ID A0A5N5PZF2_PANHP Unreviewed; 697 AA.
AC A0A5N5PZF2;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 18-JUN-2025, entry version 22.
DE RecName: Full=Protein phosphatase 1 regulatory subunit {ECO:0000256|PIRNR:PIRNR038141};
GN ORFNames=PHYPO_G00108050 {ECO:0000313|EMBL:KAB5584481.1};
OS Pangasianodon hypophthalmus (Striped catfish) (Helicophagus hypophthalmus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Pangasiidae; Pangasianodon.
OX NCBI_TaxID=310915 {ECO:0000313|EMBL:KAB5584481.1, ECO:0000313|Proteomes:UP000327468};
RN [1] {ECO:0000313|EMBL:KAB5584481.1, ECO:0000313|Proteomes:UP000327468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Indonesia {ECO:0000313|EMBL:KAB5584481.1,
RC ECO:0000313|Proteomes:UP000327468};
RC TISSUE=Blood {ECO:0000313|EMBL:KAB5584481.1};
RA Wen M., Zahm M., Roques C., Cabau C., Klopp C., Donnadieu C., Jouanno E.,
RA Avarre J.-C., Campet M., Ha T.T.T., Dugue R., Lampietro C., Louis A.,
RA Herpin A., Echchiki A., Berthelot C., Parey E., Roest-Crollius H.,
RA Braasch I., Postlethwait J., Bobe J., Montfort J., Bouchez O., Begum T.,
RA Schartl M., Guiguen Y.;
RT "A chromosome-scale genome assembly of the striped catfish, Pangasianodon
RT hypophthalmus.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAB5584481.1}.
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DR EMBL; VFJC01000003; KAB5584481.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N5PZF2; -.
DR Proteomes; UP000327468; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004857; F:enzyme inhibitor activity; IEA:TreeGrafter.
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 FunFam; 1.25.40.20:FF:000004; Phosphatase 1 regulatory subunit 12A; 1.
DR FunFam; 1.25.40.20:FF:000898; Protein phosphatase 1 regulatory subunit 12A; 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; IPR051226; PP1_Regulatory_Subunit.
DR InterPro; IPR031775; PRKG1_interact.
DR PANTHER; PTHR24179; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 12; 1.
DR PANTHER; PTHR24179:SF27; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 12C; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF15898; PRKG1_interact; 1.
DR PIRSF; PIRSF038141; PP1_12ABC_vert; 4.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 5.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 3.
DR PROSITE; PS50088; ANK_REPEAT; 4.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR038141};
KW Reference proteome {ECO:0000313|Proteomes:UP000327468};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REPEAT 113..145
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 146..178
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 239..271
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 272..304
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 597..697
FT /note="cGMP-dependent protein kinase interacting"
FT /evidence="ECO:0000259|Pfam:PF15898"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 602..691
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..14
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..352
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..405
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..485
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 697 AA; 77384 MW; B255ACFE16833E6D CRC64;
MGDAAKVQRR EQLKRWSGSS TDKQPAAPRR RWRDEEEDGR EDGDRAQDAD GHQPDRQHVK
RRRRVRFERT AEFLAICASG DTDEAKQMLK EMQVISDGDK TCGEDVVNCS NADGITALHQ
ACIDGSIEVV AFLLSRGANV NQVDNEGWTP LHVAASCGNI EIAEYLLQQG ASLSSVNCDG
DVPLDIAEDE AMEALLQEHT LKQGVDVEAA KRLEEEMIMR DARGWLTEGV PADLHHPRTR
ATPLHVAAAK GYLEAIKLLC QCGLDVSAKD GDGWTPLHAA AHWGQREACC LLAEQLCDME
ARSNGGQTPF DVADESVEAL LEDLLQRQAS WRTEQAIKDK QNAQASANGN AAKIRRSSVC
RMSSREKMSV QDQSKERGVS GGLELNEERE SSPETSTVSS PDSESITTST VSPADKTPEE
KEAEEREQER ESRTARVPPT LQRGDSAPES PSGPSTDGKK YQAPVRDEES ESQRKARSRL
MRQSRRSTQG VTLTDLKEAE RTVNRTSEPQ PSLQTVSPVV TVTPAERDTE PVKALSPEGD
SKLGVRDRRR ARRERRSTGI TTLIGETEDL DTHEATRADG TSSDTHQGDA KSSLSLDFRK
LYVDVLKENS TLREKLQETQ LQLSECKVEL ERLRQSQENG CDRPALLELE RFEKKALERK
AAELEDELKV LVDLRADNQR LKDENAALIR VISKLSR
//
