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UniProtKB/Swiss-Prot entry Q08499


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PDE4D_HUMAN
Primary accession number Q08499
Secondary accession numbers O43433 Q13549 Q13550 Q13551 Q7Z2L8 Q8IV84 Q8IVA9 Q8IVD2 Q8IVD3 Q96HL4 Q9HCX7
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on December 1, 2000 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 94)
Name and origin of the protein
Protein name cAMP-specific 3',5'-cyclic phosphodiesterase 4D
Synonyms EC 3.1.4.17
DPDE3
PDE43
Gene name
Name: PDE4D
Synonyms: DPDE3
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
PubMed=8413254 [NCBI, ExPASy, EBI, Israel, Japan]
Bolger G., Michaeli T., Martins T., St John T., Steiner B., Rodgers L., Riggs M., Wigler M., Ferguson K.;
"A family of human phosphodiesterases homologous to the dunce learning and memory gene product of Drosophila melanogaster are potential targets for antidepressant drugs.";
Mol. Cell. Biol. 13:6558-6571(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 4 AND 5).
DOI=10.1016/0014-5793(96)00300-6; PubMed=8797812 [NCBI, ExPASy, EBI, Israel, Japan]
Nemoz G., Zhang R.B., Sette C., Conti M.;
"Identification of cyclic AMP-phosphodiesterase variants from the PDE4D gene expressed in human peripheral mononuclear cells.";
FEBS Lett. 384:97-102(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
TISSUE=Heart;
DOI=10.1016/0378-1119(94)90818-4; PubMed=8125310 [NCBI, ExPASy, EBI, Israel, Japan]
Baecker P.A., Obernolte R., Bach C., Yee C., Shelton E.R.;
"Isolation of a cDNA encoding a human rolipram-sensitive cyclic AMP phosphodiesterase (PDE IVD).";
Gene 138:253-256(1994).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6), AND SEQUENCE REVISION (ISOFORM 1).
PubMed=9371713 [NCBI, ExPASy, EBI, Israel, Japan]
Bolger G.B., Erdogan S., Jones R.E., Loughney K., Scotland G., Hoffmann R., Wilkinson I., Farrell C., Houslay M.D.;
"Characterization of five different proteins produced by alternatively spliced mRNAs from the human cAMP-specific phosphodiesterase PDE4D gene.";
Biochem. J. 328:539-548(1997).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), AND ALTERNATIVE SPLICING.
TISSUE=Umbilical vein endothelial cell;
DOI=10.1006/bbrc.2000.3146; PubMed=10913353 [NCBI, ExPASy, EBI, Israel, Japan]
Miro X., Casacuberta J.M., Gutierrez-Lopez M.D., Landazuri M.O., Puigdomenech P.;
"Phosphodiesterases 4D and 7A splice variants in the response of HUVEC cells to TNF-alpha1.";
Biochem. Biophys. Res. Commun. 274:415-421(2000).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 8; 9; 10 AND 11), PHOSPHORYLATION, AND TISSUE SPECIFICITY.
DOI=10.1016/S0898-6568(03)00042-1; PubMed=12834813 [NCBI, ExPASy, EBI, Israel, Japan]
Wang D., Deng C., Bugaj-Gaweda B., Kwan M., Gunwaldsen C., Leonard C., Xin X., Hu Y., Unterbeck A., De Vivo M.;
"Cloning and characterization of novel PDE4D isoforms PDE4D6 and PDE4D7.";
Cell. Signal. 15:883-891(2003).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 10 AND 11), AND INVOLVEMENT IN SUSCEPTIBILITY TO STRK1.
DOI=10.1038/ng1245; PubMed=14517540 [NCBI, ExPASy, EBI, Israel, Japan]
Gretarsdottir S., Thorleifsson G., Reynisdottir S.T., Manolescu A., Jonsdottir S., Jonsdottir T., Gudmundsdottir T., Bjarnadottir S.M., Einarsson O.B., Gudjonsdottir H.M., Hawkins M., Gudmundsson G., Gudmundsdottir H., Andrason H., Gudmundsdottir A.S., Sigurdardottir M., Chou T.T., Nahmias J., Goss S., Sveinbjoernsdottir S., Valdimarsson E.M., Jakobsson F., Agnarsson U., Gudnason V., Thorgeirsson G., Fingerle J., Gurney M., Gudbjartsson D., Frigge M.L., Kong A., Stefansson K., Gulcher J.R.;
"The gene encoding phosphodiesterase 4D confers risk of ischemic stroke.";
Nat. Genet. 35:131-138(2003).
