ID A0A287CYH6_ICTTR Unreviewed; 1903 AA.
AC A0A287CYH6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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:ENSSTOP00000026390.1};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000026390.1, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000026390.1}
RP IDENTIFICATION.
RG Ensembl;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AGTP01051356; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01051357; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01051358; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01051359; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01051360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01051361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01051362; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01051363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01051364; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01051365; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSSTOT00000033467.1; ENSSTOP00000026390.1; ENSSTOG00000002347.3.
DR GeneTree; ENSGT00940000153617; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
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; 8.
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; 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; 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; 7.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF13927; Ig_3; 2.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00014; FNTYPEIII.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 8.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000005215};
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..1903
FT /note="protein-tyrosine-phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013375668"
FT TRANSMEM 1258..1281
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..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..516
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..813
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 814..907
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 912..1007
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1348..1603
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1523..1594
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1635..1894
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1812..1885
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 606..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1290..1309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1903 AA; 213468 MW; 8EA76349A2FA4307 CRC64;
MVHVARPLLL LLAFFLRADA ETPPRFTRTP VDQTGVSGGV ASFICQATGD PRPKIVWNKK
GKKVSNQRFE VIEFDDGSGS VLRIQPLRTP RDEAVYECVA SNKVDEIIVS TRLTVLREDQ
IPRGFPTIDM GPQLKVVERT RTATMLCAAS GNPDPEITWF KDFLPVDTSN NNGRIKQLRS
ESIGGTPIRG ALQIEQSEES DQGKYECVAT NSAGTRYSAP ANLYVRELRE VRRVPPRFSI
PPTNHEIMPG GSVNITCVAV GSPMPYVKWM LGAEDLTPED DMPIGRNVLE LNDVRQSANY
TCVAMSTLGV IEAIAQITVK ALPKPPGTPV VTESTATSIT LTWDSGNPEP VSYYIIQHKP
KNSEEPYKEI DGVATTRYSV AGLSPYSDYE FRVVAVNNIG RGPPSEPVLT QTSEQAPSSA
PRDVQARMLS STTILVQWKE PEEPNGQIQG YRVYYTMDPT QHVNNWMKHN VADSQITTIG
NLVPQKTYSV KVLAFTSIGD GPLSSDIQVI TQTGVPGQPL NFKAEPESET SILLSWTPPR
SDTIASYELV YKDGEHGEEQ RITIEPGTSY RLQGLRPNSL YYFRLSARSP QGLGASTAEI
SARTMQSKPS APPQDISCTS PSSTSILVSW QPPPVEKQNG IITEYSIKYT AVDGEDDKPH
EVLGIPSDTT KYLLEQLEKW TEYRITVTAH TDVGPGPESL SVLIRTDEDV PSGPPRKVEV
EAVNSTSVKV SWRSPVPNKQ HGQIRGYQVH YVRMENGEPK GQPMLKDVML ADAQDMIISG
LQPETSYSLT VTAYTTKGDG ARSKPKLVST TGAVPGKPRL VINHTQMNTA LIQWHPPVDT
FGPLQGYRLK FGRKDMEPLT TLEFSEKEDH FTATDIHKGA SYIFRLSARN KVGFGEEMVK
EISVPEEAPT GFPQNLHSEG TTSTSVQLSW QPPVLAERNG IITKYTVLCR DINIPLLPME
QLIVPADTSM TLTGLKPDTT YDVKVRAHTS KGPGPYSPSV QFRTLPVDQV FAKNFHVKAV
MKTSVLLSWE IPENYNSAMP FKILYDDGKM VEEVDGRATQ KLIVNLKPEK SYSFVLTNRG
NSAGGLQHRV TAKTAPDVLR TKPAFIGKTN LDGMITVQLP EVPANENIKG YYIIIVPLKK
SRGKFIKPWE SPDEMELDEL LKEISRKRRS IRYGREVELK PYIAAHFDVL PTEFTLGDDK
HYGGFTNKQL QSGQEYVFFV LAVMEHAESK MYATSPYSDP VVSMDLDPQP ITDEEEGLIW
VVGPVLAVVF IICIVIAILL YKRKRAESES RKSSIPNSKE VPSHHPTDPV ELRRLNFQTP
GMASHPPIPI LELADHIERL KANDNLKFSQ EYESIDPGQQ FTWEHSNLEV NKPKNRYANV
IAYDHSRVLL SAIEGIPGSD YVNANYIDGY RKQNAYIATQ GSLPETFGDF WRMIWEQRSA
TVVMMTKLEE RSRVKCDQYW PSRGTETHGL VQVTLLDTVE LATYCVRTFA LYKNGSSEKR
EVRQFQFTAW PDHGVPEHPT PFLAFLRRVK TCNPPDAGPM VVHCSAGVGR TGCFIVIDAM
LERIKHEKTV DIYGHVTLMR AQRNYMVQTE DQYIFIHDAL LEAVTCGNTE VPARNLYAYI
QKLTQIETGE NVTGMELEFK RLASSKAHTS RFISANLPCN KFKNRLVNIM PYESTRVCLQ
PIRGVEGSDY INASFIDGYR QQKAYIATQG PLAETTEDFW RMLWEHNSTI VVMLTKLREM
GREKCHQYWP AERSARYQYF VVDPMAEYNM PQYILREFKV TDARDGQSRT VRQFQFTDWP
EQGVPKSGEG FIDFIGQVHK TKEQFGQDGP ISVHCSAGVG RTGVFITLSI VLERMRYEGV
VDIFQTVKML RTQRPAMVQT EDQYQFCYRA ALEYLGSFDH YAT
//