ID   SHAN1_RAT               Reviewed;        2167 AA.
AC   Q9WV48; Q9QZZ8; Q9WU13; Q9WUE8;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   24-JAN-2024, entry version 206.
DE   RecName: Full=SH3 and multiple ankyrin repeat domains protein 1;
DE            Short=Shank1;
DE   AltName: Full=GKAP/SAPAP-interacting protein;
DE   AltName: Full=SPANK-1;
DE   AltName: Full=Somatostatin receptor-interacting protein;
DE            Short=SSTR-interacting protein;
DE            Short=SSTRIP;
DE   AltName: Full=Synamon;
GN   Name=Shank1;
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 1 AND 3), AND INTERACTION WITH DLGAP1
RP   AND DLG4.
RC   TISSUE=Brain;
RX   PubMed=10488079; DOI=10.1074/jbc.274.39.27463;
RA   Yao I., Hata Y., Hirao K., Deguchi M., Ide N., Takeuchi M., Takai Y.;
RT   "Synamon, a novel neuronal protein interacting with synapse-associated
RT   protein 90/postsynaptic density-95-associated protein.";
RL   J. Biol. Chem. 274:27463-27466(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND INTERACTION WITH DLGAP1.
RC   STRAIN=Sprague-Dawley;
RX   PubMed=10433268; DOI=10.1016/s0896-6273(00)80809-0;
RA   Naisbitt S., Kim E., Tu J.C., Xiao B., Sala C., Valtschanoff J.,
RA   Weinberg R.J., Worley P.F., Sheng M.;
RT   "Shank, a novel family of postsynaptic density proteins that binds to the
RT   NMDA receptor/PSD-95/GKAP complex and cortactin.";
RL   Neuron 23:569-582(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=10958799; DOI=10.1074/jbc.m006448200;
RA   Tobaben S., Suedhof T.C., Stahl B.;
RT   "The G protein-coupled receptor CL1 interacts directly with proteins of the
RT   Shank family.";
RL   J. Biol. Chem. 275:36204-36210(2000).
RN   [4]
RP   PARTIAL NUCLEOTIDE SEQUENCE (ISOFORMS 1; 2; 3; 4 AND 5), AND DEVELOPMENTAL
RP   STAGE.
RC   TISSUE=Brain;
RX   PubMed=10506216; DOI=10.1074/jbc.274.41.29510;
RA   Lim S., Naisbitt S., Yoon J., Hwang J.-I., Suh P.-G., Sheng M., Kim E.;
RT   "Characterization of the shank family of synaptic proteins. Multiple genes,
RT   alternative splicing, and differential expression in brain and
RT   development.";
RL   J. Biol. Chem. 274:29510-29518(1999).
RN   [5]
RP   PARTIAL NUCLEOTIDE SEQUENCE (ISOFORM 4).
RC   TISSUE=Brain;
RX   PubMed=10551867; DOI=10.1074/jbc.274.46.32997;
RA   Zitzer H., Hoenck H.-H., Baechner D., Richter D., Kreienkamp H.-J.;
RT   "Somatostatin receptor interacting protein defines a novel family of
RT   multidomain proteins present in human and rodent brain.";
RL   J. Biol. Chem. 274:32997-33001(1999).
RN   [6]
RP   INTERACTION WITH HOMER1, AND SUBCELLULAR LOCATION.
RX   PubMed=10433269; DOI=10.1016/s0896-6273(00)80810-7;
RA   Tu J.C., Xiao B., Naisbitt S., Yuan J.P., Petralia R.S., Brakeman P.,
RA   Doan A., Aakalu V.K., Lanahan A.A., Sheng M., Worley P.F.;
RT   "Coupling of mGluR/Homer and PSD-95 complexes by the Shank family of
RT   postsynaptic density proteins.";
RL   Neuron 23:583-592(1999).
RN   [7]
RP   INTERACTION WITH SPTAN1.
RX   PubMed=11509555; DOI=10.1074/jbc.m102454200;
RA   Bockers T.M., Mameza M.G., Kreutz M.R., Bockmann J., Weise C., Buck F.,
RA   Richter D., Gundelfinger E.D., Kreienkamp H.-J.;
RT   "Synaptic scaffolding proteins in rat brain. Ankyrin repeats of the
RT   multidomain Shank protein family interact with the cytoskeletal protein
RT   alpha-fodrin.";
RL   J. Biol. Chem. 276:40104-40112(2001).
