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Database: UniProt
Entry: A0A2K5XF46_MANLE
LinkDB: A0A2K5XF46_MANLE
Original site: A0A2K5XF46_MANLE 
ID   A0A2K5XF46_MANLE        Unreviewed;      1387 AA.
AC   A0A2K5XF46;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 38.
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:ENSMLEP00000001930.1};
OS   Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Mandrillus.
OX   NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000001930.1, ECO:0000313|Proteomes:UP000233140};
RN   [1] {ECO:0000313|Ensembl:ENSMLEP00000001930.1}
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   Ensembl; ENSMLET00000008446.1; ENSMLEP00000001930.1; ENSMLEG00000007529.1.
DR   GeneTree; ENSGT00940000155048; -.
DR   Proteomes; UP000233140; Unplaced.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
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:UP000233140};
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        708..733
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          29..292
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000259|PROSITE:PS51144"
FT   DOMAIN          320..419
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          790..1061
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          978..1052
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          1092..1352
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1269..1343
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          432..451
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          528..700
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        542..560
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        569..586
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        587..606
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        658..681
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1387 AA;  155134 MW;  D2E3B9BF6795D3A9 CRC64;
     LTEGYVGALH ENRHGSAVQI RRRKASGDPY WAYSGAYGPE HWVTSSVSCG GHHQSPVDIL
     DQHARVGEEY QELQLDGFDN ESSNKTWMKN TGKTVAILLK DDYFVSGAGL PGRFKAEKVE
     FHWGHSNGSA GSEHSIDGRR FPVEMQIFFY NPDDFDSFQT AISENRIIGA MAIFFQVSPR
     DNSALDPIIH GLKGVVHHEK ETFLDPFVLR DLLPASLGSY YRYTGSLTTP PCSEIVEWIV
     FRRPVPISYH QLEAFYSIFT TEQQDHVKSV EYLRNNFRPQ QRLHDRVVSK SAVRDAWNHD
     VTDFLENPLG TEASKVCSSP PIHMKVQPLN QTALQVSWSQ PETIYHPPIM NYMISYSWTK
     NEDEKEKTFT KDSDKDLKAT ISHVSPDSLY LFRVQAVCRN DMRSDFSQTM LFQANTTRIF
     QGTRIVKTGV PTASPASSAD MAPISSGSST WTSSGIPFSF VSMATGMGPS SSGSQATVAS
     VVTSTLLAGL GFGGGGISSF PSTVWPTRLP TAASASKQAA RPVLATTEAL ASPGPDGDSS
     PTKDSEGTEE GEKDEKSESE DGEREHEEDG EKDSEKKEKS GVTHAAEERN QTEPSPTPSS
     PNRTAEGGHH TIPGHEQDHT AIPTDQTGGR RDAGPGPDPD AVTSTQVPPT ATEEQYAGSD
     PKRPEMPSKK PVSRGDRFSE DSRFITVNPA EKNTSGMISR PAPGRMEWII PLIVVSALTF
     VCLILLIAVL VYWRKCFQTA HFYVEDSNSP RVVPNESIPI IPIPDDMEAI PVKQFVKHIG
     ELYSNNQHGF SEDFEEVQRC TADMNITAEH SNHPENKHKN RYINILAYDH SRVKLRPLPG
     KDSKHSDYIN ANYVDGYNKA KAYIATQGPL KSTFEDFWRM IWEQNTGIIV MITNLVEKGR
     RKCDQYWPTE NSEEYGNIIV TLKSTKVHAC YTVRRFSVRN TKVKKGQKGN PKGRQNERIV
     IQYHYTQWPD MGVPEYALPV LTFVRRSSAA RMPEMGPVLV 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
//
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