PDE4A_RAT
ID PDE4A_RAT Reviewed; 844 AA.
AC P54748; P14645; Q9EQR7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=cAMP-specific 3',5'-cyclic phosphodiesterase 4A;
DE EC=3.1.4.53 {ECO:0000269|PubMed:8557632};
DE AltName: Full=DPDE2;
GN Name=Pde4a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4 AND 5).
RX PubMed=2542942; DOI=10.1073/pnas.86.10.3604;
RA Davis R.L., Takayasu H., Eberwine M., Myres J.;
RT "Cloning and characterization of mammalian homologs of the Drosophila
RT dunce+ gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:3604-3608(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3; 4 AND 5).
RC TISSUE=Brain;
RX PubMed=7958996; DOI=10.1016/0378-1119(94)90155-4;
RA Bolger G.B., Rodgers L., Riggs M.;
RT "Differential CNS expression of alternative mRNA isoforms of the mammalian
RT genes encoding cAMP-specific phosphodiesterases.";
RL Gene 149:237-244(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION (ISOFORM 2), CATALYTIC
RP ACTIVITY (ISOFORM 2), BIOPHYSICOCHEMICAL PROPERTIES (ISOFORM 2), ACTIVITY
RP REGULATION (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2), AND TISSUE
RP SPECIFICITY (ISOFORM 2).
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RX PubMed=8557632; DOI=10.1074/jbc.271.2.1065;
RA Bolger G.B., McPhee I., Houslay M.D.;
RT "Alternative splicing of cAMP-specific phosphodiesterase mRNA transcripts.
RT Characterization of a novel tissue-specific isoform, RNPDE4A8.";
RL J. Biol. Chem. 271:1065-1071(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 319-677 (ISOFORMS 3/4).
RC TISSUE=Testis;
RX PubMed=2546153; DOI=10.1073/pnas.86.14.5325;
RA Swinnen J.V., Joseph D.R., Conti M.;
RT "Molecular cloning of rat homologues of the Drosophila melanogaster dunce
RT cAMP phosphodiesterase: evidence for a family of genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:5325-5329(1989).
RN [5]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
RX PubMed=11306681; DOI=10.1124/mol.59.5.996;
RA Rena G., Begg F., Ross A., MacKenzie C., McPhee I., Campbell L., Huston E.,
RA Sullivan M., Houslay M.D.;
RT "Molecular cloning, genomic positioning, promoter identification, and
RT characterization of the novel cyclic AMP-specific phosphodiesterase
RT PDE4A10.";
RL Mol. Pharmacol. 59:996-1011(2001).
RN [6]
RP FUNCTION (ISOFORM 1), CATALYTIC ACTIVITY (ISOFORM 1), PATHWAY,
RP PHOSPHORYLATION AT SER-147 (ISOFORM 1), AND MUTAGENESIS OF SER-147 AND
RP SER-161.
RX PubMed=21323643; DOI=10.1042/bj20101184;
RA MacKenzie K.F., Wallace D.A., Hill E.V., Anthony D.F., Henderson D.J.,
RA Houslay D.M., Arthur J.S., Baillie G.S., Houslay M.D.;
RT "Phosphorylation of cAMP-specific PDE4A5 (phosphodiesterase-4A5) by MK2
RT (MAPKAPK2) attenuates its activation through protein kinase A
RT phosphorylation.";
RL Biochem. J. 435:755-769(2011).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147; SER-152; SER-672 AND
RP SER-674, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [8]
RP STRUCTURE BY NMR OF 1-26 OF ISOFORM 3.
RX PubMed=8663181; DOI=10.1074/jbc.271.28.16703;
RA Smith K.J., Scotland G., Beattie J., Trayer I.P., Houslay M.D.;
RT "Determination of the structure of the N-terminal splice region of the
RT cyclic AMP-specific phosphodiesterase RD1 (RNPDE4A1) by 1H NMR and
RT identification of the membrane association domain using chimeric
RT constructs.";
RL J. Biol. Chem. 271:16703-16711(1996).
CC -!- FUNCTION: Hydrolyzes the second messenger 3',5'-cyclic AMP (cAMP),
CC which is a key regulator of many important physiological processes.
CC {ECO:0000269|PubMed:21323643, ECO:0000269|PubMed:8557632}.
