ID A0A3L8T327_CHLGU Unreviewed; 852 AA.
AC A0A3L8T327;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN ORFNames=DV515_00000038 {ECO:0000313|EMBL:RLW13433.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLW13433.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLW13433.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLW13433.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLW13433.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class subfamily. {ECO:0000256|ARBA:ARBA00009649}.
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:RLW13433.1}.
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DR EMBL; QUSF01000001; RLW13433.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8T327; -.
DR STRING; 44316.ENSEGOP00005000050; -.
DR Proteomes; UP000276834; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd14600; PTPc-N3; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR019749; Band_41_domain.
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; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
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 InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR45706; TYROSINE-PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR45706:SF5; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 3; 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 PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00295; B41; 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; 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};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Reference proteome {ECO:0000313|Proteomes:UP000276834}.
FT DOMAIN 1..342
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 447..519
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 585..840
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 758..831
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 288..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 852 AA; 96190 MW; 8D268EDFF15E1732 CRC64;
MTTVDWFAEH VKWDVQSGVG RFLWCDTITQ LPEELTGHSG AQGHGGYSAI VMNSRLRALG
GRINNIRASE LPKEKTRSEI ICNVHFLDGS VQSFKVNKQD TGQILLDMTY NQLGVTEKEY
FGLQQNETSV DSPLKIDIAE GRLSCPISSA VVLASYAVQS QLGDYNASVH CSGYLSNYNF
IPEQNKDFLT KVETLHEQHS GLKQSEAESC YINIARTLEF YGVELHSGRD LHNLDLMIGI
ASGGIAVYRK LICTSFYPWS VNNQYCRKVI GGMVWNPSMR RSLSVEHLET KSLPSRSPPV
TPNWRSPRLR HEIRKPRHSS VDNLTNEISY ITETEDVFYT YKGSPTSKDS DSEFSQNRSP
QRRSSEQESP KNVLGNSPTR SSLTHLSPKA LARSPNGVGN ISGSYPLEGV DKQFLETYDN
LTKSSSMEDS SQYYCDKNDL IEGDLLLVHI IPDEEGKFGF NLKGGVDQKM PLLVSRITPG
SPADKCIPKL NEGDQIVLIN GRDISEHTHD QVVMFIKASR ESHTRELALL VRRKVVKQFV
EPISEDEADS LTLPESILPV CSEYGGDTLD ESMEQLRRGL ESGTVLIQFE QLYRRKPGLA
VTCAKVPQNM DKNRYKDVLP YDATRIILQG DEDYINANYV NMEIPSAGIV NRYIATQGPL
PHTCAHFWQV VWDHKLSLII MLTTLTERGR TKCHQYWPDP PDVMEYGCFR VRCHSEDCTI
AYVVREMVIT NIETGQEHTV THLQYVAWPD HGVPDDSMDF LEFVTCMRPK RVKNEPVLVH
CSAGIGRTGV LVTMETAMCL IERNQPVYPL DIVRKMRDQR AMMVQTSSQY KFVCEAILRV
YKEGLVRPLD SS
//
