PTPRG_MOUSE
ID PTPRG_MOUSE Reviewed; 1442 AA.
AC Q05909;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase gamma;
DE Short=Protein-tyrosine phosphatase gamma;
DE Short=R-PTP-gamma;
DE EC=3.1.3.48;
DE Flags: Precursor;
GN Name=Ptprg;
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].
RX PubMed=8382771; DOI=10.1128/mcb.13.3.1497-1506.1993;
RA Barnea G., Silvennoinen O., Shaanan B., Honegger A.M., Canoll P.D.,
RA D'Eustachio P., Morse B., Levy J.B., Laforgia S., Huebner K.,
RA Musacchio J.M., Sap J., Schlessinger J.;
RT "Identification of a carbonic anhydrase-like domain in the extracellular
RT region of RPTP gamma defines a new subfamily of receptor tyrosine
RT phosphatases.";
RL Mol. Cell. Biol. 13:1497-1506(1993).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, and Lung;
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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 55-320 IN COMPLEX WITH CNTN4,
RP INTERACTION WITH CNTN3; CNTN4; CNTN5 AND CNTN6, AND DISULFIDE BOND.
RX PubMed=20133774; DOI=10.1073/pnas.0911235107;
RA Bouyain S., Watkins D.J.;
RT "The protein tyrosine phosphatases PTPRZ and PTPRG bind to distinct members
RT of the contactin family of neural recognition molecules.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:2443-2448(2010).
CC -!- FUNCTION: Possesses tyrosine phosphatase activity. {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 -!- SUBUNIT: Monomer; active form. Homodimer; inactive form (By
CC similarity). Interacts with CNTN3, CNTN4, CNTN5 and CNTN6.
CC {ECO:0000250, ECO:0000269|PubMed:20133774}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in brain, lung, kidney, heart, liver,
CC skeletal muscle, spleen and testes. It is developmentally regulated in
CC the brain.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 5 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L09562; AAA40022.1; -; mRNA.
DR CCDS; CCDS26816.1; -.
DR PIR; B48148; B48148.
DR RefSeq; NP_033007.2; NM_008981.3.
DR PDB; 3JXG; X-ray; 1.70 A; A/B/C/D=55-320.
DR PDB; 3KLD; X-ray; 2.00 A; B=55-320.
DR PDB; 5E5U; X-ray; 2.00 A; A/C=57-320.
DR PDBsum; 3JXG; -.
DR PDBsum; 3KLD; -.
DR PDBsum; 5E5U; -.
DR AlphaFoldDB; Q05909; -.
DR SMR; Q05909; -.
DR BioGRID; 202498; 8.
DR IntAct; Q05909; 1.
DR STRING; 10090.ENSMUSP00000022264; -.
DR GlyConnect; 2670; 1 N-Linked glycan (1 site).
DR GlyGen; Q05909; 6 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q05909; -.
DR PhosphoSitePlus; Q05909; -.
DR SwissPalm; Q05909; -.
DR CPTAC; non-CPTAC-4056; -.
DR MaxQB; Q05909; -.
DR PaxDb; Q05909; -.
DR PRIDE; Q05909; -.
DR ProteomicsDB; 302013; -.
DR ABCD; Q05909; 7 sequenced antibodies.
DR DNASU; 19270; -.
DR GeneID; 19270; -.
DR KEGG; mmu:19270; -.
DR CTD; 5793; -.
DR MGI; MGI:97814; Ptprg.
DR eggNOG; KOG0382; Eukaryota.
DR eggNOG; KOG0789; Eukaryota.
DR InParanoid; Q05909; -.
DR OrthoDB; 251520at2759; -.
DR PhylomeDB; Q05909; -.
DR BioGRID-ORCS; 19270; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Ptprg; mouse.
DR EvolutionaryTrace; Q05909; -.
DR PRO; PR:Q05909; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q05909; protein.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0010633; P:negative regulation of epithelial cell migration; ISO:MGI.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISO:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:1901998; P:toxin transport; IMP:MGI.
DR CDD; cd03122; alpha_CARP_receptor_like; 1.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.10.200.10; -; 1.
DR Gene3D; 3.90.190.10; -; 2.
DR InterPro; IPR041887; Alpha_CARP_receptor-type.
DR InterPro; IPR001148; CA_dom.
DR InterPro; IPR036398; CA_dom_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
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; PF00194; Carb_anhydrase; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF51069; SSF51069; 1.
