KAPCA_MOUSE
ID KAPCA_MOUSE Reviewed; 351 AA.
AC P05132; Q9JID0;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 249.
DE RecName: Full=cAMP-dependent protein kinase catalytic subunit alpha;
DE Short=PKA C-alpha;
DE EC=2.7.11.11;
GN Name=Prkaca; Synonyms=Pkaca;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=2833513; DOI=10.1016/s0021-9258(18)60627-1;
RA Chrivia J.C., Uhler M.D., McKnight G.S.;
RT "Characterization of genomic clones coding for the C alpha and C beta
RT subunits of mouse cAMP-dependent protein kinase.";
RL J. Biol. Chem. 263:5739-5744(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3456589; DOI=10.1073/pnas.83.5.1300;
RA Uhler M.D., Carmichael D.F., Lee D.C., Chrivia J.C., Krebs E.G.,
RA McKnight G.S.;
RT "Isolation of cDNA clones coding for the catalytic subunit of mouse cAMP-
RT dependent protein kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:1300-1304(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-153 (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=10982398; DOI=10.1091/mbc.11.9.3031;
RA San Agustin J.T., Wilkerson C.G., Witman G.B.;
RT "The unique catalytic subunit of sperm cAMP-dependent protein kinase is the
RT product of an alternative C-alpha mRNA expressed specifically in
RT spermatogenic cells.";
RL Mol. Biol. Cell 11:3031-3044(2000).
RN [5]
RP PHOSPHORYLATION AT SER-11; SER-140; THR-198 AND SER-339.
RX PubMed=8395513; DOI=10.1016/s0021-9258(17)46675-0;
RA Yonemoto W., Garrod S.M., Bell S.M., Taylor S.S.;
RT "Identification of phosphorylation sites in the recombinant catalytic
RT subunit of cAMP-dependent protein kinase.";
RL J. Biol. Chem. 268:18626-18632(1993).
RN [6]
RP PHOSPHORYLATION AT THR-198 BY PDPK1.
RX PubMed=9707564; DOI=10.1073/pnas.95.17.9849;
RA Cheng X., Ma Y., Moore M., Hemmings B.A., Taylor S.S.;
RT "Phosphorylation and activation of cAMP-dependent protein kinase by
RT phosphoinositide-dependent protein kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:9849-9854(1998).
RN [7]
RP FUNCTION.
RX PubMed=10805756; DOI=10.1128/mcb.20.11.4149-4158.2000;
RA Huang W., Zhou X., Lefebvre V., de Crombrugghe B.;
RT "Phosphorylation of SOX9 by cyclic AMP-dependent protein kinase A enhances
RT SOX9's ability to transactivate a Col2a1 chondrocyte-specific enhancer.";
RL Mol. Cell. Biol. 20:4149-4158(2000).
RN [8]
RP MYRISTOYLATION AT GLY-2, PHOSPHORYLATION AT SER-11, AND DEAMIDATION AT
RP ASN-3.
RX PubMed=11141074; DOI=10.1021/bi0021277;
RA Tholey A., Pipkorn R., Bossemeyer D., Kinzel V., Reed J.;
RT "Influence of myristoylation, phosphorylation, and deamidation on the
RT structural behavior of the N-terminus of the catalytic subunit of cAMP-
RT dependent protein kinase.";
RL Biochemistry 40:225-231(2001).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=11875122; DOI=10.1210/mend.16.3.0793;
RA Skaalhegg B.S., Huang Y., Su T., Idzerda R.L., McKnight G.S., Burton K.A.;
RT "Mutation of the Calpha subunit of PKA leads to growth retardation and
RT sperm dysfunction.";
RL Mol. Endocrinol. 16:630-639(2002).
RN [10]
RP FUNCTION IN SPERMATOZOA CAPACITATION (ISOFORM 2), AND TISSUE SPECIFICITY
RP (ISOFORM 2).
RX PubMed=15340140; DOI=10.1073/pnas.0405580101;
RA Nolan M.A., Babcock D.F., Wennemuth G., Brown W., Burton K.A.,
RA McKnight G.S.;
RT "Sperm-specific protein kinase A catalytic subunit Calpha2 orchestrates
RT cAMP signaling for male fertility.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13483-13488(2004).
RN [11]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=18367160; DOI=10.1016/j.ydbio.2008.01.045;
RA Webb R.J., Tinworth L., Thomas G.M., Zaccolo M., Carroll J.;
RT "Developmentally acquired PKA localisation in mouse oocytes and embryos.";
RL Dev. Biol. 317:36-45(2008).
RN [12]
RP FUNCTION IN MEIOSIS RESUMPTION, FUNCTION AS CDC25B KINASE, AND INTERACTION
RP WITH CDC25B.
RX PubMed=19223768; DOI=10.4161/cc.8.4.7846;
RA Pirino G., Wescott M.P., Donovan P.J.;
RT "Protein kinase A regulates resumption of meiosis by phosphorylation of
RT Cdc25B in mammalian oocytes.";
RL Cell Cycle 8:665-670(2009).
RN [13]
RP FUNCTION IN SPERMATOZOA CAPACITATION, FUNCTION AS ABL1 KINASE, AND
RP INTERACTION WITH ABL1.
