ID   PHAR1_CHICK             Reviewed;         501 AA.
AC   Q801X6;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Phosphatase and actin regulator 1;
GN   Name=PHACTR1; Synonyms=DDSG1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=12915307; DOI=10.1016/s1567-133x(03)00080-2;
RA   Shin M., Fukuda K., Yasugi S.;
RT   "Expression of DDSG1, a novel gene encoding a putative DNA-binding protein
RT   in the embryonic chicken nervous system.";
RL   Gene Expr. Patterns 3:431-436(2003).
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   -!- TISSUE SPECIFICITY: Expressed in the gizzard, and in neurons from
CC       central and peripheral nervous systems. {ECO:0000269|PubMed:12915307}.
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; AB100407; BAC67215.1; -; mRNA.
DR   RefSeq; NP_989777.1; NM_204446.1.
DR   AlphaFoldDB; Q801X6; -.
DR   SMR; Q801X6; -.
DR   STRING; 9031.ENSGALP00000036468; -.
DR   PaxDb; Q801X6; -.
DR   GeneID; 395093; -.
DR   KEGG; gga:395093; -.
DR   CTD; 221692; -.
DR   VEuPathDB; HostDB:geneid_395093; -.
DR   eggNOG; KOG4339; Eukaryota.
DR   InParanoid; Q801X6; -.
DR   OrthoDB; 1205245at2759; -.
DR   PhylomeDB; Q801X6; -.
DR   PRO; PR:Q801X6; -.
DR   Proteomes; UP000000539; 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; 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: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; IBA:GO_Central.
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; 3.
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..501
FT                   /note="Phosphatase and actin regulator 1"
FT                   /id="PRO_0000235991"
FT   REPEAT          1..18
FT                   /note="RPEL 1"
FT   REPEAT          343..368
FT                   /note="RPEL 2"
FT   REPEAT          381..406
FT                   /note="RPEL 3"
FT   REPEAT          419..444
FT                   /note="RPEL 4"
FT   REGION          21..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          295..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          382..415
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..313
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        314..329
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..415
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   501 AA;  56095 MW;  B5607F04F5E29ECA CRC64;
     MRQSREELIK RGVLKEIFDK DGELSIPNEE GALENGQPLG SGQVLSSSQV SLPALAELES
     GSAPGEPCSY EVLPTTEITD GTVSEESPTS NESGVLLSQD PTAKPVLLLP PKKSAAFPGD
     HEDTPVKQLS LLKQPPALPP KPIARIASHL TDPGAPVKLP CMPVKLSPPL PPKKVMICMP
     LGGPDLSSLS SYSTQKSSQQ PLTQHHHTVL PSQLAAHQHQ LQYGSHSQHL PSGSSTLPIH
     PSGCRMIEEL NKTLAMTMQR LESSGLHTGD NVTKTGPGGL PDMRQVPTVV IECDDNKENV
     PHEADYEDSS CLYPRQEEEE EEDEDEDNSL FTSSLAMKVC RKDSLAIKLS NRPSKRELEE
     KNILPMQTDE ERLELRQQIG TKLTRRLSQR PTAEELEQRN ILKPRNEQEE QEEKREIKRR
     LTRKLSQRPT VEELRERKIL IRFSDYVEVA DAQDYDRRAD KPWTRLTAAD KAAIRKELNE
     FKSSEMEVHE LSRHLTRFHR P