ID F5HL66_ANOGA Unreviewed; 1967 AA.
AC F5HL66;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, 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};
DE Flags: Fragment;
GN ORFNames=AgaP_AGAP004246 {ECO:0000313|EMBL:EGK97027.1};
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165 {ECO:0000313|EMBL:EGK97027.1};
RN [1] {ECO:0000313|EMBL:EGK97027.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST {ECO:0000313|EMBL:EGK97027.1};
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
RN [2] {ECO:0000313|EMBL:EGK97027.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EGK97027.1};
RG The Anopheles Genome Sequencing Consortium;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:EGK97027.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EGK97027.1};
RX PubMed=14747013; DOI=10.1016/j.pt.2003.11.003;
RA Mongin E., Louis C., Holt R.A., Birney E., Collins F.H.;
RT "The Anopheles gambiae genome: an update.";
RL Trends Parasitol. 20:49-52(2004).
RN [4] {ECO:0000313|EMBL:EGK97027.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EGK97027.1};
RX PubMed=17210077; DOI=10.1186/gb-2007-8-1-r5;
RA Sharakhova M.V., Hammond M.P., Lobo N.F., Krzywinski J., Unger M.F.,
RA Hillenmeyer M.E., Bruggner R.V., Birney E., Collins F.H.;
RT "Update of the Anopheles gambiae PEST genome assembly.";
RL Genome Biol. 8:R5.1-R5.13(2007).
RN [5] {ECO:0000313|EMBL:EGK97027.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EGK97027.1};
RG VectorBase;
RL Submitted (MAY-2011) 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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:EGK97027.1}.
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DR EMBL; AAAB01008880; EGK97027.1; -; Genomic_DNA.
DR RefSeq; XP_003436753.1; XM_003436705.1.
DR STRING; 7165.F5HL66; -.
DR PaxDb; 7165-AGAP004246-PB; -.
DR GeneID; 1274091; -.
DR KEGG; aga:AgaP_AGAP004246; -.
DR VEuPathDB; VectorBase:AGAP004246; -.
DR eggNOG; KOG0791; Eukaryota.
DR InParanoid; F5HL66; -.
DR PhylomeDB; F5HL66; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0048666; P:neuron development; IEA:UniProt.
DR CDD; cd00063; FN3; 9.
DR CDD; cd14548; R3-PTPc; 1.
DR CDD; cd12087; TM_EGFR-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 11.
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; 9.
DR Pfam; PF18861; PTP_tm; 1.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 11.
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; 6.
DR PROSITE; PS50853; FN3; 7.
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|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1159..1180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 91..183
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 184..279
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 373..464
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 551..640
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 641..735