CC -!- FUNCTION: [Isoform 1]: Efficiently hydrolyzes cAMP.
CC {ECO:0000269|PubMed:21323643}.
CC -!- FUNCTION: [Isoform 2]: Efficiently hydrolyzes cAMP.
CC {ECO:0000269|PubMed:8557632}.
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC Reaction=3',5'-cyclic AMP + H2O = AMP + H(+); Xref=Rhea:RHEA:25277,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58165,
CC ChEBI:CHEBI:456215; EC=3.1.4.53;
CC Evidence={ECO:0000269|PubMed:21323643};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25278;
CC Evidence={ECO:0000305|PubMed:21323643};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
CC Reaction=3',5'-cyclic AMP + H2O = AMP + H(+); Xref=Rhea:RHEA:25277,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58165,
CC ChEBI:CHEBI:456215; EC=3.1.4.53;
CC Evidence={ECO:0000269|PubMed:8557632};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25278;
CC Evidence={ECO:0000305|PubMed:8557632};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P27815};
CC Note=Binds 2 divalent metal cations per subunit. Site 1 may
CC preferentially bind zinc ions. {ECO:0000250|UniProtKB:P27815};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P27815};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q07343};
CC Note=Binds 2 divalent metal cations per subunit (By similarity). Site 2
CC has a preference for magnesium and/or manganese ions (By similarity).
CC {ECO:0000250|UniProtKB:P27815, ECO:0000250|UniProtKB:Q07343};
CC -!- ACTIVITY REGULATION: [Isoform 2]: Inhibited by rolipram.
CC {ECO:0000269|PubMed:8557632}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform 2]:
CC Kinetic parameters:
CC KM=5.4 uM for cAMP {ECO:0000269|PubMed:8557632};
CC -!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from
CC 3',5'-cyclic AMP: step 1/1. {ECO:0000305|PubMed:21323643}.
CC -!- SUBUNIT: Interacts with LYN (via SH3 domain). Interacts with ARRB2.
CC {ECO:0000250|UniProtKB:P27815}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytosol
CC {ECO:0000269|PubMed:8557632}. Membrane; Peripheral membrane protein
CC {ECO:0000269|PubMed:8557632}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=PDE4A5 {ECO:0000303|PubMed:21323643};
CC IsoId=P54748-1; Sequence=Displayed;
CC Name=2; Synonyms=PDE4A8;
CC IsoId=P54748-2; Sequence=VSP_004565;
CC Name=3;
CC IsoId=P54748-3; Sequence=VSP_004566, VSP_004567;
CC Name=4; Synonyms=Medium;
CC IsoId=P54748-4; Sequence=VSP_004568;
CC Name=5; Synonyms=Short;
CC IsoId=P54748-5; Sequence=VSP_004569, VSP_004570;
CC Name=6; Synonyms=PDE4A10;
CC IsoId=P54748-6; Sequence=VSP_038187;
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Isoform 2 is testis specific.
CC {ECO:0000269|PubMed:8557632}.
CC -!- PTM: [Isoform 1]: Phosphorylated by MAPKAPK2 at Ser-147; it counteracts
CC PKA-induced activation of PDE4A and modulates intracellular cAMP
CC levels. Likely involved in cellular desensitization to cAMP signaling.
CC {ECO:0000269|PubMed:21323643}.
CC -!- PTM: Proteolytically cleaved by CASP3. {ECO:0000250|UniProtKB:P27815}.
CC -!- MISCELLANEOUS: [Isoform 6]: Incomplete sequence. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC PDE4 subfamily. {ECO:0000305}.
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DR EMBL; L27057; AAC27098.1; -; mRNA.
DR EMBL; L36467; AAB00357.1; -; mRNA.
DR EMBL; L27062; AAA56859.1; -; mRNA.
DR EMBL; M25348; AAA41848.1; -; mRNA.
DR EMBL; M28411; AAA41823.1; -; mRNA.
DR EMBL; M26715; AAC37699.1; -; mRNA.
DR EMBL; M26716; AAA41101.1; -; mRNA.
DR EMBL; M26717; AAA41102.1; -; mRNA.
DR EMBL; AF110461; AAF14352.2; -; mRNA.
DR PIR; I53865; I53865.
DR PIR; I67946; I67946.
