ID A0A5A9NT23_9TELE Unreviewed; 932 AA.
AC A0A5A9NT23;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Tyrosine-protein phosphatase {ECO:0000256|PIRNR:PIRNR000927};
DE EC=3.1.3.48 {ECO:0000256|PIRNR:PIRNR000927};
GN ORFNames=E1301_Tti012791 {ECO:0000313|EMBL:KAA0712056.1};
OS Triplophysa tibetana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Nemacheilidae; Triplophysa.
OX NCBI_TaxID=1572043 {ECO:0000313|EMBL:KAA0712056.1, ECO:0000313|Proteomes:UP000324632};
RN [1] {ECO:0000313|EMBL:KAA0712056.1, ECO:0000313|Proteomes:UP000324632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TTIB1903HZAU {ECO:0000313|EMBL:KAA0712056.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAA0712056.1};
RX PubMed=30977968;
RA Yang X., Liu H., Ma Z., Zou Y., Zou M., Mao Y., Li X., Wang H., Chen T.,
RA Wang W., Yang R.;
RT "Chromosome-level genome assembly of Triplophysa tibetana, a fish adapted
RT to the harsh high-altitude environment of the Tibetan Plateau.";
RL Mol. Ecol. Resour. 19:1027-1036(2019).
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|PIRNR:PIRNR000927};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|PIRNR:PIRNR000927}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class subfamily. {ECO:0000256|ARBA:ARBA00009649,
CC ECO:0000256|PIRNR:PIRNR000927}.
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:KAA0712056.1}.
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DR EMBL; SOYY01000014; KAA0712056.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5A9NT23; -.
DR Proteomes; UP000324632; Chromosome 14.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13189; FERM_C_PTPN4_PTPN3_like; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014847; FA.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR019747; FERM_CS.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR018979; FERM_N.
DR InterPro; IPR018980; FERM_PH-like_C.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR041783; PTPN3/4_FERM_C.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR012151; Tyr_Pase_non-rcpt_typ-3/4.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR45706; TYROSINE-PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR45706:SF7; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 4; 1.
DR Pfam; PF08736; FA; 1.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PIRSF; PIRSF000927; Tyr-Ptase_nr3; 1.
DR PRINTS; PR00935; BAND41.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00295; B41; 1.
DR SMART; SM01195; FA; 1.
DR SMART; SM01196; FERM_C; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF47031; Second domain of FERM; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS00660; FERM_1; 1.
DR PROSITE; PS00661; FERM_2; 1.
DR PROSITE; PS50057; FERM_3; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR000927};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212,
KW ECO:0000256|PIRNR:PIRNR000927}; Hydrolase {ECO:0000256|PIRNR:PIRNR000927};
KW Protein phosphatase {ECO:0000256|PIRNR:PIRNR000927};
KW Receptor {ECO:0000313|EMBL:KAA0712056.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000324632}.
FT DOMAIN 28..311
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 518..590
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 658..914
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 831..905
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 379..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 855
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000927-1"
FT BINDING 823
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000927-2"
FT BINDING 855..861
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000927-2"
FT BINDING 899
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000927-2"
SQ SEQUENCE 932 AA; 105971 MW; 8D5FCCDACFB70AD9 CRC64;
MTARFRLPAG RSYDVGAVEE SRERHLLVVC NVLLLDYTVQ TFEVNKQDQG QTLLDIVYKH
LELTERDYFG LQLADDSLDS PRWLDPNKPV RKQLKRSSSH NLRFRVKFFV SDPSKLQEEY
TRYLYFLQLK QDILSGRLTC PQNTAVLLAS YAVQAEFGDY SHSEHSPGYL SEYSFLPNPP
QDFEKEVSKL HQEHNGLTPA QSEFNYLNAA RTLELYGVEL HYARDHCNAE IYIGVLSAGI
SIYKDRVRIN NFPWLKIVKI SFKSKQFFIQ LRKELSENPE SLLGFNMMSY RACKNIWKAC
VEHHTFFRLE RPVPPERNLF LHYFTLGSKY RYCGRTEAQS VQYGKERGNK NRVFARSPSK
PLVRRLMSGL DWETVSRNSL SDDRLETQSL PNRSPPDSPN HSNSVFNTEG ARVRPSSIGH
LVDHVIDDSP CQTFTNHKSA SSTQANSISL DSTPSPDVTA DEQPPALPPK QSRKDPLTQN
GRSQSQHELD DQQTEIYNTP TASGKSMNGV VPHDNLVLIK MRPDENGRFG FNVKGGADQR
MPIIVSRVAP GTPADMCMPR LNEGDQVVLI NGRDISEHTH DDVVMLIKAS CEDQSGELIL
LVRPNAIYDV DEDQEKLDLE PDFQYIPETS SLDQSHSDAD SLKSSIELLK DGLSSGTVPA
QFDQLYRKRL GMSVSCARLP QNVSKNRYRD ISPYDATRVI LKGADDYINA NYINMEIPRT
GEVKRYIACQ GPLPGTCSEF WQMVWEQSAP LVVMLTTQVE RGRVKCHQYW PNTSASGTYG
DFQVTCVSEE GNSAYLLRDL TLTHVESKED RQICQMQYMA WPDHGVPVDS SDFLNFVSQV
RSKRAETQEP VVVHCSAGIG RTGVLITMET AMCLIESGQP VYPLDIVRTM RDQRAMMIQT
PSQYRFVCEA ILKVYEEEIV KPCEIEPTEK EE
//
