ID A0A1S3Q4C9_SALSA Unreviewed; 529 AA.
AC A0A1S3Q4C9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Protein phosphatase 1B-like isoform X1 {ECO:0000313|RefSeq:XP_014034842.1, ECO:0000313|RefSeq:XP_014034843.1};
GN Name=LOC106589410 {ECO:0000313|RefSeq:XP_014034842.1,
GN ECO:0000313|RefSeq:XP_014034843.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014034843.1};
RN [1] {ECO:0000313|RefSeq:XP_014034842.1, ECO:0000313|RefSeq:XP_014034843.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014034842.1,
RC ECO:0000313|RefSeq:XP_014034843.1};
RG RefSeq;
RL Submitted (NOV-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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}. Membrane
CC {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004635}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000256|ARBA:ARBA00006702,
CC ECO:0000256|RuleBase:RU003465}.
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DR RefSeq; XP_014034842.1; XM_014179367.1.
DR RefSeq; XP_014034843.1; XM_014179368.1.
DR STRING; 8030.ENSSSAP00000104273; -.
DR PaxDb; 8030-ENSSSAP00000104273; -.
DR Ensembl; ENSSSAT00000138925; ENSSSAP00000104269; ENSSSAG00000075905.
DR GeneID; 106589410; -.
DR KEGG; sasa:106589410; -.
DR OMA; QDNRVNG; -.
DR OrthoDB; 11028at2759; -.
DR Proteomes; UP000087266; Chromosome ssa28.
DR Bgee; ENSSSAG00000075905; Expressed in ovary and 14 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 1.10.10.430; Phosphatase 2C, C-terminal domain suprefamily; 1.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR012911; PP2C_C.
DR InterPro; IPR036580; PP2C_C_sf.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR47992:SF105; PROTEIN PHOSPHATASE 1B; 1.
DR Pfam; PF00481; PP2C; 1.
DR Pfam; PF07830; PP2C_C; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR SUPFAM; SSF81601; Protein serine/threonine phosphatase 2C, C-terminal domain; 1.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003465};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Myristate {ECO:0000256|ARBA:ARBA00022707};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW ECO:0000256|RuleBase:RU003465};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266}.
FT DOMAIN 23..290
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..463
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..529
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 529 AA; 57003 MW; 4A4E9B7004315C3A CRC64;
MGAFLDKPKT EKHTAHGEGN GLHYGLSSMQ GWRVEMEDAH TAMVGLPHGL TDWSFFAVYD
GHAGSRVANY CSAHLLEHIL SGGAEFTPGT GSVEGVKDGI RTGFLKIDEY MRSFTDLRQG
LDRSGSTAVG VLLSPFHFYF INCGDSRAVL SRDGRVGFST QDHKPCNPRE KERIQNAGGS
VMIQRVNGSL AVSRALGDYD YKCVDGKGPT EQLVSPEPEV CVLERAAEGD EFVVLACDGI
WDVMSNEELC DFVRSRLQVF DDLERVCTAV VDTCLHKGSR DNMSVVLVTL PGAPKVSEEA
LKREEDLDKY LETRVEDLLG GCGEEGVPDL VSVLRNIASE NIPNLPPGGG LACKRSVIEA
VYSRLNPQRE EEGACAGGGG EEESEEGGGS STATNLLEAL RQFRLHHRGQ YRSVLEEALA
VYRLPGENTA DTGEESSSFT ADDLPDSPRP SPPSPPPSPV VIETPSSPEA EKSKDTPSPD
INQQPPLAAD INQSEPPAVD TDQPEPPAAD LVPLYPPAAE LRQPDPPPS
//