DR RefSeq; NP_037233.3; NM_013101.3. [P54748-1]
DR PDB; 1LOI; NMR; -; A=1-25.
DR PDBsum; 1LOI; -.
DR AlphaFoldDB; P54748; -.
DR SMR; P54748; -.
DR BioGRID; 247667; 4.
DR IntAct; P54748; 1.
DR STRING; 10116.ENSRNOP00000057815; -.
DR BindingDB; P54748; -.
DR ChEMBL; CHEMBL4964; -.
DR DrugCentral; P54748; -.
DR iPTMnet; P54748; -.
DR PhosphoSitePlus; P54748; -.
DR PaxDb; P54748; -.
DR PRIDE; P54748; -.
DR GeneID; 25638; -.
DR KEGG; rno:25638; -.
DR UCSC; RGD:3279; rat. [P54748-1]
DR CTD; 5141; -.
DR RGD; 3279; Pde4a.
DR eggNOG; KOG3689; Eukaryota.
DR InParanoid; P54748; -.
DR OrthoDB; 904682at2759; -.
DR PhylomeDB; P54748; -.
DR BRENDA; 3.1.4.53; 5301.
DR Reactome; R-RNO-180024; DARPP-32 events.
DR Reactome; R-RNO-418555; G alpha (s) signalling events.
DR UniPathway; UPA00762; UER00747.
DR EvolutionaryTrace; P54748; -.
DR PRO; PR:P54748; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IMP:SynGO.
DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IDA:UniProtKB.
DR GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IBA:GO_Central.
DR GO; GO:0030552; F:cAMP binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006198; P:cAMP catabolic process; IDA:UniProtKB.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISO:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IMP:SynGO.
DR GO; GO:0106070; P:regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0010738; P:regulation of protein kinase A signaling; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0007608; P:sensory perception of smell; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd00077; HDc; 1.
DR Gene3D; 1.10.1300.10; -; 1.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR040844; PDE4_UCR.
DR InterPro; IPR023088; PDEase.
DR InterPro; IPR002073; PDEase_catalytic_dom.
DR InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR InterPro; IPR023174; PDEase_CS.
DR Pfam; PF18100; PDE4_UCR; 1.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00471; HDc; 1.
DR PROSITE; PS00126; PDEASE_I_1; 1.
DR PROSITE; PS51845; PDEASE_I_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; cAMP; Cytoplasm; Hydrolase;
KW Isopeptide bond; Magnesium; Manganese; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Ubl conjugation; Zinc.
FT CHAIN 1..844
FT /note="cAMP-specific 3',5'-cyclic phosphodiesterase 4A"
FT /id="PRO_0000198808"
FT DOMAIN 343..672
FT /note="PDEase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT REGION 1..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 419
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q07343"
FT BINDING 419
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250|UniProtKB:Q08499"
FT BINDING 419
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q07343"
FT BINDING 423
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q07343"
FT BINDING 423
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P27815"
FT BINDING 459
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P27815"
FT BINDING 460
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q07343"
FT BINDING 460
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P27815"
FT BINDING 460
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q07343"
FT BINDING 460
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P27815"
FT BINDING 460
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q07343"
FT BINDING 577
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q07343"
FT BINDING 577
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P27815"
FT BINDING 628
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250|UniProtKB:Q08499"
FT BINDING 628
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q07343"
FT BINDING 631
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250|UniProtKB:Q08499"
FT BINDING 631
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q07343"
FT SITE 69..70
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250|UniProtKB:P27815"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27815"
FT MOD_RES 147
FT /note="Phosphoserine; by MAPKAPK2"
FT /evidence="ECO:0000269|PubMed:21323643,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27815"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27815"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27815"
FT MOD_RES 672
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 674
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CROSSLNK 344
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..318
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:2542942,
FT ECO:0000303|PubMed:7958996"
FT /id="VSP_004569"
FT VAR_SEQ 1..259
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:2542942,
FT ECO:0000303|PubMed:7958996"
FT /id="VSP_004568"
FT VAR_SEQ 1..234
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:2542942,
FT ECO:0000303|PubMed:7958996"
FT /id="VSP_004566"
FT VAR_SEQ 1..102
FT /note="MEPPAAPSERSLSLSLPGPREGQATLKPPPQHLWRQPRTPIRIQQRGYPDSA
FT ERSETERSPHRPIERADAVDTGDRPGLRTTRMSWPSSFHGTGTGGGSSRR -> MPSRK
FT RLTLPRIFIVRKNGNS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8557632"
FT /id="VSP_004565"
FT VAR_SEQ 1..102
FT /note="MEPPAAPSERSLSLSLPGPREGQATLKPPPQHLWRQPRTPIRIQQRGYPDSA
FT ERSETERSPHRPIERADAVDTGDRPGLRTTRMSWPSSFHGTGTGGGSSRR -> ALPLG
FT PESLTHFSFSEEDTLRHPPGRCVS (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_038187"
FT VAR_SEQ 235..256
FT /note="WCLEQLETMQTYRSVSEMASHK -> MPLVDFFCETCSKPWLVGWWDQ (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:2542942,
FT ECO:0000303|PubMed:7958996"
FT /id="VSP_004567"
FT VAR_SEQ 354..386
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:2542942,
FT ECO:0000303|PubMed:7958996"
FT /id="VSP_004570"
FT MUTAGEN 147
FT /note="S->A: Abolishes phosphorylation by MAPKAPK2."
