PDE4D_MOUSE
ID PDE4D_MOUSE Reviewed; 747 AA.
AC Q01063; B2KF58; Q6TRH9; Q8C4Q7; Q8CG05;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=cAMP-specific 3',5'-cyclic phosphodiesterase 4D;
DE EC=3.1.4.53;
DE AltName: Full=DPDE3;
GN Name=Pde4d;
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 [MRNA] (ISOFORM 7), AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ;
RX PubMed=12834813; DOI=10.1016/s0898-6568(03)00042-1;
RA Wang D., Deng C., Bugaj-Gaweda B., Kwan M., Gunwaldsen C., Leonard C.,
RA Xin X., Hu Y., Unterbeck A., De Vivo M.;
RT "Cloning and characterization of novel PDE4D isoforms PDE4D6 and PDE4D7.";
RL Cell. Signal. 15:883-891(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 9).
RA Chai H., Gaweda B., De Vivo M., Wang D.;
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 400-514.
RX PubMed=1326532; DOI=10.1016/s0021-9258(19)37015-2;
RA Repaske D.R., Swinnen J.V., Jin S.-L.C., van Wyk J.J., Conti M.;
RT "A polymerase chain reaction strategy to identify and clone cyclic
RT nucleotide phosphodiesterase cDNAs. Molecular cloning of the cDNA encoding
RT the 63-kDa calmodulin-dependent phosphodiesterase.";
RL J. Biol. Chem. 267:18683-18688(1992).
RN [6]
RP INTERACTION WITH SHANK2, AND TISSUE SPECIFICITY.
RX PubMed=17244609; DOI=10.1074/jbc.m610857200;
RA Lee J.H., Richter W., Namkung W., Kim K.H., Kim E., Conti M., Lee M.G.;
RT "Dynamic regulation of cystic fibrosis transmembrane conductance regulator
RT by competitive interactions of molecular adaptors.";
RL J. Biol. Chem. 282:10414-10422(2007).
RN [7]
RP IDENTIFICATION IN A COMPLEX WITH RYR1; FKBP1A; PKA AND PP1.
RX PubMed=18268335; DOI=10.1073/pnas.0711074105;
RA Bellinger A.M., Reiken S., Dura M., Murphy P.W., Deng S.X., Landry D.W.,
RA Nieman D., Lehnart S.E., Samaru M., LaCampagne A., Marks A.R.;
RT "Remodeling of ryanodine receptor complex causes 'leaky' channels: a
RT molecular mechanism for decreased exercise capacity.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2198-2202(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and
RC Spleen;
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).
CC -!- FUNCTION: Hydrolyzes the second messenger cAMP, which is a key
CC regulator of many important physiological processes. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
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:0000250|UniProtKB:Q08499};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25278;
CC Evidence={ECO:0000250|UniProtKB:Q08499};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q08499};
CC Note=Binds 2 divalent metal cations per subunit. Site 1 may
CC preferentially bind zinc ions. {ECO:0000250|UniProtKB:Q08499};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q08499};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q07343};
CC Note=Binds 2 divalent metal cations per subunit. Site 2 has a
CC preference for magnesium and/or manganese ions.
CC {ECO:0000250|UniProtKB:Q08499};
CC -!- ACTIVITY REGULATION: Inhibited by rolipram. Activated by phosphatidic
CC acid (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from
CC 3',5'-cyclic AMP: step 1/1.
CC -!- SUBUNIT: Homodimer for the long isoforms. Isoforms with truncated N-
CC termini are monomeric. Binds ARRB2. Interacts with PDE4DIP (By
CC similarity). Identified in a complex composed of RYR1, PDE4D, PKA,
CC FKBP1A and protein phosphatase 1 (PP1). Interacts (via N-terminal
CC region) with SHANK2 (via proline-rich region); the interaction is
CC increased in a PKA-dependent manner. {ECO:0000250,
CC ECO:0000269|PubMed:17244609, ECO:0000269|PubMed:18268335}.
CC -!- INTERACTION:
CC Q01063; P34971: Adrb1; NbExp=3; IntAct=EBI-7764239, EBI-7764182;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane. Cytoplasm, cytoskeleton.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
CC Apical cell membrane {ECO:0000250}. Note=Colocalized with SHANK2 to the
CC apical membrane of colonic crypt cells (By similarity). Found in the
CC soluble fraction, associated with membranes, and associated with the
CC cytoskeleton and the centrosome. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=7; Synonyms=PDE4D7;
CC IsoId=Q01063-1; Sequence=Displayed;
CC Name=9; Synonyms=PDE4D9;
CC IsoId=Q01063-2; Sequence=VSP_012395, VSP_012396;
CC Name=3;
CC IsoId=Q01063-3; Sequence=VSP_012394, VSP_012397;
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level). Isoform 7 is
CC detected in heart, brain, lung, kidney and testis.
CC {ECO:0000269|PubMed:12834813, ECO:0000269|PubMed:17244609}.
CC -!- INDUCTION: Up-regulated by cAMP and follicle-stimulating hormone.
CC {ECO:0000250}.
