SHAN3_MOUSE
ID SHAN3_MOUSE Reviewed; 1730 AA.
AC Q4ACU6; F8S0X0; F8S0X2; F8S0X3; F8S0X5; F8S0X6; Q69ZD8; Q9JJZ3; S6BMD3;
AC S6CCV8;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=SH3 and multiple ankyrin repeat domains protein 3;
DE Short=Shank3;
DE AltName: Full=Proline-rich synapse-associated protein 2;
DE Short=ProSAP2;
DE AltName: Full=SPANK-2;
GN Name=Shank3; Synonyms=Kiaa1650, Prosap2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=C57B16/J; TISSUE=Kidney;
RA Dehmelt L., Nalbant P., Werner A.;
RT "Interaction of the Na+/Phosphate cotransporter type II with rSHANK.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH GRIA1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=16606358; DOI=10.1111/j.1471-4159.2006.03831.x;
RA Uchino S., Wada H., Honda S., Nakamura Y., Ondo Y., Uchiyama T.,
RA Tsutsumi M., Suzuki E., Hirasawa T., Kohsaka S.;
RT "Direct interaction of post-synaptic density-95/Dlg/ZO-1 domain-containing
RT synaptic molecule Shank3 with GluR1 alpha-amino-3-hydroxy-5-methyl-4-
RT isoxazole propionic acid receptor.";
RL J. Neurochem. 97:1203-1214(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), ALTERNATIVE SPLICING,
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=24164323; DOI=10.1111/jnc.12505;
RA Waga C., Asano H., Sanagi T., Suzuki E., Nakamura Y., Tsuchiya A., Itoh M.,
RA Goto Y.I., Kohsaka S., Uchino S.;
RT "Identification of two novel Shank3 transcripts in the developing mouse
RT neocortex.";
RL J. Neurochem. 128:280-293(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 875-1730.
RC TISSUE=Brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [6]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 6; 7; 8 AND 9), ALTERNATIVE
RP SPLICING, FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND
RP INTERACTION WITH HOMER1.
RX PubMed=21558424; DOI=10.1093/hmg/ddr212;
RA Wang X., McCoy P.A., Rodriguiz R.M., Pan Y., Je H.S., Roberts A.C.,
RA Kim C.J., Berrios J., Colvin J.S., Bousquet-Moore D., Lorenzo I., Wu G.,
RA Weinberg R.J., Ehlers M.D., Philpot B.D., Beaudet A.L., Wetsel W.C.,
RA Jiang Y.H.;
RT "Synaptic dysfunction and abnormal behaviors in mice lacking major isoforms
RT of Shank3.";
RL Hum. Mol. Genet. 20:3093-3108(2011).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1634, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-122 AND TYR-555, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373; SER-375; SER-387;
RP SER-694; SER-781; SER-790; SER-801; SER-890; SER-897; SER-995; THR-1130;
RP SER-1134; SER-1159; SER-1166; THR-1234; SER-1510; SER-1521; SER-1529;
RP SER-1539; SER-1634 AND SER-1636, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP ALTERNATIVE PROMOTER USAGE.
RX PubMed=20613842; DOI=10.1038/nature09165;
RA Maunakea A.K., Nagarajan R.P., Bilenky M., Ballinger T.J., D'Souza C.,
RA Fouse S.D., Johnson B.E., Hong C., Nielsen C., Zhao Y., Turecki G.,
RA Delaney A., Varhol R., Thiessen N., Shchors K., Heine V.M., Rowitch D.H.,
RA Xing X., Fiore C., Schillebeeckx M., Jones S.J., Haussler D., Marra M.A.,
RA Hirst M., Wang T., Costello J.F.;
RT "Conserved role of intragenic DNA methylation in regulating alternative
RT promoters.";
RL Nature 466:253-257(2010).
RN [12]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=21423165; DOI=10.1038/nature09965;
RA Peca J., Feliciano C., Ting J.T., Wang W., Wells M.F., Venkatraman T.N.,
RA Lascola C.D., Fu Z., Feng G.;
RT "Shank3 mutant mice display autistic-like behaviours and striatal
RT dysfunction.";
RL Nature 472:437-442(2011).
RN [13]
RP DISRUPTION PHENOTYPE.