RN   [8]
RP   INTERACTION WITH SHARPIN.
RX   PubMed=11178875; DOI=10.1006/mcne.2000.0940;
RA   Lim S., Sala C., Yoon J., Park S., Kuroda S., Sheng M., Kim E.;
RT   "Sharpin, a novel postsynaptic density protein that directly interacts with
RT   the shank family of proteins.";
RL   Mol. Cell. Neurosci. 17:385-397(2001).
RN   [9]
RP   FUNCTION.
RX   PubMed=11498055; DOI=10.1016/s0896-6273(01)00339-7;
RA   Sala C., Piech V., Wilson N.R., Passafaro M., Liu G., Sheng M.;
RT   "Regulation of dendritic spine morphology and synaptic function by Shank
RT   and Homer.";
RL   Neuron 31:115-130(2001).
RN   [10]
RP   REVIEW.
RX   PubMed=10806096; DOI=10.1242/jcs.113.11.1851;
RA   Sheng M., Kim E.;
RT   "The Shank family of scaffold proteins.";
RL   J. Cell Sci. 113:1851-1856(2000).
RN   [11]
RP   INTERACTION WITH IGSF9.
RX   PubMed=15340156; DOI=10.1073/pnas.0405371101;
RA   Shi S.-H., Cheng T., Jan L.Y., Jan Y.-N.;
RT   "The immunoglobulin family member dendrite arborization and synapse
RT   maturation 1 (Dasm1) controls excitatory synapse maturation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13346-13351(2004).
RN   [12]
RP   FUNCTION.
RX   PubMed=18287537; DOI=10.1091/mbc.e07-08-0802;
RA   Arstikaitis P., Gauthier-Campbell C., Carolina Gutierrez Herrera R.,
RA   Huang K., Levinson J.N., Murphy T.H., Kilimann M.W., Sala C., Colicos M.A.,
RA   El-Husseini A.;
RT   "Paralemmin-1, a modulator of filopodia induction is required for spine
RT   maturation.";
RL   Mol. Biol. Cell 19:2026-2038(2008).
RN   [13]
RP   INTERACTION WITH HOMER1 AND HOMER3.
RX   PubMed=19345194; DOI=10.1016/j.cell.2009.01.050;
RA   Hayashi M.K., Tang C., Verpelli C., Narayanan R., Stearns M.H., Xu R.M.,
RA   Li H., Sala C., Hayashi Y.;
RT   "The postsynaptic density proteins Homer and Shank form a polymeric network
RT   structure.";
RL   Cell 137:159-171(2009).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540; SER-898; SER-1291 AND
RP   SER-1442, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-638 AND SER-641
RP   (ISOFORM 3), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [15]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 654-762 IN COMPLEX WITH DLGAP1,
RP   AND SUBUNIT.
RX   PubMed=12954649; DOI=10.1074/jbc.m306919200;
RA   Im Y.J., Lee J.H., Park S.H., Park S.J., Rho S.-H., Kang G.B., Kim E.,
RA   Eom S.H.;
RT   "Crystal structure of the Shank PDZ-ligand complex reveals a class I PDZ
RT   interaction and a novel PDZ-PDZ dimerization.";
RL   J. Biol. Chem. 278:48099-48104(2003).
CC   -!- FUNCTION: Seems to be an adapter protein in the postsynaptic density
CC       (PSD) of excitatory synapses that interconnects receptors of the
CC       postsynaptic membrane including NMDA-type and metabotropic glutamate
CC       receptors, and the actin-based cytoskeleton. Plays a role in the
CC       structural and functional organization of the dendritic spine and
CC       synaptic junction. Overexpression promotes maturation of dendritic
CC       spines and the enlargement of spine heads via its ability to recruit
CC       Homer to postsynaptic sites, and enhances presynaptic function.
CC       {ECO:0000269|PubMed:11498055, ECO:0000269|PubMed:18287537}.
CC   -!- SUBUNIT: May homomultimerize via its SAM domain. Interacts with the C-
CC       terminus of SSTR2 via the PDZ domain. Interacts with SHARPIN, SPTAN1
CC       and DLGAP1/GKAP. Part of a complex with DLG4/PSD-95 and DLGAP1/GKAP.