[8]
ERRATUM.
Gretarsdottir S., Thorleifsson G., Reynisdottir S.T., Manolescu A., Jonsdottir S., Jonsdottir T., Gudmundsdottir T., Bjarnadottir S.M., Einarsson O.B., Gudjonsdottir H.M., Hawkins M., Gudmundsson G., Gudmundsdottir H., Andrason H., Gudmundsdottir A.S., Sigurdardottir M., Chou T.T., Nahmias J., Goss S., Sveinbjoernsdottir S., Valdimarsson E.M., Jakobsson F., Agnarsson U., Gudnason V., Thorgeirsson G., Fingerle J., Gurney M., Gudbjartsson D., Frigge M.L., Kong A., Stefansson K., Gulcher J.R.;
Nat. Genet. 37:555-555(2005).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 12).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 8 AND 12).
TISSUE=Brain, and Testis;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
INTERACTION WITH GNB2L1.
PubMed=12193273 [NCBI, ExPASy, EBI, Israel, Japan]
Bolger G.B., McCahill A., Yarwood S.J., Steele M.S., Warwicker J., Houslay M.D.;
"Delineation of RAID1, the RACK1 interaction domain located within the unique N-terminal region of the cAMP-specific phosphodiesterase, PDE4D5.";
BMC Biochem. 3:24-24(2002).
[12]
INTERACTION WITH ARRB2, AND SUBCELLULAR LOCATION.
DOI=10.1074/jbc.M303772200; PubMed=14500724 [NCBI, ExPASy, EBI, Israel, Japan]
Bolger G.B., McCahill A., Huston E., Cheung Y.F., McSorley T., Baillie G.S., Houslay M.D.;
"The unique amino-terminal region of the PDE4D5 cAMP phosphodiesterase isoform confers preferential interaction with beta-arrestins.";
J. Biol. Chem. 278:49230-49238(2003).
[13]
HOMODIMERIZATION OF LONG ISOFORMS, ENZYME REGULATION BY ROLIPRAM AND PHOSPHATIDIC ACID, AND PHOSPHORYLATION AT SER-53 (ISOFORM 2).
DOI=10.1074/jbc.M312687200; PubMed=15131123 [NCBI, ExPASy, EBI, Israel, Japan]
Richter W., Conti M.;
"The oligomerization state determines regulatory properties and inhibitor sensitivity of type 4 cAMP-specific phosphodiesterases.";
J. Biol. Chem. 279:30338-30348(2004).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-51; SER-55 AND SER-59 (ISOFORMS 7/12), AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197 AND SER-202, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[16]
POSSIBLE INVOLVEMENT IN SUSCEPTIBILITY TO STRK1.
DOI=10.1038/ng1006-1091; PubMed=17006457 [NCBI, ExPASy, EBI, Israel, Japan]
Rosand J., Bayley N., Rost N., de Bakker P.I.W.;
"Many hypotheses but no replication for the association between PDE4D and stroke.";
Nat. Genet. 38:1091-1092(2006).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND THR-25, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan]
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-20, AND MASS SPECTROMETRY.
TISSUE=Platelet;
DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan]
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[19]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 388-715 IN COMPLEX WITH THE INHIBITOR ZARDAVERINE AND DIVALENT METAL IONS, AND MUTAGENESIS OF ASP-527 AND ARG-563.
DOI=10.1016/S0014-5793(02)03396-3; PubMed=12387865 [NCBI, ExPASy, EBI, Israel, Japan]
Lee M.E., Markowitz J., Lee J.-O., Lee H.;
"Crystal structure of phosphodiesterase 4D and inhibitor complex.";
FEBS Lett. 530:53-58(2002).
[20]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 381-739 IN COMPLEX WITH CAMP AND DIVALENT METAL IONS.
