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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//