PHAR4_PONAB
ID PHAR4_PONAB Reviewed; 702 AA.
AC Q5RAU1;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Phosphatase and actin regulator 4;
GN Name=PHACTR4;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-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 by
CC interacting with PPP1CA and preventing phosphorylation of PPP1CA at
CC 'Thr-320'. During neural tube closure, localizes to the ventral neural
CC tube and activates PP1, leading to down-regulate cell proliferation
CC within cranial neural tissue and the neural retina. Also acts as a
CC regulator of migration of enteric neural crest cells (ENCCs) by
CC activating PP1, leading to dephosphorylation and subsequent activation
CC of cofilin (COF1 or COF2) and repression of the integrin signaling
CC through the RHO/ROCK pathway (By 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH91119.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CR858921; CAH91119.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001125654.1; NM_001132182.1.
DR AlphaFoldDB; Q5RAU1; -.
DR SMR; Q5RAU1; -.
DR GeneID; 100172574; -.
DR KEGG; pon:100172574; -.
DR CTD; 65979; -.
DR eggNOG; KOG4339; Eukaryota.
DR InParanoid; Q5RAU1; -.
DR OrthoDB; 1205245at2759; -.
DR Proteomes; UP000001595; 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; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..702
FT /note="Phosphatase and actin regulator 4"
FT /id="PRO_0000287308"
FT REPEAT 63..88
FT /note="RPEL 1"
FT REPEAT 583..608
FT /note="RPEL 2"
FT REPEAT 621..646
FT /note="RPEL 3"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..268
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..363
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q501J7"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ21"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ21"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ21"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q501J7"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ21"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ21"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ21"
FT MOD_RES 358
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ21"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ21"
FT MOD_RES 432
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ21"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ21"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q501J7"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ21"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q501J7"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q501J7"
FT MOD_RES 557
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ21"
FT MOD_RES 590
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ21"
FT MOD_RES 628
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ21"
SQ SEQUENCE 702 AA; 78110 MW; 1F7AE08468E163BF CRC64;
MEDPFEEADQ PATEPGMVMD SVEAGDTTPP TKRKSKFSGV GKIFKPWKWR KKKSSDKFKE
TSEVLERKIS MRKPREELVK RGVLLEDPEQ GGEDPGKPSH AMLKNGHTTP IGNARSSSPV
QVEEEPVRLA SLRKAIPEED LKKRLGSTGS QPNSEAESVP ENVPKPPLLP PKRPLSSSHE
ASEGQAKDAT SSGGTARFII STSITTAPAA TTAATSLAKT VNLSVTPSPA PRTLPAAPAS
TNTTATPSLT HMVPAKQPPI PPPKPAHRNS NPVIAELSQA INSGTLLSKP SPPLPPKRGI
PSTSVPTLES AAAITTKTPS DEREKSTCSM GSELLPMISP RSPSPPLPTH IPPEPPRTPP
FPAKTFQVVP EIQFPPSLDL HQEIPQQEDQ KKEVPKRILD QNFGEPHIPS RLPPLPLHIR
IQQALTSPLP VTPTLEGSHR AHSLLFENSD SFSEDSSTLG RTRSLPITIE MLKVPDDEEE
EEQICPSTFS EETTPTSVIP KLPQCLREEE EKESDSDSEG PIQYRDEEDE DESYQSALAN
KVKRKDTLAM KLNHRPSEPE LNLNSWPCKS KEEWNEIRHQ IGNTLIRRLS QRPTPEELEQ
RNILQPKNEA DRQAEKREIK RRLTRKLSQR PTVAELLARK ILRFNEYVEV TDAQDYDRRA
DKPWTKLTPA DKAAIRKELN EFKSSEMEVH EESKHFTRYH RP
