ID A0A075B6H0_HUMAN Unreviewed; 1460 AA.
AC A0A075B6H0;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN Name=PTPRT {ECO:0000313|Ensembl:ENSP00000362294.4};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000362294.4, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000362294.4, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [2] {ECO:0000313|Ensembl:ENSP00000362294.4}
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 2B subfamily. {ECO:0000256|ARBA:ARBA00006396}.
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DR EMBL; AL022239; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL024473; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL035459; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL049812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL109826; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF456906; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF456910; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z93942; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_573400.3; NM_133170.3.
DR SMR; A0A075B6H0; -.
DR MassIVE; A0A075B6H0; -.
DR PeptideAtlas; A0A075B6H0; -.
DR Antibodypedia; 2780; 120 antibodies from 32 providers.
DR DNASU; 11122; -.
DR Ensembl; ENST00000373198.8; ENSP00000362294.4; ENSG00000196090.14.
DR GeneID; 11122; -.
DR UCSC; uc010ggj.4; human.
DR CTD; 11122; -.
DR HGNC; HGNC:9682; PTPRT.
DR VEuPathDB; HostDB:ENSG00000196090; -.
DR GeneTree; ENSGT00940000155326; -.
DR OMA; XPMQETV; -.
DR OrthoDB; 2875525at2759; -.
DR BioGRID-ORCS; 11122; 17 hits in 1162 CRISPR screens.
DR ChiTaRS; PTPRT; human.
DR GenomeRNAi; 11122; -.
DR Proteomes; UP000005640; Chromosome 20.
DR Bgee; ENSG00000196090; Expressed in Brodmann (1909) area 10 and 95 other cell types or tissues.
DR ExpressionAtlas; A0A075B6H0; baseline and differential.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProt.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd00063; FN3; 3.
DR CDD; cd06263; MAM; 1.
DR CDD; cd14630; R-PTPc-T-1; 1.
DR CDD; cd14634; R-PTPc-T-2; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
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; IPR000998; MAM_dom.
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; PTHR24051:SF8; PROTEIN-TYROSINE-PHOSPHATASE; 1.
DR PANTHER; PTHR24051; SUSHI DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF00629; MAM; 1.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00020; MAMDOMAIN.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00137; MAM; 1.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00740; MAM_1; 1.
DR PROSITE; PS50060; MAM_2; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE 1: Evidence at protein level;
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};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A075B6H0,
KW ECO:0007829|ProteomicsDB:A0A075B6H0};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1460
FT /note="protein-tyrosine-phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001705160"
FT DOMAIN 30..191
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 193..284
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 291..384
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 389..483
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 484..590
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 908..1162
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1082..1153
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1194..1456
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1370..1447
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 809..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..858
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1460 AA; 163974 MW; C1FDB8048A5E3731 CRC64;
MASLAALALS LLLRLQLPPL PGARAQSAAG GCSFDEHYSN CGYSVALGTN GFTWEQINTW
EKPMLDQAVP TGSFMMVNSS GRASGQKAHL LLPTLKENDT HCIDFHYYFS SRDRSSPGAL
NVYVKVNGGP QGNPVWNVSG VVTEGWVKAE LAISTFWPHF YQVIFESVSL KGHPGYIAVD
EVRVLAHPCR KAPHFLRLQN VEVNVGQNAT FQCIAGGKWS QHDKLWLQQW NGRDTALMVT
RVVNHRRFSA TVSVADTAQR SVSKYRCVIR SDGGSGVSNY AELIVKEPPT PIAPPELLAV
GATYLWIKPN ANSIIGDGPI ILKEVEYRTT TGTWAETHIV DSPNYKLWHL DPDVEYEIRV
LLTRPGEGGT GPPGPPLTTR TKCADPVHGP QNVEIVDIRA RQLTLQWEPF GYAVTRCHSY
NLTVQYQYVF NQQQYEAEEV IQTSSHYTLR GLRPFMTIRL RLLLSNPEGR MESEELVVQT
EEDVPGAVPL ESIQGGPFEE KIYIQWKPPN ETNGVITLYE INYKAVGSLD PSADLSSQRG
KVFKLRNETH HLFVGLYPGT TYSFTIKAST AKGFGPPVTT RIATKISAPS MPEYDTDTPL
NETDTTITVM LKPAQSRGAP VSVYQLVVKE ERLQKSRRAA DIIECFSVPV SYRNASSLDS
LHYFAAELKP ANLPVTQPFT VGDNKTYNGY WNPPLSPLKS YSIYFQALSK ANGETKINCV
RLATKAPMGS AQVTPGTPLC LLTTGASTQN SNTVEPEKQV DNTVKMAGVI AGLLMFIIIL
LGVMLTIKRR RNAYSYSYYL KLAKKQKETQ SGAQREMGPV ASADKPTTKL SASRNDEGFS
SSSQDVNGFT DGSRGELSQP TLTIQTHPYR TCDPVEMSYP RDQFQPAIRV ADLLQHITQM
KRGQGYGFKE EYEALPEGQT ASWDTAKEDE NRNKNRYGNI ISYDHSRVRL LVLDGDPHSD
YINANYIDGY HRPRHYIATQ GPMQETVKDF WRMIWQENSA SIVMVTNLVE VGRVKCVRYW
PDDTEVYGDI KVTLIETEPL AEYVIRTFTV QKKGYHEIRE LRLFHFTSWP DHGVPCYATG
LLGFVRQVKF LNPPEAGPIV VHCSAGAGRT GCFIAIDTML DMAENEGVVD IFNCVRELRA
QRVNLVQTEE QYVFVHDAIL EACLCGNTAI PVCEFRSLYY NISRLDPQTN SSQIKDEFQT
LNIVTPRVRP EDCSIGLLPR NHDKNRSMDV LPLDRCLPFL ISVDGESSNY INAALMDSHK
QPAAFVVTQH PLPNTVADFW RLVFDYNCSS VVMLNEMDTA QFCMQYWPEK TSGCYGPIQV
EFVSADIDED IIHRIFRICN MARPQDGYRI VQHLQYIGWP AYRDTPPSKR SLLKVVRRLE
KWQEQYDGRE GRTVVHCLNG GGRSGTFCAI CSVCEMIQQQ NIIDVFHIVK TLRNNKSNMV
ETLEQYKFVY EVALEYLSSF
//
