PTN9_MOUSE
ID PTN9_MOUSE Reviewed; 593 AA.
AC O35239; Q7TSK0;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Tyrosine-protein phosphatase non-receptor type 9;
DE EC=3.1.3.48;
DE AltName: Full=Protein-tyrosine phosphatase MEG2;
DE Short=PTPase MEG2;
GN Name=Ptpn9;
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 [MRNA].
RA Meng K., Gu M., Li F.N., Veile R.A., Donis-Keller H., Majerus P.W.;
RT "MPTP-MEG2.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Liver, Lung, Pancreas, and Testis;
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).
CC -!- FUNCTION: Protein-tyrosine phosphatase that could participate in the
CC transfer of hydrophobic ligands or in functions of the Golgi apparatus.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044};
CC -!- INTERACTION:
CC O35239; P46460: Nsf; NbExp=2; IntAct=EBI-7297868, EBI-398006;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class 3 subfamily. {ECO:0000305}.
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DR EMBL; AF013490; AAB66898.1; -; mRNA.
DR EMBL; BC053017; AAH53017.1; -; mRNA.
DR CCDS; CCDS23215.1; -.
DR RefSeq; NP_062625.2; NM_019651.2.
DR AlphaFoldDB; O35239; -.
DR SMR; O35239; -.
DR BioGRID; 207882; 1.
DR IntAct; O35239; 2.
DR MINT; O35239; -.
DR STRING; 10090.ENSMUSP00000034832; -.
DR iPTMnet; O35239; -.
DR PhosphoSitePlus; O35239; -.
DR SwissPalm; O35239; -.
DR EPD; O35239; -.
DR PaxDb; O35239; -.
DR PeptideAtlas; O35239; -.
DR PRIDE; O35239; -.
DR ProteomicsDB; 301942; -.
DR Antibodypedia; 27331; 128 antibodies from 29 providers.
DR DNASU; 56294; -.
DR Ensembl; ENSMUST00000034832; ENSMUSP00000034832; ENSMUSG00000032290.
DR GeneID; 56294; -.
DR KEGG; mmu:56294; -.
DR UCSC; uc009ptt.1; mouse.
DR CTD; 5780; -.
DR MGI; MGI:1928376; Ptpn9.
DR VEuPathDB; HostDB:ENSMUSG00000032290; -.
DR eggNOG; ENOG502QR81; Eukaryota.
DR GeneTree; ENSGT00940000157447; -.
DR HOGENOM; CLU_016977_1_0_1; -.
DR InParanoid; O35239; -.
DR OMA; QWTGHPQ; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; O35239; -.
DR TreeFam; TF351975; -.
DR BioGRID-ORCS; 56294; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Ptpn9; mouse.
DR PRO; PR:O35239; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; O35239; protein.
DR Bgee; ENSMUSG00000032290; Expressed in entorhinal cortex and 246 other tissues.
DR ExpressionAtlas; O35239; baseline and differential.
DR Genevisible; O35239; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0044306; C:neuron projection terminus; IDA:MGI.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISO:MGI.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; ISO:MGI.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 3.40.525.10; -; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR036273; CRAL/TRIO_N_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR Pfam; PF00650; CRAL_TRIO; 1.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF46938; SSF46938; 1.
DR SUPFAM; SSF52087; SSF52087; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Hydrolase; Protein phosphatase; Reference proteome.
FT CHAIN 1..593
FT /note="Tyrosine-protein phosphatase non-receptor type 9"
FT /id="PRO_0000094765"
FT DOMAIN 84..243
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT DOMAIN 303..574
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 515
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P43378"
FT CONFLICT 190
FT /note="G -> R (in Ref. 1; AAB66898)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="Q -> P (in Ref. 1; AAB66898)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="K -> T (in Ref. 1; AAB66898)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="E -> K (in Ref. 1; AAB66898)"
FT /evidence="ECO:0000305"
FT CONFLICT 277..278
FT /note="SV -> TL (in Ref. 1; AAB66898)"
FT /evidence="ECO:0000305"
FT CONFLICT 282..285
FT /note="GPHA -> SPLS (in Ref. 1; AAB66898)"
FT /evidence="ECO:0000305"
FT CONFLICT 311..312
FT /note="RR -> CL (in Ref. 1; AAB66898)"
FT /evidence="ECO:0000305"
FT CONFLICT 321..322
FT /note="CS -> RT (in Ref. 1; AAB66898)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="G -> R (in Ref. 1; AAB66898)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="I -> N (in Ref. 1; AAB66898)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="L -> M (in Ref. 1; AAB66898)"
FT /evidence="ECO:0000305"
FT CONFLICT 545
FT /note="Q -> H (in Ref. 1; AAB66898)"
FT /evidence="ECO:0000305"
FT CONFLICT 576..579
FT /note="EREG -> QKER (in Ref. 1; AAB66898)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 593 AA; 67970 MW; 053451BCD9DC7C61 CRC64;
MEPATAPRPD MAPELTPEEE QATKQFLEEI NKWTVQYNVS PLSWNVAVKF LMARKFDVLR
AVELFHCYRE TRRKEGIVKL KPHEEPLRSE ILSGKFTILN VRDPTGASIA LFTARLHHPH
KSAQHVVLQA LFYLLDRAVD SFETQRNGLV FIYDMCGSNY ANFELDLGKK VLNLLKGAFP
ARLKKVLIVG APIWFRVPYS IISLLLKDKV RERIQILKTS EVTQHLPREC LPENLGGYVK
IDLATWNFQF LPQVNGHPDP FDEIILSSLP PALDWDSVHV PGPHAMTIQE LVDYVNTRQK
RGIYEEYEDI RRENPVGTFH CSMSPGNLEK NRYGDVPCLD QTRVKLTKRS GHTQTDYINA
SFMDGYKQKN AYIGTQGPLE NTYRDFWLMV WEQKVLVIVM TTRFEEGGRR KCGQYWPLEK
DSRIRFGFLT VTNLGVENMN HYKKTTLEIH NTEERQKRQV THFQFLSWPD YGVPSSAASL
IDFLRVVRNQ QSMAVGNLGA RSKGQCPEPP IVVHCSAGIG RTGTFCSLDI CLAQLEELGT
LNVFQTVSRM RTQRAFSIQT PEQYYFCYKA ILEFAEREGM VPSGHSLLAM DGQ
