PPR3F_HUMAN
ID PPR3F_HUMAN Reviewed; 799 AA.
AC Q6ZSY5; A2VDJ8; B3KPW2; E9PCM3;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 3.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 3F;
DE Short=R3F;
GN Name=PPP1R3F;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 51-799 (ISOFORM 1).
RC TISSUE=Brain, and Prostate;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND PHOSPHORYLATION AT SER-14; SER-18;
RP SER-420 AND SER-421.
RX PubMed=21668450; DOI=10.1111/j.1471-4159.2011.07345.x;
RA Kelsall I.R., Voss M., Munro S., Cuthbertson D.J., Cohen P.T.;
RT "R3F, a novel membrane-associated glycogen targeting subunit of protein
RT phosphatase 1 regulates glycogen synthase in astrocytoma cells in response
RT to glucose and extracellular signals.";
RL J. Neurochem. 118:596-610(2011).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-547, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [6]
RP VARIANT LYS-441.
RX PubMed=23092983; DOI=10.1038/tp.2012.102;
RA Nava C., Lamari F., Heron D., Mignot C., Rastetter A., Keren B., Cohen D.,
RA Faudet A., Bouteiller D., Gilleron M., Jacquette A., Whalen S., Afenjar A.,
RA Perisse D., Laurent C., Dupuits C., Gautier C., Gerard M., Huguet G.,
RA Caillet S., Leheup B., Leboyer M., Gillberg C., Delorme R., Bourgeron T.,
RA Brice A., Depienne C.;
RT "Analysis of the chromosome X exome in patients with autism spectrum
RT disorders identified novel candidate genes, including TMLHE.";
RL Transl. Psychiatry 2:E179-E179(2012).
CC -!- FUNCTION: Glycogen-targeting subunit for protein phosphatase 1 (PP1).
CC {ECO:0000269|PubMed:21668450}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6ZSY5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZSY5-2; Sequence=VSP_045003, VSP_045004;
CC -!- TISSUE SPECIFICITY: Expressed in brain, skeletal muscle and heart.
CC {ECO:0000269|PubMed:21668450}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI31589.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG51824.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF235097; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC131588; AAI31589.1; ALT_INIT; mRNA.
DR EMBL; AK056909; BAG51824.1; ALT_INIT; mRNA.
DR CCDS; CCDS35254.1; -. [Q6ZSY5-1]
DR CCDS; CCDS55415.1; -. [Q6ZSY5-2]
DR RefSeq; NP_001171674.1; NM_001184745.1. [Q6ZSY5-2]
DR RefSeq; NP_149992.3; NM_033215.4. [Q6ZSY5-1]
DR AlphaFoldDB; Q6ZSY5; -.
DR SMR; Q6ZSY5; -.
DR BioGRID; 124607; 15.
DR IntAct; Q6ZSY5; 9.
DR MINT; Q6ZSY5; -.
DR STRING; 9606.ENSP00000055335; -.
DR CAZy; CBM21; Carbohydrate-Binding Module Family 21.
DR GlyGen; Q6ZSY5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6ZSY5; -.
DR PhosphoSitePlus; Q6ZSY5; -.
DR BioMuta; PPP1R3F; -.
DR DMDM; 226694145; -.
DR EPD; Q6ZSY5; -.
DR jPOST; Q6ZSY5; -.
DR MassIVE; Q6ZSY5; -.
DR MaxQB; Q6ZSY5; -.
DR PaxDb; Q6ZSY5; -.
DR PeptideAtlas; Q6ZSY5; -.
DR PRIDE; Q6ZSY5; -.
DR ProteomicsDB; 19470; -.
DR ProteomicsDB; 68245; -. [Q6ZSY5-1]
DR Antibodypedia; 338; 71 antibodies from 17 providers.
DR DNASU; 89801; -.
DR Ensembl; ENST00000055335.11; ENSP00000055335.6; ENSG00000049769.14. [Q6ZSY5-1]
DR Ensembl; ENST00000376188.1; ENSP00000365359.1; ENSG00000049769.14. [Q6ZSY5-2]
DR Ensembl; ENST00000466508.5; ENSP00000420687.1; ENSG00000049769.14. [Q6ZSY5-2]
DR Ensembl; ENST00000495799.5; ENSP00000417535.1; ENSG00000049769.14. [Q6ZSY5-2]
DR GeneID; 89801; -.
DR KEGG; hsa:89801; -.
DR MANE-Select; ENST00000055335.11; ENSP00000055335.6; NM_033215.5; NP_149992.3.
DR UCSC; uc004dnh.3; human. [Q6ZSY5-1]
DR CTD; 89801; -.
DR DisGeNET; 89801; -.
DR GeneCards; PPP1R3F; -.
DR HGNC; HGNC:14944; PPP1R3F.
DR HPA; ENSG00000049769; Tissue enhanced (skeletal).
