PPR18_MACMU
ID PPR18_MACMU Reviewed; 613 AA.
AC Q5TM66;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Phostensin;
DE AltName: Full=Protein phosphatase 1 F-actin cytoskeleton-targeting subunit;
DE AltName: Full=Protein phosphatase 1 regulatory subunit 18;
GN Name=PPP1R18;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15269276; DOI=10.1093/molbev/msh216;
RA Kulski J.K., Anzai T., Shiina T., Inoko H.;
RT "Rhesus macaque class I duplicon structures, organization, and evolution
RT within the alpha block of the major histocompatibility complex.";
RL Mol. Biol. Evol. 21:2079-2091(2004).
CC -!- FUNCTION: May target protein phosphatase 1 to F-actin cytoskeleton.
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with Protein phosphatase 1 (PP1). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
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DR EMBL; AB128049; BAD69760.1; -; Genomic_DNA.
DR RefSeq; NP_001098634.1; NM_001105164.1.
DR RefSeq; XP_014991336.1; XM_015135850.1.
DR AlphaFoldDB; Q5TM66; -.
DR SMR; Q5TM66; -.
DR STRING; 9544.ENSMMUP00000026249; -.
DR Ensembl; ENSMMUT00000070396; ENSMMUP00000055673; ENSMMUG00000019961.
DR GeneID; 712176; -.
DR KEGG; mcc:712176; -.
DR CTD; 170954; -.
DR VEuPathDB; HostDB:ENSMMUG00000019961; -.
DR VGNC; VGNC:104421; PPP1R18.
DR eggNOG; ENOG502RY8Q; Eukaryota.
DR GeneTree; ENSGT00530000064035; -.
DR InParanoid; Q5TM66; -.
DR OrthoDB; 592905at2759; -.
DR Proteomes; UP000006718; Chromosome 4.
DR Bgee; ENSMMUG00000019961; Expressed in spleen and 22 other tissues.
DR ExpressionAtlas; Q5TM66; baseline.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0019902; F:phosphatase binding; IEA:InterPro.
DR InterPro; IPR025903; Phostensin/Taperin_N_dom.
DR InterPro; IPR025907; Phostensin/Taperin_PP1-bd_dom.
DR InterPro; IPR026671; PPP1R18/Tprn.
DR PANTHER; PTHR21685; PTHR21685; 1.
DR Pfam; PF13914; Phostensin; 1.
DR Pfam; PF13916; Phostensin_N; 1.
PE 3: Inferred from homology;
KW Acetylation; Actin-binding; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..613
FT /note="Phostensin"
FT /id="PRO_0000050808"
FT REGION 15..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..445
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NYC8"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NYC8"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NYC8"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NYC8"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NYC8"
FT MOD_RES 199
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6NYC8"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NYC8"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NYC8"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BQ30"
FT MOD_RES 457
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BQ30"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NYC8"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BQ30"
SQ SEQUENCE 613 AA; 67999 MW; AD54CFC5CE6DB6C6 CRC64;
MATIPDWKLQ LLARRRQEEA SVRGREKAER ERLSQMPAWK RGLLERRRAK LGLSPGEPSP
VPGTAEAGPP DPDESSVLLE AIGPVHQNRF IRQERQQQQQ QQQRSEELLA ERKPVPLEAR
ERRPSPGEMR DQSPKGRESR EERLSPRETR ERRLGIGGAQ ESSLRPLEAR DWRQSPGEVG
DRSSRLSEPW KWRLSPGETP ERSLRLAESR EQSPRRKEVE SRLSPGESAY QKLGLTEAHK
WRPDSRESQE QSLVQLEATE WRLRSGEERQ GYSEKCGRKE EWPVPGVAPE ETTELSETLT
REAQGSSSTG MEAAEQRPVE DGERGMKPAE GWKWTLNSGK AREWTPRDIE AQTQKPEPSE
SAEKRLESPS VEAGEGEAEK EEAGAQGRPL RALQNCCSVP SPLPPEDAGT GGLRQQEEEA
VELQPPPPAP LSPPPPAPTA PQPPGDPLMS RLFYGVKAGP GVGAPRRSGH TFTVNPRRSV
PPTTPATPTS PATADAAVPG AGKKRYPTAE EILVLGGYLR LSRSCLAKGS PERHHKQLKI
SFSETALETT YQYPSESSVL EELGPEPEVP SAPNPPAAQP DDEEDEEELL LLQPELQGGL
RTKALIVDES CRR