RX PubMed=22699619; DOI=10.1038/nature11015;
RA Schmeisser M.J., Ey E., Wegener S., Bockmann J., Stempel A.V., Kuebler A.,
RA Janssen A.L., Udvardi P.T., Shiban E., Spilker C., Balschun D.,
RA Skryabin B.V., Dieck S.T., Smalla K.H., Montag D., Leblond C.S., Faure P.,
RA Torquet N., Le Sourd A.M., Toro R., Grabrucker A.M., Shoichet S.A.,
RA Schmitz D., Kreutz M.R., Bourgeron T., Gundelfinger E.D., Boeckers T.M.;
RT "Autistic-like behaviours and hyperactivity in mice lacking
RT ProSAP1/Shank2.";
RL Nature 486:256-260(2012).
RN [14]
RP FUNCTION IN AMPA RECEPTOR SIGNALING, AND INTERACTION WITH ARHGAP44.
RX PubMed=23739967; DOI=10.1523/jneurosci.2725-12.2013;
RA Raynaud F., Janossy A., Dahl J., Bertaso F., Perroy J., Varrault A.,
RA Vidal M., Worley P.F., Boeckers T.M., Bockaert J., Marin P., Fagni L.,
RA Homburger V.;
RT "Shank3-Rich2 interaction regulates AMPA receptor recycling and synaptic
RT long-term potentiation.";
RL J. Neurosci. 33:9699-9715(2013).
RN [15]
RP DISRUPTION PHENOTYPE.
RX PubMed=24259569; DOI=10.1523/jneurosci.3017-13.2013;
RA Kouser M., Speed H.E., Dewey C.M., Reimers J.M., Widman A.J., Gupta N.,
RA Liu S., Jaramillo T.C., Bangash M., Xiao B., Worley P.F., Powell C.M.;
RT "Loss of predominant shank3 isoforms results in hippocampus-dependent
RT impairments in behavior and synaptic transmission.";
RL J. Neurosci. 33:18448-18468(2013).
RN [16]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, ACTIN-BINDING, AND
RP INTERACTION WITH ARPC2; CYFIP2; DLG4; GKAP1; HOMER1 AND SLC17A7.
RX PubMed=24153177; DOI=10.1038/nature12630;
RA Han K., Holder J.L. Jr., Schaaf C.P., Lu H., Chen H., Kang H., Tang J.,
RA Wu Z., Hao S., Cheung S.W., Yu P., Sun H., Breman A.M., Patel A., Lu H.C.,
RA Zoghbi H.Y.;
RT "SHANK3 overexpression causes manic-like behaviour with unique
RT pharmacogenetic properties.";
RL Nature 503:72-77(2013).
RN [17]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-965, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [18]
RP INTERACTION WITH DIP2A.
RX PubMed=31600191; DOI=10.1371/journal.pbio.3000461;
RA Ma J., Zhang L.Q., He Z.X., He X.X., Wang Y.J., Jian Y.L., Wang X.,
RA Zhang B.B., Su C., Lu J., Huang B.Q., Zhang Y., Wang G.Y., Guo W.X.,
RA Qiu D.L., Mei L., Xiong W.C., Zheng Y.W., Zhu X.J.;
RT "Autism candidate gene DIP2A regulates spine morphogenesis via acetylation
RT of cortactin.";
RL PLoS Biol. 17:e3000461-e3000461(2019).
CC -!- FUNCTION: Major scaffold postsynaptic density protein which interacts
CC with multiple proteins and complexes to orchestrate the dendritic spine
CC and synapse formation, maturation and maintenance. Interconnects
CC receptors of the postsynaptic membrane including NMDA-type and
CC metabotropic glutamate receptors via complexes with GKAP/PSD-95 and
CC HOMER, respectively, and the actin-based cytoskeleton. Plays a role in
CC the structural and functional organization of the dendritic spine and
CC synaptic junction through the interaction with Arp2/3 and WAVE1 complex
CC as well as the promotion of the F-actin clusters. By way of this
CC control of actin dynamics, participates in the regulation of developing
CC neurons growth cone motility and the NMDA receptor-signaling. Also
CC modulates GRIA1 exocytosis and GRM5/MGLUR5 expression and signaling to
CC control the AMPA and metabotropic glutamate receptor-mediated synaptic
CC transmission and plasticity. May be required at an early stage of
CC synapse formation and be inhibited by IGF1 to promote synapse
CC maturation. {ECO:0000269|PubMed:21423165, ECO:0000269|PubMed:21558424,
CC ECO:0000269|PubMed:23739967, ECO:0000269|PubMed:24153177}.
