ID A0A452R2I1_URSAM Unreviewed; 1223 AA.
AC A0A452R2I1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 25.
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:ENSUAMP00000012387.1};
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:ENSUAMP00000012387.1, 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:ENSUAMP00000012387.1}
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}.
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 AlphaFoldDB; A0A452R2I1; -.
DR Ensembl; ENSUAMT00000013919.1; ENSUAMP00000012387.1; ENSUAMG00000009369.1.
DR GeneTree; ENSGT00940000155048; -.
DR Proteomes; UP000291022; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
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:SF468; 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|SAM:Phobius};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000291022};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {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 544..569
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..268
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 626..897
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 814..888
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 928..1188
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1105..1179
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 268..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1223 AA; 136939 MW; 387C25CD596289B3 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 MLFQGKPTAS PASSADMAPI SSGSSTWTSS GIPFSFVSMA
TGMGPSSSGS QATVASVVTS TLLAGLGFSG GGIPSFPSTV WPTRLPTAAS ASKQAVRPVL
ATTEALASPG PDGDSAPTKD SEGTEEGEKD EKSESEDGER EHEDEGEKDS EKKKSGVTHA
AQEPRQDEPT PTPSSPNRTA EEGGHQTLPG PGQDRTAVPT DRPDDARDAR PGLDSGSVTS
TQVPPTVTEE RFEGSDPRRP QMPSKKPVSR GDRFSEDSKF ITVNPAEKNT SGMISRPSPG
RMEWIIPLIV VSALTFVCLI LLIAVLVYWR KCFQTAHFYV EDSSSPRVVP NESIPIIPIP
DDMEAIPVKQ FVKHIGELYS NNQHGFSEDF EEVQRCTADM NITAEHSNHP DNKHKNRYIN
ILAYDHSRVK LRPLPGKDSK HSDYINANYV DGYNKAKAYI ATQGPLKSTF EDFWRMIWEQ
NTGIIIMITN LVEKGRRKCD QYWPTENSEE YGNIIVTLKS TKVHACYTVR RFSVRNTKVK
KGQKGNPKGR QNERVVIQYH YTQWPDMGVP EYALPVLTFV RRSSAARTPE MGPVLVHCSA
GVGRTGTYIV IDSMLQQIKD KSTVNVLGFL KHIRTQRNYL VQTEEQYIFI HDALLEAILG
KETEVSSNQL HSYVNSILIP GVGGKTRLEK QFKLVTQCNA KYVECFSAQK ECNKEKNRNS
SVVPSERARV GLAPLPGMKG TDYINASYIM GYYRSNEFII TQHPLPHTTK DFWRMIWDHN
AQIIVMLPDN QSLAEDEFVY WPSREESMNC EAFTVTLISK DRLCLSNEEQ IIIHDFILEA
TQDDYVLEVR HFQCPKWPNP DAPISSTFEL INVIKEEALT RDGPTIVHDE YGAVSAGMLC
ALTTLSQQLE NENAVDVFQV AKMINLMRPG VFTDIEQYQF VYKAMLSLVS TKENGNGPMT
VDKNGAVLIA DESDPAESME SLV
//