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 828..918
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 919..1018
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1232..1487
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1404..1478
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 1604..1841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1604..1674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1704..1746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1772..1788
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1789..1806
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1807..1824
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EGK97027.1"
SQ SEQUENCE 1967 AA; 221204 MW; 088774880F644900 CRC64;
LHLAQQCYGA DLVIEIPGNQ GLDDSFYRLD YYPPIGNPAP NATIASRDVG DEIQFSNGLP
GTRYNFWLYY TNSTHKDWLT WTVSITTAPD PPANLTVIPR SGKNVIINWS PPAQGNYSSF
KLKILGLSDN FATNQTVAIE DNQFQYMVRD LTPGATYQVQ AYTLYDGKES VAYTSRNFTT
KPNTPGKFIV WFRNETTLLV LWQPPYPAGI YTHYKVSIEP PDALGSVLYV QKEGEPPGPA
QAAFKGLVPG RAYNISVQTM SEDEISLPTT AQYRTVPLRP MNVTFDKKSI TENSFKVMWE
APKGTSEFDK YQVSLSTSRR QQAVLRNDNE NMAWLEFKDN LDPGKTYQVV VKTVSGKVTS
WPASGDVTLK PLPVKQLQSY TDSKTGVITI SWKPDELSTQ DEYRISYHEL ETNNGDSSTM
STNQTSFALE SLLPGRNYSV TVQALSRKME SNETVIFVVT RPSSPIIEDL KSIREGLNIS
WKSDVNSKQD KYEVTYTRND TNDGKTVLTT ESRLVFTNLY PGAGYEVKVF AVSHGLRSEP
HSYFQAVYPN PPRNMTIEKV TSNSVLVHWK PPERSEFTEY SIRYRTESEK QWIRLPSVKA
TEADVTDMTP GEKYTIQVNT VSYGVESPNP QQVNQTVRPN PVSNIAPLVD SNNITLEFPR
PEGRVETYII HWWPTEQPEQ VSMKNFTEVN TKPPLVRLLI GDLMSGVMYN FKIQTISYGL
TSDLTKLQTR TMPLIQSEVV IVNNMHTRDM VTLSYTPTPQ QSSKFDLYRF SLGDPSIPDK
EKLANDTDRK VTFTGLTPGR LYNITVWTVS GKVSSQPIQR QDRMFPDPIT MLEATSINDT
WIALKWDIPK GEYTSFEVQY LMNDSHYVQN YTVNNHITIT DLKPHRNYTI TVVVRSGTES
SVLRVSLPIS ANFQTKEALP GRMDKFAPID IQPSEITFEW SLPPNEQNGI IRQFTITYGL
DGSQHTQVKD FRPNELRGSI KALQPGKSYV FRIQAKTAIG YGPEHIWKQK MPILAPPKPE
TQVVPTEVGS SATTIEIRFR KHYFSDQNGV VTTYTIIIAE DDSKNASGLE MPSWRDVQSY
SVWPPYQVIE PYYPFKNSSV EDFTIGTENC DAKKTGYCNG PLKSGTTYKV KVRAFTAPDK
FTDTAYSYPI RTAQDNTSLI VSITVPLLII AMLVGVVLFL RRRRHTGRKT TEQRTNDNMS
LPDSTIETSR PVLVKNFAEH YRMMSADSDF RFSEEFEELK HIGRDQPCTF ADLPCNRPKN
RFTNILPYDH SRFKLQPVDD EEGSDYINAN YVPGHNSPRE FIVTQGPLHS TRDDFWRMCW
ESNSRAIVML TRTFEKGREK CDHYWPHDTV PVYYGDIKVT LLNDSHYPDW VITEFMMTRG
EQQRIIRHFH FTTWPDFGVP NPPQTLARFV RAFRERVGPD QRPIVVHCSA GVGRSGTFIT
LDRILQQIQV SDYVDIFGIV WAMRKERVWM VQTEQQYICI HQCLLVVLEG KEGTEREIHD
NQGYEEPRDD DQQSEEQLLI ENRSDDELDE VAVREQHQQN GTAGGIENHE LDRRRSATVE
IVDNELVMMQ QANFTAGETT EEELLDEEEE VEVTVDGLMI VSRKQSHVSS STPAMGGDGQ
QQEQHQHSNS NSASNNERDQ PSSGQDERSI SSNGTNSNNS ANSGYESSPH KRRSLAATSQ
ERVHDRRSLS FSTGGAEIVS KADPSSGDHQ QQHQQQQQQV QQTYQVGGPL QQQQQQQHQA
VLPPGQHHSH QPTVGGGKLH VNSNASNVVI LRADGDDDDR TMATKDDETE IDDGIDGSDE
GDDDLNAVEE VNGRDGKRCG QVEHDDDDDD DDEDDEQTHE QRELLLHRRN ERNVRAVAAA
MVAGAAAGAV ANGSSNGGGG VVGPGCGVGR YKHHSYVEVE EDEQDDDIIV IVDEDNSAAT
DSEGGGGSNR GCGGGGGATG NVGLVGGVGG TNGISDELYL KLREMGW
//
