ID W5NHI8_LEPOC Unreviewed; 1089 AA.
AC W5NHI8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Protein phosphatase 1 regulatory subunit {ECO:0000256|PIRNR:PIRNR038141};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000020097.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000020097.1}
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 EMBL; AHAT01008756; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01008757; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01008758; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01008759; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01008760; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5NHI8; -.
DR STRING; 7918.ENSLOCP00000020097; -.
DR Ensembl; ENSLOCT00000020130.1; ENSLOCP00000020097.1; ENSLOCG00000016288.1.
DR eggNOG; KOG0505; Eukaryota.
DR GeneTree; ENSGT00940000156120; -.
DR HOGENOM; CLU_000134_54_0_1; -.
DR InParanoid; W5NHI8; -.
DR Proteomes; UP000018468; Linkage group LG8.
DR Bgee; ENSLOCG00000016288; Expressed in heart and 13 other cell types or tissues.
DR GO; GO:0031672; C:A band; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR GO; GO:0004857; F:enzyme inhibitor activity; IBA:GO_Central.
DR GO; GO:0019208; F:phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd21944; IPD_MYPT1; 1.
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; 1.
DR Pfam; PF13637; Ank_4; 1.
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; 2.
DR PROSITE; PS50088; ANK_REPEAT; 3.
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:UP000018468}.
FT REPEAT 101..133
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 226..258
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 259..291
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 990..1089
FT /note="cGMP-dependent protein kinase interacting"
FT /evidence="ECO:0000259|Pfam:PF15898"
FT REGION 324..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 995..1076
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 361..383
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..524
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..761
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..833
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..874
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..908
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..947
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1089 AA; 122864 MW; 530C0B7BBB7FCB40 CRC64;
SPRPSALWDS GSIKYILPRK EIRKPRQEGM KMADAKQKRN EQLKRWLGSE TDLEPPILKK
KKTKVKFDDG AVFLAACSSG DTEEVLKLLD RGADINYANV DGLTALHQVC YRSNISAIVL
LIDAQASLEI NKRKGWPCFS DSSVSYTDIL KYLISQGANV GVVNSEGETP LDIAEEEAME
ELLQNEVNRQ GVDIEAARKE EERIMLRDAR QWLNSGQIND VRHAKSGGTA LHVAAAKGYT
EVLKLLIQAG YDVNIKDYDG WTPLHAAAHW GKEEACRVLV EHFCDMDIVN KVGQTAFDVA
DEDVLGYLEE LQKKQNMLLS EKRDKKSPLI ETTTTMDNNR PIKPLKNKET LLNEQETCVP
RIESLEQEKV DEEEEGKKDE SSCSSEEEEE EDSESETEAD KSKTSAPVNN TNSTVTQPTS
VTVSSPTIPT NQVTPSSPIK KVKFAPPPGK VSPKEEERKD ESPSSWRLGL RKTGSYGALA
EITAAKEPQK EKDTTGVMRS ASSPRLSSTL DNKDKEKEKD KGARLAYVAP TIPSRRLAST
SDIDEKENRD SAASLVRSGS YTRRRWDDDL KNNEGTTSQN KTPSYQRSTS YSLTIGRSSS
VRDVPAKSSS AISLDPNNTK PWQSPSSQYQ SYSINRSGSF GRRQDDSFSS VTSTTSSVTS
PTGSQRGLLS STSTATKTTT TTTPSSLTSR FWSDESAERE KDSGPTAVAV IPTIVNTTAT
TTTTTTSTTG TVPSTDGRER RRSYLAPVRN EESESQRKAR SRQARQSRRS TQGVTLTDLQ
EAEKTIGRSR PTRGREEEKD EKEKQDKEKQ EEKKESQARE DDYRSKYRSF EERYRPSSTT
TATSSTSSVL STSSSVDRPN SLTGITSLYP SYSRSLHRDT EKEFDKKEEE KEGEDKTEDK
SQPKSIRDRR RPREKRRSTG VSYWKDSDEN DQEQQSDSEE GTNRNEPQSD RLSRYVFYTS
SDRYDHYIGR SYGEGRKPYS GRWEREDTTD YKKLYEQILA ENEKLKAQLR DTDMELTDLK
LQLEKATQRQ ERFADRSQLE MEKRERRALE RRISEMEEEL KMLPDLKADN QRLKDENGAL
IRVISKLSK
//