DR neXtProt; NX_Q6ZSY5; -.
DR OpenTargets; ENSG00000049769; -.
DR PharmGKB; PA33656; -.
DR VEuPathDB; HostDB:ENSG00000049769; -.
DR eggNOG; KOG3986; Eukaryota.
DR GeneTree; ENSGT00390000013859; -.
DR HOGENOM; CLU_563304_0_0_1; -.
DR InParanoid; Q6ZSY5; -.
DR OMA; NMDDNTP; -.
DR OrthoDB; 1232750at2759; -.
DR PhylomeDB; Q6ZSY5; -.
DR TreeFam; TF352142; -.
DR PathwayCommons; Q6ZSY5; -.
DR SignaLink; Q6ZSY5; -.
DR BioGRID-ORCS; 89801; 11 hits in 697 CRISPR screens.
DR ChiTaRS; PPP1R3F; human.
DR GenomeRNAi; 89801; -.
DR Pharos; Q6ZSY5; Tbio.
DR PRO; PR:Q6ZSY5; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q6ZSY5; protein.
DR Bgee; ENSG00000049769; Expressed in endothelial cell and 153 other tissues.
DR ExpressionAtlas; Q6ZSY5; baseline and differential.
DR Genevisible; Q6ZSY5; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; IBA:GO_Central.
DR GO; GO:2001069; F:glycogen binding; IDA:MGI.
DR GO; GO:0008157; F:protein phosphatase 1 binding; IBA:GO_Central.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:MGI.
DR GO; GO:2000465; P:regulation of glycogen (starch) synthase activity; IDA:MGI.
DR GO; GO:0005979; P:regulation of glycogen biosynthetic process; IDA:MGI.
DR Gene3D; 2.60.40.2440; -; 1.
DR InterPro; IPR005036; CBM21_dom.
DR InterPro; IPR038175; CBM21_dom_sf.
DR Pfam; PF03370; CBM_21; 1.
DR PROSITE; PS51159; CBM21; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..799
FT /note="Protein phosphatase 1 regulatory subunit 3F"
FT /id="PRO_0000257496"
FT TOPO_DOM 1..768
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 769..789
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 790..799
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 128..284
FT /note="CBM21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00491"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 36..39
FT /note="PP1-binding motif"
FT COMPBIAS 77..99
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21668450"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21668450"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21668450"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21668450"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 589
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIG4"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIG4"
FT VAR_SEQ 1..345
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045003"
FT VAR_SEQ 354
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045004"
FT VARIANT 351
FT /note="F -> S (in dbSNP:rs17148347)"
FT /id="VAR_028918"
FT VARIANT 441
FT /note="E -> K"
FT /evidence="ECO:0000269|PubMed:23092983"
FT /id="VAR_076266"
FT CONFLICT 377
FT /note="Q -> H (in Ref. 3; BAG51824)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 799 AA; 82798 MW; 7E9EDD5515DE245D CRC64;
MARTAPVEPP LRHSAPPSPA AGEPRTSVEA AVAPRRVLFA DEALGLPLAQ LRRYRPWGGP
GAGKMAAAAG QDGGGGGGAD EDDDGEDGDE GEEEEEACPE PSPLCPVPAG GGFYLVPTFS
LPPAPGRLER LGRVMVELEA LLPPPGAVPG GAGVWVPGGR PPVLRGLVRV LNRSFEKAVH
VRASHDGWAS FCDHPARYVP RSPPWAGAGG TGAGDPILDP GLGLGPGQAS ASSPDDGGRT
DRFAFQLPFA EGAGDGARLD FVVRYETPEG TFWANNHGRN YTVLLRIAPA PTPTDAEGLP
QQQQLPQLEP QPECQGPVEA EARQLKSCMK PVRRRPAEEE LKTKNMDDNT FAMAEHPDVQ
ESVGPLVAPT PLRPWPQMTL QVSDVPMTGN PAEEGDVPRS SPPVAFTEVL QAPAIRIPPS
SPLCGLGGSP RDQASGPDAS EGATGPFLEP SQQQAEATWG VSSENGGGLE AVSGSEELLG
EDTIDQELEQ LYLSHLSRLR AAVAAGGAGG GGEGSTDGGM SPSHPLGILT DRDLILKWPG
PERALNSALA EEITLHYARL GRGVELIKDT EDPDDEGEGE EGLSVTPSSP EGDSPKESPP
EILSGARSVV ATMGDVWLPW AEGSGCDGPV VLGTEGQFIG DPEKGMGKDT SSLHMNRVIA
GVTESLGEAG TEAQIEVTSE WAGSLDPISG KEPASPVLLQ GQNPTLLSPL GAEVCLSSVA
RPHVSSQDEK DAGPSLEPPK KSPTLAVPAE CVCALPPQLR GPLTQTLGVL AGLVVVPVAL
NSGVSLLVLA LCLSLAWFS