CC       Interacts with BAIAP2 (By similarity). Interacts with IGSF9. Interacts
CC       with HOMER1 and HOMER3 (PubMed:19345194). {ECO:0000250,
CC       ECO:0000269|PubMed:10433268, ECO:0000269|PubMed:10433269,
CC       ECO:0000269|PubMed:10488079, ECO:0000269|PubMed:11178875,
CC       ECO:0000269|PubMed:11509555, ECO:0000269|PubMed:12954649,
CC       ECO:0000269|PubMed:15340156, ECO:0000269|PubMed:19345194}.
CC   -!- INTERACTION:
CC       Q9WV48; P31016: Dlg4; NbExp=3; IntAct=EBI-80909, EBI-375655;
CC       Q9WV48; P97836: Dlgap1; NbExp=7; IntAct=EBI-80909, EBI-80901;
CC       Q9WV48; P97836-5: Dlgap1; NbExp=2; IntAct=EBI-80909, EBI-6269434;
CC       Q9WV48; P21575: Dnm1; NbExp=2; IntAct=EBI-80909, EBI-80070;
CC       Q9WV48; P39052: Dnm2; NbExp=2; IntAct=EBI-80909, EBI-349613;
CC       Q9WV48; Q9Z214-2: Homer1; NbExp=4; IntAct=EBI-80909, EBI-2338999;
CC       Q9WV48; Q9EQL9: Sharpin; NbExp=7; IntAct=EBI-80909, EBI-1394695;
CC       Q9WV48; Q9ES28-2: Arhgef7; Xeno; NbExp=6; IntAct=EBI-80909, EBI-8620514;
CC       Q9WV48; Q61625: Grid2; Xeno; NbExp=5; IntAct=EBI-80909, EBI-2794106;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10433269}. Synapse
CC       {ECO:0000269|PubMed:10433269}. Postsynaptic density
CC       {ECO:0000269|PubMed:10433269}. Note=Colocalizes with alpha-latrotoxin
CC       receptor 1.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=1;
CC         IsoId=Q9WV48-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9WV48-2; Sequence=VSP_006072, VSP_006073;
CC       Name=3;
CC         IsoId=Q9WV48-3; Sequence=VSP_006074;
CC       Name=4; Synonyms=A;
CC         IsoId=Q9WV48-4; Sequence=VSP_006075;
CC       Name=5;
CC         IsoId=Q9WV48-5; Sequence=VSP_006076, VSP_006077;
CC   -!- TISSUE SPECIFICITY: Expressed only in brain (neuropil of cortex, CA1
CC       region hippocampus and molecular layer of cerebellum).
CC   -!- DEVELOPMENTAL STAGE: Expression increases from low levels at birth to
CC       high levels at 3-4 weeks before dropping slightly in adulthood.
CC       Expressed in the cortex and the molecular layer of the cerebellum at
CC       postnatal day 7. Isoform 2 expression does not change during
CC       development of both cortex and cerebellum. Isoform 4 expression
CC       decreases significantly during development of cortex but not
CC       cerebellum. {ECO:0000269|PubMed:10506216}.
CC   -!- SIMILARITY: Belongs to the SHANK family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD29417.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAF02498.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF102855; AAD04569.2; -; mRNA.
DR   EMBL; AF131951; AAD29417.1; ALT_INIT; mRNA.
DR   EMBL; AF159046; AAD42975.1; -; mRNA.
DR   EMBL; AF141904; AAF02498.1; ALT_INIT; mRNA.
DR   RefSeq; NP_113939.2; NM_031751.3. [Q9WV48-1]
DR   RefSeq; XP_017445247.1; XM_017589758.1.
DR   RefSeq; XP_017445248.1; XM_017589759.1.
DR   RefSeq; XP_017445249.1; XM_017589760.1. [Q9WV48-3]
DR   RefSeq; XP_017445250.1; XM_017589761.1. [Q9WV48-5]
DR   PDB; 1Q3O; X-ray; 1.80 A; A/B=654-762.
DR   PDB; 1Q3P; X-ray; 2.25 A; A/B=654-762.
DR   PDB; 3L4F; X-ray; 2.80 A; D=653-765.
