PHAR4_CHICK
ID PHAR4_CHICK Reviewed; 720 AA.
AC F1N8V3;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 2.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Phosphatase and actin regulator 4;
GN Name=PHACTR4;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
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; AADN02043997; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02043998; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02043999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PaxDb; F1N8V3; -.
DR VEuPathDB; HostDB:geneid_425087; -.
DR eggNOG; KOG4339; Eukaryota.
DR InParanoid; F1N8V3; -.
DR Proteomes; UP000000539; 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 3: Inferred from homology;
KW Actin-binding; Cell projection; Cytoplasm; Developmental protein;
KW Neurogenesis; Reference proteome; Repeat.
FT CHAIN 1..720
FT /note="Phosphatase and actin regulator 4"
FT /id="PRO_0000416889"
FT REPEAT 74..99
FT /note="RPEL 1"
FT REPEAT 601..626
FT /note="RPEL 2"
FT REPEAT 639..664
FT /note="RPEL 3"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..323
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..372
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..493
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..552
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..567
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..640
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 720 AA; 79686 MW; 0A7874C7ED89BADF CRC64;
MGQPRFSRPV HPAAAAEEVD HPPSDAGMGV DVLESGDTTP PTKRKSKFSG FGKIFKPWKW
RKKKSSDKFK ETSEVLERKI SMRKPREELV KRGVLLEDPE QALSSDCPGK EGSVLRKSII
LISHFRDAET PGQSEDDGGR LLYLQFQNLL LREGKEAAWP WHQAECIPVE QQVPPLGIKL
TRGLFPSAGK SQGRAAEHPG LGLTSCVLLS TSILSAPANV SAGAFLVSFL SLVCNCSEAL
RAPGGEAVTL LTDTXEVTNQ AQPPCQTAPC PPHPIPTNRN SSSVIAELSQ AINSGTGLSK
PSPPLPPKRG LLPTNPPEAA LPSKPPGDRT VTASRPTLLP MHVAPTYPPP SPSPPLPTHI
PPEPPRMPLP NSTPALDAPR SLDLPKETPP PSKDFRSLEV SKRTAEQGFG EPPGLPRLPQ
IPLHIRIQQA LASPLPVTPP ADGSHRAHSL LFENDGFGED NGTLGRTRSL PVTIEMLKVP
DDEEEEEEDQ EEEQNSGPRV YIGDVPSITV IPMLVPQVLP EEQEGEEGMS DSDSEGPILY
KDDEEDEEED ESHNSTLANK VKRKDTLAIK LGNTTTVQEE KIVFPRKSKE EWNEIRQQIG
TTLIRRLSQR PTAEELEQRN ILQPKNEADR QAEKREIKRR LTRKLSQRPT VAELQARKIL
RFNEYVEVTD AQDYDRRADK PWTKLTPADK AAIRKELNEF KSCEMEVHEE SKQFTRYHRP
