PTC71_DROME
ID PTC71_DROME Reviewed; 314 AA.
AC Q9VAH4; A8MPH7; Q8SWZ0;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Protein phosphatase PTC7 homolog fig;
DE AltName: Full=Fos intronic gene protein;
DE EC=3.1.3.16;
GN Name=fig {ECO:0000312|EMBL:AAF56936.1, ECO:0000312|FlyBase:FBgn0039694};
GN ORFNames=CG7615;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABI74754.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA), ALTERNATIVE PROMOTER
RP USAGE, AND DEVELOPMENTAL STAGE.
RX PubMed=18571877; DOI=10.1016/j.gene.2008.05.001;
RA Hudson S.G., Goldstein E.S.;
RT "The gene structure of the Drosophila melanogaster proto-oncogene, kayak,
RT and its nested gene, fos-intronic gene.";
RL Gene 420:76-81(2008).
RN [2] {ECO:0000312|EMBL:AAF56936.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAF56936.1}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000312|EMBL:AAM11295.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM11295.1};
RC TISSUE=Head {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5] {ECO:0000312|EMBL:ACI16531.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
RC STRAIN=Berkeley;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P35813, ECO:0000305};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P35813, ECO:0000305};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=alpha {ECO:0000269|PubMed:18571877};
CC IsoId=Q9VAH4-1; Sequence=Displayed;
CC Name=beta {ECO:0000269|PubMed:18571877};
CC IsoId=Q9VAH4-2; Sequence=VSP_053111;
CC -!- DEVELOPMENTAL STAGE: Isoform alpha and isoform beta are expressed both
CC maternally and zygotically. Zygotic expression is present throughout
CC embryogenesis and fades by first larval instar. Expression levels at
CC all stages are low. {ECO:0000269|PubMed:18571877}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM11295.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; DQ858472; ABI74754.1; -; mRNA.
DR EMBL; DQ858473; ABI74755.1; -; mRNA.
DR EMBL; AE014297; AAF56936.1; -; Genomic_DNA.
DR EMBL; AY094942; AAM11295.1; ALT_FRAME; mRNA.
DR EMBL; BT044569; ACI16531.1; -; mRNA.
DR RefSeq; NP_651724.1; NM_143467.4. [Q9VAH4-1]
DR AlphaFoldDB; Q9VAH4; -.
DR SMR; Q9VAH4; -.
DR BioGRID; 68375; 1.
DR IntAct; Q9VAH4; 7.
DR STRING; 7227.FBpp0084904; -.
DR PaxDb; Q9VAH4; -.
DR PRIDE; Q9VAH4; -.
DR DNASU; 43511; -.
DR EnsemblMetazoa; FBtr0085538; FBpp0084904; FBgn0039694. [Q9VAH4-1]
DR GeneID; 43511; -.
DR KEGG; dme:Dmel_CG7615; -.
DR UCSC; CG7615-RA; d. melanogaster. [Q9VAH4-1]
DR CTD; 43511; -.
DR FlyBase; FBgn0039694; fig.
DR VEuPathDB; VectorBase:FBgn0039694; -.
DR eggNOG; KOG1379; Eukaryota.
DR GeneTree; ENSGT00390000011937; -.
DR HOGENOM; CLU_029404_3_0_1; -.
DR InParanoid; Q9VAH4; -.
DR OMA; DSWFVSS; -.
DR PhylomeDB; Q9VAH4; -.
DR SignaLink; Q9VAH4; -.
DR BioGRID-ORCS; 43511; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 43511; -.
DR PRO; PR:Q9VAH4; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0039694; Expressed in testis and 9 other tissues.
DR Genevisible; Q9VAH4; DM.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; ISS:FlyBase.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0016311; P:dephosphorylation; ISS:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; ISS:FlyBase.
DR GO; GO:0010795; P:regulation of ubiquinone biosynthetic process; IMP:UniProtKB.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR InterPro; IPR039123; PPTC7.
DR PANTHER; PTHR12320; PTHR12320; 1.
DR Pfam; PF07228; SpoIIE; 1.
DR SMART; SM00331; PP2C_SIG; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 2: Evidence at transcript level;
KW Alternative promoter usage; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..314
FT /note="Protein phosphatase PTC7 homolog fig"
FT /id="PRO_0000377398"
FT DOMAIN 43..309
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT BINDING 87
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P35813"
FT BINDING 87
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P35813"
FT BINDING 88
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P35813"
FT BINDING 232
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P35813"
FT VAR_SEQ 1..152
FT /note="Missing (in isoform beta)"
FT /evidence="ECO:0000303|PubMed:18571877"
FT /id="VSP_053111"
SQ SEQUENCE 314 AA; 34838 MW; F6D2A3360D4AD8A4 CRC64;
MITCLRNWPL LLKRFSVHQI HQFTQLSGRF ERPPQSGKSS RDPYLVTVVQ GRSKKPRFPG
ERSNQRFGED SWFVSSTPLA EVMGVADGVG GWRDLGVDAG RFAKELMSCC SGQTQLSDFD
GRSPRNMLIA GFQELSHREH PVVGSSTACL ATMHRKDCTL YTANLGDSGF LVVRNGRVLH
RSVEQTHDFN TPYQLTVPPE DRKESYYCDK PEMAVSTRHS LLPGDLVLLA TDGLFDNMPE
SMLLSILNGL KERGEHDLLV GASRVVEKAR ELSMNASFQS PFAIKARQHN VSYSGGGKPD
DITLILSSVE VPNA
