ID   PDE4B_RAT               Reviewed;         736 AA.
AC   P14646; Q5RKL0; Q8VD81; Q8VD82;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 4.
DT   27-MAR-2024, entry version 171.
DE   RecName: Full=3',5'-cyclic-AMP phosphodiesterase 4B {ECO:0000305};
DE            EC=3.1.4.53 {ECO:0000269|PubMed:12441002};
DE   AltName: Full=DPDE4;
DE   AltName: Full=cAMP-specific phosphodiesterase 4B {ECO:0000305};
GN   Name=Pde4b {ECO:0000312|RGD:3280};
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] (ISOFORM 2), AND INDUCTION.
RC   TISSUE=Sertoli cell;
RX   PubMed=1655746; DOI=10.1016/s0021-9258(18)55280-7;
RA   Swinnen J.V., Tsikalas K.E., Conti M.;
RT   "Properties and hormonal regulation of two structurally related cAMP
RT   phosphodiesterases from the rat Sertoli cell.";
RL   J. Biol. Chem. 266:18370-18377(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
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).
RC   STRAIN=Wistar;
RX   PubMed=8276818; DOI=10.1016/s0021-9258(17)42355-6;
RA   Monaco L., Vicini E., Conti M.;
RT   "Structure of two rat genes coding for closely related rolipram-sensitive
RT   cAMP phosphodiesterases. Multiple mRNA variants originate from alternative
RT   splicing and multiple start sites.";
RL   J. Biol. Chem. 269:347-357(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC   TISSUE=Olfactory bulb;
RX   PubMed=9371714; DOI=10.1042/bj3280549;
RA   Huston E., Lumb S., Russell A., Catterall C., Ross A.H., Steele M.R.,
RA   Bolger G.B., Perry M.J., Owens R.J., Houslay M.D.;
RT   "Molecular cloning and transient expression in COS7 cells of a novel human
RT   PDE4B cAMP-specific phosphodiesterase, HSPDE4B3.";
RL   Biochem. J. 328:549-558(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4), BIOPHYSICOCHEMICAL
RP   PROPERTIES, PHOSPHORYLATION AT SER-56 (ISOFORM 4), TISSUE SPECIFICITY,
RP   CATALYTIC ACTIVITY, AND FUNCTION.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain cortex;
RX   PubMed=12441002; DOI=10.1042/bj20021082;
RA   Shepherd M., McSorley T., Olsen A.E., Johnston L.A., Thomson N.C.,
RA   Baillie G.S., Houslay M.D., Bolger G.B.;
RT   "Molecular cloning and subcellular distribution of the novel PDE4B4 cAMP-
RT   specific phosphodiesterase isoform.";
RL   Biochem. J. 370:429-438(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC   TISSUE=Heart;
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   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 175-736.
RC   TISSUE=Brain;
RX   PubMed=2542941; DOI=10.1073/pnas.86.10.3599;
RA   Colicelli J., Birchmeier C., Michaeli T., O'Neill K., Riggs M., Wigler M.;
RT   "Isolation and characterization of a mammalian gene encoding a high-
RT   affinity cAMP phosphodiesterase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:3599-3603(1989).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 304-663.
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   [9]
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=19103603; DOI=10.1074/jbc.m808394200;
RA   Bailey M.J., Coon S.L., Carter D.A., Humphries A., Kim J.S., Shi Q.,
RA   Gaildrat P., Morin F., Ganguly S., Hogenesch J.B., Weller J.L., Rath M.F.,
RA   Moller M., Baler R., Sugden D., Rangel Z.G., Munson P.J., Klein D.C.;
RT   "Night/day changes in pineal expression of >600 genes: central role of
RT   adrenergic/cAMP signaling.";
RL   J. Biol. Chem. 284:7606-7622(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290; SER-659 AND SER-661, AND
RP   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).
CC   -!- FUNCTION: Hydrolyzes the second messenger cAMP, which is a key
CC       regulator of many important physiological processes.
CC       {ECO:0000269|PubMed:12441002}.
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:0000269|PubMed:12441002};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25278;
CC         Evidence={ECO:0000305|PubMed:12441002};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q07343};
CC       Note=Binds 2 divalent metal cations per subunit. Site 1 may
CC       preferentially bind zinc ions. {ECO:0000250|UniProtKB:Q07343};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q07343};
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:Q07343};
CC   -!- ACTIVITY REGULATION: Inhibited by rolipram.
