PPR18_MOUSE
ID PPR18_MOUSE Reviewed; 594 AA.
AC Q8BQ30; B8JJ63; B8JJ64; Q3UDS6; Q8CEY9; Q8R3D8;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 123.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Spinal ganglion, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194 AND SER-412, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194 AND SER-510, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-437, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BQ30-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BQ30-2; Sequence=VSP_014260;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH25573.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK009340; BAC25252.1; -; mRNA.
DR EMBL; AK051656; BAC34706.1; -; mRNA.
DR EMBL; AK149943; BAE29185.1; -; mRNA.
DR EMBL; CR974451; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025573; AAH25573.1; ALT_INIT; mRNA.
DR CCDS; CCDS50094.1; -. [Q8BQ30-1]
DR RefSeq; NP_001140182.1; NM_001146710.1. [Q8BQ30-1]
DR RefSeq; NP_001140183.1; NM_001146711.1. [Q8BQ30-1]
DR RefSeq; NP_780451.1; NM_175242.1. [Q8BQ30-1]
DR RefSeq; XP_006525155.2; XM_006525092.3. [Q8BQ30-2]
DR AlphaFoldDB; Q8BQ30; -.
DR SMR; Q8BQ30; -.
DR BioGRID; 218132; 10.
DR IntAct; Q8BQ30; 3.
DR STRING; 10090.ENSMUSP00000109445; -.
DR iPTMnet; Q8BQ30; -.
DR PhosphoSitePlus; Q8BQ30; -.
DR EPD; Q8BQ30; -.
DR jPOST; Q8BQ30; -.
DR MaxQB; Q8BQ30; -.
DR PaxDb; Q8BQ30; -.
DR PeptideAtlas; Q8BQ30; -.
DR PRIDE; Q8BQ30; -.
DR ProteomicsDB; 289384; -. [Q8BQ30-1]
DR ProteomicsDB; 289385; -. [Q8BQ30-2]
DR Antibodypedia; 55922; 129 antibodies from 25 providers.
DR Ensembl; ENSMUST00000113814; ENSMUSP00000109445; ENSMUSG00000034595. [Q8BQ30-1]
DR Ensembl; ENSMUST00000122899; ENSMUSP00000120343; ENSMUSG00000034595. [Q8BQ30-1]
DR Ensembl; ENSMUST00000127442; ENSMUSP00000115753; ENSMUSG00000034595. [Q8BQ30-2]
DR Ensembl; ENSMUST00000144382; ENSMUSP00000116100; ENSMUSG00000034595. [Q8BQ30-1]
DR Ensembl; ENSMUST00000187690; ENSMUSP00000141094; ENSMUSG00000034595. [Q8BQ30-1]
DR GeneID; 76448; -.
DR KEGG; mmu:76448; -.
DR UCSC; uc008cit.2; mouse. [Q8BQ30-2]
DR UCSC; uc008ciu.2; mouse. [Q8BQ30-1]
DR CTD; 170954; -.
DR MGI; MGI:1923698; Ppp1r18.
DR VEuPathDB; HostDB:ENSMUSG00000034595; -.
DR eggNOG; ENOG502RY8Q; Eukaryota.
DR GeneTree; ENSGT00530000064035; -.
DR HOGENOM; CLU_019218_0_0_1; -.
DR InParanoid; Q8BQ30; -.
DR OMA; EWTPRDT; -.
DR OrthoDB; 592905at2759; -.
DR PhylomeDB; Q8BQ30; -.
DR TreeFam; TF337604; -.
DR BioGRID-ORCS; 76448; 7 hits in 72 CRISPR screens.
DR ChiTaRS; Ppp1r18; mouse.
DR PRO; PR:Q8BQ30; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8BQ30; protein.
DR Bgee; ENSMUSG00000034595; Expressed in granulocyte and 248 other tissues.
DR ExpressionAtlas; Q8BQ30; baseline and differential.
DR Genevisible; Q8BQ30; MM.
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 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..594
FT /note="Phostensin"
FT /id="PRO_0000050809"
FT REGION 18..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..422
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..572
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NYC8"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NYC8"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NYC8"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 198
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 412
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 437
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 589..594
FT /note="DESCRR -> GKRLRPGWRRAPPGVCGVVVL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014260"
FT CONFLICT 278
FT /note="R -> I (in Ref. 3; AAH25573)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 594 AA; 65630 MW; 6B7B10B39C5B44BA CRC64;
MTAIPDWKLQ LLARRRQEEA AVRGREKAER DRLSQMPAWK RGILERRRAK LGLPPGEGSP
VPGNAEAGPP DPDESAVLLE AIGPVHQNRF IQQERQRQQQ QQQQQRNEVL GDRKAGPLEV
LERRSSPGNL RDQSPKGRES REERLSPRES RDRRLVIGGA QESSSRSLRD WRQSPAEARD
LSSRPAEAQK WRLSPGETPE ESLRLAGSGD DSPKRKEVLE SILSPGEPGD QKASPTDVHK
WNLDSREPQK QSLIQLEATE WRLKSGEERK DYLEGCGREE EKLSSGIVPV TKEVQDITSS
EVETAEQRPT ESWKWTLNSG KARERTTWDI DTQTQKPDPP ASSEKHPGPS GMEAEEEAEK
EEAEAQSRPL RAQQNLCSGP SPLPPEHSGT EGSRQQEEEA AEPRPPTPAP LSPPPSAPTA
PQPSGDPLMS RLFYGVKPGP GVGAPRRSGH TFTVNPRRCA PPASPAPPVN PATADAAGSG
SGKKRYPTAE EILVLGGYLR LSRSCLVKGS PERHHKQLKI SFSETALETT YQYPSESSVL
EDLGPEPETP IAPLATQPDE EEEEEEEEEE LLLQPGLQGG LRTKALIVDE SCRR
