PHAR2_RAT
ID PHAR2_RAT Reviewed; 569 AA.
AC P62025;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Phosphatase and actin regulator 2;
GN Name=Phactr2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH PPP1CA AND ACTIN, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=15107502; DOI=10.1073/pnas.0401673101;
RA Allen P.B., Greenfield A.T., Svenningsson P., Haspeslagh D.C.,
RA Greengard P.;
RT "Phactrs 1-4: a family of protein phosphatase 1 and actin regulatory
RT proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7187-7192(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-457, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-357, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- SUBUNIT: Binds PPP1CA and actin.
CC -!- TISSUE SPECIFICITY: Expressed in the brain with high levels in the
CC cerebellum, specifically in the Purkinje cell layer, choroid plexus and
CC thalamus (ventral, rhomboid and anterior nuclei). Moderate to high
CC expression in the hippocampus, piriform cortex, olfactory bulb,
CC entorhinal cortex, as well as in geniculate bodies, lamboid septal
CC zone, preoptic area and ventral pallidum (at protein level).
CC {ECO:0000269|PubMed:15107502}.
CC -!- SIMILARITY: Belongs to the phosphatase and actin regulator family.
CC {ECO:0000305}.
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DR EMBL; AY500158; AAS86432.1; -; mRNA.
DR RefSeq; NP_999623.1; NM_214458.1.
DR AlphaFoldDB; P62025; -.
DR SMR; P62025; -.
DR STRING; 10116.ENSRNOP00000045608; -.
DR iPTMnet; P62025; -.
DR PhosphoSitePlus; P62025; -.
DR PaxDb; P62025; -.
DR PRIDE; P62025; -.
DR GeneID; 308291; -.
DR KEGG; rno:308291; -.
DR UCSC; RGD:1303141; rat.
DR CTD; 9749; -.
DR RGD; 1303141; Phactr2.
DR eggNOG; KOG4339; Eukaryota.
DR InParanoid; P62025; -.
DR OrthoDB; 1205245at2759; -.
DR PhylomeDB; P62025; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR PRO; PR:P62025; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR InterPro; IPR029991; Phactr2.
DR InterPro; IPR004018; RPEL_repeat.
DR PANTHER; PTHR12751:SF5; PTHR12751:SF5; 2.
DR Pfam; PF02755; RPEL; 1.
DR SMART; SM00707; RPEL; 4.
DR PROSITE; PS51073; RPEL; 4.
PE 1: Evidence at protein level;
KW Actin-binding; Phosphoprotein; Protein phosphatase inhibitor;
KW Reference proteome; Repeat.
FT CHAIN 1..569
FT /note="Phosphatase and actin regulator 2"
FT /id="PRO_0000126637"
FT REPEAT 71..96
FT /note="RPEL 1"
FT REPEAT 412..437
FT /note="RPEL 2"
FT REPEAT 450..475
FT /note="RPEL 3"
FT REPEAT 488..513
FT /note="RPEL 4"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..399
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 36
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75167"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75167"
SQ SEQUENCE 569 AA; 62201 MW; 3BF16A8DCF851AD6 CRC64;
MGQTSVSALS PQPGSVDGLD KASIANSDGP PAGSQTPPFK RKGKLSTIGK IFKPWKWRKE
KTSDKFRETS AVLERKISTR QSREELIRRG LLKELPDQDG DVTVNFENSN GHMIHIGEEA
TQEENVGKPE EGNVSVCEKG PPREEQAEEK TAGSSHPKKT TGSKASSSPS ASSTSSHPRG
PKESLTGKAG AVGTTRGKKK ISKQPAAAAS RLSPNTVTSE TSSLKGELSD TGVESLKPEE
TVAGAEEEAT GKPKAVVVAL PPVTVPPSSP ALPLPPEDPC TIALDTPMVL VSDGPTLPIS
ALETSPLPGT EEPANRTTPY SSTGLGGSRE QAKCFTTKDG LGKAGPQLLT PGQMGDSLES
FSAPEDEAPR EYQANDSDSD GPILYTDDDD EEDDDDDSTG ESALASKIRR RDTLAIKLGN
RPSKKELEDK NILQRTSEEE RQELRQQIGT KLVRRLSQRP TTEELEQRSI LKQKNEEEEQ
EAKMELKRRL SRKLSLRPTV PELQARRILR FNEYVEVTDS PDYDRRADKP WARLTPADKA
AIRKELNEFK STEMEVHEES RQFTRFHRP