DOI=10.1021/bi034653e; PubMed=14609333 [NCBI, ExPASy, EBI, Israel, Japan]
Huai Q., Colicelli J., Ke H.;
"The crystal structure of AMP-bound PDE4 suggests a mechanism for phosphodiesterase catalysis.";
Biochemistry 42:13220-13226(2003).
[21]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 381-739 IN COMPLEX WITH INHIBITOR.
DOI=10.1016/S0969-2126(03)00123-0; PubMed=12842049 [NCBI, ExPASy, EBI, Israel, Japan]
Huai Q., Wang H., Sun Y., Kim H.Y., Liu Y., Ke H.;
"Three-dimensional structures of PDE4D in complex with roliprams and implication on inhibitor selectivity.";
Structure 11:865-873(2003).
[22]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 381-714 IN COMPLEX WITH METAL IONS AND INHIBITOR.
DOI=10.1074/jbc.M311556200; PubMed=14668322 [NCBI, ExPASy, EBI, Israel, Japan]
Huai Q., Liu Y., Francis S.H., Corbin J.D., Ke H.;
"Crystal structures of phosphodiesterases 4 and 5 in complex with inhibitor 3-isobutyl-1-methylxanthine suggest a conformation determinant of inhibitor selectivity.";
J. Biol. Chem. 279:13095-13101(2004).
[23]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 380-756 IN COMPLEX WITH AMP; METAL IONS AND THE INHIBITOR ROLIPRAM.
DOI=10.1016/j.jmb.2004.01.040; PubMed=15003452 [NCBI, ExPASy, EBI, Israel, Japan]
Xu R.X., Rocque W.J., Lambert M.H., Vanderwall D.E., Luther M.A., Nolte R.T.;
"Crystal structures of the catalytic domain of phosphodiesterase 4B complexed with AMP, 8-Br-AMP, and rolipram.";
J. Mol. Biol. 337:355-365(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L20970; AAA03592.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L20969; AAC00042.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U02882; AAC13745.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U50157; AAA97890.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U50158; AAA97891.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U50159; AAA97892.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF012074; AAC00070.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF012073; AAC00069.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ250854; CAC03757.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF536975; AAN10117.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF536976; AAN10118.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF536977; AAN10119.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY388960; AAQ90404.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY245866; AAP75760.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY245867; AAP75761.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT007398; AAP36062.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC008390; AAH08390.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC036319; AAH36319.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR I61358; I61358.
RefSeq NP_001098101.1; -.
NP_006194.2; -.
UniGene Hs.117545
3D structure databases
PDB
1E9K; NMR; -; A=276-276.[ExPASy / RCSB / EBI]
1MKD; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J/K/L=388-715.[ExPASy / RCSB / EBI]
1OYN; X-ray; 2.00 A; A/B/C/D=381-740.[ExPASy / RCSB / EBI]
1PTW; X-ray; 2.30 A; A/B/C/D=381-740.[ExPASy / RCSB / EBI]
1Q9M; X-ray; 2.30 A; A/B/C/D=381-740.[ExPASy / RCSB / EBI]
1TB7; X-ray; 1.63 A; A/B=388-715.[ExPASy / RCSB / EBI]
1TBB; X-ray; 1.60 A; A/B=388-715.[ExPASy / RCSB / EBI]
1XOM; X-ray; 1.55 A; A/B=388-715.[ExPASy / RCSB / EBI]
1XON; X-ray; 1.72 A; A/B=388-715.[ExPASy / RCSB / EBI]
1XOQ; X-ray; 1.83 A; A/B=388-715.[ExPASy / RCSB / EBI]
1XOR; X-ray; 1.54 A; A/B=388-715.[ExPASy / RCSB / EBI]
1Y2B; X-ray; 1.40 A; A/B=388-715.[ExPASy / RCSB / EBI]
1Y2C; X-ray; 1.67 A; A/B=388-715.[ExPASy / RCSB / EBI]
1Y2D; X-ray; 1.70 A; A/B=388-715.[ExPASy / RCSB / EBI]
1Y2E; X-ray; 2.10 A; A/B=388-715.[ExPASy / RCSB / EBI]
1Y2K; X-ray; 1.36 A; A/B=388-715.[ExPASy / RCSB / EBI]
1ZKN; X-ray; 2.10 A; A/B/C/D=381-714.[ExPASy / RCSB / EBI]
2FM0; X-ray; 2.00 A; A/B/C/D=381-741.[ExPASy / RCSB / EBI]
2FM5; X-ray; 2.03 A; A/B/C/D=381-741.[ExPASy / RCSB / EBI]
2PW3; X-ray; 1.56 A; A/B=388-714.[ExPASy / RCSB / EBI]
2QYN; X-ray; 1.57 A; A/B=388-715.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1E9K; -.