CC -!- SUBUNIT: May homomultimerize via its SAM domain. Interacts with BAIAP2,
CC DBNL and SLC17A7/VGLUT1. Interacts with DLGAP1/GKAP, GRM1/MGLUR1,
CC GRM5/MGLUR5 and LZTS3 C-termini via its PDZ domain. Interacts with
CC ABI1, HOMER1, HOMER2, HOMER3 and CTTN/cortactin SH3 domain. Is part of
CC a complex with DLG4/PSD-95 and DLGAP1/GKAP. Interacts (via PDZ domain)
CC with the GRIA1 subunit of the AMPA receptor (via PDZ-binding motif).
CC Interacts with WASF1 and CYFIP2; the interactions mediate the
CC association of SHANK3 with the WAVE1 complex. Interacts with ARPC2; the
CC interaction probably mediates the association of SHANK3 with the Arp2/3
CC complex. Interacts (via ANK repeats) with SHARPIN and SPTAN1. Interacts
CC (via PDZ domain) with ARHGAP44 (probably via PDZ-binding motif); the
CC interaction takes place in dendritic spines and promotes GRIA1
CC exocytosis. Interacts with CAMK2A (By similarity). Interacts with DIP2A
CC (PubMed:31600191). {ECO:0000250|UniProtKB:Q9BYB0,
CC ECO:0000269|PubMed:16606358, ECO:0000269|PubMed:21558424,
CC ECO:0000269|PubMed:23739967, ECO:0000269|PubMed:24153177,
CC ECO:0000269|PubMed:31600191}.
CC -!- INTERACTION:
CC Q4ACU6; Q8BKX1: Baiap2; NbExp=6; IntAct=EBI-771450, EBI-771498;
CC Q4ACU6; Q5SQX6: Cyfip2; NbExp=3; IntAct=EBI-771450, EBI-773783;
CC Q4ACU6; Q91XM9: Dlg2; NbExp=4; IntAct=EBI-771450, EBI-400138;
CC Q4ACU6; Q9D415: Dlgap1; NbExp=4; IntAct=EBI-771450, EBI-400152;
CC Q4ACU6; Q9Z2Y3: Homer1; NbExp=8; IntAct=EBI-771450, EBI-396980;
CC Q4ACU6-1; O60741: HCN1; Xeno; NbExp=4; IntAct=EBI-16201983, EBI-11173743;
CC Q4ACU6-1; Q9UL51: HCN2; Xeno; NbExp=3; IntAct=EBI-16201983, EBI-1751885;
CC Q4ACU6-1; Q9P1Z3: HCN3; Xeno; NbExp=3; IntAct=EBI-16201983, EBI-11178054;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Synapse. Postsynaptic density. Cell
CC projection, dendritic spine {ECO:0000250}. Note=In neuronal cells,
CC extends into the region subjacent to the postsynaptic density (PSD).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=10;
CC Comment=Additional isoform seem to exist. These isoforms may be the
CC product of multiple intragenic promoter and/or alternative splicing.
CC {ECO:0000269|PubMed:21558424, ECO:0000269|PubMed:24164323};
CC Name=1; Synonyms=A, Alpha;
CC IsoId=Q4ACU6-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=Q4ACU6-2; Sequence=VSP_053612, VSP_053613, VSP_053614,
CC VSP_053615;
CC Name=4; Synonyms=C3, Beta;
CC IsoId=Q4ACU6-3; Sequence=VSP_053611;
CC Name=5; Synonyms=C4;
CC IsoId=Q4ACU6-6; Sequence=VSP_053611, VSP_053614, VSP_053615;
CC Name=6; Synonyms=D1;
CC IsoId=Q4ACU6-7; Sequence=VSP_053609;
CC Name=7; Synonyms=D2;
CC IsoId=Q4ACU6-8; Sequence=VSP_053608;
CC Name=8; Synonyms=E1;
CC IsoId=Q4ACU6-9; Sequence=VSP_053607;
CC Name=9; Synonyms=E2;
CC IsoId=Q4ACU6-10; Sequence=VSP_053607, VSP_053613;
CC Name=3; Synonyms=C1;
CC IsoId=Q4ACU6-11; Sequence=VSP_053610;
CC Name=10; Synonyms=F;
CC IsoId=Q4ACU6-12; Sequence=VSP_053606;
CC -!- TISSUE SPECIFICITY: In brain, highly expressed in striatum, thalamus,
CC hippocampus and granule cells of the cerebellum.
