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Database: UniProt
Entry: A0A0V1HS18_9BILA
LinkDB: A0A0V1HS18_9BILA
Original site: A0A0V1HS18_9BILA 
ID   A0A0V1HS18_9BILA        Unreviewed;      2097 AA.
AC   A0A0V1HS18;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   Name=ATP9B {ECO:0000313|EMBL:KRZ13321.1};
GN   ORFNames=T11_1975 {ECO:0000313|EMBL:KRZ13321.1};
OS   Trichinella zimbabwensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ13321.1, ECO:0000313|Proteomes:UP000055024};
RN   [1] {ECO:0000313|EMBL:KRZ13321.1, ECO:0000313|Proteomes:UP000055024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ13321.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRZ13321.1}.
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DR   EMBL; JYDP01000033; KRZ13321.1; -; Genomic_DNA.
DR   Proteomes; UP000055024; 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   CDD; cd00063; FN3; 9.
DR   CDD; cd14553; R-PTPc-LAR-1; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 12.
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; 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; 7.
DR   Pfam; PF07679; I-set; 2.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PRINTS; PR00014; FNTYPEIII.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 9.
DR   SMART; SM00409; IG; 3.
DR   SMART; SM00408; IGc2; 2.
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; 6.
DR   SUPFAM; SSF48726; Immunoglobulin; 3.
DR   PROSITE; PS50853; FN3; 9.
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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000055024};
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..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..2097
FT                   /note="protein-tyrosine-phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006879395"
FT   TRANSMEM        1385..1411
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1655..1679
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          19..114
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          129..219
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          227..311
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          318..413
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          418..512
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          516..606
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          611..726
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          730..832
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          834..931
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          934..1026
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1031..1124
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1126..1228
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1519..1794
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1714..1785
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          1826..2085
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          2003..2076
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          398..423
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          652..682
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        654..674
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2097 AA;  235900 MW;  E0ABB0F6D2995CBA CRC64;
     MSLLVLCLML IVGLVATDPD VDDDLFLTKP QDSVVLLNSK IGFICEVKSS DQLVKIEWLR
     NGNSVHPARY MVEAVDDTTS ALLIEPVRER DNNTEIGCAL LDADDGQLLA KSTARLGVVD
     AQHLAPGFPK VVEGPKLRTV EKGGSATLTC RVVGDPKPSI LWLRNALPVN MTNRRYSIST
     LGNPGSLVIQ NADESDEGRY ECVARNRNGV THSQSAHLYV KVRVFPPFFS RRPESRYQVM
     PGGSVNLSCV AVGHPMPRVF WRRGSGEDLE DAFKAPYGRN VLTLTAVDKT ENYSCVAFSS
     LGNIESSTTV EVKALAYPPS NLRVLKQNSN SVELAWDPVI AAPDNNIVLY YLIEYRPKYA
     DLSDFFTLKV VNQTETNVTN LQPYTQYEFH VRSVTAVGHS RPSRPVETTT HEAPPQGPPK
     NVHSRAVSVS SIMVQWEPPE KPNGFIVAYM VYYTSQPTEP FSVWSTKEVG NERLTTVGDL
     QPNVVYTVRV QARNSAGFGP VSEPVSVVTQ PGIPGQPQNV KATAIGARRI LLTWESPLFS
     SDITGYVLRY NSTLTDHVEE EVGGSKTERV VENLTPNTDY SFQVYAKSQR GKGLFSRAVR
     QRTNPSVPSG APESVVVEAL SSRQLRVIWE PPLKSQQNGL ITGYRINWEP LINADDDADG
     DDDDDDDDND DDDSAVGTLE HSAEKQRSVV IDKLMPYTDY QITVAARTVK GYGPPSEPAI
     ARTHDDVPGA PLNLKVTPLN ASSAHVAWQE PINKNGILVG YSVHIEELDH LGLPLHSGMM
     FPAHRVASDK NETVVHDLIP NTNYSFRVNA YNRKGDGLFT KALVVSMPSL PPSEPRDLSV
     ELIQREMPVK LLLKWNEPEK TYAKPVLRYR IRYGMLDNFN NTVETQFTNL TSLILKNLKN
     GRSYEFAVAA ENKQGFGLSK KLVVTTPTAA PSGPPYDVRY EIDPSAKRLQ FSWEPPLLDE
     RNGEITGYET RLSIPSRNDI VREIHESTVS FLMGEVGVRY GFAVRAKNSR GYGPWSEPVT
     VETQSDLSQM EVKNVTVQAM STTSALVVWK PVNERRVRGY KVLYTAEPSD RAWRDKEILN
     PAADRLLIED LMPKVHYAFC VKTILIDGAV TECSENAFEV IQPKYVVHDV NVEKLHSSFV
     QLRWEYDGPR PASFYVKYRG KKRYKTQIDE WKELSIDGLT TETEQQVLNV TNLRPYTNYT
     FDVGVVWLND THQHYYLPQT VDIVTKKSVP PFITAPVVLE SLNSKEVLLR LEAATEEYGP
     VSYYWLVVVP AEFPRIPDKI ENKEVLHAKT YHPMPGDLYV AARLTRREIL AMKGGLFTLG
     DGLRYADFTN FPLNNKIHYK TFLRAFLDDE AESDFNEPSQ TSSMYSAEFS PLTMIAGPKV
     SGSSLWIVGP IIALIVVGFI IGIVCFFVFS LNKKNKLPTK QGSVNKVTLG PVGPTETSRL
     LKDAHGNTTV VNGPAVNAYS SKMPNMYCGA GAGDQMEMQS VFYPQPPPTV ASASPHSPIP
     VIEFAAHIDH LKANDNLMFS REYESIETGQ QQTWDHSNFD YNKPKNRYAN VVAYDHSRVV
     LSKLADIAGS DYINANYIDG YHRSKAYIAT QGPMPETFND FWRMVWEENS ATVVMLTKLE
     ERTRIKCDQY WPSRGSALYG LVNVAMKDTT ELAHYTLRVF QISLVIILRS YFTILRLLIN
     LLSKQGQSEV REVRHLQFTA WPDHGVPEHP TPFLIFLKRV KAVNPAESGP VIVHCSAGVG
     RTGAYIVVDT MLDRLRYENT IDIYGCVTAI RSQRNYMVQT EEQYVFIHDA VLDAVQSGCT
     EVPVSKLFLH IENLLQYQAM ENATGMELEF RHLSTLKFPN AKFTAANRPC NKLKNRLVNV
     VPYDWSRVCL TPLPHADGSD YINASFVDGY RLRKMYIATQ GPMTNTVNDF WRMLWEHNST
     IIVMLTKLRE LGREKCCQYW PSDQAEKYDY LLVEPIAEYN MPQYVLREFK LTDSRNGQSK
     TIRHFQYTEW PEQGVPKSSD FLIDFIGQVH KTREQFGQEG PITVHCSTGV SRTGVFIALS
     ILLERIRFEC VVDIFTVVKL LRAQRPNMVQ SEDQYKFLHQ AAMEYLGSFD HFALPQF
//
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