CC -!- PTM: Sumoylation of long isoforms by PIAS4 augments their activation by
CC PKA phosphorylation and represses their inhibition by ERK
CC phosphorylation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC PDE4 subfamily. {ECO:0000305}.
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DR EMBL; AF536978; AAN10120.1; -; mRNA.
DR EMBL; AY388962; AAQ90406.1; -; mRNA.
DR EMBL; AK081466; BAC38226.1; -; mRNA.
DR EMBL; CT025605; CAQ51656.1; -; Genomic_DNA.
DR EMBL; AC161585; CAQ51656.1; JOINED; Genomic_DNA.
DR EMBL; AC163650; CAQ51656.1; JOINED; Genomic_DNA.
DR EMBL; M94541; AAA37368.1; ALT_TERM; mRNA.
DR CCDS; CCDS49359.1; -. [Q01063-1]
DR RefSeq; NP_035186.1; NM_011056.3. [Q01063-1]
DR RefSeq; XP_006517710.1; XM_006517647.2. [Q01063-2]
DR AlphaFoldDB; Q01063; -.
DR SMR; Q01063; -.
DR BioGRID; 232023; 3.
DR CORUM; Q01063; -.
DR DIP; DIP-29706N; -.
DR IntAct; Q01063; 6.
DR MINT; Q01063; -.
DR STRING; 10090.ENSMUSP00000112991; -.
DR BindingDB; Q01063; -.
DR ChEMBL; CHEMBL3846; -.
DR iPTMnet; Q01063; -.
DR PhosphoSitePlus; Q01063; -.
DR MaxQB; Q01063; -.
DR PaxDb; Q01063; -.
DR PRIDE; Q01063; -.
DR ProteomicsDB; 287811; -. [Q01063-1]
DR ProteomicsDB; 287812; -. [Q01063-2]
DR ProteomicsDB; 287813; -. [Q01063-3]
DR Antibodypedia; 23607; 487 antibodies from 39 providers.
DR DNASU; 238871; -.
DR Ensembl; ENSMUST00000074103; ENSMUSP00000073742; ENSMUSG00000021699. [Q01063-2]
DR Ensembl; ENSMUST00000120664; ENSMUSP00000113024; ENSMUSG00000021699. [Q01063-3]
DR Ensembl; ENSMUST00000122041; ENSMUSP00000113488; ENSMUSG00000021699. [Q01063-1]
DR Ensembl; ENSMUST00000177907; ENSMUSP00000136485; ENSMUSG00000021699. [Q01063-1]
DR GeneID; 238871; -.
DR KEGG; mmu:238871; -.
DR UCSC; uc007rvg.2; mouse. [Q01063-1]
DR UCSC; uc007rvj.2; mouse. [Q01063-2]
DR CTD; 5144; -.
DR MGI; MGI:99555; Pde4d.
DR VEuPathDB; HostDB:ENSMUSG00000021699; -.
DR eggNOG; KOG3689; Eukaryota.
DR GeneTree; ENSGT00940000155674; -.
DR HOGENOM; CLU_005940_5_2_1; -.
DR InParanoid; Q01063; -.
DR OMA; NKATITX; -.
DR OrthoDB; 1420258at2759; -.
DR PhylomeDB; Q01063; -.
DR BRENDA; 3.1.4.53; 3474.
DR Reactome; R-MMU-180024; DARPP-32 events.
DR Reactome; R-MMU-418555; G alpha (s) signalling events.
DR UniPathway; UPA00762; UER00747.
DR BioGRID-ORCS; 238871; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Pde4d; mouse.
DR PRO; PR:Q01063; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q01063; protein.
DR Bgee; ENSMUSG00000021699; Expressed in hindlimb stylopod muscle and 109 other tissues.
DR ExpressionAtlas; Q01063; baseline and differential.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034704; C:calcium channel complex; IDA:BHF-UCL.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0030016; C:myofibril; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0034705; C:potassium channel complex; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:BHF-UCL.
DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IDA:BHF-UCL.
DR GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IBA:GO_Central.
DR GO; GO:0051117; F:ATPase binding; IPI:BHF-UCL.
DR GO; GO:0031698; F:beta-2 adrenergic receptor binding; ISO:MGI.
DR GO; GO:0030552; F:cAMP binding; ISO:MGI.
DR GO; GO:0004112; F:cyclic-nucleotide phosphodiesterase activity; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:1901363; F:heterocyclic compound binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR GO; GO:0071875; P:adrenergic receptor signaling pathway; ISO:MGI.
DR GO; GO:0007568; P:aging; IMP:MGI.
DR GO; GO:0006198; P:cAMP catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0071320; P:cellular response to cAMP; IDA:MGI.
DR GO; GO:0071872; P:cellular response to epinephrine stimulus; IMP:BHF-UCL.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:MGI.
DR GO; GO:0061028; P:establishment of endothelial barrier; ISS:UniProtKB.
DR GO; GO:0007613; P:memory; ISO:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0043951; P:negative regulation of cAMP-mediated signaling; ISO:MGI.
DR GO; GO:0045822; P:negative regulation of heart contraction; IMP:BHF-UCL.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IMP:BHF-UCL.
