ID A0A452E9I2_CAPHI Unreviewed; 1038 AA.
AC A0A452E9I2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 25.
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:ENSCHIP00000008830.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000008830.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000008830.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000008830.1}
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 EMBL; LWLT01000018; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_017916577.1; XM_018061088.1.
DR AlphaFoldDB; A0A452E9I2; -.
DR STRING; 9925.ENSCHIP00000008830; -.
DR Ensembl; ENSCHIT00000016594.1; ENSCHIP00000008830.1; ENSCHIG00000011891.1.
DR GeneID; 106503050; -.
DR KEGG; chx:106503050; -.
DR CTD; 54434; -.
DR GeneTree; ENSGT00940000156133; -.
DR OMA; ADCMYPP; -.
DR OrthoDB; 5490735at2759; -.
DR Proteomes; UP000291000; Chromosome 17.
DR Bgee; ENSCHIG00000011891; Expressed in spleen and 16 other cell types or tissues.
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:UP000291000}.
FT DOMAIN 249..304
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT DOMAIN 308..449
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 370..427
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 913..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 987..1038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..890
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..932
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..1001
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1038 AA; 113615 MW; 85A67399FAD04C5E CRC64;
MALVTLQRSP TPSAASSSAS NSELEAGSDE DRKLNHSLSE SFFMVKGAAL FLQQGSSPQG
QRSLQHPHKH AGDLPQHLQV MINLLRCEDR IKLAVRLESA WAERVRYMVV VDSSGRQDTE
ESILLGVDFS SKESKSCTIG MVLRLWSDTK IHLDGDGGFS VSTAGRMHVF KPVSVQAMWS
ALQVLHKACE VARRHNYFPG GVALLWASYY ESCIGSEQSC INEWNAMQDL ESTRPDSPAL
FADKPTEGER TERLIKAKLR SIMMSQDLEN VTSKEIRNEL EKQMNCNLKE FKEFIDNEML
LILGQMDKPS LIFDHLYLGS EWNASNLEEL QGSGVDYILN VTREIDNFFP GLFAYHNIRV
YDEETTDLLA HWNEAYHFIN KAKRNRSKCL VHCKMGVSRS ASTVIAYAMK EFGWTLEKAY
NYVKQKRSIT RPNAGFMRQL SEYEGILDAS KQRHNKLWRQ QADDSCLQQP VDDPAGPGDF
QPETLDSTPE AQLPCLDAAA PLPQFPGSGA LGGPALPCCF RRLSDPLLRA PGDEMGGPVH
LEYLERDALL EEGAQLAEVS QPARPPPEGP GLCEREVTKR PEPGSPQAQG SSSPQAEEME
GEEALGAGRW GRPAAQLDNL LNRENLNNNN SKRSCPDDLE HDAIFGILNK VKPSYKSCAD
CMYPAAGGTP EAFGERCKNP GAPAICTQPT FLPQLTSSPV ASRSRALEKL ASGPTETAPF
LPPIGSRRPD TSGPGAGAAP EPPASLPEPS RETHKALPKS LVKNSHCDNP PGLEAAKEDL
SPKKDPKLAK DLRLLFSKEA EKPTSNSYLV QHQESIIQLQ KAGLVRKHTR ELERLKGTPA
EPAAPCRDGP AAIPEENQDL PLPGRAPGPE KPEPSPTLLE GAPLKSPPPF LCRPDHASHF
SRDFLKTICY TPTSSSMSSN LTRSSSSDSI HSVRGKPGLV KQRTQEIETR LRLAGLTVSS
PLKRSHSLAK LGSLNLSTED LCSEADVSTA ADSQDTRLSE SSLLHEPPVV ARSPAATSKP
SGKSAPENLK SPSWLGKS
//