RX PubMed=19560455; DOI=10.1016/j.ydbio.2009.06.022;
RA Baker M.A., Hetherington L., Curry B., Aitken R.J.;
RT "Phosphorylation and consequent stimulation of the tyrosine kinase c-Abl by
RT PKA in mouse spermatozoa; its implications during capacitation.";
RL Dev. Biol. 333:57-66(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [15]
RP PHOSPHORYLATION AT TYR-331.
RX PubMed=21866565; DOI=10.1002/jcb.23325;
RA Caldwell G.B., Howe A.K., Nickl C.K., Dostmann W.R., Ballif B.A.,
RA Deming P.B.;
RT "Direct modulation of the protein kinase A catalytic subunit alpha by
RT growth factor receptor tyrosine kinases.";
RL J. Cell. Biochem. 113:39-48(2012).
RN [16]
RP IDENTIFICATION IN A COMPLEX WITH MROH2B AND TCP11, INTERACTION WITH MROH2B
RP AND TCP11, AND SUBCELLULAR LOCATION.
RX PubMed=27105888; DOI=10.1096/fj.201500136r;
RA Stanger S.J., Law E.A., Jamsai D., O'Bryan M.K., Nixon B., McLaughlin E.A.,
RA Aitken R.J., Roman S.D.;
RT "A novel germ cell protein, SPIF (sperm PKA interacting factor), is
RT essential for the formation of a PKA/TCP11 complex that undergoes
RT conformational and phosphorylation changes upon capacitation.";
RL FASEB J. 30:2777-2791(2016).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=1862342; DOI=10.1126/science.1862342;
RA Knighton D.R., Zheng J., ten Eyck L.F., Ashford V.A., Xuong N.-H.,
RA Taylor S.S., Sowadski J.M.;
RT "Crystal structure of the catalytic subunit of cyclic adenosine
RT monophosphate-dependent protein kinase.";
RL Science 253:407-414(1991).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF COMPLEX WITH INHIBITOR.
RX PubMed=8443157; DOI=10.1021/bi00060a005;
RA Zheng J., Knighton D.R., ten Eyck L.F., Karlsson R., Xuong N.-H.,
RA Taylor S.S., Sowadski J.M.;
RT "Crystal structure of the catalytic subunit of cAMP-dependent protein
RT kinase complexed with MgATP and peptide inhibitor.";
RL Biochemistry 32:2154-2161(1993).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF COMPLEX WITH INHIBITOR.
RX PubMed=9109651; DOI=10.1021/bi961947+;
RA Narayana N., Cox S., Shaltiel S., Taylor S.S., Xuong N.;
RT "Crystal structure of a polyhistidine-tagged recombinant catalytic subunit
RT of cAMP-dependent protein kinase complexed with the peptide inhibitor
RT PKI(5-24) and adenosine.";
RL Biochemistry 36:4438-4448(1997).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=9261084; DOI=10.1016/s0969-2126(97)00246-3;
RA Narayana N., Cox S., Nguyen-Huu X., ten Eyck L.F., Taylor S.S.;
RT "A binary complex of the catalytic subunit of cAMP-dependent protein kinase
RT and adenosine further defines conformational flexibility.";
RL Structure 5:921-935(1997).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH ATP ANALOG.
RX PubMed=17889648; DOI=10.1016/j.cell.2007.07.018;
RA Kim C., Cheng C.Y., Saldanha S.A., Taylor S.S.;
RT "PKA-I holoenzyme structure reveals a mechanism for cAMP-dependent
RT activation.";
RL Cell 130:1032-1043(2007).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS).
RX PubMed=17932298; DOI=10.1126/science.1146447;
RA Wu J., Brown S.H., von Daake S., Taylor S.S.;
RT "PKA type IIalpha holoenzyme reveals a combinatorial strategy for isoform
RT diversity.";
RL Science 318:274-279(2007).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH ADP, SUBUNIT, AND
RP MUTAGENESIS OF LYS-286 AND PHE-328.
RX PubMed=19122195; DOI=10.1074/jbc.m805862200;
RA Yang J., Kennedy E.J., Wu J., Deal M.S., Pennypacker J., Ghosh G.,
RA Taylor S.S.;
RT "Contribution of non-catalytic core residues to activity and regulation in
RT protein kinase A.";
RL J. Biol. Chem. 284:6241-6248(2009).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS) IN COMPLEX WITH ATP ANALOGS.
RX PubMed=19748511; DOI=10.1016/j.jmb.2009.09.014;
RA Brown S.H.J., Wu J., Kim C., Alberto K., Taylor S.S.;
RT "Novel isoform-specific interfaces revealed by PKA RIIbeta holoenzyme
RT structures.";
RL J. Mol. Biol. 393:1070-1082(2009).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH ATP ANALOG AND
RP SUBSTRATE PEPTIDE, AND ACTIVITY REGULATION.
