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Database: UniProt
Entry: A0A452R2I1_URSAM
LinkDB: A0A452R2I1_URSAM
Original site: A0A452R2I1_URSAM 
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}.
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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
//
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