PSRC1_MOUSE
ID PSRC1_MOUSE Reviewed; 329 AA.
AC Q9D0P7; Q8K4L8; Q9QXY5;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Proline/serine-rich coiled-coil protein 1;
GN Name=Psrc1; Synonyms=Dda3;
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 [MRNA], POSSIBLE FUNCTION, TISSUE SPECIFICITY, AND
RP INDUCTION.
RC STRAIN=ICR X Swiss Webster;
RX PubMed=10618717; DOI=10.1038/sj.onc.1203167;
RA Lo P.-K., Chen J.-Y., Lo W.-C., Chen B.-F., Hsin J.-P., Tang P.-P.,
RA Wang F.-F.;
RT "Identification of a novel mouse p53 target gene DDA3.";
RL Oncogene 18:7765-7774(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RC STRAIN=ICR X Swiss Webster;
RX PubMed=12427559; DOI=10.1016/s0167-4781(02)00512-2;
RA Lo P.-K., Wang F.-F.;
RT "Cloning and characterization of human and mouse DDA3 genes.";
RL Biochim. Biophys. Acta 1579:214-218(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, Placenta, and Thymus;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-47, AND INDUCTION.
RC STRAIN=ICR X Swiss Webster;
RX PubMed=12082536; DOI=10.1038/sj.onc.1205417;
RA Hsieh S.C., Lo P.K., Wang F.F.;
RT "Mouse DDA3 gene is a direct transcriptional target of p53 and p73.";
RL Oncogene 21:3050-3057(2002).
RN [6]
RP INTERACTION WITH APC2.
RX PubMed=17310996; DOI=10.1038/sj.onc.1210304;
RA Hsieh P.-C., Chang J.-C., Sun W.-T., Hsieh S.-C., Wang M.-C., Wang F.-F.;
RT "p53 downstream target DDA3 is a novel microtubule-associated protein that
RT interacts with end-binding protein EB3 and activates beta-catenin
RT pathway.";
RL Oncogene 26:4928-4940(2007).
RN [7]
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: Required for normal progression through mitosis. Required for
CC normal congress of chromosomes at the metaphase plate, and for normal
CC rate of chromosomal segregation during anaphase. Plays a role in the
CC regulation of mitotic spindle dynamics. Increases the rate of turnover
CC of microtubules on metaphase spindles, and contributes to the
CC generation of normal tension across sister kinetochores. Recruits KIF2A
CC and ANKRD53 to the mitotic spindle and spindle poles. May participate
CC in p53/TP53-regulated growth suppression (By similarity).
CC {ECO:0000250|UniProtKB:Q6PGN9}.
CC -!- SUBUNIT: Interacts with APC2 (PubMed:17310996). Interacts with KIF2A
CC (By similarity). Interacts with ANKRD53; recruits ANKRD53 to the
CC spindle during mitosis (By similarity). {ECO:0000250|UniProtKB:Q6PGN9,
CC ECO:0000269|PubMed:17310996}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12427559}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:12427559}.
CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Note=Detected at
CC the mitotic spindle and spindle poles. Diffusely distributed throughout
CC the cell during interphase (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, brain and lung. Weaker
CC expression in kidney and testis. {ECO:0000269|PubMed:10618717}.
CC -!- INDUCTION: Induced by adriamycin and mitomycin C, in a p53-dependent
CC manner, in NIH3T3 cells. This induction is inhibited by actinomycin D.
CC Also induced by cisplatin in a p73-dependent manner in embryonic cells.
CC {ECO:0000269|PubMed:10618717, ECO:0000269|PubMed:12082536}.
CC -!- PTM: Phosphorylated during mitosis. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PSRC1 family. {ECO:0000305}.
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DR EMBL; AF156598; AAF24174.1; -; mRNA.
DR EMBL; AF322890; AAN73433.1; -; Genomic_DNA.
DR EMBL; AK017302; BAB30682.1; -; mRNA.
DR EMBL; AK011197; BAB27461.1; -; mRNA.
DR EMBL; AK041835; BAC31079.1; -; mRNA.
DR EMBL; AK167415; BAE39503.1; -; mRNA.
DR EMBL; BC019165; AAH19165.1; -; mRNA.
DR EMBL; AF284692; AAM45430.1; -; Genomic_DNA.
DR CCDS; CCDS17758.1; -.
DR RefSeq; NP_001177090.1; NM_001190161.1.
DR RefSeq; NP_064360.1; NM_019976.3.
DR AlphaFoldDB; Q9D0P7; -.
DR SMR; Q9D0P7; -.
