PHAR4_BOVIN
ID PHAR4_BOVIN Reviewed; 712 AA.
AC F1MCY2; A6QP20;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Phosphatase and actin regulator 4;
GN Name=PHACTR4;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DAAA02006337; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC149103; AAI49104.1; -; mRNA.
DR RefSeq; NP_001095477.1; NM_001102007.1.
DR AlphaFoldDB; F1MCY2; -.
DR SMR; F1MCY2; -.
DR STRING; 9913.ENSBTAP00000003535; -.
DR PaxDb; F1MCY2; -.
DR PRIDE; F1MCY2; -.
DR Ensembl; ENSBTAT00000003535; ENSBTAP00000003535; ENSBTAG00000002727.
DR GeneID; 514644; -.
DR KEGG; bta:514644; -.
DR CTD; 65979; -.
DR VEuPathDB; HostDB:ENSBTAG00000002727; -.
DR VGNC; VGNC:32806; PHACTR4.
DR eggNOG; KOG4339; Eukaryota.
DR GeneTree; ENSGT00940000157582; -.
DR HOGENOM; CLU_015753_1_1_1; -.
DR InParanoid; F1MCY2; -.
DR OMA; XKNEADR; -.
DR OrthoDB; 1205245at2759; -.
DR TreeFam; TF316316; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000002727; Expressed in metanephros cortex and 105 other tissues.
DR ExpressionAtlas; F1MCY2; baseline and differential.
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..712
FT /note="Phosphatase and actin regulator 4"
FT /id="PRO_0000416888"
FT REPEAT 72..97
FT /note="RPEL 1"
FT REPEAT 593..618
FT /note="RPEL 2"
FT REPEAT 631..656
FT /note="RPEL 3"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..372
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..557
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..626
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q501J7"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ21"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ21"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ21"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q501J7"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ21"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ21"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ21"
FT MOD_RES 441
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ21"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ21"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q501J7"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ21"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q501J7"
FT MOD_RES 526
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q501J7"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ21"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ21"
FT MOD_RES 638
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ21"
FT CONFLICT 39
FT /note="P -> S (in Ref. 2; AAI49104)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="P -> L (in Ref. 2; AAI49104)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 712 AA; 78821 MW; 7B1B4E417F314F43 CRC64;
MGQADISRPV NPDGVEEIGQ PTADLGMVMD CVEAGDITPP TKRKSKFSGF GKIFKPWKWR
KKKSDKFKET SEVLERKISM RKPREELVKR GLLLEDSEQG GEDPGKLSHA TLKNGHTTLI
GSTRSSSPVQ VEEESERIAS LRKPVPEEEP KKRLGSSGSQ PHSEAEFVPE SIPKQPLLPP
KRHLSSSHEA NEGQAKDATS SGSLARPSSS ASTTAITTAP AATMAATNPA KTVHSSGPPS
QAPRTLPAAP ASTHTTATLS LTHTGPAKQP PIPPPKPTHR NSNPVIAELS QAINSGTLLS
KPSPPLPPKR GIPSALVPTS ESAAATTATK APSDQREKSA CSVGSEPLLT PSSSPLPAHI
PPEPPQSPPF PAKTFQVVPE IEFPPSLDLP QEIPQQESQK REVPKRMLDH SFGEPQVPPR
LPPVPLHIRI QQALTSPLPV TPPLEGSHRA HSLLFENSDN FSEDSSTLGR TRSLPITIEM
LKVPDDEEEE EQSHIFAFDE DVASTSVIPK LPQCLQEEEE GKESDSDSEG PIQYRDEEDE
DESHHSALAN KVKRKDTLAM KLNHKPSEPE MNMNSWPRKS KEEWNEIRHQ IGNTLIRRLS
QRPTPEELEQ RNILQPKNEA DRQAEKREIK RRLTRKLSQR PTVAELLARK ILRFNEYVEV
TDAHDYDRRA DKPWTKLTPA DKAAIRKELN EFKSSEMEVH EDSKHFTRYH RP
