ID A0A3Q0DCF9_MESAU Unreviewed; 1629 AA.
AC A0A3Q0DCF9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-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=Ptprf {ECO:0000313|RefSeq:XP_021090792.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_021090792.1};
RN [1] {ECO:0000313|RefSeq:XP_021090792.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=28071753;
RA McCann K.E., Sinkiewicz D.M., Norvelle A., Huhman K.L.;
RT "De novo assembly, annotation, and characterization of the whole brain
RT transcriptome of male and female Syrian hamsters.";
RL Sci. Rep. 7:40472-40472(2017).
RN [2] {ECO:0000313|RefSeq:XP_021090792.1}
RP IDENTIFICATION.
RG RefSeq;
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 -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 2A subfamily. {ECO:0000256|ARBA:ARBA00010504}.
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DR RefSeq; XP_021090792.1; XM_021235133.1.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt.
DR CDD; cd00063; FN3; 5.
DR CDD; cd05738; IgI_2_RPTP_IIa_LAR_like; 1.
DR CDD; cd05739; IgI_3_RPTP_IIa_LAR_like; 1.
DR CDD; cd14629; R-PTP-F-2; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 8.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
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; PTHR46957; CYTOKINE RECEPTOR; 1.
DR PANTHER; PTHR46957:SF8; PROTEIN TYROSINE PHOSPHATASE RECEPTOR TYPE S; 1.
DR Pfam; PF00041; fn3; 4.
DR Pfam; PF07679; I-set; 3.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 5.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR SUPFAM; SSF49265; Fibronectin type III; 3.
DR SUPFAM; SSF48726; Immunoglobulin; 3.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Receptor {ECO:0000256|ARBA:ARBA00023170,
KW ECO:0000313|RefSeq:XP_021090792.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1629
FT /note="protein-tyrosine-phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018098699"
FT TRANSMEM 972..995
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 33..123
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 135..230
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 238..320
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 327..417
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 422..516
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 520..610
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 615..723
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1074..1329
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1249..1320
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1361..1620
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1538..1611
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
SQ SEQUENCE 1629 AA; 181592 MW; 32D3F2E8E977EFA0 CRC64;
MAPEPTPGRM MVPLVPALVM LGLMAGAHGD SKPVFVKVPE DQTGLSGGVA SFVCQATGEP
KPRITWMKKG KKVSSQRFEV IEFDDGAGSV LRIQPLRVQR DEAIYECTAT NSLGEINTSA
KLSVLEEDQL PSGFPTIDMG PQLKVVEKAR TATMLCAAGG TPDPEISWFK DFLPVDPTLS
NGRIKQLRSG GSPIRGALQI ESSEESDQGK YECVATNSAG TRYSAPANLY VRVRRVAPRF
SIPPSSQEVM PGGSVNLTCV AVGAPMPYVK WMMGAEELTK EDEMPVGRNV LELSNVMRSA
NYTCVAISSL GMIEATAQVT VKALPKPPID LVVTETTATS VTLTWDSGNA EPVSYYGIQY
RAAGTDGPFQ EVDGVATTRY SIGGLSPFSE YAFRVLAVNS IGRGPPSEAV RARTGEQAPS
SPPRRVQARM LSASTMLVQW EPPEEPNGLV RGYRVYYTPD SRRPLSAWHK HNTDAGLLTT
VGSLLPGITY SLRVLAFTAV GDGPPSPTIQ VKTQQGVPAQ PADFQAEAES DTRIQLSWLL
PPQERITKYE LVYWAAEDEG QQHKVTFDPT SSYTLEDLKP DTVYHFQLAA RSDLGVGVFT
PTIEARTAQS MPSGPPRKVE VEPLNSTAVH VSWKLPVPNK QHGQIRGYQV TYVRLENGEP
RGQPIIQDVM LAEAQWRPEE SEDYETTISG LTPETTYSIT VAAYTTKGDG ARSKPKVVTT
AGAVFAKNFR VAAAMKTSVL LSWEVPDSYK SAVPFKILYN GQSVEVDGHS MRKLIADLQP
NTEYSFVLMN RGSSAGGLQH LVSIRTAPDL LPNKPLPASA FIEDGRFSLS MPQVQEPSLV
RWFYIVVVPI DRVGGNLLTP RWNTPEELEL DELLEAIEQG GEERRRRRRQ AERLKPYVAA
QVDVLPDTFT LGDKKNYRGF YNRPLSPDLS YQCFVLASLK EPMDQKRYAS SPYSDEIVVQ
VTPAQQQEEP EMLWVTGPVL AVILIILIVI AILLFKRKRT HSPSSKDEQS IGLKDSLLAH
SSDPVEMRRL NYQTPGSSAP SCPNISSMRD HPPIPITDLA DNIERLKAND GLKFSQEYES
IDPGQQFTWE NSNSEVNKPK NRYANVIAYD HSRVLLTSID GVPGSDYINA NYIDGYRKQN
AYIATQGPLP ETMGDFWRMV WEQRTATVVM MTRLEEKSRV KCDQYWPARG TETYGLIQVT
LVDTVELATY TMRTFALHKS GSSEKRELRQ FQFMAWPDHG VPEYPTPILA FLRRVKACNP
LDAGPMVVHC SAGVGRTGCF IVIDAMLERM KHEKTVDIYG HVTCMRSQRN YMVQTEDQYV
FIHEALLEAA MCGHTEVPAR NLYAHIQKLG QVPPGESVTA MELEFKLLAN SKAHTSRFIS
ANLPCNKFKN RLVNIMPYEL TRVCLQPIRG VEGSDYINAS FLDGYRQQKA YIATQGPLAE
STEDFWRMLW EHNSTIIVML TKLREMGREK CHQYWPAERS ARYQYFVVDP MAEYNMPQYI
LREFKVTDAR DGQSRTIRQF QFTDWPEQGV PKTGEGFIDF IGQVHKTKEQ FGQDGPITVH
CSAGVGRTGV FITLSIALER MRYEGVVDMF QTVKTLRTQR PAMVQTEDQY QLCYRAALEY
LGSFDHYAT
//
