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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
 
 
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