PHAR3_MOUSE
ID PHAR3_MOUSE Reviewed; 558 AA.
AC Q8BYK5; Q8BYS8; Q8C058; Q9DB87;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Phosphatase and actin regulator 3;
DE AltName: Full=Scaffold-associated PP1-inhibiting protein;
DE Short=Scapinin;
GN Name=Phactr3; Synonyms=Scapin1;
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] (ISOFORM 1), AND INTERACTION WITH PPP1CA AND
RP ACTIN.
RC STRAIN=C57BL/6J;
RX PubMed=15107502; DOI=10.1073/pnas.0401673101;
RA Allen P.B., Greenfield A.T., Svenningsson P., Haspeslagh D.C.,
RA Greengard P.;
RT "Phactrs 1-4: a family of protein phosphatase 1 and actin regulatory
RT proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7187-7192(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Hypothalamus, and Olfactory bulb;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229 AND THR-235, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 -!- SUBUNIT: Binds PPP1CA and actin; thus inhibiting the protein
CC phosphatase 1 (PP1) activity. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250}. Note=Localized to
CC the nuclear matrix-intermediate filament scaffold. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8BYK5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BYK5-2; Sequence=VSP_009093;
CC Name=3;
CC IsoId=Q8BYK5-3; Sequence=VSP_009094;
CC Name=4;
CC IsoId=Q8BYK5-4; Sequence=VSP_009095;
CC -!- SIMILARITY: Belongs to the phosphatase and actin regulator family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY501387; AAS86433.1; -; mRNA.
DR EMBL; AK005136; BAB23834.1; -; mRNA.
DR EMBL; AK032242; BAC27776.1; -; mRNA.
DR EMBL; AK038449; BAC30003.1; -; mRNA.
DR EMBL; AK039213; BAC30278.1; -; mRNA.
DR EMBL; BC058621; AAH58621.1; -; mRNA.
DR EMBL; BC059869; AAH59869.1; -; mRNA.
DR CCDS; CCDS17158.1; -. [Q8BYK5-1]
DR CCDS; CCDS17159.1; -. [Q8BYK5-4]
DR CCDS; CCDS50837.1; -. [Q8BYK5-3]
DR CCDS; CCDS50839.1; -. [Q8BYK5-2]
DR RefSeq; NP_001007155.1; NM_001007154.3. [Q8BYK5-4]
DR RefSeq; NP_001171260.1; NM_001177789.1. [Q8BYK5-3]
DR RefSeq; NP_001171261.1; NM_001177790.1.
DR RefSeq; NP_001171262.1; NM_001177791.1. [Q8BYK5-2]
DR RefSeq; NP_083082.1; NM_028806.2. [Q8BYK5-1]
DR RefSeq; XP_006500793.1; XM_006500730.2. [Q8BYK5-4]
DR AlphaFoldDB; Q8BYK5; -.
DR SMR; Q8BYK5; -.
DR BioGRID; 216561; 2.
DR STRING; 10090.ENSMUSP00000104543; -.
DR iPTMnet; Q8BYK5; -.
DR PhosphoSitePlus; Q8BYK5; -.
DR MaxQB; Q8BYK5; -.
DR PaxDb; Q8BYK5; -.
DR PRIDE; Q8BYK5; -.
DR ProteomicsDB; 287692; -. [Q8BYK5-1]
DR ProteomicsDB; 287693; -. [Q8BYK5-2]
DR ProteomicsDB; 287694; -. [Q8BYK5-3]
DR ProteomicsDB; 287695; -. [Q8BYK5-4]
DR Antibodypedia; 29289; 112 antibodies from 22 providers.
DR DNASU; 74189; -.
DR Ensembl; ENSMUST00000103065; ENSMUSP00000099354; ENSMUSG00000027525. [Q8BYK5-4]
DR Ensembl; ENSMUST00000103066; ENSMUSP00000099355; ENSMUSG00000027525. [Q8BYK5-1]
DR Ensembl; ENSMUST00000108915; ENSMUSP00000104543; ENSMUSG00000027525. [Q8BYK5-2]
DR Ensembl; ENSMUST00000108916; ENSMUSP00000104544; ENSMUSG00000027525. [Q8BYK5-3]
DR GeneID; 74189; -.