DR   PDB; 3QJM; X-ray; 2.31 A; A/B=654-768.
DR   PDB; 3QJN; X-ray; 2.71 A; A/B/C/D/E/F/G/H=654-768.
DR   PDB; 7A9B; X-ray; 2.00 A; A/B=654-763.
DR   PDBsum; 1Q3O; -.
DR   PDBsum; 1Q3P; -.
DR   PDBsum; 3L4F; -.
DR   PDBsum; 3QJM; -.
DR   PDBsum; 3QJN; -.
DR   PDBsum; 7A9B; -.
DR   AlphaFoldDB; Q9WV48; -.
DR   SMR; Q9WV48; -.
DR   BioGRID; 249365; 6.
DR   CORUM; Q9WV48; -.
DR   ELM; Q9WV48; -.
DR   IntAct; Q9WV48; 21.
DR   MINT; Q9WV48; -.
DR   STRING; 10116.ENSRNOP00000026100; -.
DR   GlyGen; Q9WV48; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9WV48; -.
DR   PhosphoSitePlus; Q9WV48; -.
DR   PaxDb; 10116-ENSRNOP00000026100; -.
DR   ABCD; Q9WV48; 3 sequenced antibodies.
DR   Ensembl; ENSRNOT00000026100.6; ENSRNOP00000026100.3; ENSRNOG00000019207.9. [Q9WV48-1]
DR   Ensembl; ENSRNOT00000044257.6; ENSRNOP00000039860.3; ENSRNOG00000019207.9. [Q9WV48-3]
DR   Ensembl; ENSRNOT00000092327.2; ENSRNOP00000075838.1; ENSRNOG00000019207.9. [Q9WV48-4]
DR   Ensembl; ENSRNOT00000104599.1; ENSRNOP00000084101.1; ENSRNOG00000019207.9. [Q9WV48-2]
DR   Ensembl; ENSRNOT00055010800; ENSRNOP00055008384; ENSRNOG00055006632. [Q9WV48-1]
DR   Ensembl; ENSRNOT00060011489; ENSRNOP00060008610; ENSRNOG00060006997. [Q9WV48-1]
DR   Ensembl; ENSRNOT00065053894; ENSRNOP00065044332; ENSRNOG00065031240. [Q9WV48-1]
DR   GeneID; 78957; -.
DR   KEGG; rno:78957; -.
DR   UCSC; RGD:621011; rat. [Q9WV48-1]
DR   AGR; RGD:621011; -.
DR   CTD; 50944; -.
DR   RGD; 621011; Shank1.
DR   eggNOG; KOG0504; Eukaryota.
DR   eggNOG; KOG4375; Eukaryota.
DR   GeneTree; ENSGT00940000153561; -.
DR   HOGENOM; CLU_001824_1_0_1; -.
DR   InParanoid; Q9WV48; -.
DR   OMA; ENCRPTE; -.
DR   OrthoDB; 2247290at2759; -.
DR   PhylomeDB; Q9WV48; -.
DR   Reactome; R-RNO-6794361; Neurexins and neuroligins.
DR   EvolutionaryTrace; Q9WV48; -.
DR   PRO; PR:Q9WV48; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000019207; Expressed in frontal cortex and 4 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0030425; C:dendrite; ISO:RGD.
DR   GO; GO:0043197; C:dendritic spine; IDA:BHF-UCL.
DR   GO; GO:0060076; C:excitatory synapse; ISS:BHF-UCL.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR   GO; GO:0016020; C:membrane; ISO:RGD.
DR   GO; GO:0043005; C:neuron projection; ISS:BHF-UCL.
DR   GO; GO:0005886; C:plasma membrane; ISS:BHF-UCL.
DR   GO; GO:0014069; C:postsynaptic density; IDA:BHF-UCL.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:RGD.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR   GO; GO:0045202; C:synapse; IDA:BHF-UCL.
DR   GO; GO:0071532; F:ankyrin repeat binding; IPI:BHF-UCL.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; IPI:RGD.
DR   GO; GO:0042802; F:identical protein binding; IPI:BHF-UCL.
DR   GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:RGD.
DR   GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR   GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
DR   GO; GO:0017124; F:SH3 domain binding; IPI:BHF-UCL.
