ID A0A2K6FDQ6_PROCO Unreviewed; 1021 AA.
AC A0A2K6FDQ6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN Name=SSH1 {ECO:0000313|Ensembl:ENSPCOP00000012104.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000012104.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000012104.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC Evidence={ECO:0000256|ARBA:ARBA00001482};
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC {ECO:0000256|ARBA:ARBA00009580}.
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DR AlphaFoldDB; A0A2K6FDQ6; -.
DR STRING; 379532.ENSPCOP00000012104; -.
DR Ensembl; ENSPCOT00000022696.1; ENSPCOP00000012104.1; ENSPCOG00000017592.1.
DR GeneTree; ENSGT00940000156133; -.
DR OMA; ADCMYPP; -.
DR Proteomes; UP000233160; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; IEA:Ensembl.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
DR GO; GO:0071318; P:cellular response to ATP; IEA:Ensembl.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IEA:InterPro.
DR GO; GO:0051246; P:regulation of protein metabolic process; IEA:Ensembl.
DR CDD; cd14570; DSP_slingshot_1; 1.
DR CDD; cd11652; SSH-N; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR014876; DEK_C.
DR InterPro; IPR027233; DSP_SSH1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR043587; Phosphatase_SSH-like.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR043588; SSH-N.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR45864:SF5; PROTEIN PHOSPHATASE SLINGSHOT HOMOLOG 1; 1.
DR PANTHER; PTHR45864; SLINGSHOT PROTEIN PHOSPHATASE HOMOLOG; 1.
DR Pfam; PF08766; DEK_C; 1.
DR Pfam; PF00782; DSPc; 1.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF109715; DEK C-terminal domain; 1.
DR PROSITE; PS51998; DEK_C; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000233160}.
FT DOMAIN 226..281
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT DOMAIN 285..426
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 347..404
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 435..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 962..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..759
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..915
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..989
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 998..1021
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1021 AA; 112709 MW; EDE3D2CA9F2A1157 CRC64;
LEAGSDEDRK LNLSLSESFF MVKGAALFLQ QGNSPQGQRS LQHPHKHAGD LPQHLQVMIN
LLRCEDRIKL AVRLESAWTD RVRYMVVVYS SGRQDTEENI LLGVDFSSKE SKSCTIGMVL
RLWSDTKIHL DGDGGFSVST AGRMHIFKPV SVQAMWSALQ VLHKACEVAR RHNYFPGGVA
LIWATYYESC IGSEQSRINE WNAMQDLEST RPDSPALFVD KPTEGERTER LIKAKLRSIM
MSQDLENVTS KEIRNELEKQ MNCNLKEFKE FIDNEMLLIL GQMDKPSLIF DHLYLGSEWN
ASNLEELQGS GVDYILNVTR EIDNFFPGLF AYHNIRVYDE ETTDLLAHWN EAYHFINKAK
RNHSKCLVHC KMGVSRSAST VIAYAMKEFG WPLEKAYNYV KQKRSITRPN AGFMRQLSEY
EGILDASKQR HNKLWGQQTE SSLQPPADGP AGPGDFSPET LDSTPETRLP CLEDTAQPGL
GPSLPCCFRR LSDPFLPSPD GETGSSVQLE DLERDALSEE AAQPVETHKT ARHPQEGPGL
CEKDARKKLE FMSPAARRGS LPQAEEMDGD NGPGPGRWGR PPTQLNRENL NNNNSKRSCP
DDFEQDAMFG ILNKVKPSYR SCADCMYPPA SGASDAFRER CEDPGAPAIC TQPAFLPHVT
SCPMALTASR ARALEKPASS PAETPPLLPP AGSRRPDTSG SGAAAAPELP ASLLEPSRET
PKVLPKSLLL KNSHCDKNPP SMEVVKEESP PKKDPKPAKD LRLLFSNEAE KPTTNSYLMQ
HQESIIQLQK AGLVRKHTKE LERLKSAPAD PASAFRDCTA GRLEASIPEE NQGPAALREP
GPLPFPSLAG SDEKAEAAPL PLEGASLRSP PHFLCRLDHT SHFSKDFLKT ICYTPTSSSM
SSNLTRSSSS DSIHSVRGKP GLVKQRTQEI ETRLRLAGLT VSSPLKRSHS LAKLGSLNFS
TEDLSSEADP STVADSQDAT MSESSFLHEP QAAPRNPPAT SRPSGTSALE HLKSPSWASK
S
//