RX PubMed=20890288; DOI=10.1038/nchembio.452;
RA Masterson L.R., Cheng C., Yu T., Tonelli M., Kornev A., Taylor S.S.,
RA Veglia G.;
RT "Dynamics connect substrate recognition to catalysis in protein kinase A.";
RL Nat. Chem. Biol. 6:821-828(2010).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-351 IN COMPLEX WITH PRKAR2B,
RP SUBUNIT, AND PHOSPHORYLATION AT SER-140 AND THR-198.
RX PubMed=22323819; DOI=10.1126/science.1213979;
RA Zhang P., Smith-Nguyen E.V., Keshwani M.M., Deal M.S., Kornev A.P.,
RA Taylor S.S.;
RT "Structure and allostery of the PKA RIIbeta tetrameric holoenzyme.";
RL Science 335:712-716(2012).
CC -!- FUNCTION: Phosphorylates a large number of substrates in the cytoplasm
CC and the nucleus (By similarity). Phosphorylates CDC25B, ABL1, NFKB1,
CC CLDN3, PSMC5/RPT6, PJA2, RYR2, RORA, SOX9 and VASP (PubMed:10805756,
CC PubMed:19223768). Regulates the abundance of compartmentalized pools of
CC its regulatory subunits through phosphorylation of PJA2 which binds and
CC ubiquitinates these subunits, leading to their subsequent proteolysis
CC (By similarity). RORA is activated by phosphorylation. Required for
CC glucose-mediated adipogenic differentiation increase and osteogenic
CC differentiation inhibition from osteoblasts (By similarity). Involved
CC in chondrogenesis by mediating phosphorylation of SOX9
CC (PubMed:10805756). Involved in the regulation of platelets in response
CC to thrombin and collagen; maintains circulating platelets in a resting
CC state by phosphorylating proteins in numerous platelet inhibitory
CC pathways when in complex with NF-kappa-B (NFKB1 and NFKB2) and I-kappa-
CC B-alpha (NFKBIA), but thrombin and collagen disrupt these complexes and
CC free active PRKACA stimulates platelets and leads to platelet
CC aggregation by phosphorylating VASP. RYR2 channel activity is
CC potentiated by phosphorylation in presence of luminal Ca(2+), leading
CC to reduced amplitude and increased frequency of store overload-induced
CC Ca(2+) release (SOICR) characterized by an increased rate of Ca(2+)
CC release and propagation velocity of spontaneous Ca(2+) waves, despite
CC reduced wave amplitude and resting cytosolic Ca(2+). PSMC5/RPT6
CC activation by phosphorylation stimulates proteasome. Negatively
CC regulates tight junctions (TJs) in ovarian cancer cells via CLDN3
CC phosphorylation. NFKB1 phosphorylation promotes NF-kappa-B p50-p50 DNA
CC binding. Involved in embryonic development by down-regulating the
CC Hedgehog (Hh) signaling pathway that determines embryo pattern
CC formation and morphogenesis (By similarity). Prevents meiosis
CC resumption in prophase-arrested oocytes via CDC25B inactivation by
CC phosphorylation (PubMed:19223768). May also regulate rapid eye movement
CC (REM) sleep in the pedunculopontine tegmental (PPT) (By similarity).
CC Phosphorylates APOBEC3G and AICDA. Phosphorylates HSF1; this
CC phosphorylation promotes HSF1 nuclear localization and transcriptional
CC activity upon heat shock (By similarity).
CC {ECO:0000250|UniProtKB:P17612, ECO:0000250|UniProtKB:P27791,
CC ECO:0000269|PubMed:10805756, ECO:0000269|PubMed:19223768}.
CC -!- FUNCTION: [Isoform 2]: Phosphorylates and activates ABL1 in sperm
CC flagellum to promote spermatozoa capacitation.
CC {ECO:0000269|PubMed:15340140, ECO:0000269|PubMed:19560455}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.11;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.11;
CC -!- ACTIVITY REGULATION: Allosterically activated by various compounds,
CC including ATP. Activated by cAMP; the nucleotide acts as a dynamic and
CC allosteric activator by coupling the two lobes of apo PKA, enhancing
CC the enzyme dynamics synchronously and priming it for catalysis.
CC {ECO:0000269|PubMed:20890288}.
CC -!- SUBUNIT: A number of inactive tetrameric holoenzymes are produced by
CC the combination of homo- or heterodimers of the different regulatory
CC subunits associated with two catalytic subunits. Protein kinase A
CC holoenzyme is comprised of two catalytic (C) and two regulatory (R)
CC subunits which keep the enzyme in an inhibited state before activation
CC by cyclic-AMP. cAMP causes the dissociation of the inactive holoenzyme
CC into a dimer of regulatory subunits bound to four cAMP and two free
CC monomeric catalytic subunits. The cAMP-dependent protein kinase
CC catalytic subunit binds PJA2. Both isoforms 1 and 2 forms activate
CC cAMP-sensitive PKAI and PKAII holoenzymes by interacting with
CC regulatory subunit (R) of PKA, PRKAR1A/PKR1 and PRKAR2A/PKR2,
CC respectively. Interacts with PRKAR1A and PRKAR2B (By similarity).