DR   GO; GO:0030159; F:signaling receptor complex adaptor activity; IDA:RGD.
DR   GO; GO:0031877; F:somatostatin receptor binding; IPI:UniProtKB.
DR   GO; GO:0098919; F:structural constituent of postsynaptic density; ISO:RGD.
DR   GO; GO:0030160; F:synaptic receptor adaptor activity; IDA:BHF-UCL.
DR   GO; GO:0030534; P:adult behavior; ISO:RGD.
DR   GO; GO:0008306; P:associative learning; ISS:BHF-UCL.
DR   GO; GO:0060997; P:dendritic spine morphogenesis; ISS:BHF-UCL.
DR   GO; GO:0050894; P:determination of affect; ISO:RGD.
DR   GO; GO:0046959; P:habituation; ISS:BHF-UCL.
DR   GO; GO:0007616; P:long-term memory; ISS:BHF-UCL.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR   GO; GO:0032232; P:negative regulation of actin filament bundle assembly; ISS:BHF-UCL.
DR   GO; GO:0050885; P:neuromuscular process controlling balance; ISS:BHF-UCL.
DR   GO; GO:0042048; P:olfactory behavior; ISS:BHF-UCL.
DR   GO; GO:0060999; P:positive regulation of dendritic spine development; IDA:UniProtKB.
DR   GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISS:BHF-UCL.
DR   GO; GO:0035418; P:protein localization to synapse; ISS:BHF-UCL.
DR   GO; GO:0065003; P:protein-containing complex assembly; IDA:BHF-UCL.
DR   GO; GO:2000311; P:regulation of AMPA receptor activity; ISS:BHF-UCL.
DR   GO; GO:0060013; P:righting reflex; ISS:BHF-UCL.
DR   GO; GO:0035176; P:social behavior; ISO:RGD.
DR   GO; GO:0060074; P:synapse maturation; IDA:UniProtKB.
DR   GO; GO:0071625; P:vocalization behavior; ISO:RGD.
DR   CDD; cd17175; FERM_F0_SHANK1; 1.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   CDD; cd09506; SAM_Shank1_2_3; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR041489; PDZ_6.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR24135; SH3 AND MULTIPLE ANKYRIN REPEAT DOMAINS PROTEIN; 1.
DR   PANTHER; PTHR24135:SF3; SH3 AND MULTIPLE ANKYRIN REPEAT DOMAINS PROTEIN 1; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF17820; PDZ_6; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00248; ANK; 6.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00454; SAM; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 3.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   Genevisible; Q9WV48; RN.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ANK repeat; Cytoplasm; Differentiation;
KW   Methylation; Neurogenesis; Phosphoprotein; Reference proteome; Repeat;
KW   SH3 domain; Synapse.
FT   CHAIN           1..2167
FT                   /note="SH3 and multiple ankyrin repeat domains protein 1"
FT                   /id="PRO_0000174672"
FT   REPEAT          195..210
FT                   /note="ANK 1"
FT   REPEAT          212..245
FT                   /note="ANK 2"
FT   REPEAT          246..278
FT                   /note="ANK 3"
FT   REPEAT          279..312
FT                   /note="ANK 4"
FT   REPEAT          313..345
FT                   /note="ANK 5"
FT   REPEAT          346..378
FT                   /note="ANK 6"
FT   REPEAT          379..395
FT                   /note="ANK 7"
FT   DOMAIN          554..613
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          663..757
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          2104..2167
FT                   /note="SAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          413..432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          453..546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          841..894
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          917..1233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1245..1294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1308..1417
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1429..1725
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1740..1787
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1842..1866
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1898..1988
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2002..2029
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        454..495
