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Database: UniProt
Entry: A0A1U8CN93_MESAU
LinkDB: A0A1U8CN93_MESAU
Original site: A0A1U8CN93_MESAU 
ID   A0A1U8CN93_MESAU        Unreviewed;      1920 AA.
AC   A0A1U8CN93;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 2.
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=Ptprs {ECO:0000313|RefSeq:XP_012976904.2};
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_012976904.2};
RN   [1] {ECO:0000313|RefSeq:XP_012976904.2}
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_012976904.2}
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_012976904.2; XM_013121450.2.
DR   STRING; 10036.ENSMAUP00000003264; -.
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; 7.
DR   CDD; cd05738; IgI_2_RPTP_IIa_LAR_like; 1.
DR   CDD; cd05739; IgI_3_RPTP_IIa_LAR_like; 1.
DR   CDD; cd14627; R-PTP-S-2; 1.
DR   CDD; cd14625; R-PTPc-S-1; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 11.
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; 6.
DR   Pfam; PF07679; I-set; 2.
DR   Pfam; PF13927; Ig_3; 1.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PRINTS; PR00014; FNTYPEIII.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 8.
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; 5.
DR   SUPFAM; SSF48726; Immunoglobulin; 3.
DR   PROSITE; PS50853; FN3; 7.
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_012976904.2};
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..1920
FT                   /note="protein-tyrosine-phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018300419"
FT   TRANSMEM        1271..1294
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..224
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          236..318
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          325..415
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          420..514
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          518..607
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          612..709
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          714..822
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          920..1021
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1024..1108
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1365..1620
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1540..1611
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          1652..1911
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1829..1902
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          695..715
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1299..1326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1920 AA;  213432 MW;  BFEAF6B684676DC1 CRC64;
     MAPTWNPSVV SVVGPVGLFL VLLARGCAAE EPPRFIKEPK DQIGVSGGVA SFVCQATGDP
     KPRVTWNKKG KKVNSQRFET IDFDESSGAV LRIQPLRTPR DENVYECVAQ NSVGEITVHA
     KLTVLREDQL PPGFPNIDMG PQLKVVERTR TATMLCAASG NPDPEITWFK DFLPVDPSAS
     NGRIKQLRSG ALQIESSEET DQGKYECVAT NSAGVRYSSP ANLYVRELRE VRRVAPRFSI
     LPMSHEIMPG GNVNITCVAV GSPMPYVKWM QGAEDLTPED DMPVGRNVLE LTDVKDSANY
     TCVAMSSLGV IEAVAQITVK SLPKAPGTPV VTENTATSIT VTWDSGNPDP VSYYVIEYKS
     KSQDGPYQIK EDITTTRYSI GGLSPNSEYE IWVSAVNSIG QGPPSESVVT RTGEQAPASA
     PRNVQARMLS ATTMIVQWEE PVEPNGLIRG YRVYYTMEPE HPVGNWQKHN VDDSLLTTVG
     SLLEDETYTV RVLAFTSVGD GPLSDPIQVK TQQGVPGQPM NLRAEAKSET SIGLSWSAPR
     QESVIKYELL FREGDRGREV GRTFDPTTAF VVEDLKPNTE YAFRLAARSP QGLGAFTAVV
     RQRTLQAKPS APPQDVKCTS LRSTAILVSW RPPPPETHNG ALVGYSVRYR PLGSEDPDPK
     EVNNIPPTTT QILLEALEKW TEYRVTAVAY TEVGPGPESS PVVVRTDEDV PSAPPRKVEA
     EALNATAIRV LWRSPTPGRQ HGQIRGYQVH YVRMEGAEAR GPPRIKDIML ADAQWEMDDT
     AEYEMVITNL QPETAYSITV AAYTMKGDGA RSKPKVVVTK GAVLGRPTLS VQQTPEGSLL
     ARWEPPADAA EDPVLGYRLQ FGREDAAPAT LELAAWERRF AAPAHKGATY VFRLAARGRA
     GLGEEAAAAL SIPEDAPRGF PQILGAAGNA SAGSVLLRWL PPVPAERNGA IVKYTVSVRE
     AGAPGPATET ELAAAAEPGA ETALTLQGLR PETAYELRVR AHTRRGPGPF SPPLRYRLAR
     DPVSPKNFKV KMIMKTSVLL SWEFPDNYNS PTPYKIQYNG LTLDVDGRTT KKLITHLKPH
     TFYNFVLTNR GSSLGGLQQT VTARTAFNML SGKPSVAPKP DNDGFIVVYL PDGQSPVTVQ
     NYFIVMVPLR KSRGGQFPVL LGSPEDMDLE ELIQDISRLQ RRSLRHSRQL EVPRPYIAAR
     FSILPAVFHP GNQKQYGGFD NRGLEPGHRY VLFVLAVLQK NEPTFAASPF SDPFQLDNPD
     PQPIVDGEEG LIWVIGPVLA VVFIVCIVIA ILLYKNKPDS KRKDSEPRTK CLLNNADLAP
     HHPKDPVEMR RINFQTPGML SHPPIPIADM AEHMERLKAN DSLKLSQEYE SIDPGQQFTW
     EHSNLEANKP KNRYANVIAY DHSRVILQPL EGIMGSDYIN ANYVDGYRRQ NAYIATQGPL
     PETFGDFWRM VWEQRSATVV MMTRLEEKSR IKCDQYWPNR GTETYGFIQV TLLDTMELAT
     FCVRTFSLHK NGSSEKREVR HFQFTAWPDH GVPEYPTPFL AFLRRVKTCN PPDAGPIVVH
     CSAGVGRTGC FIVIDAMLER IKTEKTVDVY GHVTLMRSQR NYMVQTEDQY SFIHEALLEA
     VGCGNTEVPA RSLYTYIQKL AQVEPGEHVT GMELEFKRLA SSKAHTSRFI TASLPCNKFK
     NRLVNILPYE SSRVCLQPIR GVEGSDYINA SFIDGYRQQK AYIATQGPLA ETTEDFWRAL
     WENNSTIVVM LTKLREMGRE KCHQYWPAER SARYQYFVVD PMAEYNMPQY ILREFKVTDA
     RDGQSRTVRQ FQFTDWPEQG APKSGEGFID FIGQVHKTKE QFGQDGPISV HCSAGVGRTG
     VFITLSIVLE RMRYEGVVDI FQTVKVLRTQ RPAMVQTEDE YQFCFQAALE YLGSFDHYAT
//
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