PHR4B_DANRE
ID PHR4B_DANRE Reviewed; 754 AA.
AC Q6PEI3; F1QNE2;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Phosphatase and actin regulator 4B;
GN Name=phactr4b; ORFNames=zgc:63484;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-642, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18307296; DOI=10.1021/pr700667w;
RA Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA Slijper M., Heck A.J.R.;
RT "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT analysis down to a single embryo.";
RL J. Proteome Res. 7:1555-1564(2008).
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; AL954327; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR855299; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC058052; AAH58052.1; -; mRNA.
DR RefSeq; NP_956964.1; NM_200670.1.
DR AlphaFoldDB; Q6PEI3; -.
DR SMR; Q6PEI3; -.
DR STRING; 7955.ENSDARP00000075509; -.
DR iPTMnet; Q6PEI3; -.
DR PaxDb; Q6PEI3; -.
DR PRIDE; Q6PEI3; -.
DR Ensembl; ENSDART00000044235; ENSDARP00000044234; ENSDARG00000032221.
DR GeneID; 393643; -.
DR KEGG; dre:393643; -.
DR CTD; 393643; -.
DR ZFIN; ZDB-GENE-040426-1131; phactr4b.
DR eggNOG; KOG4339; Eukaryota.
DR GeneTree; ENSGT00940000157582; -.
DR InParanoid; Q6PEI3; -.
DR OrthoDB; 1205245at2759; -.
DR TreeFam; TF316316; -.
DR PRO; PR:Q6PEI3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 16.
DR Bgee; ENSDARG00000032221; Expressed in early embryo and 32 other tissues.
DR ExpressionAtlas; Q6PEI3; 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 1: Evidence at protein level;
KW Actin-binding; Cell projection; Cytoplasm; Developmental protein;
KW Neurogenesis; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..754
FT /note="Phosphatase and actin regulator 4B"
FT /id="PRO_0000287309"
FT REPEAT 61..86
FT /note="RPEL 1"
FT REPEAT 635..660
FT /note="RPEL 2"
FT REPEAT 673..698
FT /note="RPEL 3"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..360
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..444
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..475
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..504
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..554
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..593
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 642
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
FT CONFLICT 2
FT /note="E -> K (in Ref. 2; AAH58052)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="P -> L (in Ref. 2; AAH58052)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="P -> A (in Ref. 2; AAH58052)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="P -> S (in Ref. 2; AAH58052)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="M -> L (in Ref. 2; AAH58052)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="A -> D (in Ref. 2; AAH58052)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="T -> A (in Ref. 2; AAH58052)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="D -> E (in Ref. 2; AAH58052)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 754 AA; 84195 MW; 62F9144901A164AA CRC64;
MENRDDEVEH QHSTMGSEGG TAGDGTPPPK RKGKFSTLGK IFKPWKWRKK KSSEKFKETS
EVLERKMSMR RPRQELIEQG VLKELPDNES GEAHGHKAPY VKNGHTLPVG VGGSLALEQV
HSPSESEFRI NPVWLPQPED RRARAPSDGD HRGALGPRAS NQDDGRRGGW SVGTEDWKNN
LAWHGEDIRR GGRAHAEMDK RPGLMKAPSE DGRRTRPEPD WKPTLPRHSS VEEGRGRRES
DSSQYLPNSE MMRDTLREPL PPKQSIMPPK WLMTSTPEPG SDSLPRTPVH NPAAPSFCSS
NSSSSSSAGK PLRNVSSAGA NTAPPGGAPL TTSSAPCSMG TIPNHPSKQP PMPPPKPINR
SNNPAIMAEL TQGGMNLVPA KPSPPMPPKR TTPVTKRNPE DSPLTIASLP SILSEDMRAN
IPGGYQLPPP PPSPPLPTHI PPSPPRAHTH HLLHQHSYPY PLPQPLPVHF DPPSPPEDPP
ARDEDDYSDE EEEEEDDEDD EEPPPDHLPS PQSQPELEPR SRRCLVGELS VSVIPEGNNS
SEEEEDEEDQ HPEESDSDGP VLYKDDESDE DEEDDSPPSA LASRVKRKDT LALKLSSRPS
APDRQAPERQ AKSEHSGLSW QSKEQWEAIR TQIGTALTRR LSQRPTAEEL EQRNILQPKN
EADRQAEVRE IKRRLTRKLS QRPTVAELQA RKILRFHEYV EVTSAQDYDR RADKPWTKLT
PADKAAIRKE LNEFKSSEME VHEESRIYTR FHRP