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        500..514
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        925..946
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        947..981
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1004..1025
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1033..1050
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1066..1088
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1143..1157
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1165..1189
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1205..1224
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1377..1400
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1588..1619
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1622..1639
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1647..1676
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1691..1711
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1846..1862
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1917..1948
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1961..1988
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         43
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:D3YZU1"
FT   MOD_RES         186
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:D3YZU1"
FT   MOD_RES         540
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         544
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:D3YZU1"
FT   MOD_RES         671
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:D3YZU1"
FT   MOD_RES         791
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:D3YZU1"
FT   MOD_RES         898
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         958
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:D3YZU1"
FT   MOD_RES         1059
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:D3YZU1"
FT   MOD_RES         1098
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:D3YZU1"
FT   MOD_RES         1109
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:D3YZU1"
FT   MOD_RES         1257
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:D3YZU1"
FT   MOD_RES         1291
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         1429
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:D3YZU1"
FT   MOD_RES         1442
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         1901
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:D3YZU1"
FT   MOD_RES         2022
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:D3YZU1"
FT   MOD_RES         2042
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:D3YZU1"
FT   MOD_RES         2080
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:D3YZU1"
FT   VAR_SEQ         1..614
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_006072"
FT   VAR_SEQ         615..654
FT                   /note="SQEGRQESRSDKAKRLFRHYTVGSYDSFDAPSLIDGIDSG -> MALSAVGG
FT                   GPGGGALPQPPPALSSSWPALGPRRRSVWYIY (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_006073"
FT   VAR_SEQ         646..654
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:10488079"
FT                   /id="VSP_006074"
FT   VAR_SEQ         797..804
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:10433268"
FT                   /id="VSP_006075"
FT   VAR_SEQ         1930..1943
FT                   /note="LSEDSQTSLLSKPS -> QYRIVVKSSDFGDF (in isoform 5)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_006076"
FT   VAR_SEQ         1944..2167
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_006077"
FT   CONFLICT        1141
FT                   /note="S -> T (in Ref. 1; AAD04569)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1174
FT                   /note="S -> N (in Ref. 2; AAD29417)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1246
FT                   /note="R -> K (in Ref. 1; AAD04569)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1323