CC Interacts with NFKB1, NFKB2 and NFKBIA in platelets; these interactions
CC are disrupted by thrombin and collagen. Binds to ABL1 in spermatozoa
CC and with CDC25B in oocytes. Interacts with APOBEC3G and AICDA (By
CC similarity). Interacts with RAB13; downstream effector of RAB13
CC involved in tight junction assembly (By similarity). Found in a complex
CC at least composed of MROH2B isoform 2, PRKACA isoform 2 and TCP11
CC (PubMed:27105888). Interacts with MROH2B isoform 2 (PubMed:27105888).
CC Interacts with HSF1 (By similarity). Isoform 2 interacts with TCP11
CC (PubMed:27105888). {ECO:0000250, ECO:0000250|UniProtKB:P17612,
CC ECO:0000269|PubMed:22323819}.
CC -!- INTERACTION:
CC P05132; P63248: Pkia; NbExp=4; IntAct=EBI-400564, EBI-2931786;
CC P05132; P61014: Pln; NbExp=2; IntAct=EBI-400564, EBI-10148373;
CC P05132; P31324: Prkar2b; NbExp=15; IntAct=EBI-400564, EBI-455340;
CC P05132; P39717: GPB2; Xeno; NbExp=2; IntAct=EBI-400564, EBI-20711;
CC P05132; P00514: PRKAR1A; Xeno; NbExp=6; IntAct=EBI-400564, EBI-1041635;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18367160}. Cell
CC membrane {ECO:0000250}. Nucleus {ECO:0000250}. Mitochondrion
CC {ECO:0000269|PubMed:18367160}. Membrane {ECO:0000250|UniProtKB:P17612};
CC Lipid-anchor {ECO:0000250|UniProtKB:P17612}. Note=Translocates into the
CC nucleus (monomeric catalytic subunit) (By similarity). The inactive
CC holoenzyme is found in the cytoplasm. Distributed throughout the
CC cytoplasm in meiotically incompetent oocytes. Associated to
CC mitochondrion as meiotic competence is acquired. Aggregates around the
CC germinal vesicles (GV) at the immature GV stage oocytes. Colocalizes
CC with HSF1 in nuclear stress bodies (nSBs) upon heat shock (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:P17612}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell projection, cilium, flagellum
CC {ECO:0000269|PubMed:27105888}. Cytoplasmic vesicle, secretory vesicle,
CC acrosome {ECO:0000269|PubMed:27105888}. Note=Expressed in the midpiece
CC region of the sperm flagellum (By similarity). Colocalizes with MROH2B
CC and TCP11 on the acrosome and tail regions in round spermatids and
CC spermatozoa regardless of the capacitation status of the sperm
CC (PubMed:27105888). {ECO:0000250, ECO:0000269|PubMed:27105888}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=C-alpha-1;
CC IsoId=P05132-1; Sequence=Displayed;
CC Name=2; Synonyms=C-alpha-2, C-alpha-S, C(s);
CC IsoId=P05132-2; Sequence=VSP_004760;
CC -!- TISSUE SPECIFICITY: Isoform 2 is sperm specific.
CC -!- DEVELOPMENTAL STAGE: Accumulates in oocytes before fertilization but
CC fades out after fertilization. {ECO:0000269|PubMed:18367160}.
CC -!- PTM: Autophosphorylated. Phosphorylation is enhanced by vitamin K(2)
CC (By similarity). Phosphorylated on threonine and serine residues.
CC Phosphorylation on Thr-198 is required for full activity. {ECO:0000250,
CC ECO:0000269|PubMed:8395513, ECO:0000269|PubMed:9707564}.
CC -!- PTM: Asn-3 is partially deaminated to Asp-3 giving rise to 2 major
CC isoelectric variants, called CB and CA respectively.
CC -!- PTM: When myristoylated, Ser-11 is autophosphorylated probably in
CC conjunction with deamidation of Asn-3. {ECO:0000269|PubMed:11141074,
CC ECO:0000269|PubMed:8395513}.
CC -!- PTM: Phosphorylated at Tyr-331 by activated receptor tyrosine kinases
CC EGFR and PDGFR; this increases catalytic efficiency.
CC {ECO:0000269|PubMed:21866565}.
CC -!- DISRUPTION PHENOTYPE: Frequent early postnatal lethality. Survivals are
CC runted accompanied with mature sperm exhibiting defective forward
CC motility. {ECO:0000269|PubMed:11875122}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. cAMP subfamily. {ECO:0000305}.
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DR EMBL; M19960; AAA39937.1; -; Genomic_DNA.
DR EMBL; M18240; AAA39937.1; JOINED; Genomic_DNA.
DR EMBL; M18241; AAA39937.1; JOINED; Genomic_DNA.
DR EMBL; M19953; AAA39937.1; JOINED; Genomic_DNA.
DR EMBL; M19954; AAA39937.1; JOINED; Genomic_DNA.
DR EMBL; M19955; AAA39937.1; JOINED; Genomic_DNA.
DR EMBL; M19956; AAA39937.1; JOINED; Genomic_DNA.
DR EMBL; M19957; AAA39937.1; JOINED; Genomic_DNA.
DR EMBL; M19958; AAA39937.1; JOINED; Genomic_DNA.
DR EMBL; M19959; AAA39937.1; JOINED; Genomic_DNA.
