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Database: UniProt
Entry: Q9TUB9_RABIT
LinkDB: Q9TUB9_RABIT
Original site: Q9TUB9_RABIT 
ID   Q9TUB9_RABIT            Unreviewed;       142 AA.
AC   Q9TUB9;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   SubName: Full=cAMP-dependent protein kinase subunit R2 beta {ECO:0000313|EMBL:AAF00037.1};
DE   Flags: Fragment;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986 {ECO:0000313|EMBL:AAF00037.1};
RN   [1] {ECO:0000313|EMBL:AAF00037.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=10198423;
RA   Qi Z., Hao C.M., Salter K., Redha R., Breyer M.D.;
RT   "Type II cAMP-dependent protein kinase regulates electrogenic ion transport
RT   in rabbit collecting duct.";
RL   Am. J. Physiol. 276:F622-F628(1999).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC   -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC       family. {ECO:0000256|ARBA:ARBA00005753}.
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DR   EMBL; AF089895; AAF00037.1; -; mRNA.
DR   AlphaFoldDB; Q9TUB9; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00038; CAP_ED; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   InterPro; IPR018488; cNMP-bd_CS.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   PANTHER; PTHR11635; CAMP-DEPENDENT PROTEIN KINASE REGULATORY CHAIN; 1.
DR   PANTHER; PTHR11635:SF156; CAMP-DEPENDENT PROTEIN KINASE TYPE II-BETA REGULATORY SUBUNIT; 1.
DR   PRINTS; PR00103; CAMPKINASE.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR   PROSITE; PS00888; CNMP_BINDING_1; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
PE   2: Evidence at transcript level;
KW   cAMP {ECO:0000256|ARBA:ARBA00023149};
KW   cAMP-binding {ECO:0000256|ARBA:ARBA00022566};
KW   Kinase {ECO:0000313|EMBL:AAF00037.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022566};
KW   Transferase {ECO:0000313|EMBL:AAF00037.1}.
FT   DOMAIN          81..142
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          47..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAF00037.1"
FT   NON_TER         142
FT                   /evidence="ECO:0000313|EMBL:AAF00037.1"
SQ   SEQUENCE   142 AA;  16034 MW;  3464077A12A2208B CRC64;
     AEEPAHSDSE NGEEEEEEEE EAADAGAFNA PVINRFTRRA SVCAEAYNPD EEEDDAESRI
     IHPKTDDQRN RLQEACKDIL LFKNLDPEQM SQVLDAMFEK LVKEGEHVID QGDDGDNFYV
     IDRGTFDIYV KCDGVGRCVG NY
//
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