FT                   /note="A -> T (in Ref. 1; AAD04569)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1331
FT                   /note="S -> D (in Ref. 1; AAD04569)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1726
FT                   /note="S -> N (in Ref. 2; AAD29417)"
FT                   /evidence="ECO:0000305"
FT   STRAND          657..667
FT                   /evidence="ECO:0007829|PDB:1Q3O"
FT   STRAND          670..672
FT                   /evidence="ECO:0007829|PDB:1Q3P"
FT   STRAND          675..682
FT                   /evidence="ECO:0007829|PDB:1Q3O"
FT   HELIX           685..689
FT                   /evidence="ECO:0007829|PDB:7A9B"
FT   STRAND          694..696
FT                   /evidence="ECO:0007829|PDB:1Q3P"
FT   STRAND          698..705
FT                   /evidence="ECO:0007829|PDB:1Q3O"
FT   HELIX           710..713
FT                   /evidence="ECO:0007829|PDB:1Q3O"
FT   STRAND          721..725
FT                   /evidence="ECO:0007829|PDB:1Q3O"
FT   HELIX           735..744
FT                   /evidence="ECO:0007829|PDB:1Q3O"
FT   TURN            745..747
FT                   /evidence="ECO:0007829|PDB:1Q3O"
FT   STRAND          748..757
FT                   /evidence="ECO:0007829|PDB:1Q3O"
FT   MOD_RES         Q9WV48-3:638
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         Q9WV48-3:641
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   2167 AA;  226335 MW;  3F478B5A7B18BA86 CRC64;
     MTHSPATSED EERHSASECP EGGSESDSSP DGPGRGPQGT RGRGSGAPGN LASTRGLQGR
     SMSVPDDAHF SMMVFRIGIP DLHQTKCLRF NPDATIWTAK QQVLCALSES LQDVLNYGLF
     QPATSGRDAN FLEEERLLRE YPQSFEKGVP YLEFRYKTRV YKQTNLDEKQ LAKLHTKTGL
     KKFLEYVQLG TSDKVARLLD KGLDPNYHDS DSGETPLTLA AQTEGSVEVI RTLCLGGAHI
     DFRARDGMTA LHKAACARHC LALTALLDLG GSPNYKDRRG LTPLFHTAMV GGDPRCCELL
     LYNRAQLGIA DENGWQEIHQ ACQRGHSQHL EHLLFYGAEP GAQNASGNTA LHICALYNKE
     TCARILLYRG ANKDVKNNNG QTPFQVAVIA GNFELGELIR NHREQDVVPF QESPKYAARR
     RGPPGAGLTV PPALLRANSD TSMALPDWMV FSAPGASSSG TPGPTSGPQG QSQPSAPSTK
     LSSGTLRSAS SPRGARARSP SRGRHPEDAK RQPRGRPSSS GTPRDGPAGG TGGSGGPGGS
     LGSRGRRRKL YSAVPGRSFM AVKSYQAQGE GEISLSKGEK IKVLSIGEGG FWEGQVKGRV
     GWFPSDCLEE VANRSQEGRQ ESRSDKAKRL FRHYTVGSYD SFDAPSLIDG IDSGSDYIIK
     EKTVLLQKKD SEGFGFVLRG AKAQTPIEEF TPTPAFPALQ YLESVDEGGV AWRAGLRMGD
     FLIEVNGQNV VKVGHRQVVN MIRQGGNTLM VKVVMVTRHP DMDEAVHKKA SQQAKRLPPP
     AISLRSKSMT SELEEMVSPW KKKIEYEQQP AAVPSMEKKR TVYQMALNKL DEILAAAQQT
     ISASESPGPG GLASLGKHRP KGFFATESSF DPHHRSQPSY DRPSFLPPGP GLMLRQKSIG
     AAEDDRPYLA PPAMKFSRSL SVPGSEDIPP PPTTSPPEPP YSTPPAPSSS GRLTPSPRGG
     PFNPSSGGPL PASSPSSFDG PSPPDTRGGG REKSLYHSAA LPPAHHHPPH HHHHHAPPPQ
     PHHHHAHPPH PPEMETGGSP DDPPPRLALG PQPSLRGWRG GGPSPTSGAP SPSHHSSSGG
     SSGPTQAPAL RYFQLPPRAA SAAMYVPARS GRGRKGPLVK QTKVEGEPQK GSIPSASSPT
     SPALPRSEPP PAGPSEKNSI PIPTIIIKAP STSSSGRSSQ GSSTEAEPPT QPDGAGGGGS
     SPSPAPATSP VPPSPSPVPT PASPSGPATL DFTSQFGAAL VGAARREGGW QNEARRRSTL
     FLSTDAGDED GGDSGLGPGG PPGPRLRHSK SIDEGMFSAE PYLRLESGGS SGGYGAYAAG
     SRAYGGSGSS SAFTSFLPPR PLVHPLTGKA LDPASPLGLA LAARERALKE SSEGGGTPQP
     PPRPPSPRYD APPPTLHHHS PHSPHSPHAR HEPVLRLWGD PARRELGYRA GLGSQEKALT
     ASPPAARRSL LHRLPPTAPG VGPLLLQLGP EPPTPHPGVS KAWRTAAPEE PERLPLHVRF
     LENCQARPPP AGTRGSSTED GPGVPPPSPR RVLPTSPTSP RGNEENGLPL LVLPPPAPSV
     DVDDGEFLFA EPLPPPLEFS NSFEKPESPL TPGPPHPLPD PPSPATPLPA APPPAVAAAP
     PTLDSTASSL TSYDSEVATL TQGAPAAPGD PPAPGPPAPA APAPPAPQPG PDPPPGTDSG
     IEEVDSRSSS DHPLETISSA STLSSLSAEG GGNTGGVAGG GAGVASGTEL LDTYVAYLDG
     QAFGGSGTPG PPYPPQLMTP SKLRGRALGT SGNLRPGPSG GLRDPVTPTS PTVSVTGAGT
     DGLLALSACP GPSTAGVAGG PVAVEPEVPP VPLPAASSLP RKLLPWEEGP GPPPPPLPGP
     LSQPQASALA TVKASIISEL SSKLQQFGGS STAGGALPWA RGGSGGSTDS HHGGASYIPE
     RTSSLQRQRL SEDSQTSLLS KPSSSIFQNW PKPPLPPLPT GSGVSSSTAA APGATSPSAS
     SASASTRHLQ GVEFEMRPPL LRRAPSPSLL PASDHKVSPA PRPSSLPILP SGPIYPGLFD
     IRSSPTGGAG GSTDPFAPVF VPPHPGISGG LGGALSGASR SLSPTRLLSL PPDKPFGAKP
     LGFWTKFDVA DWLEWLGLSE HRAQFLDHEI DGSHLPALTK EDYVDLGVTR VGHRMNIDRA
     LKFFLER
//