DR EMBL; M12303; AAA39936.1; -; mRNA.
DR EMBL; BC003238; AAH03238.1; -; mRNA.
DR EMBL; BC054834; AAH54834.1; -; mRNA.
DR EMBL; AF239743; AAF76425.1; -; mRNA.
DR CCDS; CCDS22463.1; -. [P05132-1]
DR CCDS; CCDS85574.1; -. [P05132-2]
DR PIR; A28619; OKMSCA.
DR RefSeq; NP_001264827.1; NM_001277898.1. [P05132-2]
DR RefSeq; NP_032880.1; NM_008854.5. [P05132-1]
DR PDB; 1APM; X-ray; 2.00 A; E=2-351.
DR PDB; 1ATP; X-ray; 2.20 A; E=2-351.
DR PDB; 1BKX; X-ray; 2.60 A; A=2-351.
DR PDB; 1BX6; X-ray; 2.10 A; A=2-351.
DR PDB; 1FMO; X-ray; 2.20 A; E=2-351.
DR PDB; 1J3H; X-ray; 2.90 A; A/B=2-351.
DR PDB; 1JBP; X-ray; 2.20 A; E=2-351.
DR PDB; 1JLU; X-ray; 2.25 A; E=2-351.
DR PDB; 1L3R; X-ray; 2.00 A; E=2-351.
DR PDB; 1RDQ; X-ray; 1.26 A; E=2-351.
DR PDB; 1RE8; X-ray; 2.10 A; A=2-351.
DR PDB; 1REJ; X-ray; 2.20 A; A=2-351.
DR PDB; 1REK; X-ray; 2.30 A; A=2-351.
DR PDB; 1SYK; X-ray; 2.80 A; A/B=2-351.
DR PDB; 2CPK; X-ray; 2.70 A; E=2-351.
DR PDB; 2ERZ; X-ray; 2.20 A; E=1-351.
DR PDB; 2QCS; X-ray; 2.20 A; A=2-351.
DR PDB; 2QUR; X-ray; 2.50 A; A=2-351.
DR PDB; 2QVS; X-ray; 2.50 A; E=2-351.
DR PDB; 3FHI; X-ray; 2.00 A; A=2-351.
DR PDB; 3FJQ; X-ray; 1.60 A; E=2-351.
DR PDB; 3IDB; X-ray; 1.62 A; A=2-351.
DR PDB; 3IDC; X-ray; 2.70 A; A=2-351.
DR PDB; 3J4Q; EM; 35.00 A; D/E=1-351.
DR PDB; 3J4R; EM; 35.00 A; D/E=1-351.
DR PDB; 3O7L; X-ray; 2.80 A; B/D=2-351.
DR PDB; 3OW3; X-ray; 1.90 A; A=2-351.
DR PDB; 3PVB; X-ray; 3.30 A; A=7-351.
DR PDB; 3QAL; X-ray; 1.70 A; E=2-351.
DR PDB; 3QAM; X-ray; 1.92 A; E=2-351.
DR PDB; 3TNP; X-ray; 2.30 A; C/F=2-351.
DR PDB; 3TNQ; X-ray; 3.10 A; B=2-351.
DR PDB; 3X2U; X-ray; 2.40 A; A=1-351.
DR PDB; 3X2V; X-ray; 1.77 A; A=1-351.
DR PDB; 3X2W; X-ray; 1.70 A; A=1-351.
DR PDB; 4DFX; X-ray; 1.35 A; E=2-351.
DR PDB; 4DFY; X-ray; 3.00 A; A/E=1-351.
DR PDB; 4DFZ; X-ray; 2.00 A; E=2-351.
DR PDB; 4DG0; X-ray; 2.00 A; E=2-351.
DR PDB; 4DG2; X-ray; 2.00 A; E=2-351.
DR PDB; 4DG3; X-ray; 1.80 A; E=1-351.
DR PDB; 4DH1; X-ray; 2.00 A; A=16-351.
DR PDB; 4DH3; X-ray; 2.20 A; A=2-351.
DR PDB; 4DH5; X-ray; 2.20 A; A=2-351.
DR PDB; 4DH7; X-ray; 1.80 A; A=2-351.
DR PDB; 4DH8; X-ray; 2.30 A; A=2-351.
DR PDB; 4DIN; X-ray; 3.70 A; A=2-351.
DR PDB; 4HPT; X-ray; 2.15 A; E=2-351.
DR PDB; 4HPU; X-ray; 1.55 A; E=2-351.
DR PDB; 4IAC; X-ray; 2.15 A; A=2-351.
DR PDB; 4IAD; X-ray; 1.90 A; A=2-351.
DR PDB; 4IAF; X-ray; 2.20 A; A=2-351.
DR PDB; 4IAI; X-ray; 1.55 A; A=2-351.
DR PDB; 4IAK; X-ray; 1.60 A; A=2-351.
DR PDB; 4IAY; X-ray; 2.00 A; A=2-351.
DR PDB; 4IAZ; X-ray; 1.85 A; A=2-351.
DR PDB; 4IB0; X-ray; 1.87 A; A=2-351.
DR PDB; 4IB1; X-ray; 1.63 A; A=2-351.
