ID   PTN9_RAT                Reviewed;         593 AA.
AC   Q641Z2; Q8K3Y9;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   24-JAN-2024, entry version 132.
DE   RecName: Full=Tyrosine-protein phosphatase non-receptor type 9;
DE            EC=3.1.3.48;
GN   Name=Ptpn9;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 532-593.
RC   STRAIN=Wistar;
RA   Heneberg P., Draber P.;
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
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   -!- 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; BC082041; AAH82041.1; -; mRNA.
DR   EMBL; AF520784; AAM98071.1; -; mRNA.
DR   RefSeq; NP_001013058.1; NM_001013040.1.
DR   AlphaFoldDB; Q641Z2; -.
DR   SMR; Q641Z2; -.
DR   IntAct; Q641Z2; 2.
DR   MINT; Q641Z2; -.
DR   STRING; 10116.ENSRNOP00000023831; -.
DR   iPTMnet; Q641Z2; -.
DR   PhosphoSitePlus; Q641Z2; -.
DR   jPOST; Q641Z2; -.
DR   PaxDb; 10116-ENSRNOP00000023831; -.
DR   Ensembl; ENSRNOT00000023831.7; ENSRNOP00000023831.5; ENSRNOG00000017600.7.
DR   Ensembl; ENSRNOT00055049552; ENSRNOP00055040769; ENSRNOG00055028611.
DR   Ensembl; ENSRNOT00060033399; ENSRNOP00060027326; ENSRNOG00060019254.
DR   Ensembl; ENSRNOT00065030395; ENSRNOP00065024172; ENSRNOG00065018139.
DR   GeneID; 266611; -.
DR   KEGG; rno:266611; -.
DR   UCSC; RGD:628726; rat.
DR   AGR; RGD:628726; -.
DR   CTD; 5780; -.
DR   RGD; 628726; Ptpn9.
DR   eggNOG; ENOG502QR81; Eukaryota.
DR   GeneTree; ENSGT00940000157447; -.
DR   InParanoid; Q641Z2; -.
DR   OMA; DLASWNF; -.
DR   OrthoDB; 2911650at2759; -.
DR   PhylomeDB; Q641Z2; -.
DR   TreeFam; TF351975; -.
DR   PRO; PR:Q641Z2; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000017600; Expressed in stomach and 19 other cell types or tissues.
DR   ExpressionAtlas; Q641Z2; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0044306; C:neuron projection terminus; ISO:RGD.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:RGD.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0010977; P:negative regulation of neuron projection development; ISO:RGD.
DR   GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:RGD.
DR   CDD; cd14543; PTPc-N9; 1.
DR   CDD; cd00170; SEC14; 1.
DR   Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR   Gene3D; 1.10.8.20; N-terminal domain of phosphatidylinositol transfer protein sec14p; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 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   PANTHER; PTHR19134; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR19134:SF285; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 9; 1.
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; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR   SUPFAM; SSF46938; CRAL/TRIO N-terminal domain; 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   2: Evidence at transcript 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_0000094766"
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..21
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   BINDING         470
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         515..521
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         559
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P43378"
SQ   SEQUENCE   593 AA;  67962 MW;  377836BB6B10D33D CRC64;
     MEPATAPRPD MAPELTPEEE QATKQFLEEI NKWTVQYNVS PLSWNVAVKF LMARKFDVLR
     AVELFHCYRE TRRKEGIVKL KPHEEPLRSE ILSGKFTILN VRDPTGASIA LFTARLHHPH
     KSVQHVVLQA LFYLLDRAVD SFETQRNGLV FIYDMCGSNY ANFELDLGKK VLNLLKGAFP
     ARLKKVLIVG APIWFRVPYS IISLLLKDKV RERIQILKTS EVTQHLPREC LPENLGGYIK
     IDLATWNFQF LPQVNGHPDP FDEIILFSLP PALDWDSVHV PGPHAMTIQE LVDYVNTRQK
     QGIYEEYEDI RRENPVGTFH CSMSPGNLEK NRYGDVPCLD QTRVKLTKRS GHTQTDYINA
     SFMDGYKQKN AYIGTQGPLE NTYRDFWLMV WEQKVLVIVM TTRFEEGGRR KCGQYWPLEK
     DSRIQFGFLT VTNLGVENMN HYKKTTLEIH NTEERQKRQV THFQFLSWPD YGVPSSAASL
     IDFLRVVRSQ QSMAVGSLGA RSKGQCPEPP IVVHCSAGIG RTGTFCSLDI CLAQLEELGT
     LNVFQTVSRM RTQRAFSIQT PEQYYFCYKA ILEFAEREGM VPSGHSLLAM DGQ
//