PTN3_MOUSE
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 03-AUG-2022, entry version 120.
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=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: 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_035337.2; NM_011207.2.
DR RefSeq; XP_006538161.1; XM_006538098.2.
DR RefSeq; XP_006538162.1; XM_006538099.3.
DR RefSeq; XP_006538163.1; XM_006538100.2.
DR AlphaFoldDB; A2ALK8; -.
DR SMR; A2ALK8; -.
DR BioGRID; 244476; 6.
DR IntAct; A2ALK8; 1.
DR MINT; A2ALK8; -.
DR STRING; 10090.ENSMUSP00000075063; -.
DR iPTMnet; A2ALK8; -.
DR PhosphoSitePlus; A2ALK8; -.
DR EPD; A2ALK8; -.
DR MaxQB; A2ALK8; -.
DR PaxDb; A2ALK8; -.
DR PeptideAtlas; A2ALK8; -.
DR PRIDE; A2ALK8; -.
DR ProteomicsDB; 301958; -.
DR Antibodypedia; 29434; 247 antibodies from 33 providers.
DR DNASU; 545622; -.
DR Ensembl; ENSMUST00000075637; ENSMUSP00000075063; ENSMUSG00000038764.
DR GeneID; 545622; -.
DR KEGG; mmu:545622; -.
DR UCSC; uc008sya.2; mouse.
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; EHHSFFQ; -.
DR OrthoDB; 96595at2759; -.
DR PhylomeDB; A2ALK8; -.
DR TreeFam; TF315900; -.
DR Reactome; R-MMU-182971; EGFR downregulation.
DR Reactome; R-MMU-5675221; Negative regulation of MAPK pathway.
DR BioGRID-ORCS; 545622; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Ptpn3; mouse.
DR PRO; PR:A2ALK8; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; A2ALK8; protein.
DR Bgee; ENSMUSG00000038764; Expressed in medial dorsal nucleus of thalamus and 223 other tissues.
DR ExpressionAtlas; A2ALK8; baseline and differential.
DR Genevisible; A2ALK8; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR GO; GO:0001784; F:phosphotyrosine residue binding; ISO:MGI.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0017080; F:sodium channel regulator activity; ISO:MGI.
DR GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
DR GO; GO:0051045; P:negative regulation of membrane protein ectodomain proteolysis; ISO:MGI.
DR GO; GO:0045930; P:negative regulation of mitotic cell cycle; ISO:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; ISO:MGI.
DR GO; GO:0098902; P:regulation of membrane depolarization during action potential; ISO:MGI.
DR GO; GO:2000649; P:regulation of sodium ion transmembrane transporter activity; ISO:MGI.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13189; FERM_C_PTPN4_PTPN3_like; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.90.190.10; -; 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 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; SSF47031; SSF47031; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR SUPFAM; SSF54236; SSF54236; 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 436..469
FT /note="Polar residues"
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
