ID A0A3Q3AJR1_KRYMA Unreviewed; 1077 AA.
AC A0A3Q3AJR1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Protein phosphatase 1 regulatory subunit {ECO:0000256|PIRNR:PIRNR038141};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000016450.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000016450.1}
RP IDENTIFICATION.
RG Ensembl;
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_017267157.1; XM_017411668.1.
DR AlphaFoldDB; A0A3Q3AJR1; -.
DR STRING; 37003.ENSKMAP00000016450; -.
DR Ensembl; ENSKMAT00000016681.1; ENSKMAP00000016450.1; ENSKMAG00000012279.1.
DR GeneID; 108233296; -.
DR CTD; 4659; -.
DR GeneTree; ENSGT00940000156120; -.
DR OMA; RKYETNA; -.
DR OrthoDB; 5482573at2759; -.
DR Proteomes; UP000264800; Unplaced.
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:UP000264800}.
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 978..1077
FT /note="cGMP-dependent protein kinase interacting"
FT /evidence="ECO:0000259|Pfam:PF15898"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 976..1064
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 302..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..542
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..691
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..744
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..816
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..866
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..895
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..946
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1077 AA; 120096 MW; 2610178BD649FDDA CRC64;
MKMADAKQKR NEQLKRWLGS ETDQEPPVLK KKKTKVKFDD GAVFLAACSS GDTEEVLRLI
DRGADINYAN VDGLTALHQA CIDDNVDMVT FLVEHGANIN QPDNEGWIPL HAASSCGYLD
IAEYLISQGA NVGVVNSEGE TPLDIAEEEA MEELLQNEIN RQGLDIEAAR KEEERIMLRD
ARQWLNSGQI QDSRHSKSGG TALHVAAAKA YVEVLKLLIQ AGYDVNIKDN DGWTPLHAAA
HWGKEEACRI LVENLCDMDI VNKMGQTAFD VADEDVLGYL EELQKKQNLL MSEKKDVKKS
PLIETTTTGD NNQSLQPLKS KETLLLEPEK TAPRIETLEP EKVDEEDEGK KDDSSCSSEE
DEEEDSESET EEKPKPTPAV SSSTTPAPTP VSVSSPTSPT NQVTTPTSPI KKVPQPAGKV
STKVEEEKKD ESPASWRLGL RKTGSYGALS EITATKDAQR EKDTTGVMRS ASSPRLSSTL
DNKEKEKEKD KGTRLAYVAP TIPRRLASTS DMDEKENRDS TALKRSGSYT RRRWDDDLKN
SDGSSFTNRM PSYQRSTSHT LALGRSGSTR DVPAKSSSTS SLDPNTCNTK PWQPPASHYQ
SYSIYRSSSF GRRHEDLSSS TTTSSSSSTT SSSSSTTTTT TSSSVTSPTG HRGLLSSLGS
SSTRTGSASL TSRYWSEESA EREKEKEKES AAVIPTINTG STTTTTSTTT TTGLLTTGTG
SERRRSYLTP VRDEESESQR KARSRQARQS RRSTQGVTLT DLQEAEKTIG RNRTPKTREE
EKEEKEKQDK EKQEEKKETE TKEDDYRSKY RSYEERYRPS SSSSTSAIST VSAASTTPYS
SSTLSSSSSS LSRPNSLTGI TSSYSRSSRD TEKETDKKEE EKEGEDKSQP RSIRDRRRPR
EKRRSTGVSF WTQDGDENDP DQQSDTEEGS TKGEPHSDRL SRNESTSSLD RNDALFSRSY
GESRRPYSSR LDRDDATDYK KLYEQILAEN EKLKAQLRET DLELADLKLQ LEKATQRQER
YADRSQLEME KRERRALERK ISEMEEELKM LPDLKADNQR LKDENGALIR VISKLSK
//