1MKD; -.
1OYN; -.
1PTW; -.
1Q9M; -.
1TB7; -.
1TBB; -.
1XOM; -.
1XON; -.
1XOQ; -.
1XOR; -.
1Y2B; -.
1Y2C; -.
1Y2D; -.
1Y2E; -.
1Y2K; -.
1ZKN; -.
2FM0; -.
2FM5; -.
2PW3; -.
2QYN; -.
ModBase Q08499.
Protein-protein interaction databases
IntAct Q08499; -.
PTM databases
PhosphoSite Q08499; -.
Organism-specific databases
H-InvDB HIX0024990; -.
HIX0057518; -.
HGNC HGNC:8783; PDE4D.
GenAtlas PDE4D.
MIM 600129; gene. [NCBI / EBI]
606799; phenotype. [NCBI / EBI]
PharmGKB PA33130; -.
GeneCards Q08499.
Gene expression databases
ArrayExpress Q08499; -.
GermOnline ENSG00000113448; Homo sapiens.
Ontologies
GO
GO:0005626; Cellular component: insoluble fraction (traceable author statement from ProtInc).
GO:0005625; Cellular component: soluble fraction (traceable author statement from ProtInc).
GO:0004115; Molecular function: 3',5'-cyclic-AMP phosphodiesterase activity (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR003607; Met-dep_phosphohydro_HD.
IPR002073; PDEase.
Graphical view of domain structure.
Pfam PF00233; PDEase_I; 1.
Pfam graphical view of domain structure.
PRINTS PR00387; PDIESTERASE1.
SMART SM00471; HDc; 1.
SMART graphical view of domain structure.
PROSITE PS00126; PDEASE_I; 1.
BLOCKS Q08499.
Genome annotation databases
Ensembl ENSG00000113448; Homo sapiens. [Contig view]
GeneID 5144; -.
KEGG hsa:5144; -.
Phylogenomic databases
HOVERGEN Q08499; -.
Other
DrugBank DB00131; Adenosine monophosphate.
DB00651; Dyphylline.
SOURCE PDE4D; Homo sapiens.
ProtoNet Q08499.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; cAMP; Cytoplasm; Cytoskeleton; Hydrolase; Membrane; Metal-binding; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   809  809     cAMP-specific 3',5'-cyclic phosphodiesterase 4D. PRO_0000198814
COMPBIAS   42    88  47     Pro-rich. 
METAL   466   466        Divalent metal cation 1. 
METAL   502   502        Divalent metal cation 1. 
METAL   503   503        Divalent metal cation 1. 
METAL   503   503        Divalent metal cation 2. 
METAL   620   620        Divalent metal cation 1. 
BINDING   462   462        cAMP. 
BINDING   620   620        cAMP. 
BINDING   623   623        cAMP. 
BINDING   671   671        cAMP. 
MOD_RES   18    18        Phosphoserine. 
MOD_RES   20    20        Phosphoserine. 
MOD_RES   25    25        Phosphothreonine. 
MOD_RES   197   197        Phosphoserine. 
MOD_RES   202   202        Phosphoserine. 