CC {ECO:0000269|PubMed:21423165, ECO:0000269|PubMed:21558424,
CC ECO:0000269|PubMed:24153177}.
CC -!- DEVELOPMENTAL STAGE: Isoform 3 is weakly expressed at 17 dpc but its
CC expression increases after birth. {ECO:0000269|PubMed:24164323}.
CC -!- DOMAIN: In isoform 1, the N-terminal region preceding the ANK repeats
CC interacts with the 6 ANK repeats in an intramolecular manner, thereby
CC restricting access to ligands, such as SHARPIN and SPTAN1.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Animals deficient for isoforms 1-7 exhibit self-
CC injourious repetitive grooming and deficits in social interaction. They
CC show defects at striatal synapses and cortico-striatal circuits with an
CC increase in striatal volume, dendritic length, and surface area and a
CC decrease of spine density, length and thickness of PSD. They seem to
CC have an altered molecular composition of postsynaptic machinery in the
CC striatum (PubMed:21423165). In contrast, animals deficient for isoforms
CC 1 and 2 exhibit a normal initiation of social interaction with a
CC perturbed recognition of social novelty (PubMed:21423165). In
CC PubMed:21558424, animals deficient for isoforms 1 and 2 show abnormal
CC social behaviors, communication patterns, repetitive behaviors,
CC learning and memory. In CA1 hippocampus, the synaptic plasticity is
CC impaired with longer dendritic spines, decreased spine density and
CC deficient long-term potentiation. The expression of specific synaptic
CC scaffolding proteins and receptor subunits are altered. Animals
CC deficient for isoforms 1-5 exhibit self-injourious repetitive grooming,
CC brain-region-specific up-regulation of ionotropic glutamate receptors
CC and increased levels of SHANK2 (PubMed:22699619). Animals deficient for
CC predominant isoforms containing exon 21 exhibit motor-coordination
CC deficits, hypersensitivity to heat, novelty avoidance, altered
CC locomotor response to novelty and minimal social abnormalities. They
CC show a decrease in NMDA-AMPA excitatory postsynaptic current ratio in
CC hippocampal CA1, reduced long-term potentiation and deficits in
CC hippocampus-dependent spatial learning and memory (PubMed:24259569).
CC {ECO:0000269|PubMed:21423165, ECO:0000269|PubMed:21558424,
CC ECO:0000269|PubMed:22699619, ECO:0000269|PubMed:24259569}.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative promoter usage and
CC alternative splicing. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative splicing of isoform
CC 3. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: Produced by alternative splicing of isoform
CC 3. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 6]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 7]: Produced by alternative splicing of isoform
CC 6. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 8]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 9]: Produced by alternative splicing of isoform
CC 8. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 10]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SHANK family. {ECO:0000305}.
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DR EMBL; AJ245904; CAB89816.1; -; mRNA.
DR EMBL; AB841411; BAN67189.1; -; mRNA.
DR EMBL; AB841412; BAN67190.1; -; mRNA.
DR EMBL; AC122401; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC137513; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB231013; BAE16756.1; -; mRNA.
DR EMBL; AK173228; BAD32506.1; -; mRNA.
DR EMBL; HQ405757; AEB77764.1; -; mRNA.
DR EMBL; HQ405758; AEB77765.1; -; mRNA.
DR EMBL; HQ405759; AEB77766.1; -; mRNA.
DR EMBL; HQ405760; AEB77767.1; -; mRNA.
DR EMBL; HQ405761; AEB77768.1; -; mRNA.
DR EMBL; HQ405762; AEB77769.1; -; mRNA.
DR EMBL; HQ405763; AEB77770.1; -; mRNA.
DR RefSeq; NP_067398.2; NM_021423.3.
DR PDB; 3O5N; X-ray; 1.83 A; A/B/C/D/E/F/G/H=562-669.
DR PDB; 5IZU; X-ray; 2.49 A; A/C=533-665.
DR PDB; 6KYH; X-ray; 3.30 A; A/B/C/D=8-362.
DR PDB; 6KYK; X-ray; 2.82 A; A/B=1-368.
DR PDBsum; 3O5N; -.
DR PDBsum; 5IZU; -.
DR PDBsum; 6KYH; -.
DR PDBsum; 6KYK; -.
DR AlphaFoldDB; Q4ACU6; -.
DR SMR; Q4ACU6; -.
DR BioGRID; 208407; 262.
DR DIP; DIP-32262N; -.
