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Database: UniProt
Entry: A0A0N5B4T4_STREA
LinkDB: A0A0N5B4T4_STREA
Original site: A0A0N5B4T4_STREA 
ID   A0A0N5B4T4_STREA        Unreviewed;      1579 AA.
AC   A0A0N5B4T4;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
OS   Strongyloides papillosus (Intestinal threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0000108300.1};
RN   [1] {ECO:0000313|WBParaSite:SPAL_0000108300.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) 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}.
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DR   STRING; 174720.A0A0N5B4T4; -.
DR   WBParaSite; SPAL_0000108300.1; SPAL_0000108300.1; SPAL_0000108300.
DR   Proteomes; UP000046392; 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:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0036211; P:protein modification process; IEA:UniProt.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000242; PTP_cat.
DR   InterPro; IPR041201; PTPRJ_TM.
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:SF3; PROTEIN-TYROSINE-PHOSPHATASE; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF18861; PTP_tm; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 5.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        953..978
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          686..789
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1195..1457
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1372..1448
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          1001..1034
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1066..1088
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1579 AA;  179172 MW;  ED248778EE914A6C CRC64;
     MKKYLLFSKI KLLLIFVISY LFFYLAKCNS VEQQTPFNVN NNQNNAIINS QTNERIPENL
     INHASISTIL NEFSKQFTIK KDDSDPSRLL NVLLPTNFLN YHQFIAKVTD ISPSVDFPLR
     DVNRTFLAFP SDSSIINIHG LHAGHKYDIA IYGRIVNETH LIKKETIFMD PVPLNFHDNA
     SIIVMHTNIT MRALKPERAL QDTFRVEYIQ LSPPKRYPIL DVHDIPEQKY VDFYLGNLNP
     GRDYDVKVTS IRADIPSQPW QGVITTKPLQ VANITVTDSV DSNDSNCVHL SWMLPIQSGA
     DKFKILYGPT TAVESGMHSL EVEYTKNAVK ICDFIIPGVD FLFIVSAEKS NQLSDPQKTT
     FTVKPQAPIN LSLQPNIDKG LYKLTIYLNN SSKSKADSCK YSIIDDNSNK MEGEMTTEVI
     DGTLSCNTYL NLIPGKRYEV SANTFSNKKG SIKILRNMAL APGFDMKYFD LSLIENNGII
     TIKWPRNEVK LRRLVDIWSR IIGNGSTLQV KIESSSDGKI IRNYSTNPST AKDIIIPNLI
     RGACYNIEIY TLTENGIVSN DKYEKNIRIS MTAYDINTEN ISKTSTIVTF NETGKIGEWY
     ENSVDCKLAI LINDIHGNNI YDKVFNMQKA DEMIFSKIIL NNLKSYTKYA VNSQITCGKA
     DDKMCPQSTR TMNMITFETE QDVPGYIKNL TIKPLNSYSC HVSWKPPTEP NGFITRYLII
     INPDKSNLIG EVPWTLTVNG NFDSNNKKID SIVDNLVGGQ KYSITVLAVT VAGTSSVSNT
     DNTIHIQMPI GAPPKPSTTV EVIQNTIRSS DLSIRYNMRM LSSKNGPITK IGIIVAEVDP
     KTEMPREPPS HNVLSSPSSS YTWYKVQNYE ISPPYITSIT NLKPQKNWGT KSISEVIGIE
     PNCESKDPDT ICNGPLKANT MYRFKLRMYT ADNLWTDTNY SDIAKTDLLK SGFMFRTILL
     FILLALCIAI AIILLICINN CRMSKKNNEK KRPVLFGGCS SSNSNGSSSL GIDRNYGSSS
     KNSTSSSSEV SPNHRQNQWT AFKMLIRNRT AEIVNKFSLD QSSFTNHHTS KDTNNTTSNC
     INTNSQRLPN SSRISMFENI EDNNNKTPIS SPIIISHTNG QMVNSSIVRP INNSTKTLKQ
     RTGFDKRLEN IGTVPPKIIL QTVMKVDNPS RNRPVKIEDF LEHVRLMSAD SDFRFSEEYE
     ELRNIGITQP CIASELPINR AKNRFTNILP YDHSRVKLIS SDDDDGSDYI NANYIPGFNS
     RREFIAAQGP LPSTRDHFWQ MVWEQQVPFI VALTKCVEKG RDKCHQYWPD QDQLSVLYND
     IEVTLAKETM YDDYVLRELH LTNMSYDNLP KKVVYHLHYK AWPDFGVPNH PGGILHIVRL
     FRSKVPPSKN CRPSIIHCSA GVGRSGTFIA IDRLLQCMAI NQPLDVFGIV HEMRLERCQM
     VQNEQQYVFI HLCIAHAIEQ EMLKKQNYMN MMSINQLPQQ NINQNQLLNG IPNTNIQYSQ
     DYDSQYSSPQ RYNGMLVDQH LPYATQRTMN TSLQEPSNIW INPYQQGQPI EGYHTIDIRE
     FHQNPIFIEE DEGIAESGL
//
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