ID G1SQJ0_RABIT Unreviewed; 1166 AA.
AC G1SQJ0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Dual specificity phosphatase 27, atypical {ECO:0000313|Ensembl:ENSOCUP00000005371.3};
GN Name=STYXL2 {ECO:0000313|Ensembl:ENSOCUP00000005371.3};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000005371.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000005371.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000005371.3,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000005371.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000005371.3};
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 EMBL; AAGW02000124; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02000125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1SQJ0; -.
DR SMR; G1SQJ0; -.
DR STRING; 9986.ENSOCUP00000005371; -.
DR Ensembl; ENSOCUT00000006201.4; ENSOCUP00000005371.3; ENSOCUG00000006203.4.
DR GeneTree; ENSGT00940000159723; -.
DR HOGENOM; CLU_009343_0_0_1; -.
DR InParanoid; G1SQJ0; -.
DR Proteomes; UP000001811; Chromosome 13.
DR Bgee; ENSOCUG00000006203; Expressed in skeletal muscle tissue and 12 other cell types or tissues.
DR ExpressionAtlas; G1SQJ0; baseline.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd14576; DSP_iDUSP27; 1.
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:UP000001811}.
FT DOMAIN 132..280
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 201..260
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..1166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..441
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..800
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..1003
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1075
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1082..1119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1128..1150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1166 AA; 129657 MW; 49B666E635CFDA98 CRC64;
MATQGDPEDE QVVPSEEDEA DVRTVQARYL RSPSPSQRSM VSDAETESIF MEPIHLSSAV
AAKQIINEEF KPRGLRAEAE CPGMLESAEQ LLVEDLYNRV REKMDDTSLY NTPCVMDLQR
ALLQDRQEAP RNEVDEVWPN IFIAEKSVAV NKGRLKRLGI THILNAAHGT GVYTGPDFYT
GLEIQYLGVE VDDFPEVDIS QHFRKAAEFL DEALLTYRGK VLVSSEMGVS RSAVLVVAYL
MIFHNMAILE ALLTLRRKRP ICPNEGFLKQ LRELNEKLME ERDEDEADAD ADADSDGAAG
STLGARVQAL TVEEDDDITS LLSGSSLGKA SRASKPPTLI DEEEEEKLYE AWKRGQGLGT
GQGPQGGDGR CSASAGQGGA QPEDGDAEDE DVERLIQEWQ SRNERYQAQG HRRWGREEEE
EEEESEAGSS VGRRRRHTLS ESSTFESLSS RDVRILKQQL QRGRQSPGPR RRSDSVSTDS
TWDVWNERLQ EIEREASRSY HCRSKREQVE AGSRAREDDE ESVSSEASSF YNFCSRNKDK
LTALERWKIK RIQFGFHKKD SEAGDSSSEQ GAVDAEGARK PADVSLSAYQ AWKLKHQKQV
GSENKEEVLE LSKGEDAVLA KKRQRRLELL ERSRQTLEES QSLGGWEAES SAASGSIPLS
AFWSAAPSVS ADGDTASVLS SQSLRSHLSQ ASNPTTPLPT LPVGPGDTIS IASIQNWIAN
VVSETLAQKQ NEMLLLSRPP SVASFKAAAP AASCLGDDQV SMLSGQSSSS LGACLPPQSQ
ARPSSDTQSV LSSSTALGSR AEGTGGRVRG TSKPIYSLFA DNVDLKELGR KEREMQAQLS
EKMSEYKVEK LASDNKRSSL FKKKKVKAEE DDVLGDRDED TDSAIGSFRY SSRSNSQKPE
TDASSSLAVS NHYENSSRAG REMDSSISRW LSGLGTEEKS PPQSDWSGSS RGKYTRSSLF
RETESKSSSY KFSKSQSQEQ DTTSYHEANG SSVRSSSRFS ASSTKEGRET HKFSRSTFSE
TSSSREASPE PYFFRRTPEP PEGAESPELP RPSWARPRDW EDVEESSKSD FSEFGAKRKF
TQSFMRSDEE GEKEKTENRE EGRFASGRRS QYRRSTDREE EEEMDDEAII AAWRRRQEET
RTKLQRRSHS ARTELSPPPL SPAIKG
//
