PHR4A_XENLA
ID PHR4A_XENLA Reviewed; 694 AA.
AC Q5HZA1;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Phosphatase and actin regulator 4-A;
GN Name=phactr4-a;
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=Egg;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2005) 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; BC089117; AAH89117.1; -; mRNA.
DR RefSeq; NP_001089977.1; NM_001096508.1.
DR AlphaFoldDB; Q5HZA1; -.
DR SMR; Q5HZA1; -.
DR PRIDE; Q5HZA1; -.
DR DNASU; 735048; -.
DR GeneID; 735048; -.
DR KEGG; xla:735048; -.
DR CTD; 735048; -.
DR Xenbase; XB-GENE-5930087; phactr4.S.
DR OMA; DDERGQH; -.
DR OrthoDB; 1205245at2759; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 735048; Expressed in egg cell and 19 other tissues.
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..694
FT /note="Phosphatase and actin regulator 4-A"
FT /id="PRO_0000287310"
FT REPEAT 55..80
FT /note="RPEL 1"
FT REPEAT 576..601
FT /note="RPEL 2"
FT REPEAT 613..638
FT /note="RPEL 3"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..293
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..328
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..382
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..467
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..529
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 694 AA; 76367 MW; F16CB9279EFFA65D CRC64;
MEDRSEEGGD HSEMPSAPST PPSKRKSKFA GFGKFFKPWK WRKRKSSDSF RETSEVLERK
ISTRKPREEL IKRGLLVEVP EEDGSIPSES PPLRNGHMSV EPANPPEDSG GLKRKTRPDS
TGPRPKSGET TVQPCATAEV APLEPHATAE VSPVQPQASA EVTPVQPLPV SEVAPMQPLP
VNEVAPMQPL PVNEVAPKQP HHVSEVASVV SRPTSEVAPV QKVSRDFSKQ PLLPPKRPLS
ISTSVTQESA VAGQKSDSSN RLQSSAPVPT PRTIHPPASS KQPPVPPPKP QNRNSNPLMA
ELSLALAGSP LSPAGSRPSP PLPPKRAMPP STDAVTNKEN ALGPASLPPT PANEIITPSP
PSPPASSHIP VSNPPVPPLT LAPPYTEVEK EQSASPIPLH IRIQQALNSP QPLPLLDSSQ
RAQSLLFMQN DMGPSEEGTR VRSLPVTIEL LKVPDDEDDE SLEDESLSPE SSESHTSKVY
IGDVPSVTVI PSYLPTCVQE EEEGGVSDTD SEGPVLYRDD EEEEEEEETS ALANKVKRKD
TLAMKLSGRM ASEDSNSEFP QRSREEWNQI RQDIGTQLNR RLSQRPTAEE LEQRNILQKN
EADRLAEKKE IKRRLTRKLS QRPTVAELVE RKILRFNEYV EATDAHDYDR RADKPWTRLT
PADKAAIRKE LNEFKSTEMA VHAESKHFTR FHRP
