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Database: UniProt
Entry: A0A099ZLJ7_TINGU
LinkDB: A0A099ZLJ7_TINGU
Original site: A0A099ZLJ7_TINGU 
ID   A0A099ZLJ7_TINGU        Unreviewed;      1390 AA.
AC   A0A099ZLJ7;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-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};
DE   Flags: Fragment;
GN   ORFNames=N309_01528 {ECO:0000313|EMBL:KGL82746.1};
OS   Tinamus guttatus (White-throated tinamou).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX   NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL82746.1, ECO:0000313|Proteomes:UP000053641};
RN   [1] {ECO:0000313|EMBL:KGL82746.1, ECO:0000313|Proteomes:UP000053641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL82746.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (JUN-2014) 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   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class 2B subfamily. {ECO:0000256|ARBA:ARBA00006396}.
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DR   EMBL; KL895572; KGL82746.1; -; Genomic_DNA.
DR   STRING; 94827.A0A099ZLJ7; -.
DR   Proteomes; UP000053641; 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; 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   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};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Receptor {ECO:0000313|EMBL:KGL82746.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053641};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          1..120
FT                   /note="MAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50060"
FT   DOMAIN          122..213
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          220..313
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          318..412
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          413..519
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          833..1093
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1013..1084
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          1125..1387
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1301..1378
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          705..729
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        712..729
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KGL82746.1"
FT   NON_TER         1390
FT                   /evidence="ECO:0000313|EMBL:KGL82746.1"
SQ   SEQUENCE   1390 AA;  156595 MW;  BE29DD9130D655B0 CRC64;
     GSFMMVNSSG RASGQKAHLL LPTLKENDTH CIDFHYYLSS RDRSSPGSLN VYVKVNGGPQ
     GNPIWNVSGI VTEGWVKAEL AISTFWPHFY QVIFESVSLK GHPGYIAVDE VRVLAHPCRK
     APHFLRLQNV EVNVGQNATF QCIAGGKWSQ HDKLWLQQWN GRDTALMVTR VVNHRRFSAT
     VSVGDTSQRS ISKYRCVIRS DGGSGVSNYA ELIVKEPPTP IAPPELLAVG ATYLWIKPNA
     NSIIGDGPII LKEVEYRTTT GNWAETHIVD SPNYKLWHLD PDVEYEIRVL LTRPGEGGTG
     PPGPPLTTRT KCADPVHGPQ NVEVVDIRSR QLTLQWEPFG YAVTRCHSYN LTVQYQYVFN
     QQKFEAEELI QTSSHYTLRG LRPFMTIRLR LALSNPEGKM ESEELVVQTE EDVPGPVPLE
     SIQGGPFEEK IYVQWKPPNE TNGIITLYEI TYKAVGSLDP SADLSSQRGK VFKLRNETHH
     LFVGLYPGTT YSFTIKASTV KGFGPPITTR IATKISAPSM PEYDTDSPLN ETDTTITVLP
     VPGSARQVAF GVYQLVVKEE KPQKARRAAD IVECFSVPVS YKNASSLDSP HYFAAELKPI
     NLPVTQPFTV GDNKTYNGYW NAPLSPLKSY SIYFQALSKA NGETKINCVR LATKGASTQN
     SNAVEPEKQV DSTVKMAGVI AGLLMFVIIL LGAMLTIKRR KLAKKQKETQ TSTQREMGPV
     ATSDKTSTKL SAVHNEEAFS SSCQDVNGFT SPSPCSFSVQ SKTLQSKSLL NSYYSDSSHG
     EMTQPTLTIQ THPYRSCEPV EMSYPRGQFQ PAIRVADLLQ HITQMKRGQG YGFKEEYEAL
     PEGQTASWDT AKEDENRNKN RYGNIISYDH SRVRLQLLDG DPHSDYINAN YIDGYHRPRH
     YIATQGKFIL AWPMQETVKD FWRMIWQENS ASVVMVTNLV EVGRVKCVRY WPDDTEVYGD
     IKVTLIETEP LAEYVIRTFT VQKKGYHEIR EIRQFHFTSW PDHGVPCYAT GLLGFVRQVK
     FLNPPEAGPI VVHCSAGAGR TGCFIAIDIM LDMAENEGVV DIFNCVRELR SQRVNLVQTE
     EQYVFVHDAI LEACLCGNTA IPVCEFRSIY YNISRLDPQT NSSQIKDEFQ TLNIVTPRVR
     PEDCSIGLLP RNHDKNRCMD VLPLDRCLPF LISVDGESSN YINAALMDSH KQPAAFIVTQ
     HPLPNTIADF WRLVFDYNCS SVVMLNEMDA AQLCMQYWPE KTSCCYGPIQ VEFVSADIDE
     DIINRIFRIC NMARPQDGYR IVQHLQYIGW PAYRDTPPSK RSLLKVVRRL EKWQEQYDGR
     DGRTVVHCLN GGGRSGTFCA ICSVCEMIQQ QNIIDVFHIV KTLRNNKSNM VESLEQYRFV
     YEVALEYLSS
//
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