DR KEGG; mmu:74189; -.
DR UCSC; uc008ohj.2; mouse. [Q8BYK5-3]
DR UCSC; uc008ohk.2; mouse. [Q8BYK5-1]
DR UCSC; uc008ohl.2; mouse. [Q8BYK5-2]
DR CTD; 116154; -.
DR MGI; MGI:1921439; Phactr3.
DR VEuPathDB; HostDB:ENSMUSG00000027525; -.
DR eggNOG; KOG4339; Eukaryota.
DR GeneTree; ENSGT00940000157562; -.
DR HOGENOM; CLU_015753_3_1_1; -.
DR InParanoid; Q8BYK5; -.
DR OMA; SRPADEM; -.
DR OrthoDB; 1205245at2759; -.
DR TreeFam; TF316316; -.
DR BioGRID-ORCS; 74189; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q8BYK5; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8BYK5; protein.
DR Bgee; ENSMUSG00000027525; Expressed in piriform cortex and 117 other tissues.
DR ExpressionAtlas; Q8BYK5; baseline and differential.
DR Genevisible; Q8BYK5; MM.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0008157; F:protein phosphatase 1 binding; IEA:InterPro.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR InterPro; IPR029990; Phactr3.
DR InterPro; IPR004018; RPEL_repeat.
DR PANTHER; PTHR12751:SF7; PTHR12751:SF7; 1.
DR Pfam; PF02755; RPEL; 1.
DR SMART; SM00707; RPEL; 4.
DR PROSITE; PS51073; RPEL; 4.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Coiled coil; Nucleus; Phosphoprotein;
KW Protein phosphatase inhibitor; Reference proteome; Repeat.
FT CHAIN 1..558
FT /note="Phosphatase and actin regulator 3"
FT /id="PRO_0000126639"
FT REPEAT 92..117
FT /note="RPEL 1"
FT REPEAT 400..425
FT /note="RPEL 2"
FT REPEAT 438..463
FT /note="RPEL 3"
FT REPEAT 476..501
FT /note="RPEL 4"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 449..485
FT /evidence="ECO:0000255"
FT COMPBIAS 10..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 69
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96KR7"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 235
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..40
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009095"
FT VAR_SEQ 1..38
FT /note="MAASEDGSSCLVSRGRSQSDPSFLSDSSATSTDAGENP -> MQTANQMLSL
FT NFRRMKSGTAAVRTRARHRPPGSGPSRCG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009093"
FT VAR_SEQ 1..38
FT /note="MAASEDGSSCLVSRGRSQSDPSFLSDSSATSTDAGENP -> MRGQGRGHAR
FT WPAPLRSLLRAFGPQDTTTGGLEQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009094"
SQ SEQUENCE 558 AA; 62652 MW; 8D7D1D5F5BEE37A9 CRC64;
MAASEDGSSC LVSRGRSQSD PSFLSDSSAT STDAGENPDE MDQTPPARSE PLVSGIRTPP
VRRNSKLATL GRIFKPWKWR KKKNEKLKQT TSALEKKMAG RQGREELIKQ GLLEMMEQDS
ENKACSPKEG SQPVQSEPPA GEQETLTSEG AQPGSPSASG TDQVSQDELL SSDAHLDDTA
NIPSASTAEE ADAGSLLPTT DEPSQALAGS DSLDSPPRSL ERSVSQLPSP PLLPTPPPKA
SSKATKNVTG QAALFQGPSM KNNEPALRGQ LATPTGSPHV TTVHRPLPPS RVMEELHRAL
ATKHRQDSFQ GRECRGSPKK RMDVRLSRTS SMERGKERDE AWSFDGASEN KWTATKDSEE
NKENLMLSSE LKDDMLLYQD EEALNDSIIS GTLPRKCKKE LLAVKLRNRP SKQELEDRNI
FPRRTDEERQ EIRQQIEMKL SKRLSQRPAV EELERRNILK QRNDQTEQEE RREIKQRLTR
KLNQRPTVDE LRDRKILIRF SDYVEVARAQ DYDRRADKPW TRLSAADKAA IRKELNEYKS
NEMEVHASSK HLTRFHRP