DR PDB; 4IB3; X-ray; 2.20 A; A=2-351.
DR PDB; 4NTS; X-ray; 2.90 A; A/B=2-351.
DR PDB; 4NTT; X-ray; 3.50 A; A/B=2-351.
DR PDB; 4O21; X-ray; 1.95 A; A=16-351.
DR PDB; 4O22; X-ray; 1.70 A; A=16-351.
DR PDB; 4WBB; X-ray; 2.80 A; B=2-351.
DR PDB; 4X6Q; X-ray; 2.52 A; C=2-351.
DR PDB; 4X6R; X-ray; 2.40 A; A=2-351.
DR PDB; 4XW4; X-ray; 1.82 A; A=15-351.
DR PDB; 4XW5; X-ray; 1.95 A; A=15-351.
DR PDB; 4XW6; X-ray; 1.90 A; A=15-351.
DR PDB; 5JR7; X-ray; 3.56 A; A/C=2-351.
DR PDB; 5X3F; X-ray; 3.38 A; B=5-351.
DR PDB; 6E21; Other; 2.00 A; A=2-351.
DR PDB; 6MM5; X-ray; 1.95 A; E=16-351.
DR PDB; 6MM6; X-ray; 2.39 A; C/E=16-351.
DR PDB; 6MM7; X-ray; 1.85 A; A/D=16-351.
DR PDB; 6MM8; X-ray; 1.85 A; C=16-351.
DR PDBsum; 1APM; -.
DR PDBsum; 1ATP; -.
DR PDBsum; 1BKX; -.
DR PDBsum; 1BX6; -.
DR PDBsum; 1FMO; -.
DR PDBsum; 1J3H; -.
DR PDBsum; 1JBP; -.
DR PDBsum; 1JLU; -.
DR PDBsum; 1L3R; -.
DR PDBsum; 1RDQ; -.
DR PDBsum; 1RE8; -.
DR PDBsum; 1REJ; -.
DR PDBsum; 1REK; -.
DR PDBsum; 1SYK; -.
DR PDBsum; 2CPK; -.
DR PDBsum; 2ERZ; -.
DR PDBsum; 2QCS; -.
DR PDBsum; 2QUR; -.
DR PDBsum; 2QVS; -.
DR PDBsum; 3FHI; -.
DR PDBsum; 3FJQ; -.
DR PDBsum; 3IDB; -.
DR PDBsum; 3IDC; -.
DR PDBsum; 3J4Q; -.
DR PDBsum; 3J4R; -.
DR PDBsum; 3O7L; -.
DR PDBsum; 3OW3; -.
DR PDBsum; 3PVB; -.
DR PDBsum; 3QAL; -.
DR PDBsum; 3QAM; -.
DR PDBsum; 3TNP; -.
DR PDBsum; 3TNQ; -.
DR PDBsum; 3X2U; -.
DR PDBsum; 3X2V; -.
DR PDBsum; 3X2W; -.
DR PDBsum; 4DFX; -.
DR PDBsum; 4DFY; -.
DR PDBsum; 4DFZ; -.
DR PDBsum; 4DG0; -.
DR PDBsum; 4DG2; -.
DR PDBsum; 4DG3; -.
DR PDBsum; 4DH1; -.
DR PDBsum; 4DH3; -.
DR PDBsum; 4DH5; -.
DR PDBsum; 4DH7; -.
DR PDBsum; 4DH8; -.
DR PDBsum; 4DIN; -.
DR PDBsum; 4HPT; -.
DR PDBsum; 4HPU; -.
DR PDBsum; 4IAC; -.
DR PDBsum; 4IAD; -.
DR PDBsum; 4IAF; -.
DR PDBsum; 4IAI; -.
DR PDBsum; 4IAK; -.
DR PDBsum; 4IAY; -.
DR PDBsum; 4IAZ; -.
DR PDBsum; 4IB0; -.
DR PDBsum; 4IB1; -.
DR PDBsum; 4IB3; -.
DR PDBsum; 4NTS; -.
DR PDBsum; 4NTT; -.
DR PDBsum; 4O21; -.
DR PDBsum; 4O22; -.
DR PDBsum; 4WBB; -.
DR PDBsum; 4X6Q; -.
DR PDBsum; 4X6R; -.
DR PDBsum; 4XW4; -.
DR PDBsum; 4XW5; -.
DR PDBsum; 4XW6; -.
DR PDBsum; 5JR7; -.
DR PDBsum; 5X3F; -.
DR PDBsum; 6E21; -.
DR PDBsum; 6MM5; -.
DR PDBsum; 6MM6; -.
DR PDBsum; 6MM7; -.
DR PDBsum; 6MM8; -.
DR AlphaFoldDB; P05132; -.
DR BMRB; P05132; -.
DR SMR; P05132; -.
DR BioGRID; 202192; 62.
DR CORUM; P05132; -.
DR DIP; DIP-6086N; -.
DR ELM; P05132; -.
DR IntAct; P05132; 23.
DR MINT; P05132; -.
DR STRING; 10090.ENSMUSP00000005606; -.
DR BindingDB; P05132; -.