DR IntAct; Q4ACU6; 436.
DR MINT; Q4ACU6; -.
DR STRING; 10090.ENSMUSP00000104932; -.
DR iPTMnet; Q4ACU6; -.
DR PhosphoSitePlus; Q4ACU6; -.
DR SwissPalm; Q4ACU6; -.
DR jPOST; Q4ACU6; -.
DR MaxQB; Q4ACU6; -.
DR PaxDb; Q4ACU6; -.
DR PeptideAtlas; Q4ACU6; -.
DR PRIDE; Q4ACU6; -.
DR ProteomicsDB; 261215; -. [Q4ACU6-1]
DR ProteomicsDB; 261216; -. [Q4ACU6-2]
DR ProteomicsDB; 261217; -. [Q4ACU6-3]
DR ProteomicsDB; 261218; -. [Q4ACU6-6]
DR ProteomicsDB; 261219; -. [Q4ACU6-7]
DR ProteomicsDB; 261220; -. [Q4ACU6-8]
DR ProteomicsDB; 261221; -. [Q4ACU6-9]
DR ProteomicsDB; 261222; -. [Q4ACU6-10]
DR ProteomicsDB; 261223; -. [Q4ACU6-11]
DR ProteomicsDB; 261224; -. [Q4ACU6-12]
DR ABCD; Q4ACU6; 4 sequenced antibodies.
DR Antibodypedia; 47836; 153 antibodies from 18 providers.
DR DNASU; 58234; -.
DR Ensembl; ENSMUST00000109309; ENSMUSP00000104932; ENSMUSG00000022623. [Q4ACU6-1]
DR Ensembl; ENSMUST00000230807; ENSMUSP00000155608; ENSMUSG00000022623. [Q4ACU6-6]
DR GeneID; 58234; -.
DR KEGG; mmu:58234; -.
DR UCSC; uc007xha.2; mouse. [Q4ACU6-1]
DR UCSC; uc007xhb.2; mouse. [Q4ACU6-2]
DR UCSC; uc033gwe.1; mouse. [Q4ACU6-3]
DR UCSC; uc033gwf.1; mouse. [Q4ACU6-6]
DR UCSC; uc056zac.1; mouse. [Q4ACU6-10]
DR CTD; 85358; -.
DR MGI; MGI:1930016; Shank3.
DR VEuPathDB; HostDB:ENSMUSG00000022623; -.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG4375; Eukaryota.
DR GeneTree; ENSGT00940000153561; -.
DR HOGENOM; CLU_001824_2_0_1; -.
DR InParanoid; Q4ACU6; -.
DR OMA; HYRNHAV; -.
DR OrthoDB; 98033at2759; -.
DR PhylomeDB; Q4ACU6; -.
DR TreeFam; TF324593; -.
DR Reactome; R-MMU-6794361; Neurexins and neuroligins.
DR Reactome; R-MMU-8853659; RET signaling.
DR BioGRID-ORCS; 58234; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Shank3; mouse.
DR EvolutionaryTrace; Q4ACU6; -.
DR PRO; PR:Q4ACU6; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q4ACU6; protein.
DR Bgee; ENSMUSG00000022623; Expressed in medial dorsal nucleus of thalamus and 198 other tissues.
DR ExpressionAtlas; Q4ACU6; baseline and differential.
DR Genevisible; Q4ACU6; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0060170; C:ciliary membrane; ISS:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0060076; C:excitatory synapse; IC:BHF-UCL.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:BHF-UCL.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0043005; C:neuron projection; IDA:BHF-UCL.
DR GO; GO:0044309; C:neuron spine; IDA:BHF-UCL.
DR GO; GO:0014069; C:postsynaptic density; ISS:BHF-UCL.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:BHF-UCL.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:BHF-UCL.
DR GO; GO:0043621; F:protein self-association; ISS:BHF-UCL.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
DR GO; GO:0017124; F:SH3 domain binding; ISS:BHF-UCL.
DR GO; GO:0098919; F:structural constituent of postsynaptic density; IDA:SynGO.
DR GO; GO:0030160; F:synaptic receptor adaptor activity; ISS:BHF-UCL.
DR GO; GO:0008270; F:zinc ion binding; ISS:BHF-UCL.
DR GO; GO:0030534; P:adult behavior; ISO:MGI.
DR GO; GO:0097113; P:AMPA glutamate receptor clustering; IMP:BHF-UCL.
DR GO; GO:0008306; P:associative learning; IMP:MGI.
