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
//