ECO:0000255"
FT COMPBIAS 460..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 377
FT /note="Tubulin binding"
FT /evidence="ECO:0000250"
FT SITE 387
FT /note="Tubulin binding"
FT /evidence="ECO:0000250"
FT MOD_RES 470
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:O43663"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43663"
FT MOD_RES 568
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43663"
FT MOD_RES 575
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43663"
FT MOD_RES 599
FT /note="Phosphothreonine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:O43663"
FT CONFLICT 347
FT /note="V -> A (in Ref. 2; AAH05475)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 603 AA; 70290 MW; 267E2966FF237BD1 CRC64;
MRRSEVLADE SITCLQKALT HLREIWELIG IPEEQRLQRT EVVKKHIKDL LDRMIAEEES
LRERLLKSIS ICQKELSTLC SELQVKPFQE EKDTTILQLE KDLRTQVELM RKQKKERKQE
LKLLQEQEQE LRDILCMPPC DVDSTSVPTL EELKLFRQRV ATLRETKESR REEFVNIKKQ
IILCMEELEH SPDTSFERDV VCEDESAFCL SLENIATLQK LLKQLEMKKS QNEAECEGLR
TQIRELWDRL QIPEEEREPV EAIMTGSKTK IRNALKLEVD RLEELKMQNI KQVIEKIRVE
LAQFWDQCFY SQEQRQAFAP YYSEDYTENL LHLHDAEIVR LRNYYDVHKE LFQGVQKWEE
SWKLFLEFER KASDPGRFTN RGGNLLKEEK ERAKLQKTLP KLEEELKARI EQWEQEHSTA
FVVNGQKFME YVTEQWELHR LEKERAKQER QLKNKKQTEA EMLYGSTPRT PSKRPGQTPK
KSGKMNTTTM SSATPNSSIR PVFGGSVYRS PMSRLPPSGS KSVVTSLCSG KKTPRAAQLR
ANKENLDLNG SILSGGYPGS TPLQHNCSIK SVASTYSEFS RELSKASRSD ATSRILNSTN
IQS
