KAP0_MESAU
ID KAP0_MESAU Reviewed; 167 AA.
AC P86244;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=cAMP-dependent protein kinase type I-alpha regulatory subunit {ECO:0000250|UniProtKB:P10644};
DE Flags: Fragments;
GN Name=PRKAR1A {ECO:0000250|UniProtKB:P10644};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20400973; DOI=10.1038/aja.2010.19;
RA Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT (GP96) are unique to hamster caput epididymal spermatozoa.";
RL Asian J. Androl. 12:344-355(2010).
CC -!- FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases
CC involved in cAMP signaling in cells. {ECO:0000250}.
CC -!- SUBUNIT: The inactive holoenzyme is composed of two regulatory chains
CC and two catalytic chains. Activation by cAMP releases the two active
CC catalytic monomers and the regulatory dimer. Interacts with PRKACA and
CC PRKACB (By similarity). PRKAR1A also interacts with RFC2; the complex
CC may be involved in cell survival. Interacts with AKAP4. Interacts with
CC RARA; the interaction occurs in the presence of cAMP or FSH and
CC regulates RARA transcriptional activity. Interacts with the
CC phosphorylated form of PJA2. Interacts with CBFA2T3. Interacts with
CC PRKX; regulates this cAMP-dependent protein kinase (By similarity).
CC Interacts with smAKAP; this interaction may target PRKAR1A to the
CC plasma membrane. Interacts with AICDA (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P10644}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}.
CC -!- PTM: The pseudophosphorylation site binds to the substrate-binding
CC region of the catalytic chain, resulting in the inhibition of its
CC activity. {ECO:0000250|UniProtKB:P10644}.
CC -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC family. {ECO:0000255}.
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DR AlphaFoldDB; P86244; -.
DR SMR; P86244; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR Pfam; PF00027; cNMP_binding; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
DR PROSITE; PS00888; CNMP_BINDING_1; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
PE 1: Evidence at protein level;
KW cAMP; cAMP-binding; Cell membrane; Disulfide bond; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN <1..>167
FT /note="cAMP-dependent protein kinase type I-alpha
FT regulatory subunit"
FT /id="PRO_0000394420"
FT MOTIF <30..33
FT /note="Pseudophosphorylation motif"
FT /evidence="ECO:0000250|UniProtKB:Q9DBC7"
FT BINDING 51..78
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9DBC7"
FT BINDING 79..>167
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9DBC7"
FT BINDING 147
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9DBC7"
FT BINDING 156
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9DBC7"
FT MOD_RES 12
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10644"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10644"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10644"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBC7"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09456"
FT DISULFID 5
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q9DBC7"
FT NON_CONS 11..12
FT /evidence="ECO:0000305"
FT NON_CONS 29..30
FT /evidence="ECO:0000305"
FT NON_CONS 48..49
FT /evidence="ECO:0000305"
FT NON_CONS 60..61
FT /evidence="ECO:0000305"
FT NON_CONS 68..69
FT /evidence="ECO:0000305"
FT NON_CONS 85..86
FT /evidence="ECO:0000305"
FT NON_CONS 102..103
FT /evidence="ECO:0000305"
FT NON_CONS 126..127
FT /evidence="ECO:0000305"
FT NON_CONS 138..139
FT /evidence="ECO:0000305"
FT NON_CONS 156..157
FT /evidence="ECO:0000305"
FT NON_TER 1
FT /evidence="ECO:0000305"
FT NON_TER 167
FT /evidence="ECO:0000305"
SQ SEQUENCE 167 AA; 18794 MW; B44BFAA5D9300C50 CRC64;
SLRECELYVQ KTDSREDEIS PPPPNPVVKR GAISAEVYTE EDAASYVRNV LFSHLDDNER
ILMGSTLRMY EEFLSKVSIL ESLDKLTVAD ALEPVQFEDG QKIVVQGEPG DEFFIILEGT
AAVLQRRSEN EEFVEVGRLG PSDYFGEIAL LMNRPRVLGP CSDILKR