CC       {ECO:0000250|UniProtKB:Q07343}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform 4]:
CC       Kinetic parameters:
CC         KM=5.4 uM for cAMP {ECO:0000269|PubMed:12441002};
CC         Note=Vmax values for isoforms 2, 3 and 4 relative to isoform 1 are
CC         3.8, 1.6 and 2.1. {ECO:0000269|PubMed:12441002};
CC   -!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from
CC       3',5'-cyclic AMP: step 1/1. {ECO:0000305|PubMed:12441002}.
CC   -!- SUBUNIT: [Isoform 5]: Interacts with DISC1.
CC       {ECO:0000250|UniProtKB:Q07343}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm
CC       {ECO:0000250|UniProtKB:Q07343}. Cell membrane
CC       {ECO:0000250|UniProtKB:Q07343}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1; Synonyms=PDE4B1 {ECO:0000303|PubMed:12441002};
CC         IsoId=P14646-3; Sequence=Displayed;
CC       Name=2; Synonyms=PDE4B2 {ECO:0000303|PubMed:12441002};
CC         IsoId=P14646-2; Sequence=VSP_026678, VSP_004573;
CC       Name=3; Synonyms=PDE4B3 {ECO:0000303|PubMed:12441002};
CC         IsoId=P14646-1; Sequence=VSP_026679;
CC       Name=4; Synonyms=PDE4B4 {ECO:0000303|PubMed:12441002};
CC         IsoId=P14646-4; Sequence=VSP_026680;
CC       Name=5;
CC         IsoId=P14646-5; Sequence=VSP_026679, VSP_026681;
CC   -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12441002,
CC       ECO:0000269|PubMed:19103603}.
CC   -!- TISSUE SPECIFICITY: [Isoform 3]: Expressed in brain, heart, lung and
CC       liver. {ECO:0000269|PubMed:12441002}.
CC   -!- TISSUE SPECIFICITY: [Isoform 4]: Expressed in liver and brain.
CC       {ECO:0000269|PubMed:12441002}.
CC   -!- INDUCTION: In Sertoli cells, induced by FSH. In the pineal gland,
CC       exhibits night/day variations with a 7-fold increased expression at
CC       night. Up-regulation is due to a large degree to the release of
CC       norepinephrine from nerve terminals in the pineal gland and cAMP
CC       signaling pathway. {ECO:0000269|PubMed:1655746,
CC       ECO:0000269|PubMed:19103603}.
CC   -!- MISCELLANEOUS: [Isoform 4]: Activated by phosphorylation at Ser-56.
CC       Mutagenesis of Ser-56 abolishes activation. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC       PDE4 subfamily. {ECO:0000305}.
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DR   EMBL; L27058; AAA74478.1; -; mRNA.
DR   EMBL; U01291; AAA18926.1; -; Unassigned_DNA.
DR   EMBL; U01289; AAA18926.1; JOINED; Unassigned_DNA.
DR   EMBL; U01293; AAA18926.1; JOINED; Unassigned_DNA.
DR   EMBL; U01294; AAA18926.1; JOINED; Unassigned_DNA.
DR   EMBL; U01295; AAA18926.1; JOINED; Unassigned_DNA.
DR   EMBL; U01296; AAA18926.1; JOINED; Unassigned_DNA.
DR   EMBL; U01297; AAA18926.1; JOINED; Unassigned_DNA.
DR   EMBL; U01298; AAA18926.1; JOINED; Unassigned_DNA.
DR   EMBL; U01290; AAA18926.1; JOINED; Unassigned_DNA.
DR   EMBL; U95748; AAB96560.1; -; mRNA.
DR   EMBL; AF202732; AAL31763.1; -; mRNA.
DR   EMBL; AF202733; AAL31764.1; -; mRNA.
DR   EMBL; BC085704; AAH85704.1; -; mRNA.
DR   EMBL; J04563; AAA66039.1; -; mRNA.
DR   EMBL; M25350; AAA41846.1; -; mRNA.
DR   EMBL; M28413; AAA41824.1; -; mRNA.
DR   PIR; A40949; A40949.
DR   PIR; I59143; I59143.
DR   RefSeq; NP_058727.2; NM_017031.2.
DR   AlphaFoldDB; P14646; -.
DR   SMR; P14646; -.
DR   BioGRID; 246764; 2.
DR   STRING; 10116.ENSRNOP00000008278; -.
DR   BindingDB; P14646; -.
DR   ChEMBL; CHEMBL3382; -.
DR   DrugCentral; P14646; -.
DR   iPTMnet; P14646; -.
