PHR4B_XENLA
ID PHR4B_XENLA Reviewed; 697 AA.
AC Q5XHF3;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Phosphatase and actin regulator 4-B;
GN Name=phactr4-b;
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=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) 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; BC084104; AAH84104.1; -; mRNA.
DR RefSeq; NP_001088191.1; NM_001094722.1.
DR AlphaFoldDB; Q5XHF3; -.
DR SMR; Q5XHF3; -.
DR DNASU; 495016; -.
DR GeneID; 495016; -.
DR KEGG; xla:495016; -.
DR CTD; 495016; -.
DR Xenbase; XB-GENE-6254546; phactr4.L.
DR OrthoDB; 1205245at2759; -.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 495016; 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..697
FT /note="Phosphatase and actin regulator 4-B"
FT /id="PRO_0000287311"
FT REPEAT 42..67
FT /note="RPEL 1"
FT REPEAT 579..604
FT /note="RPEL 2"
FT REPEAT 616..641
FT /note="RPEL 3"
FT REGION 63..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..292
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..381
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..468
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..532
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 697 AA; 77490 MW; 20B2EEFAFDF31837 CRC64;
MPSAPSTPPS KRKSKFSGFG KFFKPWKWRK RKSSDSFRET QEVLERKISM RKPREELVKR
GLIVDVPEED VSIPSESPPL RNGHMNVKHA NLPEDSGGLK RKTRPDSTGH RPKSGETTAQ
PRSTAEVAPM ELHATADVSP MQPQASAEVA PAQPRPASEV GQVQPRPISE VAPMQPRPIS
EVAPVHPRHV PEKTSEKYRP KSEVAPVRTS RPTSEVAPVQ KVSRDFSKQP LLPPKRPLSS
STSVTQESAV GGQKFDPSTR PQSSTPVPTP RTIHPPVSSK QPPVPPPKPQ NRNSNPLMAE
LSLALAGNTL SPAGSRPSPP LPPKRAMPPS TDAVTNKEKA LRPASLPPIP ANEIAAPSPP
SPPVSSRIPA PNPPVPPLTL APPISEVEKE RSASPIPLHI RIQQALNSPQ PLPLLDSSQR
AQSLLFMQHE VGPSEEGTRV RSLPVTIELL KVPDDDDDED ELSLEDESLS PDSSESHPSR
VYIGDVPSVT VIPSYLPTCV QEEDEEEGVS DTDSEGPVLY REEDEDEEEE ETSSLANKVK
RKDTLAMKLS GRMAPQDSNT ELPHRSKDEW NQIRQQIGTQ LNRRLSQRPT AEELEQRNIL
QKNEADRLAE KKEIKRRLTR KLSQRPTVAE LLERKILRFN EYVEVTDAHD YDRRADKPWT
RLTPADKAAI RKELNEFKST EMAVHDESKH FTRFHRP
