PHAR1_RAT
ID PHAR1_RAT Reviewed; 580 AA.
AC P62024; Q4KMC2;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Phosphatase and actin regulator 1;
GN Name=Phactr1;
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], INTERACTION WITH PPP1CA AND ACTIN, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF ARG-576; PHE-577; HIS-578;
RP ARG-579 AND PRO-580.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
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].
RC 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).
CC -!- FUNCTION: Binds actin monomers (G actin) and plays a role in multiple
CC processes including the regulation of actin cytoskeleton dynamics,
CC actin stress fibers formation, cell motility and survival, formation of
CC tubules by endothelial cells, and regulation of PPP1CA activity (By
CC similarity). Involved in the regulation of cortical neuron migration
CC and dendrite arborization (By similarity).
CC {ECO:0000250|UniProtKB:Q2M3X8}.
CC -!- SUBUNIT: Interacts (via RPEL repeats) with ACTA1 and PPP1CA; ACTA1 and
CC PPP1CA compete for the same binding site.
CC {ECO:0000269|PubMed:15107502}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15107502}. Synapse
CC {ECO:0000269|PubMed:15107502}. Nucleus {ECO:0000250}. Note=Cytoplasmic
CC in resting cells, and is imported into the nucleus upon serum
CC stimulation. Interaction with actin prevents nuclear import (By
CC similarity). Enriched at synapses. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Selectively expressed in brain. High levels are
CC found in the olfactory tubercle, nucleus accumbens core and shell,
CC caudate-putamen, cerebral cortex, hippocampus and piriform cortex.
CC Moderate to high levels in the olfactory bulb, arcuate and ventromedial
CC hypothalamus, subthalamic nucleus, amygdala, lateral septum, habenula
CC and thalamus. Low expression, if any, in substantia nigra pars
CC compacta/pars reticula and globus pallidus (at protein level).
CC {ECO:0000269|PubMed:15107502}.
CC -!- DOMAIN: Binds three actin monomers via the three C-terminal RPEL
CC repeats. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phosphatase and actin regulator family.
CC {ECO:0000305}.
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DR EMBL; AY494977; AAS77487.1; -; mRNA.
DR EMBL; BC098634; AAH98634.1; -; mRNA.
DR RefSeq; NP_999622.2; NM_214457.2.
DR AlphaFoldDB; P62024; -.
DR SMR; P62024; -.
DR BioGRID; 258561; 1.
DR ELM; P62024; -.
DR STRING; 10116.ENSRNOP00000043053; -.
DR iPTMnet; P62024; -.
DR PhosphoSitePlus; P62024; -.
DR PaxDb; P62024; -.
DR PRIDE; P62024; -.
DR GeneID; 306844; -.
DR KEGG; rno:306844; -.
DR UCSC; RGD:1303187; rat.
DR CTD; 221692; -.
DR RGD; 1303187; Phactr1.
DR eggNOG; KOG4339; Eukaryota.
DR InParanoid; P62024; -.
DR OrthoDB; 1205245at2759; -.
DR PhylomeDB; P62024; -.
DR PRO; PR:P62024; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0008157; F:protein phosphatase 1 binding; IDA:RGD.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0031032; P:actomyosin structure organization; ISS:UniProtKB.
DR GO; GO:0048870; P:cell motility; ISO:RGD.
DR GO; GO:0021987; P:cerebral cortex development; ISS:UniProtKB.
DR GO; GO:0140059; P:dendrite arborization; ISS:UniProtKB.
DR GO; GO:2001222; P:regulation of neuron migration; ISS:UniProtKB.
DR GO; GO:0042325; P:regulation of phosphorylation; IDA:RGD.
DR GO; GO:0043149; P:stress fiber assembly; ISS:UniProtKB.
DR InterPro; IPR029987; Phactr1.
DR InterPro; IPR004018; RPEL_repeat.
DR PANTHER; PTHR12751:SF6; PTHR12751:SF6; 2.
DR Pfam; PF02755; RPEL; 4.
DR SMART; SM00707; RPEL; 4.
DR PROSITE; PS51073; RPEL; 4.
PE 1: Evidence at protein level;
KW Actin-binding; Cytoplasm; Nucleus; Phosphoprotein;
KW Protein phosphatase inhibitor; Reference proteome; Repeat; Synapse.
FT CHAIN 1..580
FT /note="Phosphatase and actin regulator 1"
FT /id="PRO_0000126635"
FT REPEAT 138..163
FT /note="RPEL 1"
FT REPEAT 422..447
FT /note="RPEL 2"
FT REPEAT 460..485
FT /note="RPEL 3"
FT REPEAT 498..523
FT /note="RPEL 4"
FT REGION 330..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 108..129
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 330..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2M3X8"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2M3X8"
FT MOD_RES 104
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q2M3X8"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0D0"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0D0"
FT MUTAGEN 576
FT /note="R->A: No effect on PPP1CA-binding."
FT /evidence="ECO:0000269|PubMed:15107502"
FT MUTAGEN 577
FT /note="F->A: Strongly reduces PPP1CA-binding."
FT /evidence="ECO:0000269|PubMed:15107502"
FT MUTAGEN 578
FT /note="H->A: Reduces PPP1CA-binding."
FT /evidence="ECO:0000269|PubMed:15107502"
FT MUTAGEN 579
FT /note="R->A: No effect on PPP1CA-binding."
FT /evidence="ECO:0000269|PubMed:15107502"
FT MUTAGEN 580
FT /note="P->A: No effect on PPP1CA-binding."
FT /evidence="ECO:0000269|PubMed:15107502"
FT CONFLICT 262
FT /note="A -> T (in Ref. 2; AAH98634)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 580 AA; 66216 MW; 443E6E7DDA22F381 CRC64;
MDYPKMDYFL DVESAHRLLD VESAQRFFYS QGAQARRATL LLPPTLMAAS SEDDIDRRPI
RRVRSKSDTP YLAEARISFN LGAAEEVERL AAMRSDSLVP GTHTPPIRRR SKFANLGRIF
KPWKWRKKKS EKFKHTSAAL ERKISMRQSR EELIKRGVLK EIYDKDGELS ISNEDDSLTN
GQSLSSSQLS LPALSEMEPV PMPRDPCSYE VLQASDIMDG PDPGAPVKLP CLPVKLSPPL
PPKKVLICMP VGGPELSLAS YAAQKSSQQA VAQHHHTVLP SQMQHQLQYG SHGQHLPSST
GTLPMHPSGC RMIDELNKTL AMTMQRLESS EQRVPCSTSY HSSGLHSSDG VTKAGPLGLP
EIRQVPTVVI ECDDNKENVP HEPDYEDSSC LYAREEEEEE EDEDDDASLY TSSLAMKVCR
KDSLAIKLSN RPSKRELEEK NILPRQTDEE RLELRQQIGT KLTRRLSQRP TAEELEQRNI
LKPRNEQEEQ EEKREIKRRL TRKLSQRPTV EELRERKILI RFSDYVEVAD AQDYDRRADK
PWTRLTAADK AAIRKELNEF KSTEMEVHEL SRHLTRFHRP