DR   PhosphoSitePlus; P14646; -.
DR   PaxDb; 10116-ENSRNOP00000007738; -.
DR   GeneID; 24626; -.
DR   KEGG; rno:24626; -.
DR   UCSC; RGD:3280; rat. [P14646-3]
DR   AGR; RGD:3280; -.
DR   CTD; 5142; -.
DR   RGD; 3280; Pde4b.
DR   VEuPathDB; HostDB:ENSRNOG00000005905; -.
DR   eggNOG; KOG3689; Eukaryota.
DR   InParanoid; P14646; -.
DR   OrthoDB; 240889at2759; -.
DR   PhylomeDB; P14646; -.
DR   TreeFam; TF314638; -.
DR   BRENDA; 3.1.4.53; 5301.
DR   Reactome; R-RNO-180024; DARPP-32 events.
DR   SABIO-RK; P14646; -.
DR   UniPathway; UPA00762; UER00747.
DR   PRO; PR:P14646; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Bgee; ENSRNOG00000005905; Expressed in frontal cortex and 20 other cell types or tissues.
DR   ExpressionAtlas; P14646; baseline and differential.
DR   GO; GO:0071944; C:cell periphery; ISO:RGD.
DR   GO; GO:0005813; C:centrosome; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
DR   GO; GO:0043197; C:dendritic spine; ISO:RGD.
DR   GO; GO:0060076; C:excitatory synapse; ISO:RGD.
DR   GO; GO:0000930; C:gamma-tubulin complex; ISO:RGD.
DR   GO; GO:0016020; C:membrane; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR   GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR   GO; GO:0008021; C:synaptic vesicle; ISO:RGD.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; ISO:RGD.
DR   GO; GO:0030018; C:Z disc; ISO:RGD.
DR   GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IDA:RGD.
DR   GO; GO:0005246; F:calcium channel regulator activity; ISO:RGD.
DR   GO; GO:0030552; F:cAMP binding; ISO:RGD.
DR   GO; GO:0043015; F:gamma-tubulin binding; ISO:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0044325; F:transmembrane transporter binding; ISO:RGD.
DR   GO; GO:0006198; P:cAMP catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0071872; P:cellular response to epinephrine stimulus; ISO:RGD.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:RGD.
DR   GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISO:RGD.
DR   GO; GO:0050900; P:leukocyte migration; ISO:RGD.
DR   GO; GO:0071878; P:negative regulation of adenylate cyclase-activating adrenergic receptor signaling pathway; ISO:RGD.
DR   GO; GO:1901898; P:negative regulation of relaxation of cardiac muscle; ISO:RGD.
DR   GO; GO:0030593; P:neutrophil chemotaxis; ISO:RGD.
DR   GO; GO:0001780; P:neutrophil homeostasis; ISO:RGD.
DR   GO; GO:0032743; P:positive regulation of interleukin-2 production; ISO:RGD.
DR   GO; GO:0032729; P:positive regulation of type II interferon production; ISO:RGD.
DR   GO; GO:1902514; P:regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; ISO:RGD.
DR   GO; GO:0086004; P:regulation of cardiac muscle cell contraction; ISO:RGD.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; ISO:RGD.
DR   CDD; cd00077; HDc; 1.
DR   Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 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   PANTHER; PTHR11347:SF108; CAMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE 4B; 1.
DR   PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR   Pfam; PF18100; PDE4_UCR; 1.
DR   Pfam; PF00233; PDEase_I; 1.
DR   PRINTS; PR00387; PDIESTERASE1.
DR   SMART; SM00471; HDc; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
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; Hydrolase; Magnesium;
KW   Manganese; Membrane; Metal-binding; Phosphoprotein; Reference proteome;
KW   Zinc.
