ID A0A1S3N0Q2_SALSA Unreviewed; 1111 AA.
AC A0A1S3N0Q2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Protein phosphatase 1 regulatory subunit {ECO:0000256|PIRNR:PIRNR038141};
GN Name=LOC106576312 {ECO:0000313|RefSeq:XP_014008890.1};
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_014008890.1};
RN [1] {ECO:0000313|RefSeq:XP_014008890.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014008890.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBUNIT: PP1 comprises a catalytic subunit, and one or several
CC targeting or regulatory subunits. {ECO:0000256|PIRNR:PIRNR038141}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|PIRNR:PIRNR038141}.
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DR RefSeq; XP_014008890.1; XM_014153415.1.
DR AlphaFoldDB; A0A1S3N0Q2; -.
DR GeneID; 106576312; -.
DR OrthoDB; 5482573at2759; -.
DR Proteomes; UP000087266; Chromosome ssa17.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019208; F:phosphatase regulator activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 6.10.140.390; -; 1.
DR Gene3D; 6.10.250.1820; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR017401; MYPT1/MYPT2/Mbs85.
DR InterPro; IPR031775; PRKG1_interact.
DR PANTHER; PTHR24179; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 12; 1.
DR PANTHER; PTHR24179:SF20; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 12A; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF15898; PRKG1_interact; 1.
DR PIRSF; PIRSF038141; PP1_12ABC_vert; 2.
DR SMART; SM00248; ANK; 6.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 4.
DR PROSITE; PS50088; ANK_REPEAT; 4.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR038141};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266}.
FT REPEAT 72..104
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 105..137
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 198..230
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 231..263
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 994..1099
FT /note="cGMP-dependent protein kinase interacting"
FT /evidence="ECO:0000259|Pfam:PF15898"
FT REGION 323..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 992..1100
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 323..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..611
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..693
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..748
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..821
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..878
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..909
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..954
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..969
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..991
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1111 AA; 123650 MW; 9F76FD1D9FAD736E CRC64;
MKMADAKQKR NEQLKRWLGS ETDIEPPILK KKKTKVKFDD GAVFLAACSS GDTEEVLRMI
DRGADINYAN VDGLTALHQA CIDDNVDMVT FLVEHGAAIN QPDNEGWIPL HAAASCGYMD
IAEYLIGQGA SVGVVNSEGE TPLDIAEEEA MEELLKNEIN RQGVDIEAAR KEEERIMLRD
ARQWLNSGTI NDVRHAKSGG TALHVAAAKG YAEVLKLLIQ AGYDVNIKDF DGWTPLHAAS
HWGKEEACKI LVENLCDMDL INKVGQTSFD VADEDVLGYL EELQKKQNLL NSEKKDVKKS
PLIETTTTGD NNQNLKSIKS KETLLLEPEK PALRIETLEP EKVDEEEEGK KDQESSCSSE
EEEEEDSESE TEADKSKTPV PVSNSNGTTV VPAPTSVTVS STSPTSPTNQ VAQQVSPAGK
VSPKEVSPKD KQEDDKTKKS DESPASWRLG LRKTGSYGAL AEITATKEAQ KEKDTAGVMR
SASSPRLSSS LDNKDKEKEK DKGTRLAYVA PTIPRRLAST SDIDEKENRD SAASLVRSGS
YTRRRWDDEL KNSEGSASTT RTTPSYQRST SHTLTLGRSG STRDVPAKSS SASSLDPITC
NTKPWQSPAS HYQSYSIYRS GSFGRRHEDL GSTTSSSTST TTTSSVTSPT GHRDRSLLSS
LGSSTRTGSS SLTSRYWAEE SAEREKEREK ESAAVIPTIN TGSTTTTTST TGTIIGSDGR
ERRRSDMRTS YLTPVRDEES ESQRKARSRQ ARQSRRSTQG VTLTDLQEAE KTIGRSRPIR
TRDEEKEEKE KQDKEKQEEK KETGETKEDD YRSRYRSFEE TYQRYRPSAT STTTLSTAST
PSSTSSSSLN RPNSLTGITS SSLNRPNSLT GITSSYSRSS RDTEKESDKK QQEEEKEGED
KSQPRSIRDR RRPREKRRST GVSFWTQDGS DDNDPDQSAD SEEGSIKGEP QSDRLSRNES
STSSSDRYDH LGSRGYGEGR RSFSSRLDRD DSTDYKKLYE QILAENEKLK AQLRDTDLQL
NDLKLQLEKA TQRQERFADR SQLEMEKRER RALERKISDM EEELKNLPEV KQVQALRQVK
ERLQAENRAL ARVVVKLSQS ACSQLPPSVD L
//