VAR_SEQ   1   302        Missing (in isoform 5). VSP_004580
VAR_SEQ   1   291        Missing (in isoform 8). VSP_012383
VAR_SEQ   1   269        MEAEGSSAPARAGSGEGSDSAGGATLKAPKHLWRHEQHHQ YPLRQPQFRLLHPHHHLPPPPPPSPQPQPQCPLQPPPPPP LPPPPPPPGAARGRYASSGATGRVRHRGYSDTERYLYCRA MDRTSYAVETGHRPGLKKSRMSWPSSFQGLRRFDVDNGTS AGRSPLDPMTSPGSGLILQANFVHSQRRESFLYRSDSDYD LSPKSMSRNSSIASDIHGDDLIVTPFAQVLASLRTVRNNF AALTNLQDRAPSKRSPMCNQPSINKATIT -> MKEQPSCAGTGHPMAGYGRMAPFELASGPVKRLRTESPF PCLFA (in isoform 4). VSP_004579
VAR_SEQ   1   205        Missing (in isoform 3). VSP_004578
VAR_SEQ   1   152        MEAEGSSAPARAGSGEGSDSAGGATLKAPKHLWRHEQHHQ YPLRQPQFRLLHPHHHLPPPPPPSPQPQPQCPLQPPPPPP LPPPPPPPGAARGRYASSGATGRVRHRGYSDTERYLYCRA MDRTSYAVETGHRPGLKKSRMSWPSSFQGLRR -> MMHVNNFFRRHSWIC (in isoform 2). VSP_004577
VAR_SEQ   1   152        MEAEGSSAPARAGSGEGSDSAGGATLKAPKHLWRHEQHHQ YPLRQPQFRLLHPHHHLPPPPPPSPQPQPQCPLQPPPPPP LPPPPPPPGAARGRYASSGATGRVRHRGYSDTERYLYCRA MDRTSYAVETGHRPGLKKSRMSWPSSFQGLRR -> MAQQTSPDTLTVPEVDNPHCPNPWLNEDLVKSLRENLLQH EKSKTARKSVSPKLSPVISPRNSPRLLRRMLLSSNIPKQR RFTVAHTC (in isoform 6, isoform 7 and isoform 12). VSP_012384
VAR_SEQ   1   130        Missing (in isoform 10). VSP_012385
VAR_SEQ   1   122        Missing (in isoform 9). VSP_012386
VAR_SEQ   1    61        Missing (in isoform 11). VSP_012387
VAR_SEQ   62   152        PPSPQPQPQCPLQPPPPPPLPPPPPPPGAARGRYASSGAT GRVRHRGYSDTERYLYCRAMDRTSYAVETGHRPGLKKSRM SWPSSFQGLRR -> MKRNTCDLLSRSKSASEETLHSSNEEEDPFRGMEPYLVRR LSCRNIQLPPLAFRQLEQADLKSESENIQRPTSLPLKILP LIAITSAESSG (in isoform 11). VSP_012388
VAR_SEQ   123   152        RTSYAVETGHRPGLKKSRMSWPSSFQGLRR -> MAFVWDPLGATVPGPSTRAKSRLRFSKSYS (in isoform 9). VSP_012389
VAR_SEQ   131   152        GHRPGLKKSRMSWPSSFQGLRR -> MSIIMKPRSRSTSSLRTAEAVC (in isoform 10). VSP_012390
VAR_SEQ   270   283        EEAYQKLASETLEE -> GSWMELNPYTLLDM (in isoform 12). VSP_023326
VAR_SEQ   270   279        EEAYQKLASE -> GLYNGIIAFL (in isoform 7). VSP_012391
VAR_SEQ   280   809        Missing (in isoform 7). VSP_012392
VAR_SEQ   284   809        Missing (in isoform 12). VSP_023327
VAR_SEQ   292   306        ETLQTRHSVSEMASN -> MPEANYLLSVSWGYI (in isoform 8). VSP_012393
MUTAGEN   527   527        D->R: Abolishes homodimerization. 
MUTAGEN   563   563        R->D: Abolishes homodimerization. 
CONFLICT   510   510        S -> F (in Ref. 10; AAH36319). 
CONFLICT   549   549        D -> G (in Ref. 6; AAN10119). 
CONFLICT   644   644        R -> P (in Ref. 2). 
CONFLICT   769   769        C -> R (in Ref. 3; AAA97890/AAA97891/AAA97892). 
STRAND   383   386  4      
HELIX   389   397  9      
HELIX   398   400  3      
HELIX   408   414  7      
HELIX   419   430  12      
HELIX   433   436  4      
HELIX   441   453  13      
STRAND   460   463  4      
HELIX