GenomeNet

Database: UniProt
Entry: F6VU58_MONDO
LinkDB: F6VU58_MONDO
Original site: F6VU58_MONDO 
ID   F6VU58_MONDO            Unreviewed;       922 AA.
AC   F6VU58;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 2.
DT   27-MAR-2024, entry version 92.
DE   RecName: Full=Tyrosine-protein phosphatase non-receptor type {ECO:0000256|PIRNR:PIRNR000927};
DE            EC=3.1.3.48 {ECO:0000256|PIRNR:PIRNR000927};
GN   Name=PTPN4 {ECO:0000313|Ensembl:ENSMODP00000000389.3};
OS   Monodelphis domestica (Gray short-tailed opossum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX   NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000000389.3, ECO:0000313|Proteomes:UP000002280};
RN   [1] {ECO:0000313|Ensembl:ENSMODP00000000389.3, ECO:0000313|Proteomes:UP000002280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17495919; DOI=10.1038/nature05805;
RA   Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., Duke S.,
RA   Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., Kamal M.,
RA   Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., Benos P.V.,
RA   Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., Deakin J.E.,
RA   Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., Gu W., Hore T.A.,
RA   Huttley G.A., Kleber M., Jirtle R.L., Koina E., Lee J.T., Mahony S.,
RA   Marra M.A., Miller R.D., Nicholls R.D., Oda M., Papenfuss A.T., Parra Z.E.,
RA   Pollock D.D., Ray D.A., Schein J.E., Speed T.P., Thompson K.,
RA   VandeBerg J.L., Wade C.M., Walker J.A., Waters P.D., Webber C.,
RA   Weidman J.R., Xie X., Zody M.C., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Bloom T., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M.,
RA   Samollow P.B., Lander E.S., Lindblad-Toh K.;
RT   "Genome of the marsupial Monodelphis domestica reveals innovation in non-
RT   coding sequences.";
RL   Nature 447:167-177(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMODP00000000389.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: May act at junctions between the membrane and the
CC       cytoskeleton. {ECO:0000256|PIRNR:PIRNR000927}.
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;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000927};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|PIRNR:PIRNR000927}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class subfamily. {ECO:0000256|ARBA:ARBA00009649,
CC       ECO:0000256|PIRNR:PIRNR000927}.
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DR   RefSeq; XP_016289073.1; XM_016433587.1.
DR   AlphaFoldDB; F6VU58; -.
DR   STRING; 13616.ENSMODP00000000389; -.
DR   Ensembl; ENSMODT00000000397.4; ENSMODP00000000389.3; ENSMODG00000000325.4.
DR   KEGG; mdo:100012975; -.
DR   CTD; 5775; -.
DR   eggNOG; KOG0792; Eukaryota.
DR   GeneTree; ENSGT00940000157211; -.
DR   HOGENOM; CLU_001645_7_0_1; -.
DR   InParanoid; F6VU58; -.
DR   OMA; MRWLDPS; -.
DR   OrthoDB; 5345383at2759; -.
DR   TreeFam; TF315900; -.
DR   Proteomes; UP000002280; Chromosome 4.
DR   Bgee; ENSMODG00000000325; Expressed in cerebellum and 19 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR   GO; GO:0035254; F:glutamate receptor binding; IEA:Ensembl.
DR   GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; IEA:Ensembl.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13189; FERM_C_PTPN4_PTPN3_like; 1.
DR   CDD; cd17194; FERM_F1_PTPN4; 1.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 2.30.42.10; -; 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; IPR014847; FA.
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:SF7; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 4; 1.
DR   Pfam; PF08736; FA; 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; SM01195; FA; 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; PS00660; FERM_1; 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   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR000927};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212,
KW   ECO:0000256|PIRNR:PIRNR000927}; Hydrolase {ECO:0000256|PIRNR:PIRNR000927};
KW   Protein phosphatase {ECO:0000256|PIRNR:PIRNR000927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002280}.
FT   DOMAIN          29..312
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   DOMAIN          517..589
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          655..911
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          828..902
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          381..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          450..473
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        852
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000927-1"
FT   BINDING         820
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000927-2"
FT   BINDING         852..858
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000927-2"
FT   BINDING         896
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000927-2"
SQ   SEQUENCE   922 AA;  105541 MW;  A1AD867C47C6364B CRC64;
     MTARFRLPAG RTYNVRASEL ARDRQHTEVV CNILLLDNTV QAFKVNKHDQ GQVLLDIVFK
     HLDLTERDYF GLQLADDSTD NPRWLDPNKP IRKQLKRGSP YSLNLRVKFF VSDPNKLQEE
     YTRYQYFLQI KQDILTGRLP CPYNTAALLA SFAIQSELGD YDHSENLPGY LSDYSFIPGQ
     PQDFEKEVAK LHQQHIGLSP AEAEFNYLNT ARTLELYGVE LHYARDQSNN EIMIGVMSGG
     ILINKNRIRM NTFPWLKIVK ISFKCKQFFI QLRKELHESR ETLLGFNMVN YRACKNLWKA
     CVEHHTFFRL DRPLPPQKNF FAHYFTLGSK FRYCGRTEVQ SVQYGKEKAN KDRVFARSPS
     KPLARKLMDW EVVSRNSLSD ERLETQSLPS RSPPGTPNHR NSAFTQEGTR LRPSSVGHLV
     DHIVHTSPSE VFVNHRSPSS TQANSIILES SPSQENSEDG QPPALPPKQS KKNSWNQINF
     SYSQQDLDNH INETFDVPTS PEKSTPNGGI PHDNLVVIKM KPDENGRFGF NVKGGYDQKM
     PVIVSRVAPG TSADLCVPRL NEGDQVVLIN GRDIAEHTHD QVVMFIKASC ERHSGELVLL
     VRPNAVYDVV EEKFENEPDF QYIPEKSPLD GVHQNDNALR ESMIQLAEGL DTGTILTQFD
     QLYRKKPGMT MSCAKLPQNI SKNRYRDISP YDATRVILKE NDDYINANYI NMEIPSSSII
     NQYIACQGPL PNTCMDFWQM TWEQGSSVVV MLTTQVERGR VKCHQYWPEL TESSSYGNFQ
     VTCHSEEGNS AYVFRNITLY NLEKNESRQL TQIQYIAWPD HGVPDDSSDF LDFVCHVRNK
     RAGKEEPIIV HCSAGIGRTG VLITMETAMC LIECNQPVYP LDIVRTMRDQ RAMMIQTPSQ
     YKFVCEAILK VYEEGFIKPV KT
//
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