ID A0A452R280_URSAM Unreviewed; 1267 AA.
AC A0A452R280;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN Name=PTPRG {ECO:0000313|Ensembl:ENSUAMP00000012377.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000012377.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000012377.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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|ARBA:ARBA00001490};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 5 subfamily. {ECO:0000256|ARBA:ARBA00006246}.
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DR AlphaFoldDB; A0A452R280; -.
DR STRING; 9643.ENSUAMP00000012377; -.
DR Ensembl; ENSUAMT00000013909.1; ENSUAMP00000012377.1; ENSUAMG00000009369.1.
DR GeneTree; ENSGT00940000155048; -.
DR Proteomes; UP000291022; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0010633; P:negative regulation of epithelial cell migration; IEA:Ensembl.
DR CDD; cd00063; FN3; 1.
DR CDD; cd17670; R-PTP-G-2; 1.
DR CDD; cd17667; R-PTPc-G-1; 1.
DR Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
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 PANTHER; PTHR19134; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR19134:SF449; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE GAMMA; 1.
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; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR SUPFAM; SSF51069; Carbonic anhydrase; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
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 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000291022};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 559..584
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..143
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000259|PROSITE:PS51144"
FT DOMAIN 171..270
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 670..941
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 858..932
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 972..1232
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1149..1223
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 283..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1267 AA; 141830 MW; 1F52D9CC402B7B35 CRC64;
MCEVWVLSES KLGAATQWMI CEGGGEGIFN QSCFLYIIIV PFFSFFLHTE KETFLDPFVL
RDLLPASLGS YYRYTGSLTT PPCSEIVEWI VFRRPVPISY HQLEAFYSIF TTEQQDHVKS
VEYLRNNFRP QQGLNGRVVS KSAVRDAWNH DMTDFLENPL GTEASKVCSS PPIHMKVQPL
NQTALQVSWS QPETIYHPPI MNYMISYSWT KNEDEKEKTF TKDSDKDLKA TISHVSPDSL
YLFRVQAVCR NDMRSDFSQT MLFQANTTRI FQGTRIVKTG VPTASPASSA DMAPISSGSS
TWTSSGIPFS FVSMATGMGP SSSGSQATVA SVVTSTLLAG LGFSGGGIPS FPSTVWPTRL
PTAASASKQA VRPVLATTEA LASPGPDGDS APTKDSEGTE EGEKDEKSES EDGEREHEDE
GEKDSEKKKS GVTHAAQEPR QDEPTPTPSS PNRTAEEGGH QTLPGPGQDR TAVPTDRPDD
ARDARPGLDS GSVTSTQVPP TVTEERFEGS DPRRPQMPSK KPVSRGDRFS EDSKFITVNP
AEKNTSGMIS RPSPGRMEWI IPLIVVSALT FVCLILLIAV LVYWRGCNKI KSKGFPRRFR
EVPSSGERGE KGSRKCFQTA HFYVEDSSSP RVVPNESIPI IPIPDDMEAI PVKQFVKHIG
ELYSNNQHGF SEDFEEVQRC TADMNITAEH SNHPDNKHKN RYINILAYDH SRVKLRPLPG
KDSKHSDYIN ANYVDGYNKA KAYIATQGPL KSTFEDFWRM IWEQNTGIII MITNLVEKGR
RKCDQYWPTE NSEEYGNIIV TLKSTKVHAC YTVRRFSVRN TKVKKGQKGN PKGRQNERVV
IQYHYTQWPD MGVPEYALPV LTFVRRSSAA RTPEMGPVLV HCSAGVGRTG TYIVIDSMLQ
QIKDKSTVNV LGFLKHIRTQ RNYLVQTEEQ YIFIHDALLE AILGKETEVS SNQLHSYVNS
ILIPGVGGKT RLEKQFKLVT QCNAKYVECF SAQKECNKEK NRNSSVVPSE RARVGLAPLP
GMKGTDYINA SYIMGYYRSN EFIITQHPLP HTTKDFWRMI WDHNAQIIVM LPDNQSLAED
EFVYWPSREE SMNCEAFTVT LISKDRLCLS NEEQIIIHDF ILEATQDDYV LEVRHFQCPK
WPNPDAPISS TFELINVIKE EALTRDGPTI VHDEYGAVSA GMLCALTTLS QQLENENAVD
VFQVAKMINL MRPGVFTDIE QYQFVYKAML SLVSTKENGN GPMTVDKNGA VLIADESDPA
ESMESLV
//
