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Database: UniProt
Entry: A0A1S3G0M7_DIPOR
LinkDB: A0A1S3G0M7_DIPOR
Original site: A0A1S3G0M7_DIPOR 
ID   A0A1S3G0M7_DIPOR        Unreviewed;      1487 AA.
AC   A0A1S3G0M7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 36.
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|RefSeq:XP_012881854.1};
OS   Dipodomys ordii (Ord's kangaroo rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC   Dipodomyinae; Dipodomys.
OX   NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012881854.1};
RN   [1] {ECO:0000313|RefSeq:XP_012881854.1}
RP   IDENTIFICATION.
RC   TISSUE=Kidney {ECO:0000313|RefSeq:XP_012881854.1};
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_012881854.1; XM_013026400.1.
DR   GeneID; 105993216; -.
DR   CTD; 5789; -.
DR   OrthoDB; 2875525at2759; -.
DR   Proteomes; UP000081671; 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   GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt.
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   CDD; cd14628; R-PTP-D-2; 1.
DR   CDD; cd14624; R-PTPc-D-1; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 7.
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; IPR045905; R-PTP-delta_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; 2.
DR   Pfam; PF13927; Ig_3; 1.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 4.
DR   SMART; SM00409; IG; 4.
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; 3.
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_012881854.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000081671};
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..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..1487
FT                   /note="protein-tyrosine-phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010200739"
FT   TRANSMEM        842..865
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          24..114
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          126..215
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          223..305
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          312..402
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          407..503
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          505..594
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          932..1187
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1107..1178
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          1219..1478
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1396..1469
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          874..893
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1487 AA;  167560 MW;  805E12F5F1068606 CRC64;
     MVHITRPLLL LLAFFLRVDA ETPPRFTRTP VDQTGVSGGV ASFICQATGD PRPKIVWNKK
     GKKVSNQRFE VIEFDDGSGS VLRIQPLRTP RDEAIYECVA SNNVGEISVS TRLTVLREDQ
     IPRGFPTIDM GPQLKVVERT RTATMLCAAS GNPDPEITWF KDFLPVDTSN NNGRIKQLRS
     GALQIEQSEE SDQGKYECVA TNSAGTRYSA PANLYVRVRR VPPRFSIPPT NHEIMPGGSV
     NITCVAVGSP MPYVKWMLGA EDLTPEDDMP IGRNVLELND VRQSANYTCV AMSTLGVIEA
     IAQITVKALP KPPGTPVVTE STATSITLTW DSGNPEPVSY YIIQHKPKNS EEPYKEIDGV
     ATTRYSVAGL SPYSDYEFRV VAVNNIGRGP PSEPVLTQTS EQAPSSAPRD VQARMLSSTT
     ILVQWKEPEE PNGQIQGYRV YYTMDPTQHV NNWMKHNVAD SQITTIGNLV PQKTYSVKVL
     AFTSIGDGPL SSDIQVITQT GVPGQPLNFK AEPESETSIL LSWTPPRSDT IASYELVYKD
     GELGEEQRVT IEPGTSYRLQ GLKPNSLYYF RLAARSPQGL GASTTEISAR TMQSMFAKNF
     HVKAVMKTSV LLSWEIPENY NSAMPFKILY DDGKMVEEVD GRATQKLIVN LKPEKSYSFV
     LTNRGNSAGG LQHRVTAKTA PDVLRTKPAF IGKTNLDGMI TVQLPEVPAN ENIKGYYIII
     VPLKKSRGKF IKPWESPDEM ELDELLKEIS RKRRSIRYGR EVELKPYIAA HFDVLPTEFT
     LGDDKHYGGF TNKQLQSGQE YVFFVLAVME HAESMYATSP YSDPVVSMDL DPQPITDEEE
     GLIWVVGPVL AVVFIICIVI AILLYKRKRA ESESRKSSIP NSKEVPSHHP TDPVELRRLN
     FQTPGMASHP PIPILELADH IERLKANDNL KFSQEYESID PGQQFTWEHS NLEVNKPKNR
     YANVIAYDHS RVLLSAIEGI PGSDYVNANY IDGYRKQNAY IATQGSLPET FGDFWRMIWE
     QRSATIVMMT KLEERSRVKC DQYWPSRGTE THGLVQVTLL DTVELATYCV RTFALYKNGS
     SEKREVRQFQ FTAWPDHGVP EHPTPFLAFL RRVKTCNPPD AGPMVVHCSA GVGRTGCFIV
     IDAMLERIKH EKTVDIYGHV TLMRAQRNYM VQTEDQYIFI HDALLEAVTC GNTEVPARNL
     YAYIQKLTQI ETGENVTGME LEFKRLASSK AHTSRFISAN LPCNKFKNRL VNIMPYESTR
     VCLQPIRGVE GSDYINASFI DGYRQQKAYI ATQGPLAETT EDFWRMLWEH NSTIVVMLTK
     LREMGREKCH QYWPAERSAR YQYFVVDPMA EYNMPQYILR EFKVTDARDG QSRTVRQFQF
     TDWPEQGVPK SGEGFIDFIG QVHKTKEQFG QDGPISVHCS AGVGRTGVFI TLSIVLERMR
     YEGVVDIFQT VKMLRTQRPA MVQTEDQYQF CYRAALEYLG SFDHYAT
//
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