ID   PHAR4_XENTR             Reviewed;         706 AA.
AC   F7EC58; B1H185;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Phosphatase and actin regulator 4;
GN   Name=phactr4;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20431018; DOI=10.1126/science.1183670;
RA   Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA   Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA   Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA   Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA   Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA   Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA   Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA   Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA   Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT   "The genome of the Western clawed frog Xenopus tropicalis.";
RL   Science 328:633-636(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=N6; TISSUE=Intestine;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Regulator of protein phosphatase 1 (PP1) required for neural
CC       tube and optic fissure closure, and enteric neural crest cell (ENCCs)
CC       migration during development. Acts as an activator of PP1. During
CC       neural tube closure, localizes to the ventral neural tube and activates
CC       PP1, leading to down-regulate cell proliferation within cranial neural
CC       tissue and the neural retina. Also acts as a regulator of migration of
CC       enteric neural crest cells (ENCCs) by activating PP1, leading to
CC       repression of the integrin signaling through the rho/rock pathway (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Binds ppp1ca and actin. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection,
CC       lamellipodium {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phosphatase and actin regulator family.
CC       {ECO:0000305}.
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DR   EMBL; AAMC01036115; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAMC01036116; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC160513; AAI60513.1; -; mRNA.
DR   RefSeq; NP_001120266.1; NM_001126794.1.
DR   RefSeq; XP_012811931.1; XM_012956477.1.
DR   AlphaFoldDB; F7EC58; -.
DR   SMR; F7EC58; -.
DR   PaxDb; F7EC58; -.
DR   GeneID; 100145319; -.
DR   KEGG; xtr:100145319; -.
DR   CTD; 65979; -.
DR   Xenbase; XB-GENE-5930004; phactr4.
DR   eggNOG; KOG4339; Eukaryota.
DR   HOGENOM; CLU_015753_1_0_1; -.
DR   InParanoid; F7EC58; -.
DR   OMA; XKNEADR; -.
DR   OrthoDB; 1205245at2759; -.
DR   TreeFam; TF316316; -.
DR   Proteomes; UP000008143; Chromosome 2.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR   GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR   GO; GO:0008157; F:protein phosphatase 1 binding; ISS:UniProtKB.
DR   GO; GO:0072542; F:protein phosphatase activator activity; ISS:UniProtKB.
DR   GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0061386; P:closure of optic fissure; ISS:UniProtKB.
DR   GO; GO:0048484; P:enteric nervous system development; ISS:UniProtKB.
DR   GO; GO:2001045; P:negative regulation of integrin-mediated signaling pathway; ISS:UniProtKB.
DR   GO; GO:0001755; P:neural crest cell migration; ISS:UniProtKB.
DR   GO; GO:0001843; P:neural tube closure; ISS:UniProtKB.
DR   GO; GO:0043085; P:positive regulation of catalytic activity; ISS:UniProtKB.
DR   GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR   GO; GO:0007266; P:Rho protein signal transduction; ISS:UniProtKB.
DR   InterPro; IPR029984; Phactr4.
DR   InterPro; IPR004018; RPEL_repeat.
DR   PANTHER; PTHR12751:SF4; PTHR12751:SF4; 1.
DR   Pfam; PF02755; RPEL; 3.
DR   SMART; SM00707; RPEL; 3.
DR   PROSITE; PS51073; RPEL; 3.
PE   2: Evidence at transcript level;
KW   Actin-binding; Cell projection; Cytoplasm; Developmental protein;
KW   Neurogenesis; Reference proteome; Repeat.
FT   CHAIN           1..706
FT                   /note="Phosphatase and actin regulator 4"
FT                   /id="PRO_0000416891"
FT   REPEAT          42..67
FT                   /note="RPEL 1"
FT   REPEAT          588..613
FT                   /note="RPEL 2"
FT   REPEAT          625..650
FT                   /note="RPEL 3"
FT   REGION          65..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          196..380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          385..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          459..579
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..109
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..279
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..302
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..380
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        461..475
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        507..541
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        542..556
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        122
FT                   /note="C -> R (in Ref. 2; AAI60513)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   706 AA;  78224 MW;  18366B944E903BB7 CRC64;
     MPSAPSTPPS KRKSKFAGFG KFFKPWKWRK RKSSDSFRET SEVLERKISM RKPREELVKR
     GLLVEVPEED VSIPSESPPL RNGHMSVEHA NPPEDIGGLK RKTRQDSTGS RPKSGETTVQ
     PCATAEVAPV EPCTATEVAS VQPHATAEVA PIQPLATAEV SPVQHCATAE VAPVQPRPVS
     EVASVQPCPV SEVVPVHPRH LSEKNSEKYR PMSEVAPGAS RPTSEVAPLQ KVSRDFSKQP
     LLPPKRPLSS SSSVTQESVL GGQKPDPSTR QQSSVPVPTP RTIHPLPFSK QPPVPPPKPQ
     NRSSNPLMAE LSLALGGSTL SPAGSRPSPP IPPKRVVVPS TDAVNNKEKA LRPASLPPIP
     ANEISIPSPP SPPISSHIPV SNPPVPMLTL APPNTEVEKE QSASPLPLHI RIQQALNSPQ
     PLPLLDSSQR AQSLLFMQNE VPSEEGTRVR SLPVTIELLK VPDDDDDDNS LEDESLSPES
     SESHPSRVYI GDVPSVTVIP NYLPTCVQEE EEEEEEGVSD TDSEGPVLYR EDDEEEEEEE
     TSSLANKVKR KDTLAMKLSG RMGPHDSNPE FPQRSREEWN QIRQQIGSQL NRRLSQRPSA
     EELEQRNILQ KNEADRLAEK KEIKRRLTRK LSQRPTVAEL VERKILRFNE YVEVTDAHDY
     DRRADKPWTR LTPADKAAIR KELNEFKSTE MAVHEESKHF TRFHRP