FT   CHAIN           1..736
FT                   /note="3',5'-cyclic-AMP phosphodiesterase 4B"
FT                   /id="PRO_0000198810"
FT   DOMAIN          330..659
FT                   /note="PDEase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT   REGION          51..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          96..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          685..736
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        713..736
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        406
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q07343"
FT   BINDING         406
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /evidence="ECO:0000250|UniProtKB:Q08499"
FT   BINDING         406
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:Q07343"
FT   BINDING         410
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:Q07343"
FT   BINDING         410
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q07343"
FT   BINDING         446
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q07343"
FT   BINDING         447
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:Q07343"
FT   BINDING         447
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q07343"
FT   BINDING         447
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:Q07343"
FT   BINDING         447
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q07343"
FT   BINDING         447
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q07343"
FT   BINDING         564
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:Q07343"
FT   BINDING         564
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q07343"
FT   BINDING         615
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /evidence="ECO:0000250|UniProtKB:Q08499"
FT   BINDING         615
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:Q07343"
FT   BINDING         618
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /evidence="ECO:0000250|UniProtKB:Q08499"
FT   BINDING         618
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:Q07343"
FT   MOD_RES         290
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         659
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         661
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   VAR_SEQ         1..172
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:1655746,
FT                   ECO:0000303|PubMed:7958996, ECO:0000303|PubMed:8276818"
FT                   /id="VSP_026678"
FT   VAR_SEQ         1..93
FT                   /note="MKKSRSVMAVTADDNLKDYFECSLSKSYSSSSYTLGIDLWRGRRCCSGNLQL
FT                   PPLSQRQSERARTPEGDGISRPTTLPLTTLPSIAITTVSQE -> MTAKNSSKELPASE
FT                   SEVCIKTFKEQMRLELELPKLPGNRPTSPKISPRSSPRNSPCFFRKLLVNKSIRQRRRF
FT                   TVAHT (in isoform 3 and isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:9371714"
FT                   /id="VSP_026679"
FT   VAR_SEQ         1..93
FT                   /note="MKKSRSVMAVTADDNLKDYFECSLSKSYSSSSYTLGIDLWRGRRCCSGNLQL
FT                   PPLSQRQSERARTPEGDGISRPTTLPLTTLPSIAITTVSQE -> MLHVNDLPPPRRHS
FT                   WI (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:12441002"
FT                   /id="VSP_026680"
FT   VAR_SEQ         173..211
FT                   /note="LASLRIVRNNFTLLTNLHGAPNKRSPAASQAPVTRVSLQ -> MKEQGGTVS
FT                   GAGSSRGGGDSAMASLQPLQPNYLSVCLFA (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:1655746,
FT                   ECO:0000303|PubMed:7958996, ECO:0000303|PubMed:8276818"
FT                   /id="VSP_004573"
FT   VAR_SEQ         710..736
FT                   /note="VIDPENRDSLEETDIDIATEDKSLIDT -> KPCHAANGLALPVGGGNAAST
FT                   QPRCGHV (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_026681"
FT   CONFLICT        178
FT                   /note="I -> S (in Ref. 5; AAL31763/AAL31764 and 6;
FT                   AAH85704)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        531
FT                   /note="T -> S (in Ref. 3; AAA18926)"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         P14646-4:56
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:12441002"
SQ   SEQUENCE   736 AA;  83375 MW;  C48F576EFA8DF498 CRC64;
     MKKSRSVMAV TADDNLKDYF ECSLSKSYSS SSYTLGIDLW RGRRCCSGNL QLPPLSQRQS
     ERARTPEGDG ISRPTTLPLT TLPSIAITTV SQECFDVENG PSPGRSPLDP QASSSSGLVL
     HAAFPGHSQR RESFLYRSDS DYDLSPKAMS RNSSLPSEQH GDDLIVTPFA QVLASLRIVR
     NNFTLLTNLH GAPNKRSPAA SQAPVTRVSL QEESYQKLAM ETLEELDWCL DQLETIQTYR
     SVSEMASNKF KRMLNRELTH LSEMSRSGNQ VSEYISNTFL DKQNDVEIPS PTQKDREKKK
     KQQLMTQISG VKKLMHSSSL NNTSISRFGV NTENEDHLAK ELEDLNKWGL NIFNVAGYSH
     NRPLTCIMYA IFQERDLLKT FKISSDTFVT YMMTLEDHYH SDVAYHNSLH AADVAQSTHV
     LLSTPALDAV FTDLEILAAI FAAAIHDVDH PGVSNQFLIN TNSELALMYN DESVLENHHL
     AVGFKLLQEE HCDIFQNLTK KQRQTLRKMV IDMVLATDMS KHMSLLADLK TMVETKKVTS
     SGVLLLDNYT DRIQVLRNMV HCADLSNPTK SLELYRQWTD RIMEEFFQQG DKERERGMEI
     SPMCDKHTAS VEKSQVGFID YIVHPLWETW ADLVQPDAQD ILDTLEDNRN WYQSMIPQSP
     SPPLDERSRD CQGLMEKFQF ELTLEEEDSE GPEKEGEGPN YFSSTKTLCV IDPENRDSLE
     ETDIDIATED KSLIDT
//