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Database: UniProt
Entry: K7FZD6_PELSI
LinkDB: K7FZD6_PELSI
Original site: K7FZD6_PELSI 
ID   K7FZD6_PELSI            Unreviewed;      1411 AA.
AC   K7FZD6;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   Name=PTPRU {ECO:0000313|Ensembl:ENSPSIP00000013396.1};
OS   Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC   Trionychidae; Pelodiscus.
OX   NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000013396.1, ECO:0000313|Proteomes:UP000007267};
RN   [1] {ECO:0000313|Proteomes:UP000007267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG   Soft-shell Turtle Genome Consortium;
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000007267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA   White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA   Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA   Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA   Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT   into the development and evolution of the turtle-specific body plan.";
RL   Nat. Genet. 45:701-706(2013).
RN   [3] {ECO:0000313|Ensembl:ENSPSIP00000013396.1}
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   -!- 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; AGCU01012564; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01012565; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01012566; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01012567; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01012568; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01012569; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01012570; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01012571; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01012572; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01012573; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSPSIT00000013459.1; ENSPSIP00000013396.1; ENSPSIG00000011351.1.
DR   GeneTree; ENSGT00940000157151; -.
DR   HOGENOM; CLU_001645_0_1_1; -.
DR   Proteomes; UP000007267; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd00063; FN3; 3.
DR   CDD; cd06263; MAM; 1.
DR   CDD; cd14632; R-PTPc-U-1; 1.
DR   CDD; cd14637; R-PTPc-U-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; IPR003599; Ig_sub.
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:SF10; PROTEIN-TYROSINE-PHOSPHATASE-RELATED; 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; SM00409; IG; 1.
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   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   Reference proteome {ECO:0000313|Proteomes:UP000007267};
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|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        721..746
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          2..164
FT                   /note="MAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50060"
FT   DOMAIN          166..257
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          264..359
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          362..460
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          461..567
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          873..1109
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1029..1100
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          1141..1404
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1320..1395
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          799..829
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        799..819
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1411 AA;  159576 MW;  B90B9C54DBE67045 CRC64;
     AAGCTFEEDV DLNQCEYNQR EDDDFEWELI RSYAMPHLTS DLPHGSYLMV NSSQHAPGQK
     AHLLFQTLSE NDTHCLQFSY FMYSRDGHSP GSLNVYVKVT GGPLGSMVWD MAGSHGRLWH
     QAELAVSMFW PNEYQVLFEA VISGEHRGYL GLDDILLLNY PCSKAPHFSR LGDVEVNAGQ
     NATFQCVAAG KALEAERFLL QRQNGAVAPA ASVKHISHRR FLATFQLDEV SKEEQDLYRC
     VSQSVRGSGV SNFAELIVKE PPTPIAPPQL FRAGSTYLII QLNTNSIIGD GPIVRKEIEY
     RMTSGPWSEV HAVSMQTYKL WHLDPDTEYE ISVLLTRPGD GGTGKPGPPL ISRTKCAEPM
     RAPKGLAFSE IQSRQLTLQW EPLGYNLTRC HTYVVSLCYR YFVGTSHNQT FRECVKMEHS
     THRYTIKNLL PYKNVHVKLI LSNPEGRKEG KEMIFQTDED VPGGIASESL TFTPLEDMIF
     LKWEEPAEAN GLITQYEISY QSIESSDPAV NVPGPRRTVS KLRNETYHVF SNLHPGTTYL
     FSVRARTGKG FGQTALTEIT TNISAPSFDY GDMPSPLSES ESTITVLLRP AQGRGAPIST
     YQVIVEEDRP KKMRRELGGQ DCFPVPLTFD DAVARGSVHY FGGELPPSSL PEAKPFTVGD
     NLTYGGYWNP PLEPKKAYLI YFQATSNLKG ETRLNCIRIA RKAACKESKR PLEVSQHSEE
     MGLILGICAG GLVVLIILLG AIIVVIRKGK PVNMTKATIN YRHEKTHMMS AIDRSFTDQS
     TLQEDERLGL SFMDAHNYSN RGDQRSSAVN ESSSLLGGSP RRQCGRKGSP YHTGQLHPAV
     RVADLLQHIN QMKTAEGYGF KQEYESFFEG WDASKKKDKT KGRQDHMPTY DRHRVKLHPL
     LGDPNSDYIN ANYIDGYHRS NHFIATQGPK QEMVYDFWRM VWQEHCSSIV MITKLVEVGR
     VKCSKYWPDD TEMYGDIKIS LVKSEMLAEY AVRTFALERR GYSARHEVKQ FHFTSWPEHG
     VPYHATGLLA FIRRVKATTP PDAGPIVIHC SAGTGRTGCY IVLDVMLDMA ECEGVVDIYN
     CVKTLCSRRI NMIQTEEQYV FIHDAILEAC LCGETAIPVS EFKPTYKEMV RIEPQSNSSQ
     LREEFQTLNS VTPHLDVEEC SIALLPRNRE KNRSMDVLPP DRCLPFLISM DGDSNNYINA
     ALTDSYTKSA AFIVTLHPLQ NTTTDFWRLV YDYGCTSIVM LNQLNQSNSA WPCLQYWPEP
     GLQQYGPIEV EYVSRSADED LVARLFRVQN ITRLQEGHLM VRHFQYLRWS AYRDTPDSKK
     SFLHLLAQVE KWQEESGDGR TVVHCLNGGG RSGTFCASTM ILEMIKCHNM VDVFYAAKTL
     RNYKPNMVEN LEQYHFCYDI ALEYLESLET R
//
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