DR BioGRID; 208155; 3.
DR IntAct; Q9D0P7; 1.
DR STRING; 10090.ENSMUSP00000099689; -.
DR iPTMnet; Q9D0P7; -.
DR PhosphoSitePlus; Q9D0P7; -.
DR EPD; Q9D0P7; -.
DR MaxQB; Q9D0P7; -.
DR PaxDb; Q9D0P7; -.
DR PeptideAtlas; Q9D0P7; -.
DR PRIDE; Q9D0P7; -.
DR ProteomicsDB; 302002; -.
DR Antibodypedia; 33753; 234 antibodies from 22 providers.
DR DNASU; 56742; -.
DR Ensembl; ENSMUST00000090561; ENSMUSP00000088049; ENSMUSG00000068744.
DR Ensembl; ENSMUST00000102629; ENSMUSP00000099689; ENSMUSG00000068744.
DR GeneID; 56742; -.
DR KEGG; mmu:56742; -.
DR UCSC; uc008qyv.2; mouse.
DR CTD; 84722; -.
DR MGI; MGI:1913099; Psrc1.
DR VEuPathDB; HostDB:ENSMUSG00000068744; -.
DR eggNOG; ENOG502S467; Eukaryota.
DR GeneTree; ENSGT00940000154189; -.
DR HOGENOM; CLU_067830_0_0_1; -.
DR InParanoid; Q9D0P7; -.
DR OMA; PCDSREE; -.
DR OrthoDB; 1567239at2759; -.
DR PhylomeDB; Q9D0P7; -.
DR TreeFam; TF338374; -.
DR BioGRID-ORCS; 56742; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Psrc1; mouse.
DR PRO; PR:Q9D0P7; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9D0P7; protein.
DR Bgee; ENSMUSG00000068744; Expressed in animal zygote and 162 other tissues.
DR ExpressionAtlas; Q9D0P7; baseline and differential.
DR Genevisible; Q9D0P7; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:BHF-UCL.
DR GO; GO:0030496; C:midbody; IDA:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005819; C:spindle; IDA:BHF-UCL.
DR GO; GO:0005876; C:spindle microtubule; ISO:MGI.
DR GO; GO:0000922; C:spindle pole; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; IDA:BHF-UCL.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0001578; P:microtubule bundle formation; IDA:BHF-UCL.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISS:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; IMP:BHF-UCL.
DR GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; IMP:BHF-UCL.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IDA:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:BHF-UCL.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; ISS:UniProtKB.
DR InterPro; IPR026658; DDA3.
DR InterPro; IPR026657; DDA3/GTSE-1.
DR InterPro; IPR032768; GTSE1_N.
DR PANTHER; PTHR21584; PTHR21584; 1.
DR PANTHER; PTHR21584:SF1; PTHR21584:SF1; 1.
DR Pfam; PF15259; GTSE1_N; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton; Mitosis;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..329
FT /note="Proline/serine-rich coiled-coil protein 1"
FT /id="PRO_0000273729"
FT REPEAT 38..41
FT /note="1"
FT REPEAT 68..71
FT /note="2"
FT REPEAT 103..106
FT /note="3"
FT REPEAT 194..197
FT /note="4"
FT REPEAT 212..215
FT /note="5"
FT REGION 38..215
FT /note="5 X 4 AA repeats of P-X-X-P"
FT REGION 93..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 70..94
FT /evidence="ECO:0000255"
FT COMPBIAS 130..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGN9"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGN9"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGN9"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGN9"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGN9"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGN9"
FT CONFLICT 188
FT /note="R -> G (in Ref. 4; BAB27461)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="R -> S (in Ref. 4; BAB27461)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 329 AA; 34707 MW; A269CBC53ACC3D31 CRC64;
MEDLKEDIKF IVDETLDFGG LSPSDSHEEE DITVLVSPEK PLRRGLAHRS NPNEVAPALQ
GVRFSLGPLS PEKLEEILDE ANRLAAQLEE CALKDRERAG TGPGRPSPRG KPSPRRETFV
LKDSPVRDLL PTVSSWSTPP PSSLAGLRSS DKKGSARAVR VASGKKPSSI KKESPTCNLF
PASKSPGRSP LAQPILPPRR KTGFGARTTA SPPIPVRPVP QSSASNSQCS SRLQGAAVKS
SSRLPVPSAI PKPATRVPLI GRSLPPGKGA LAPDSLSTQK GHPSAIGHRA SVSQKTNLPT
TSAARGRTTS AARGRAQPLR KAAVPGPTR
