ID   PTN3_MOUSE              Reviewed;         913 AA.
AC   A2ALK8;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   28-JAN-2026, entry version 136.
DE   RecName: Full=Tyrosine-protein phosphatase non-receptor type 3;
DE            EC=3.1.3.48;
GN   Name=Ptpn3;
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 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   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
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: May act at junctions between the membrane and the
CC       cytoskeleton. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-phospho-L-tyrosyl-[protein] + H2O = L-tyrosyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:20101, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:61978; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10044};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm,
CC       cytoskeleton {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class subfamily. {ECO:0000305}.
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DR   EMBL; AL805921; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS51181.1; -.
DR   RefSeq; NP_001371044.1; NM_001384115.1.
DR   RefSeq; NP_035337.2; NM_011207.2.
DR   RefSeq; XP_006538162.1; XM_006538099.4.
DR   RefSeq; XP_006538163.1; XM_006538100.4.
DR   AlphaFoldDB; A2ALK8; -.
DR   SMR; A2ALK8; -.
DR   BioGRID; 244476; 6.
DR   FunCoup; A2ALK8; 284.
DR   IntAct; A2ALK8; 1.
DR   MINT; A2ALK8; -.
DR   STRING; 10090.ENSMUSP00000075063; -.
DR   iPTMnet; A2ALK8; -.
DR   PhosphoSitePlus; A2ALK8; -.
DR   PaxDb; 10090-ENSMUSP00000075063; -.
DR   PeptideAtlas; A2ALK8; -.
DR   ProteomicsDB; 301958; -.
DR   Antibodypedia; 29434; 235 antibodies from 33 providers.
DR   DNASU; 545622; -.
DR   Ensembl; ENSMUST00000075637.11; ENSMUSP00000075063.5; ENSMUSG00000038764.15.
DR   GeneID; 545622; -.
DR   KEGG; mmu:545622; -.
DR   UCSC; uc008sya.2; mouse.
DR   AGR; MGI:105307; -.
DR   CTD; 5774; -.
DR   MGI; MGI:105307; Ptpn3.
DR   VEuPathDB; HostDB:ENSMUSG00000038764; -.
DR   eggNOG; KOG0792; Eukaryota.
DR   GeneTree; ENSGT00940000157888; -.
DR   HOGENOM; CLU_001645_7_0_1; -.
DR   InParanoid; A2ALK8; -.
DR   OMA; GIFHIRC; -.
DR   OrthoDB; 5854685at2759; -.
DR   PhylomeDB; A2ALK8; -.
DR   Reactome; R-MMU-182971; EGFR downregulation.
DR   Reactome; R-MMU-5675221; Negative regulation of MAPK pathway.
DR   BioGRID-ORCS; 545622; 1 hit in 78 CRISPR screens.
DR   PRO; PR:A2ALK8; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; A2ALK8; protein.
DR   Bgee; ENSMUSG00000038764; Expressed in medial dorsal nucleus of thalamus and 226 other cell types or tissues.
DR   ExpressionAtlas; A2ALK8; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISO:GO_Central.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:GO_Central.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0051117; F:ATPase binding; ISO:GO_Central.
DR   GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR   GO; GO:0001784; F:phosphotyrosine residue binding; ISO:GO_Central.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0017080; F:sodium channel regulator activity; ISO:GO_Central.
DR   GO; GO:0051045; P:negative regulation of membrane protein ectodomain proteolysis; ISO:GO_Central.
DR   GO; GO:0045930; P:negative regulation of mitotic cell cycle; ISO:GO_Central.
DR   GO; GO:0098902; P:regulation of membrane depolarization during action potential; ISO:GO_Central.
DR   GO; GO:1902305; P:regulation of sodium ion transmembrane transport; ISO:GO_Central.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13189; FERM_C_PTPN4_PTPN3_like; 1.
DR   CDD; cd06706; PDZ_PTPN3-4-like; 1.
DR   CDD; cd14600; PTPc-N3; 1.
DR   FunFam; 2.30.29.30:FF:000002; Band 4.1-like protein 5 isoform 1; 1.
DR   FunFam; 2.30.42.10:FF:000045; Tyrosine-protein phosphatase non-receptor type; 1.
