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Database: UniProt
Entry: A0A2K6LI56_RHIBE
LinkDB: A0A2K6LI56_RHIBE
Original site: A0A2K6LI56_RHIBE 
ID   A0A2K6LI56_RHIBE        Unreviewed;      1308 AA.
AC   A0A2K6LI56;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   Name=PTPRD {ECO:0000313|Ensembl:ENSRBIP00000023208.1};
OS   Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000023208.1, ECO:0000313|Proteomes:UP000233180};
RN   [1] {ECO:0000313|Ensembl:ENSRBIP00000023208.1, ECO:0000313|Proteomes:UP000233180}
RP   NUCLEOTIDE SEQUENCE.
RA   Wu, C.-I. and Zhang, Y.;
RT   "Genome of Rhinopithecus bieti.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSRBIP00000023208.1}
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   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class 2A subfamily. {ECO:0000256|ARBA:ARBA00010504}.
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DR   Ensembl; ENSRBIT00000047101.1; ENSRBIP00000023208.1; ENSRBIG00000035517.1.
DR   GeneTree; ENSGT00940000153617; -.
DR   Proteomes; UP000233180; 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   CDD; cd00063; FN3; 4.
DR   CDD; cd05738; IgI_2_RPTP_IIa_LAR_like; 1.
DR   CDD; cd05739; IgI_3_RPTP_IIa_LAR_like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 6.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 3.
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; 3.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF13927; Ig_3; 1.
DR   Pfam; PF00102; Y_phosphatase; 3.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 4.
DR   SMART; SM00409; IG; 3.
DR   SMART; SM00408; IGc2; 2.
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; 2.
DR   PROSITE; PS50853; FN3; 3.
DR   PROSITE; PS50835; IG_LIKE; 2.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000233180};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
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        785..808
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          68..157
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          165..247
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          254..344
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          349..445
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          447..536
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          889..1299
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1217..1290
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          816..862
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        845..862
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1308 AA;  147409 MW;  9DC8C34AC0D75148 CRC64;
     MFERIWKRFT KKVTLAAWLP RGIEYPADMI CLGSGENFNV GGRKISYERV RFRRPHLPLE
     DQIPRGFPTI DMGPQLKVVE RTRTATMLCA ASGNPDPEIT WFKDFLPVDT SNNNGRIKQL
     RSGALQIEQS EESDQGKYEC VATNSAGTRY SAPANLYVRV RRVPPRFSIP PTNHEIMPGG
     SVNITCVAVG SPMPYVKWML GAEDLTPEDD MPIGRNVLEL NDVRQSANYT CVAMSTLGVI
     EAIAQITVKA LPKPPGTPVV TESTATSITL TWDSGNPEPV SYYIIQHKPK NSEEPYKEID
     GVATTRYSVA GLSPYSDYEF RVVAVNNIGR GPPSEPVLTQ TSEQAPSSAP RDVQARMLSS
     TTILVQWKEP EEPNGQIQGY RVYYTMDPTQ HVNNWMKHNV ADSQITTIGN LVPQKTYSVK
     VLAFTSIGDG PLSGDIQVIT QTGVPGQPLN FKAEPESETS ILLSWTPPRS DTIANYELVY
     KDGEHGEEQR ITIEPGTSYR LQGLKPNSLY YFRLAARSPQ GLGASTAEIS ARTMQSMFAK
     NFHVKAVMKT SVLLSWEIPE NYNSAMPFKI LYDDGKMVEE VDGRATQKLI VNLKPEKSYS
     FVLTNRGNSA GGLQHRVTAK TAPDVLRTKP AFIGKTNLDG MITVQLPEVP ANENIKGYYI
     IIVPLKKSRG KFIKPWESPD EMELDELLKE ISRKRRSIRY GREVELKPYI AAHFDVLPTE
     FTLGDDKHYG GFTNKQLQSG QEYVFFVLAV MEHAESKMYA TSPYSDPVVS MDLDPQPITD
     EEEGLIWVVG PVLAVVFIIC IVIAILLYKR KRAESDSRKS SIPNSKEIPS HHPTDPVELR
     RLNFQTPGSD DSGYPGNLHS SSMASHPPIP ILELADHIER LKANDNLKFS QEYESIDPGQ
     QFTWEHSNLE VNKPKNRYAN VIAYDHSRVL LSAIEGIPGS DYVNANYIDG YRKQNAYIAT
     QGSLPETFGD FWRMIWEQRS ATVVMMTKLE ERSRVKCDQY WPSRGTETHG LVQVTLLDTV
     ELATYCVRTF ALYKNGSSEK REVRQFQFTA WPDHGVPEHP TPFLAFLRRV KTCNPPDAGP
     MVVHCSSKAH TSRFISANLP CNQFKNRLVN IMPYESTRVC LQPIRVVGGS DYINACFVDA
     LIFTCALEKC HQYWPAERSA RYQYFVVDPM AEYNMPQYIL RKFKVTDARD GQSRTVRRFQ
     FTHWPEQGVA KSGEGFIDFI GQVHKTKQQF GQDGPISVHC SMGVGRTGVF ITLSIVLERM
     RYEGVVDIFQ TVKMLRTQRP AMVQTEDQYQ FCYRAALEYL GSFDHYAT
//
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