ID A0A3B5R923_XIPMA Unreviewed; 1085 AA.
AC A0A3B5R923;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Dual specificity phosphatase 27, atypical {ECO:0000313|Ensembl:ENSXMAP00000040102.1};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000040102.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000040102.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000040102.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A3B5R923; -.
DR Ensembl; ENSXMAT00000037996.1; ENSXMAP00000040102.1; ENSXMAG00000006366.2.
DR GeneTree; ENSGT00940000159723; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR020405; Atypical_DUSP_subfamA.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR45682; AGAP008228-PA; 1.
DR PANTHER; PTHR45682:SF4; SERINE_THREONINE_TYROSINE-INTERACTING-LIKE PROTEIN 2; 1.
DR Pfam; PF00782; DSPc; 1.
DR PRINTS; PR01908; ADSPHPHTASE.
DR PRINTS; PR01909; ADSPHPHTASEA.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000002852}.
FT DOMAIN 120..268
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 189..247
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 330..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..1041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..887
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..966
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..1002
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1028
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1085 AA; 120546 MW; 8998418E99D241B2 CRC64;
TPQICFSRLT SSSSSSSSSP SFSMTSLTSR FSDASSIVME PIHLSSAVAA KKIISEELPP
RAARPESVPE SMLESAEQLM VEDLYNRVRD MLDDRSPYNT PCVLDIQRAM VRDRLEAPAN
LVDEVWPNIH IAEKSVAVNK ARLKRMGITH ILNTAHGTGV YTGQAFYANM NIQYRGIELD
DFPDADIAAH FRPAAEFLDE ALLTHKGKVL VVSMMGVSRS AILVASYLMI FQNMTIMEAL
TAIRKKRAIN PNEGFLKQLR EFNETLMEER DDDDETLSQC SVIDARAQTD GEEERSVVKV
KAQSIMMEEE EDGESVTSSI VSSAAAAALR NGPLRNRDQE PGHREIDLPG QTGTEDGAED
DDDGLDGMIR EWQRRNEKYR SEEWWEAQLH GEEDSVSAGL PKAAKQEDDG ESVTSEDIRA
VKERLRHRNK RPSSDAVSTS SCTSYSDLWK QRLKEIEEQA AARYRKTEDD NGSESTGPEG
GNKNVDDEVD SILSDTSSMY NFCLKNKEKM TPLERWRIKR IQFGWNKKDR EDGEKSSAAD
GEEESKTPSF QDVNLTAYQA WKLRQQKRLG EENTEEILEL SRGDDSATIK RRQRREEILE
RSKKTLEESQ SMCGWESESC ISGGTVPLSA FWAGAGVTGP PSVANDDNMS MLSGRSSTMS
SVSQPRSTRS TQSAGQALPP VLPAVPGPAG EPMVNLTSIQ NWIANIVTET IKQKQSELSL
PPPSRAGSEL SFGAAPSMLA GRGAQDDRAS WVSGASCSST RSKAHGRATS VLSSDGLSGR
RSALGSDIGS VLGSKKTRIT TTSVPLFSLF QDQVNLGKLD AIEKEIKSEM REKGETYEKK
KILEDNKRST LYKKKKLKED EDEEQDRKRK EEEFLEETKK KEKPKRSYGL SGCLNLNPVI
EKDRNTSIDD WLRSVRPPPG KLSSAAEADP SQDPYDDLDA SASQFDFSDH RGSFAAEDDE
EAFGVTSRYR PRFGDDPSGE DAEYSCNGFT QSRRQAGRSS ADGTDGISPH RRFAHRSRFD
GSEAAGRRDS DEDEEEEEDV EAFIAQTRRR IRARAAAEAE DDEVLCAWRE QQGAKARRKV
LGCEE
//
