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Database: UniProt
Entry: A0A151MNG3_ALLMI
LinkDB: A0A151MNG3_ALLMI
Original site: A0A151MNG3_ALLMI 
ID   A0A151MNG3_ALLMI        Unreviewed;       105 AA.
AC   A0A151MNG3;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=cAMP-dependent protein kinase inhibitor alpha {ECO:0000256|ARBA:ARBA00040416};
GN   Name=PKIA-1 {ECO:0000313|EMBL:KYO25940.1};
GN   ORFNames=Y1Q_0003725 {ECO:0000313|EMBL:KYO25940.1};
OS   Alligator mississippiensis (American alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO25940.1};
RN   [1] {ECO:0000313|EMBL:KYO25940.1, ECO:0000313|Proteomes:UP000050525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO25940.1};
RX   PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA   St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA   Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA   Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA   Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA   Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA   McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA   Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA   Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA   Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA   Ray D.A.;
RT   "Sequencing three crocodilian genomes to illuminate the evolution of
RT   archosaurs and amniotes.";
RL   Genome Biol. 13:415-415(2012).
CC   -!- FUNCTION: Extremely potent competitive inhibitor of cAMP-dependent
CC       protein kinase activity, this protein interacts with the catalytic
CC       subunit of the enzyme after the cAMP-induced dissociation of its
CC       regulatory chains. {ECO:0000256|ARBA:ARBA00002844}.
CC   -!- SIMILARITY: Belongs to the PKI family. {ECO:0000256|ARBA:ARBA00006393}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KYO25940.1}.
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DR   EMBL; AKHW03005657; KYO25940.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151MNG3; -.
DR   Proteomes; UP000050525; Unassembled WGS sequence.
DR   GO; GO:0004862; F:cAMP-dependent protein kinase inhibitor activity; IEA:InterPro.
DR   InterPro; IPR004171; cAMP_dep_PKI.
DR   PANTHER; PTHR15416:SF2; CAMP-DEPENDENT PROTEIN KINASE INHIBITOR ALPHA; 1.
DR   PANTHER; PTHR15416; CAMP-DEPENDENT PROTEIN KINASE INHIBITOR/PKI; 1.
DR   Pfam; PF02827; PKI; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..38
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           39..105
FT                   /note="cAMP-dependent protein kinase inhibitor alpha"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007585338"
FT   REGION          78..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..105
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   105 AA;  11056 MW;  FECBB92B11CC3D66 CRC64;
     MRAGDSARGR GRCAELVAAK VLLCGYLLAM TDVESTYADF IASGRTGRRN ALHDILVSST
     GGNSSELALK LAELDINKTE GEGDAQRNPN EQTGEAQGEA AKQES
//
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