DR   FunFam; 3.10.20.90:FF:000104; Tyrosine-protein phosphatase non-receptor type; 1.
DR   FunFam; 3.90.190.10:FF:000023; Tyrosine-protein phosphatase non-receptor type; 1.
DR   FunFam; 1.20.80.10:FF:000003; Tyrosine-protein phosphatase non-receptor type 4; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 3.10.20.90; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 1; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR   InterPro; IPR035963; FERM_2.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000242; PTP_cat.
DR   InterPro; IPR041783; PTPN3/4_FERM_C.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR012151; Tyr_Pase_non-rcpt_typ-3/4.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR45706; TYROSINE-PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR45706:SF5; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 3; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PIRSF; PIRSF000927; Tyr-Ptase_nr3; 1.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM01196; FERM_C; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF47031; Second domain of FERM; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   PROSITE; PS50106; PDZ; 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   Cell membrane; Cytoplasm; Cytoskeleton; Hydrolase; Membrane;
KW   Phosphoprotein; Protein phosphatase; Reference proteome.
FT   CHAIN           1..913
FT                   /note="Tyrosine-protein phosphatase non-receptor type 3"
FT                   /id="PRO_0000320074"
FT   DOMAIN          29..312
FT                   /note="FERM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT   DOMAIN          510..582
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          646..901
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   REGION          364..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          417..473
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..393
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        441..453
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        454..470
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        842
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT                   ECO:0000255|PROSITE-ProRule:PRU10044"
FT   BINDING         811
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         842..848
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         886
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         357
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P26045"
FT   MOD_RES         359
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P26045"
FT   MOD_RES         367
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P26045"
FT   MOD_RES         376
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P26045"
FT   MOD_RES         381
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P26045"
FT   MOD_RES         425
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P26045"
SQ   SEQUENCE   913 AA;  103896 MW;  8D86101FA691142A CRC64;
     MTSRLRALGG RINNTRTSEL PKEKTRSEVI CSIRFLDGLV QTFKVNKQDL GQSLLDMAYG
     HLGVTEKEYF GLQHGDDPVD SPRWLEASKP LRKQLKGGFP CTLHFRVRYF IPDPNTLQQE
     QTRHLYFLQL KMDVCEGRLT CPLNSAVVLA SYAVQSHFGD FNSSIHHPGY LADSQFIPDQ
     NDDFLSKVES LHEQHSGLKQ SEAESCYINI ARTLDFYGVE LHGGRDLHNL DLMIGIASAG
     IAVYRKYICT SFYPWVNILK ISFKRKKFFI HQRQKQAESR EHIVAFNMLN YRSCKNLWKS
     CVEHHSFFQA KKLLPQEKNV LSQYWTLGSR NPKKSVNNQY CKKVIGGMVW NPVMRRSLSV
     ERLETKSLPS RSPPITPNWR SPRLRHEIRK PRHSSADNLA NEMTYITETE DVFYTYKGPL
     SPKDSDSEVS QNHSPHRESL SENNPAQSCL TQKSSSSVSP SSNAPGSCSP DGVDQRFLED
     YHKVTKGGFV EDASQYYCDK SDDGDGYLVL IRITPDEEGR FGFNLKGGVD QKMPLVVSRI
     NPESPADTCM PKLNEGDQIV LINGRDISEH THDQVVMFIK ASRESHSREL ALVIRRKAVR
     SLAEIRSEDE LSQLFPEAMF PACPEGGDSL EGSMELLKKG LESGTVLIQF EQLYRKKPGL
     AVSFAKLPQN LDKNRYKDVL PYDTTRVLLQ GNEDYINASY VNMEMPAANL VNKYIATQGP
     LPNTCAQFWQ VVWDQKLSLV VMLTTLTERG RTKCHQYWPD PPDIMDHGIF HIQCQTEDCT
     IAYVSREMLV TNTETGEEHT VTHLQYVAWP DHGVPDDSSD FLEFVKYVRS LRVDGEPALV
     HCSAGIGRTG VLVTMETAMC LIERNLPVYP LDIVRKMRDQ RAMMVQTSSQ YKFVCEAILR
     VYEEGLVQRL DPS
//