ID H2PAD6_PONAB Unreviewed; 1445 AA.
AC H2PAD6; A0A2J8TEK5;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 80.
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:ENSPPYP00000015384.3};
GN ORFNames=CR201_G0035576 {ECO:0000313|EMBL:PNJ31436.1};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000015384.3, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000015384.3, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PNJ31436.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Susie {ECO:0000313|EMBL:PNJ31436.1};
RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT "High-resolution comparative analysis of great ape genomes.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPPYP00000015384.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 EMBL; NDHI03003502; PNJ31436.1; -; Genomic_DNA.
DR STRING; 9601.ENSPPYP00000015384; -.
DR Ensembl; ENSPPYT00000015997.3; ENSPPYP00000015384.3; ENSPPYG00000013752.3.
DR eggNOG; KOG0382; Eukaryota.
DR eggNOG; KOG0789; Eukaryota.
DR GeneTree; ENSGT00940000155048; -.
DR HOGENOM; CLU_001120_0_0_1; -.
DR OMA; DRFPEEH; -.
DR OrthoDB; 2903434at2759; -.
DR TreeFam; TF351978; -.
DR Proteomes; UP000001595; Chromosome 3.
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; cd03122; alpha_CARP_receptor_like; 1.
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; 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 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:UP000001595};
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 737..762
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 58..321
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000259|PROSITE:PS51144"
FT DOMAIN 349..448
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 848..1119
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1036..1110
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1150..1410
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1327..1401
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 461..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..727
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 598..615
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1445 AA; 161881 MW; 3881509548EC614F CRC64;
MRRLLEPCWW ILFVKITSSV LHYVVCFPAL TEGYVGALHE NRHGSTVQIR RRKASGDPYW
AYSGAYGPEH WVTSSVSCGG HHQSPVDILD QYARVGEEYQ ELQLDGFDNE SSNKTWMKNT
GKTVAILLKD DYFVSGAGLP GRFKAEKVEF HWGHSNGSAG SEHSINGRRF PVEMQIFFYN
PDDFDSFQTA ISENRIIGAM AIFFQVSPRD NSALDPIIHG LKGVVHHEKE TFLDPFVLRD
LLPASLGSYY RYTGSLTTPP CSEVVEWIVF RRPVPISYHQ LEAFYSIFTT EQQDHVKSVE
YLRNNFRPQQ DLHDRVVSKS AVRDAWNHDM TDFLENPLGT EASKVCSSPP IHMKVQPLNQ
TALQVSWSQP ETIYHPPIMN YMISYSWTKN EDEKEKTFTK DSDKDLKATI SHVSPDSLYL
FRVQAVCRND MRSDFSQTML FQANTTRIFQ GTRIVKTGVP TASPASSADM APISSGSSTW
TSSGIPFSFV SMATGMGPSS SGSQATVASV VTSTLLAGLG FGGGGISSFP STVWPTRLPT
AASASKQAAR PVLATTEALA SPGPDGDSSP TKDSEGTEEG EKDEKSESED GEREHEEDGE
KDSEKKEKSG VTHAAKERNQ TEPSPTPSSP NRTAEGGHQT IPGHEQDHTA VPTDQTGGRR
DAGPGPDPDM VTSTQVPPTA TEEQYAGSDP KRPEMPSKKP VSHGDRFSED SRFITVNPAE
KNTSGMISRP APGRMEWIIP LIVVSALTFV CLILLIAVLV YWRGCNKIKS KGFPRRFREV
PSSGERGEKG SRKCFQTAHF YVEDSSSPRV VPNESIPIIP IPDDMEAIPV KQFVKHISEL
YSNNQHGFSE DFEEVQRCTA DMNITAEHSN HPENKHKNRY INILAYDHSR VKLRPLPGKD
SKHSDYINAN YVDGYNKAKA YIATQGPLKS TFEDFWRMIW EQNTGIIVMI TNLVEKGRRK
CDQYWPTENS EEYGNVIVTL KSTKVHACYT VRRFSVRNTK VKKGQKGNPK GRQNERVVIQ
YHYTQWPDMG VPEYALPVLT FVRRSSAARM PEMGPVLVHC SAGVGRTGTY IVIDSMLQQI
KDKSTVNVLG FLKHIRTQRN YLVQTEEQYI FIHDALLEAI LGKETEVSSN QLHSYVNSIL
IPGVGGKTRL EKQFKLVTQC NAKYVECFSA QKECNKEKNR NSSVVPSERA RVGLAPLPGM
KGTDYINASY IMGYYRSNEF IITQHPLPHT TKDFWRMIWD HNAQIIVMLP DNQSLAEDEF
VYWPSREESM NCEAFTVTLI SKDRLCLSNE EQIIIHDFIL EATQDDYVLE VRHFQCPKWP
NPDAPISSTF ELINVIKEEA LTRDGPTIVH DEYGAVSAGM LCALTTLSQQ LENENAVDVF
QVAKMINLMR PGVFTDIEQY QFVYKAMLSL VSTKENGNGP MTVDKNGAVL IADESDPAES
MESLV
//
