PHAR3_RAT
ID PHAR3_RAT Reviewed; 517 AA.
AC Q6RFY2;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Phosphatase and actin regulator 3;
DE AltName: Full=Scaffold-associated PP1-inhibiting protein;
DE Short=Scapinin;
GN Name=Phactr3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- SUBUNIT: Binds actin and PPP1CA; 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 -!- TISSUE SPECIFICITY: Diffusely expressed throughout the brain cortex,
CC with highest levels in the cortex and the hippocampus and lower levels
CC in the striatum and thalamus. {ECO:0000269|PubMed:15107502}.
CC -!- SIMILARITY: Belongs to the phosphatase and actin regulator family.
CC {ECO:0000305}.
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DR EMBL; AY500157; AAS86431.1; -; mRNA.
DR RefSeq; NP_999624.1; NM_214459.2.
DR AlphaFoldDB; Q6RFY2; -.
DR SMR; Q6RFY2; -.
DR STRING; 10116.ENSRNOP00000009906; -.
DR iPTMnet; Q6RFY2; -.
DR PhosphoSitePlus; Q6RFY2; -.
DR PRIDE; Q6RFY2; -.
DR GeneID; 362284; -.
DR KEGG; rno:362284; -.
DR CTD; 116154; -.
DR RGD; 1303029; Phactr3.
DR eggNOG; KOG4339; Eukaryota.
DR InParanoid; Q6RFY2; -.
DR OrthoDB; 1205245at2759; -.
DR PhylomeDB; Q6RFY2; -.
DR PRO; PR:Q6RFY2; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; TAS:RGD.
DR GO; GO:0003779; F:actin binding; IDA:RGD.
DR GO; GO:0008157; F:protein phosphatase 1 binding; IEA:InterPro.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; TAS:RGD.
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; Coiled coil; Nucleus; Phosphoprotein;
KW Protein phosphatase inhibitor; Reference proteome; Repeat.
FT CHAIN 1..517
FT /note="Phosphatase and actin regulator 3"
FT /id="PRO_0000126640"
FT REPEAT 52..77
FT /note="RPEL 1"
FT REPEAT 359..384
FT /note="RPEL 2"
FT REPEAT 397..422
FT /note="RPEL 3"
FT REPEAT 435..460
FT /note="RPEL 4"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 41..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 408..444
FT /evidence="ECO:0000255"
FT COMPBIAS 46..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 29
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96KR7"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 194
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BYK5"
SQ SEQUENCE 517 AA; 58461 MW; 8016593B93B3B43C CRC64;
MDQTPPARSE PLVSGIRTPP VRRNSKLATL GRIFKPWKWR KKKNEKLKQT TSALEKKMAG
RQGREELIKQ GLLEMMEQDS ESKACSPKEG SQPAQSEPSA GEQETLTSEG VQPGSPSASG
TDQASQDELL SSDAHPDDTA KMSSASSGEE ADAGNLLPTT DEPSQEALSG SLDSPPRTLE
RSASQLPSPP LLPTPPPKAS SKATKNVTGQ AALFQGSSMK NNEPVLRGQL PTPTGSPHLT
TVHRPLPPSR VIEELHRALA TKHRQDSFQG RECRGSPKKR MDVRLSRTSS MERGKERDEA
WSFDGASENK WTAAKDSEEN KENLILSSEL KDDLLLYQDE EALNDSIISG TLPRKCKKEL
LAVKLRNRPS KQELEDRNIF PRRTDEERQE IRQQIEMKLS KRLSQRPAVE ELERRNILKQ
RNDQTEQEER REIKQRLTRK LNQRPTVDEL RDRKILIRFS DYVEVARAQD YDRRADKPWT
RLSAADKAAI RKELNEYKSN EMEVHASSKH LTRFHRP
