GenomeNet

Database: UniProt
Entry: A0A0G2K4R1_RAT
LinkDB: A0A0G2K4R1_RAT
Original site: A0A0G2K4R1_RAT 
ID   A0A0G2K4R1_RAT          Unreviewed;       784 AA.
AC   A0A0G2K4R1;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Protein phosphatase 1 regulatory subunit {ECO:0000256|PIRNR:PIRNR038141};
GN   Name=Ppp1r12c {ECO:0000313|Ensembl:ENSRNOP00000073139.1,
GN   ECO:0000313|RGD:1584883};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000073139.1, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000073139.1, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000073139.1,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0007829|PubMed:22673903}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [3] {ECO:0000313|Ensembl:ENSRNOP00000073139.1}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000073139.1};
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, cytoskeleton, stress fiber
CC       {ECO:0000256|ARBA:ARBA00004529}.
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DR   RefSeq; NP_001178875.2; NM_001191946.2.
DR   AlphaFoldDB; A0A0G2K4R1; -.
DR   SMR; A0A0G2K4R1; -.
DR   STRING; 10116.ENSRNOP00000073139; -.
DR   PaxDb; 10116-ENSRNOP00000030133; -.
DR   Ensembl; ENSRNOT00000086122.2; ENSRNOP00000073139.1; ENSRNOG00000053828.2.
DR   GeneID; 499076; -.
DR   KEGG; rno:499076; -.
DR   AGR; RGD:1584883; -.
DR   CTD; 54776; -.
DR   RGD; 1584883; Ppp1r12c.
DR   eggNOG; KOG0505; Eukaryota.
DR   GeneTree; ENSGT00940000161425; -.
DR   InParanoid; A0A0G2K4R1; -.
DR   OMA; MTDARTW; -.
DR   OrthoDB; 5482573at2759; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000053828; Expressed in colon and 19 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0001725; C:stress fiber; IEA:UniProtKB-SubCell.
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   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: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; 4.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 4.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
PE   1: Evidence at protein level;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR038141};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:A0A0G2K4R1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494}.
FT   REPEAT          104..136
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          137..169
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          230..262
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          263..295
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          685..784
FT                   /note="cGMP-dependent protein kinase interacting"
FT                   /evidence="ECO:0000259|Pfam:PF15898"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          320..688
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        329..357
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        448..462
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        523..551
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        625..646
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        662..688
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   784 AA;  84766 MW;  D690CBEC11D104F7 CRC64;
     MSGEDGPAAG PGAAAAAAAA RERRQEQLRQ WGARAGADPG PGERRARTVR FERAAEFLAA
     CAGGDLDEAR LMLRAADPGP GSGAATDPAV PPPARAVLDS TNADGISALH QACIDENLEV
     VRFLVEQGAT VNQADNEGWT PLHVAASCGY LDIARYLLSH GANIAAVNSD GDLPLDLAES
     DAMEGLLKAE ITRRGVDVEA AKRAEEELLL HDTRCWLNGG AMPEARHPRT GASALHVAAA
     KGYIEVMRLL LQAGYDTELR DGDGWTPLHA AAHWGVEDAC RLLAEHGGGM DSLTHAGQRP
     CDLADEDVMN LLEELAQKQE DLRNQKEASQ GRGQESQVPS NSKHRRSSVC RLSSREKISL
     QDLSKERRPG GAGGLPIGDE DEGEEALAEH PAVEPRALNG VSSPASSSPK SPVPPEEAPF
     SRRFGLQKTG SSGALGPSER KGTEGVLGLQ RSASSSVIEK ASTQAREPRL ARITPTPAQK
     VPEPFTLSEA AAPPSDHSAP PSRTEPGSPV KPNVLTASAA PLADSRDRDR RRSYQMPVRD
     EESESQRKAR SRLMRQSRRS TQGVTLTDLK EAEKVAGKVP EPEQPALPSL DPSRRPRVPG
     VENAEGPAQR AEAPEGQGQG PQAAREHRKA GHERRGPAEG EEAVPAERSP ECSTVDGGST
     VRRQRSQRDL ILESKQQHEE PDGGFRKLYT ELRRENERLR EALTETTLRL AQLKVELERA
     TQRQERFAER PALLELERFE RRALERKAAE LEEELKALSD LRADNQRLKD ENAALIRVIS
     KLSK
//
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