DR iPTMnet; P05132; -.
DR PhosphoSitePlus; P05132; -.
DR EPD; P05132; -.
DR jPOST; P05132; -.
DR MaxQB; P05132; -.
DR PaxDb; P05132; -.
DR PeptideAtlas; P05132; -.
DR PRIDE; P05132; -.
DR ProteomicsDB; 269063; -. [P05132-1]
DR ProteomicsDB; 269064; -. [P05132-2]
DR Antibodypedia; 4159; 526 antibodies from 41 providers.
DR DNASU; 18747; -.
DR Ensembl; ENSMUST00000005606; ENSMUSP00000005606; ENSMUSG00000005469. [P05132-1]
DR Ensembl; ENSMUST00000211558; ENSMUSP00000147256; ENSMUSG00000005469. [P05132-2]
DR GeneID; 18747; -.
DR KEGG; mmu:18747; -.
DR UCSC; uc009mll.3; mouse. [P05132-1]
DR UCSC; uc009mlm.2; mouse. [P05132-2]
DR CTD; 5566; -.
DR MGI; MGI:97592; Prkaca.
DR VEuPathDB; HostDB:ENSMUSG00000005469; -.
DR eggNOG; KOG0616; Eukaryota.
DR GeneTree; ENSGT00940000162186; -.
DR HOGENOM; CLU_000288_63_5_1; -.
DR InParanoid; P05132; -.
DR OMA; WQDSRNL; -.
DR OrthoDB; 963519at2759; -.
DR PhylomeDB; P05132; -.
DR TreeFam; TF313399; -.
DR BRENDA; 2.7.11.11; 3474.
DR Reactome; R-MMU-163615; PKA activation.
DR Reactome; R-MMU-164378; PKA activation in glucagon signalling.
DR Reactome; R-MMU-180024; DARPP-32 events.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-MMU-392517; Rap1 signalling.
DR Reactome; R-MMU-422356; Regulation of insulin secretion.
DR Reactome; R-MMU-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-MMU-442720; CREB1 phosphorylation through the activation of Adenylate Cyclase.
DR Reactome; R-MMU-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling.
DR Reactome; R-MMU-5578775; Ion homeostasis.
DR Reactome; R-MMU-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-MMU-5610787; Hedgehog 'off' state.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-MMU-8853659; RET signaling.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR Reactome; R-MMU-8963896; HDL assembly.
DR Reactome; R-MMU-9634597; GPER1 signaling.
DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR BioGRID-ORCS; 18747; 4 hits in 77 CRISPR screens.
DR ChiTaRS; Prkaca; mouse.
DR EvolutionaryTrace; P05132; -.
DR PRO; PR:P05132; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P05132; protein.
DR Bgee; ENSMUSG00000005469; Expressed in dentate gyrus of hippocampal formation granule cell and 273 other tissues.
DR Genevisible; P05132; MM.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:UniProtKB.
DR GO; GO:0005930; C:axoneme; ISO:MGI.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IMP:CAFA.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0097546; C:ciliary base; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043197; C:dendritic spine; IDA:SynGO.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0031588; C:nucleotide-activated protein kinase complex; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0044853; C:plasma membrane raft; ISO:MGI.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0036126; C:sperm flagellum; IDA:UniProtKB.
DR GO; GO:0097225; C:sperm midpiece; ISS:UniProtKB.
DR GO; GO:0004679; F:AMP-activated protein kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IDA:CAFA.
DR GO; GO:0004691; F:cAMP-dependent protein kinase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:CAFA.
DR GO; GO:0030145; F:manganese ion binding; IMP:CAFA.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; IPI:CAFA.
DR GO; GO:0004672; F:protein kinase activity; IDA:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0070417; P:cellular response to cold; IMP:MGI.
DR GO; GO:0071333; P:cellular response to glucose stimulus; ISO:MGI.
DR GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
DR GO; GO:0071374; P:cellular response to parathyroid hormone stimulus; IMP:MGI.
DR GO; GO:0001707; P:mesoderm formation; IGI:MGI.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IMP:MGI.
DR GO; GO:0006397; P:mRNA processing; ISO:MGI.
DR GO; GO:0051447; P:negative regulation of meiotic cell cycle; ISO:MGI.
DR GO; GO:1901621; P:negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning; IGI:MGI.
DR GO; GO:0001843; P:neural tube closure; IGI:MGI.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:CAFA.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; IMP:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
DR GO; GO:0006611; P:protein export from nucleus; IMP:MGI.
DR GO; GO:0010737; P:protein kinase A signaling; IBA:GO_Central.
DR GO; GO:1990044; P:protein localization to lipid droplet; IMP:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:2000810; P:regulation of bicellular tight junction assembly; ISO:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:UniProtKB.
DR GO; GO:0043457; P:regulation of cellular respiration; ISO:MGI.
DR GO; GO:0045667; P:regulation of osteoblast differentiation; ISO:MGI.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; ISO:MGI.
DR GO; GO:0070613; P:regulation of protein processing; IGI:MGI.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; ISO:MGI.
DR GO; GO:0048240; P:sperm capacitation; IDA:UniProtKB.
