ID   PHAR1_XENLA             Reviewed;         586 AA.
AC   Q6GLU8;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Phosphatase and actin regulator 1;
GN   Name=phactr1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds actin monomers (G actin) and plays a role in the
CC       reorganization of the actin cytoskeleton and in formation of actin
CC       stress fibers. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts (via RPEL repeats) with ACTA1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Synapse {ECO:0000250}.
CC       Nucleus {ECO:0000250}. Note=Enriched at synapses (By similarity).
CC       Cytoplasmic in resting cells, and is imported into the nucleus upon
CC       serum stimulation. Interaction with actin prevents nuclear import (By
CC       similarity). {ECO:0000250}.
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; BC074353; AAH74353.1; -; mRNA.
DR   RefSeq; NP_001086228.1; NM_001092759.1.
DR   AlphaFoldDB; Q6GLU8; -.
DR   SMR; Q6GLU8; -.
DR   DNASU; 444657; -.
DR   GeneID; 444657; -.
DR   CTD; 444657; -.
DR   Xenbase; XB-GENE-5959325; phactr1.S.
DR   OrthoDB; 1205245at2759; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   Bgee; 444657; Expressed in brain and 19 other tissues.
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; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; ISS:UniProtKB.
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:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR   GO; GO:0031032; P:actomyosin structure organization; ISS:UniProtKB.
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; 1.
DR   Pfam; PF02755; RPEL; 4.
DR   SMART; SM00707; RPEL; 4.
DR   PROSITE; PS51073; RPEL; 4.
PE   2: Evidence at transcript level;
KW   Actin-binding; Cytoplasm; Nucleus; Protein phosphatase inhibitor;
KW   Reference proteome; Repeat; Synapse.
FT   CHAIN           1..586
FT                   /note="Phosphatase and actin regulator 1"
FT                   /id="PRO_0000235992"
FT   REPEAT          92..117
FT                   /note="RPEL 1"
FT   REPEAT          428..453
FT                   /note="RPEL 2"
FT   REPEAT          466..491
FT                   /note="RPEL 3"
FT   REPEAT          504..529
FT                   /note="RPEL 4"
FT   REGION          373..414
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           62..83
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        373..393
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        394..414
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   586 AA;  66369 MW;  B06E4D26E1734617 CRC64;
     MAASSEEETD RRPIRRVRSK SDTPYLAEVR ISLNLETAEE VERLAAMRSD SLVPGTHTPP
     IRRRSKFATL GRLFKPWKWR KKKSEKFKQT SAALERKISM RQSREELIKR GVLKEMYDKD
     GDLHNEEGLM ENGQAVSSGS SSLPIITELE LTSMAGDTCA YEVLPTSELM DGTVSEDLSS
     EPGSLSQDPS YKPAMLLPPK KTVGFPVDQE DTPVKQITLL KQPPALPPKP ISRIANHIAD
     SGAPVKLPCM PGKMSPPLPP KKVMICMPLG GTDFPYGPYS NQKSSQHHHT VLPSQLAAHQ
     LQYGSQHFST GSSSISIHPS IPPGCRVIEE LNKTLAMTMQ RLESSGLHGG ESITKSGLSG
     YCDMRQVPTV VIECEDDKEN VPHETSYDDS SCLYSRDEEE DDDDDDDDED DDSSLYTNSL
     ALKVLRKDSL AIKLSNRPSK RELEEKNILP MQTDEERLES RQQIGTKLTR RLSQRPTAEE
     LEQRNILKPR NEQEEQEEKR EIKRRLTRKL SQRPTVEELR EKKILISFSD YVELADAQDY
     DRRADKPWTR LTAADKAAIR KELNEFKSTE MEVHELSRHL TRFHRP