DR SUPFAM; SSF52799; SSF52799; 2.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
KW Phosphoprotein; Protein phosphatase; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..1442
FT /note="Receptor-type tyrosine-protein phosphatase gamma"
FT /id="PRO_0000025442"
FT TOPO_DOM 20..733
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 734..759
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 760..1442
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 58..321
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT DOMAIN 349..448
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 845..1116
FT /note="Tyrosine-protein phosphatase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT DOMAIN 1147..1407
FT /note="Tyrosine-protein phosphatase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 461..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1412..1442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..707
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1057
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 1025
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1057..1063
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1101
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 1348
FT /note="Ancestral active site"
FT MOD_RES 1179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23470"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 719
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 78..261
FT /evidence="ECO:0000269|PubMed:20133774"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:3JXG"
FT HELIX 68..73
FT /evidence="ECO:0007829|PDB:3JXG"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:3JXG"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:3JXG"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:3JXG"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:3JXG"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:3JXG"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:3JXG"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:3JXG"
FT STRAND 143..152
FT /evidence="ECO:0007829|PDB:3JXG"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:3JXG"
FT STRAND 171..179
FT /evidence="ECO:0007829|PDB:3JXG"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:3JXG"
FT HELIX 187..192
FT /evidence="ECO:0007829|PDB:3JXG"
FT STRAND 197..206
FT /evidence="ECO:0007829|PDB:3JXG"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:3JXG"
FT HELIX 215..222
FT /evidence="ECO:0007829|PDB:3JXG"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:3JXG"
FT HELIX 238..241
FT /evidence="ECO:0007829|PDB:3JXG"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:3JXG"
FT STRAND 265..272
FT /evidence="ECO:0007829|PDB:3JXG"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:3JXG"
FT HELIX 278..285
FT /evidence="ECO:0007829|PDB:3JXG"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:3JXG"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:3JXG"
SQ SEQUENCE 1442 AA; 161243 MW; 5887715568FBECD8 CRC64;
MRRLLEPCWW ILFLKITSSV LHYVVCFPAL TEGYVGTLQE SRQDSSVQIR RRKASGDPYW
AYSGAYGPEH WVTSSVSCGG SHQSPIDILD HHARVGDEYQ ELQLDGFDNE SSNKTWMKNT
GKTVAILLKD DYFVSGAGLP GRFKAEKVEF HWGHSNGSAG SEHSVNGRRF PVEMQIFFYN
PDDFDSFQTA ISENRIIGAM AIFFQVSPRD NSALDPIIHG LKGVVHHEKE TFLDPFILRD
LLPASLGSYY RYTGSLTTPP CSEIVEWIVF RRPVPISYHQ LEAFYSIFTT EQQDHVKSVE
YLRNNFRPQQ ALNDRVVSKS AVRDAWNHDL ADFLDNPLGT EASKVCSSPP IHMKVQPLNQ
TALQVSWSQP ETIYHPPIMN YMISYSWTKN EDEKEKTFTK DSDKDLKATI SHVSPDSLYL
FRVQAVCRND MRSDFSQTML FQANTTRIFQ GTRIVKTGVP TASPASSADM APISSGSSTW
TSSGIPFSFV SMATGMGPSS SGSQATVASV VTSTLLAGLG FGGGGISSFP STVWPTRLPT
ASAASKQAGR TVLATTEALA SPGPDVHSAP SKDSEGTEEG EKEEKSESED GEREHEEEEK
DSEKKEKSEA THTAAESDRT APAPTPSSPH RTAAEGGHQT IPGRRQDHSA PATDQPGHVA
PDLDPLVDTA TQVPPTATEE HYSGSDPRRP EMPSKKPMSR GDRFSEDSKF ITVNPAEKNT
SGMLSRPSPG RMEWIIPLIV VSALTFVCLV LLIAVLVYWR GCNKIKSKGF PRRSREVPSS
GERGEKGSRK CFQTAHFYVE DSSSPRVVPN ESVPIIPIPD DMEAIPVKQF GKHIGELYSN
SQHGFSEDFE EVQRCTADMN ITAEHSNHPD NKHKNRYINI LAYDHSRVKL RPLPGKDSKH
SDYINANYVD GYNKAKAYIA TQGPLKSTFE DFWRMIWEQN TGIIIMITNL VEKGRRKCDQ
YWPTENTEEY GNIIVTLKST KVHACYTVRR LSVRNTKVKK GQKGNPKGRQ NERTVIQYHY
TQWPDMGVPE YALPVLTFVR RSSAARMPDM GPVLVHCSAG VGRTGTYIVI DSMLQQIKDK
STVNVLGFLK HIRTQRNYLV QTEEQYIFIH DALLEAILGK ETAVSSSQLH SYVNSILIPG
VGGKTRLEKQ FKLITQCNAK YVECFSAQKE CNKEKNRNSS VVPAERARVG LAPLPGMKGT
DYINASYIMG YYRSNEFIIT QHPLPHTTKD FWRMIWDHNA QIIVMLPDNQ SLAEDEFVYW
PSREESMNCE AFTVTLISKD RLCLSNEEQI IIHDFILEAT QDDYVLEVRH FQCPKWPNPD
APISSTFELI NVIKEEALTR DGPTIVHDEY GAVSAGMLCA LTTLSQQLEN ENAVDVFQVA
KMINLMRPGV FTDIEQYQFV YKAMLSLIST KENGNGPMTG DKNGAVLTAE ESDPAESMES
LV