DR GO; GO:0048792; P:spontaneous exocytosis of neurotransmitter; ISO:MGI.
DR CDD; cd14209; STKc_PKA; 1.
DR IDEAL; IID50138; -.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR044109; STKc_PKA.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; cAMP; Cell membrane;
KW Cell projection; Cilium; Cytoplasm; Cytoplasmic vesicle; Flagellum; Kinase;
KW Lipoprotein; Membrane; Mitochondrion; Myristate; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11141074"
FT CHAIN 2..351
FT /note="cAMP-dependent protein kinase catalytic subunit
FT alpha"
FT /id="PRO_0000086053"
FT DOMAIN 44..298
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 299..351
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ACT_SITE 167
FT /note="Proton acceptor"
FT BINDING 50..58
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 122..128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 169..172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 3
FT /note="Deamidated asparagine; partial"
FT /evidence="ECO:0000269|PubMed:11141074"
FT MOD_RES 11
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:11141074,
FT ECO:0000269|PubMed:8395513"
FT MOD_RES 49
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P17612"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22323819,
FT ECO:0000305|PubMed:8395513"
FT MOD_RES 196
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P17612"
FT MOD_RES 198
FT /note="Phosphothreonine; by PDPK1"
FT /evidence="ECO:0000269|PubMed:22323819,
FT ECO:0000269|PubMed:8395513, ECO:0000269|PubMed:9707564"
FT MOD_RES 331
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:21866565"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:8395513"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:11141074"
FT VAR_SEQ 1..15
FT /note="MGNAAAAKKGSEQES -> MASSSND (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10982398"
FT /id="VSP_004760"
FT MUTAGEN 198
FT /note="T->D: No phosphorylation by PDPK1."
FT MUTAGEN 286
FT /note="K->P: Impaired inhibition by the R-subunit."
FT /evidence="ECO:0000269|PubMed:19122195"
FT MUTAGEN 328
FT /note="F->A: Reduced catalytic activity and impaired
FT inhibition by the R-subunit."
FT /evidence="ECO:0000269|PubMed:19122195"
FT CONFLICT 33
FT /note="T -> D (in Ref. 2; AAA39936)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="N -> D (in Ref. 2; AAA39936)"
FT /evidence="ECO:0000305"
FT HELIX 3..7
FT /evidence="ECO:0007829|PDB:4DFX"
FT TURN 9..12
FT /evidence="ECO:0007829|PDB:4DFX"
FT HELIX 16..32
FT /evidence="ECO:0007829|PDB:1RDQ"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:1RDQ"
FT STRAND 44..52
FT /evidence="ECO:0007829|PDB:1RDQ"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:1RDQ"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:1RDQ"
FT STRAND 69..76
FT /evidence="ECO:0007829|PDB:1RDQ"
FT HELIX 77..82
FT /evidence="ECO:0007829|PDB:1RDQ"
FT HELIX 86..96
FT /evidence="ECO:0007829|PDB:1RDQ"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:1RDQ"
FT STRAND 114..122
FT /evidence="ECO:0007829|PDB:1RDQ"
FT HELIX 129..136
FT /evidence="ECO:0007829|PDB:1RDQ"
FT HELIX 141..160
FT /evidence="ECO:0007829|PDB:1RDQ"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:1BKX"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:1RDQ"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:1RDQ"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:1RDQ"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:1RE8"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:6MM6"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:1RDQ"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:1RDQ"
FT HELIX 219..234
FT /evidence="ECO:0007829|PDB:1RDQ"
FT HELIX 244..253
FT /evidence="ECO:0007829|PDB:1RDQ"
FT HELIX 264..273
FT /evidence="ECO:0007829|PDB:1RDQ"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:1RDQ"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:4XW6"
FT TURN 286..289
FT /evidence="ECO:0007829|PDB:1RDQ"
FT HELIX 290..293
FT /evidence="ECO:0007829|PDB:1RDQ"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:1RDQ"
FT HELIX 303..307
FT /evidence="ECO:0007829|PDB:1RDQ"
FT STRAND 321..326
FT /evidence="ECO:0007829|PDB:1REK"
FT TURN 345..350
FT /evidence="ECO:0007829|PDB:1RDQ"
SQ SEQUENCE 351 AA; 40571 MW; 02F85D66EB21A1FA CRC64;
MGNAAAAKKG SEQESVKEFL AKAKEDFLKK WETPSQNTAQ LDQFDRIKTL GTGSFGRVML
VKHKESGNHY AMKILDKQKV VKLKQIEHTL NEKRILQAVN FPFLVKLEFS FKDNSNLYMV
MEYVAGGEMF SHLRRIGRFS EPHARFYAAQ IVLTFEYLHS LDLIYRDLKP ENLLIDQQGY
IQVTDFGFAK RVKGRTWTLC GTPEYLAPEI ILSKGYNKAV DWWALGVLIY EMAAGYPPFF
ADQPIQIYEK IVSGKVRFPS HFSSDLKDLL RNLLQVDLTK RFGNLKNGVN DIKNHKWFAT
TDWIAIYQRK VEAPFIPKFK GPGDTSNFDD YEEEEIRVSI NEKCGKEFTE F
