SHAN1_RAT
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 03-AUG-2022, entry version 199.
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=6; IntAct=EBI-80909, EBI-80901;
CC Q9WV48; P97836-5: Dlgap1; NbExp=2; IntAct=EBI-80909, EBI-6269434;
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 -!- 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. [Q9WV48-1]
DR RefSeq; XP_017445248.1; XM_017589759.1. [Q9WV48-4]
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; 18.
DR MINT; Q9WV48; -.
DR STRING; 10116.ENSRNOP00000026100; -.
DR iPTMnet; Q9WV48; -.
DR PhosphoSitePlus; Q9WV48; -.
DR PaxDb; Q9WV48; -.
DR PRIDE; Q9WV48; -.
DR ABCD; Q9WV48; 3 sequenced antibodies.
DR Ensembl; ENSRNOT00000026100; ENSRNOP00000026100; ENSRNOG00000019207. [Q9WV48-1]
DR Ensembl; ENSRNOT00000044257; ENSRNOP00000039860; ENSRNOG00000019207. [Q9WV48-3]
DR Ensembl; ENSRNOT00000092327; ENSRNOP00000075838; ENSRNOG00000019207. [Q9WV48-4]
DR Ensembl; ENSRNOT00000104599; ENSRNOP00000084101; ENSRNOG00000019207. [Q9WV48-2]
DR GeneID; 78957; -.
DR KEGG; rno:78957; -.
DR UCSC; RGD:621011; rat. [Q9WV48-1]
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; DYEPAMG; -.
DR OrthoDB; 468249at2759; -.
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 tissues.
DR Genevisible; Q9WV48; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0042802; F:identical protein binding; IPI:BHF-UCL.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:RGD.
DR GO; GO:0008022; F:protein C-terminus 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: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: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:0099173; P:postsynapse organization; ISO:RGD.
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 Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.30.42.10; -; 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 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; SSF47769; SSF47769; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF50156; SSF50156; 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.
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