FT /evidence="ECO:0000269|PubMed:21323643"
FT MUTAGEN 161
FT /note="S->A: Does not affect phosphorylation by MAPKAPK2."
FT /evidence="ECO:0000269|PubMed:21323643"
FT CONFLICT 130
FT /note="A -> R (in Ref. 5; AAF14352)"
FT /evidence="ECO:0000305"
FT CONFLICT 465..466
FT /note="GV -> AL (in Ref. 4; AAA41848/AAA41823)"
FT /evidence="ECO:0000305"
FT CONFLICT 603..604
FT /note="GD -> AH (in Ref. 4; AAA41848/AAA41823)"
FT /evidence="ECO:0000305"
FT CONFLICT 833
FT /note="A -> T (in Ref. 1; AAC37699/AAA41101/AAA41102 and 5;
FT AAF14352)"
FT /evidence="ECO:0000305"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:1LOI"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:1LOI"
FT HELIX 20..23
FT /evidence="ECO:0007829|PDB:1LOI"
SQ SEQUENCE 844 AA; 93439 MW; 1A5F5101E4DBF1B6 CRC64;
MEPPAAPSER SLSLSLPGPR EGQATLKPPP QHLWRQPRTP IRIQQRGYPD SAERSETERS
PHRPIERADA VDTGDRPGLR TTRMSWPSSF HGTGTGGGSS RRLEAENGPT PSPGRSPLDS
QASPGLVLHA GATTSQRRES FLYRSDSDYD MSPKAVSRSS SVASEAHAED LIVTPFAQVL
ASLRSVRSNF SLLTNVPIPS NKRSPLGGPP SVCKATLSEE TCQQLARETL EELDWCLEQL
ETMQTYRSVS EMASHKFKRM LNRELTHLSE MSRSGNQVSE YISNTFLDKQ NEVEIPSPTP
RQRAFQQPPP SVLRQSQPMS QITGLKKLVH TGSLNTNVPR FGVKTDQEDL LAQELENLSK
WGLNIFCVSE YAGGRSLSCI MYTIFQERDL LKKFHIPVDT MMMYMLTLED HYHADVAYHN
SLHAADVLQS THVLLATPAL DAVFTDLEIL AALFAAAIHD VDHPGVSNQF LINTNSELAL
MYNDESVLEN HHLAVGFKLL QEENCDIFQN LSKRQRQSLR KMVIDMVLAT DMSKHMTLLA
DLKTMVETKK VTSSGVLLLD NYSDRIQVLR NMVHCADLSN PTKPLELYRQ WTDRIMAEFF
QQGDRERERG MEISPMCDKH TASVEKSQVG FIDYIVHPLW ETWADLVHPD AQDILDTLED
NRDWYHSAIR QSPSPPLEEE PGGLGHPSLP DKFQFELTLE EEEEEDSLEV PGLPTTEETF
LAAEDARAQA VDWSKVKGPS TTVVEVAERL KQETASAYGA PQESMEAVGC SFSPGTPILP
DVRTLSSSEE APGLLGLPST AAEVEAPRDH LAATRACSAC SGTSGDNSAI ISAPGRWGSG
GDPA
