PPR18_PIG
ID PPR18_PIG Reviewed; 618 AA.
AC Q767M0;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 70.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Large white;
RX PubMed=14673549; DOI=10.1007/s00251-003-0627-0;
RA Shigenari A., Ando A., Renard C., Chardon P., Shiina T., Kulski J.K.,
RA Yasue H., Inoko H.;
RT "Nucleotide sequencing analysis of the swine 433-kb genomic segment located
RT between the non-classical and classical SLA class I gene clusters.";
RL Immunogenetics 55:695-705(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; AB113356; BAD08432.1; -; Genomic_DNA.
DR RefSeq; NP_001121952.1; NM_001128480.1.
DR AlphaFoldDB; Q767M0; -.
DR STRING; 9823.ENSSSCP00000030846; -.
DR PaxDb; Q767M0; -.
DR PeptideAtlas; Q767M0; -.
DR PRIDE; Q767M0; -.
DR GeneID; 100151743; -.
DR KEGG; ssc:100151743; -.
DR CTD; 170954; -.
DR eggNOG; ENOG502RY8Q; Eukaryota.
DR InParanoid; Q767M0; -.
DR OrthoDB; 592905at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
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..618
FT /note="Phostensin"
FT /id="PRO_0000050810"
FT REGION 15..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..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..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..451
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 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NYC8"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NYC8"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NYC8"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NYC8"
FT MOD_RES 205
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6NYC8"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NYC8"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BQ30"
FT MOD_RES 462
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BQ30"
FT MOD_RES 535
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BQ30"
SQ SEQUENCE 618 AA; 67962 MW; 50B85D4553DEEB38 CRC64;
MATIPDWKLQ LLARRRQEEA AVRGREKAER ERLSQMPAWK RGLLERRRAK LGLSPGEPSP
APGTTEAGPP DPDKSAVLLE AIGPVHQNRF IRQERQQQQQ QQQQQQQQQR SEELLAERRP
GLLEAREWRS SPGEMRDQSP KERESREERL SPREARERRL GIGGARESSP RPLESRDWRQ
SPGEAGDRSS RLSEVRKWRL SPGETPERSL RPAEPQEQSP RRKEVVESRL SPADSDHEKL
GLTDAHKRRP DSGESQEQSL VLEASEWRLS SGEERKDCLE ECGRKEERTL PGMVPEDITG
SPETLTMEAA GSSSGGVEAA DQRPIPVEDG ERDLRLSEGW KWTLNSGKVR DRTPRDTETQ
SQKPESAEKH LGPLGAEAGE GEAEKEEAGA QGRPLSALQN RCSVPSPLPP EDAGTGGSRQ
QEEEAGELRP PPAAPLSPPP PAPPAPQPPG DPLMSRLFYG VKAGPGVGAP RRSGHTFTVN
PRRSAPPAAA ATPATPATAD AAVPGAGKKR YPTAEEILVL GGYLRLSRSC LAKGSPERHH
KQLKISFSET ALETTYQYPS ESSVLEELGP EPEAPSAPSP PAAQPDDEED EEELLLLQRE
LQGGLRTKAL IVDESCRR
