PHR4A_DANRE
ID PHR4A_DANRE Reviewed; 725 AA.
AC F1QIC4;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 2.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Phosphatase and actin regulator 4A;
GN Name=phactr4a;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
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; AL954687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F1QIC4; -.
DR SMR; F1QIC4; -.
DR PaxDb; F1QIC4; -.
DR PRIDE; F1QIC4; -.
DR ZFIN; ZDB-GENE-051030-69; phactr4a.
DR eggNOG; KOG4339; Eukaryota.
DR InParanoid; F1QIC4; -.
DR PRO; PR:F1QIC4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; 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:SF20; PTHR12751:SF20; 5.
DR Pfam; PF02755; RPEL; 3.
DR SMART; SM00707; RPEL; 3.
DR PROSITE; PS51073; RPEL; 3.
PE 3: Inferred from homology;
KW Actin-binding; Cell projection; Cytoplasm; Developmental protein;
KW Neurogenesis; Reference proteome; Repeat.
FT CHAIN 1..725
FT /note="Phosphatase and actin regulator 4A"
FT /id="PRO_0000416890"
FT REPEAT 75..100
FT /note="RPEL 1"
FT REPEAT 606..631
FT /note="RPEL 2"
FT REPEAT 644..669
FT /note="RPEL 3"
FT REGION 1..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..234
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..322
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..417
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 725 AA; 80323 MW; 0FA3A20CA7D2B293 CRC64;
MGQGASTQTL NPNLAYITDD EVDHSMPESD GANPGAGNPS AKSKGKFPSL GKIFKPWKWR
KKKTSDKFKE TSEGLVLERK MSVRKPREEL IERGLLKDIP ENESNDVNHK APPVKNGHTG
PVPGDRKSDS GSEIDQDRRM DDTGERKEKR KRIGKRNDGT ERMTEMIQSF QKMSLMQRSV
GVQFVPEPKP ASTSTKESQP PPKQAILPPK RVIAAPSSAE PAPVPPPPIA KPPPRTVSLN
VDDSSRTILI PSLIAGDREV PPTVPAHTTP ATVSTHKTLP TVPAHMTPPT VPAHVTTPAA
PAHSNPPAVL LKQPPMPPPK PVHHSSNTAL QGLDLSTVDP SQVPVPVKRS PPIPPKRNTP
VTKRNSGDSS ANLPEPPPPA PTSVPIPAAA PISAPPSTQS DPPSPTTEPP SQPPPLPLHI
RIQRALNSPG PVHPNPEGSQ RAHSLLFETP PDLINEALGG GRYSLPVTIE PLRLPEDDDF
DMEEELQKLR AGPRPTQKPE LEPRSRRGLV EDPQVAVIPE DAGSESSEEE EDESDSDQSI
KYRDDNEEDD DEEDVPKSGL ASRVKRKDTL ALKLERQQEK EKSQEEDSST WNNKEQWEAV
RNKIGTALTR RLSQRPTAQE LEQRNILLAK NEEVRRAERS EIKRRLTRKL SQRPTIADLQ
ARKILRFHEY VESTHAQDYD RRADKPWTKL TPADKAAIRK ELNEFKSSEM EVHEESRIFT
RFHRP