DR GO; GO:1901898; P:negative regulation of relaxation of cardiac muscle; IMP:BHF-UCL.
DR GO; GO:0030593; P:neutrophil chemotaxis; IMP:MGI.
DR GO; GO:1990266; P:neutrophil migration; IMP:MGI.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; ISO:MGI.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; ISO:MGI.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; ISO:MGI.
DR GO; GO:0032754; P:positive regulation of interleukin-5 production; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISO:MGI.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
DR GO; GO:0043949; P:regulation of cAMP-mediated signaling; ISO:MGI.
DR GO; GO:0086004; P:regulation of cardiac muscle cell contraction; IMP:BHF-UCL.
DR GO; GO:1901844; P:regulation of cell communication by electrical coupling involved in cardiac conduction; IC:BHF-UCL.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0002027; P:regulation of heart rate; IMP:BHF-UCL.
DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IMP:BHF-UCL.
DR GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; IMP:BHF-UCL.
DR GO; GO:0010469; P:regulation of signaling receptor activity; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0006939; P:smooth muscle contraction; IMP:MGI.
DR GO; GO:0050852; P:T cell receptor signaling pathway; ISO:MGI.
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 PROSITE; PS00126; PDEASE_I_1; 1.
DR PROSITE; PS51845; PDEASE_I_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; cAMP; Cell membrane; Cytoplasm; Cytoskeleton;
KW Hydrolase; Isopeptide bond; Magnesium; Manganese; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Ubl conjugation; Zinc.
FT CHAIN 1..747
FT /note="cAMP-specific 3',5'-cyclic phosphodiesterase 4D"
FT /id="PRO_0000198815"
FT DOMAIN 325..654
FT /note="PDEase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..679
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..737
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 401
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q07343"
FT BINDING 401
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250|UniProtKB:Q08499"
FT BINDING 401
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q08499"
FT BINDING 405
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q08499"
FT BINDING 441
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q08499"
FT BINDING 442
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q08499"
FT BINDING 442
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q08499"
FT BINDING 442
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q07343"
FT BINDING 442
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q08499"
FT BINDING 442
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q08499"
FT BINDING 559
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q08499"
FT BINDING 559
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q08499"
FT BINDING 562
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q08499"
FT BINDING 610
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250|UniProtKB:Q08499"
FT BINDING 610
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q08499"
FT BINDING 613
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250|UniProtKB:Q08499"
FT BINDING 613
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q08499"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08499"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08499"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08499"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08499"
FT CROSSLNK 326
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..163
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012394"
FT VAR_SEQ 1..69
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_012395"
FT VAR_SEQ 70..91
FT /note="RPTSLPLKILPLIAVTSADSSG -> MSIIMKPRSRSTSSLRTTEAVC (in
FT isoform 9)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_012396"
FT VAR_SEQ 164..208
FT /note="PFAQVLASLRTVRNNFAALTNLQDRAPSKRSPMCNQPSINKATIT -> MKE
FT QPSCAGTGHPSMAGYGRMAPFELAGGPVKRLRTESSFPCLFA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012397"
FT CONFLICT 403..404
FT /note="NI -> SR (in Ref. 5; AAA37368)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 747 AA; 84563 MW; 68402163664B3676 CRC64;
MERDTCDVLS RSKSASEETL HSCNEEEDPF RGMEPYLVRR LSSRSIQLPP LAFRQLEQAD
LRSESENIPR PTSLPLKILP LIAVTSADSS GFDVDNGTSA GRSPLDPMTS PGSGLILQAN
FVHSQRRESF LYRSDSDYDL SPKSMSRNSS IASDIHGDDL IVTPFAQVLA SLRTVRNNFA
ALTNLQDRAP SKRSPMCNQP SINKATITEE AYQKLASETL EELDWCLDQL ETLQTRHSVS
EMASNKFKRM LNRELTHLSE MSRSGNQVSE YISNTFLDKQ HEVEIPSPTQ KEKEKKKRPM
SQISGVKKLM HSSSLTNSCI PRFGVKTEQE DVLAKELEDV NKWGLHVFRI AELSGNRPLT
VIMHTIFQER DLLKTFKIPV DTLITYLMTL EDHYHADVAY HNNIHAADVV QSTHVLLSTP
ALEAVFTDLE ILAAIFASAI HDVDHPGVSN QFLINTNSEL ALMYNDSSVL ENHHLAVGFK
LLQEENCDIF QNLTKKQRQS LRKMVIDIVL ATDMSKHMNL LADLKTMVET KKVTSSGVLL
LDNYSDRIQV LQNMVHCADL SNPTKPLQLY RQWTDRIMEE FFRQGDRERE RGMEISPMCD
KHNASVEKSQ VGFIDYIVHP LWETWADLVH PDAQDILDTL EDNREWYQST IPQSPSPAPD
DQEEGRQGQT EKFQFELTLE EDCESDTEKD SGSQVEEDTS CSDSKTLCTQ DSESTEIPLD
EQVEEEAVAE EESQPETCVP DDCCPDT