DR GO; GO:0048854; P:brain morphogenesis; IMP:BHF-UCL.
DR GO; GO:0060997; P:dendritic spine morphogenesis; IMP:BHF-UCL.
DR GO; GO:0001838; P:embryonic epithelial tube formation; IGI:MGI.
DR GO; GO:0035640; P:exploration behavior; IMP:CACAO.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0014009; P:glial cell proliferation; IMP:MGI.
DR GO; GO:0097117; P:guanylate kinase-associated protein clustering; IMP:BHF-UCL.
DR GO; GO:0007612; P:learning; IMP:BHF-UCL.
DR GO; GO:0007611; P:learning or memory; IMP:MGI.
DR GO; GO:0040011; P:locomotion; IMP:CACAO.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0035641; P:locomotory exploration behavior; IMP:BHF-UCL.
DR GO; GO:0060292; P:long-term synaptic depression; IMP:CACAO.
DR GO; GO:0060291; P:long-term synaptic potentiation; IMP:CACAO.
DR GO; GO:0000165; P:MAPK cascade; IGI:MGI.
DR GO; GO:0007613; P:memory; IMP:BHF-UCL.
DR GO; GO:0032232; P:negative regulation of actin filament bundle assembly; IDA:MGI.
DR GO; GO:0045794; P:negative regulation of cell volume; IMP:BHF-UCL.
DR GO; GO:0061351; P:neural precursor cell proliferation; IMP:MGI.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IMP:BHF-UCL.
DR GO; GO:0097114; P:NMDA glutamate receptor clustering; IMP:BHF-UCL.
DR GO; GO:2000969; P:positive regulation of AMPA receptor activity; IMP:BHF-UCL.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; IMP:BHF-UCL.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IMP:BHF-UCL.
DR GO; GO:1900451; P:positive regulation of glutamate receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0048170; P:positive regulation of long-term neuronal synaptic plasticity; IMP:BHF-UCL.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IMP:BHF-UCL.
DR GO; GO:0051835; P:positive regulation of synapse structural plasticity; IMP:BHF-UCL.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IMP:BHF-UCL.
DR GO; GO:0097107; P:postsynaptic density assembly; IMP:BHF-UCL.
DR GO; GO:1904717; P:regulation of AMPA glutamate receptor clustering; IMP:MGI.
DR GO; GO:2000822; P:regulation of behavioral fear response; IMP:BHF-UCL.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; IMP:BHF-UCL.
DR GO; GO:2000821; P:regulation of grooming behavior; IMP:BHF-UCL.
DR GO; GO:1900452; P:regulation of long-term synaptic depression; IMP:BHF-UCL.
DR GO; GO:1900271; P:regulation of long-term synaptic potentiation; IMP:BHF-UCL.
DR GO; GO:0050807; P:regulation of synapse organization; ISO:MGI.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IMP:MGI.
DR GO; GO:0097396; P:response to interleukin-17; IMP:MGI.
DR GO; GO:0035176; P:social behavior; IMP:BHF-UCL.
DR GO; GO:0021773; P:striatal medium spiny neuron differentiation; IMP:BHF-UCL.
DR GO; GO:0007416; P:synapse assembly; IMP:BHF-UCL.
DR GO; GO:0042297; P:vocal learning; ISO:MGI.
DR GO; GO:0071625; P:vocalization behavior; IMP:BHF-UCL.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 1.25.40.20; -; 2.
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; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF00536; SAM_1; 1.
DR Pfam; PF07653; SH3_2; 1.
DR SMART; SM00248; ANK; 5.
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; 4.
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; Actin-binding; Alternative promoter usage;
KW Alternative splicing; ANK repeat; Cell projection; Coiled coil; Cytoplasm;
KW Methylation; Phosphoprotein; Reference proteome; Repeat; SH3 domain;
KW Synapse.
FT CHAIN 1..1730
FT /note="SH3 and multiple ankyrin repeat domains protein 3"
FT /id="PRO_0000291257"
FT REPEAT 148..178
FT /note="ANK 1"
FT REPEAT 182..211
FT /note="ANK 2"
FT REPEAT 215..245
FT /note="ANK 3"
FT REPEAT 249..278
FT /note="ANK 4"
FT REPEAT 282..311
FT /note="ANK 5"
FT REPEAT 315..345
FT /note="ANK 6"
FT DOMAIN 470..529
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 570..664
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1667..1730
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 1..75
FT /note="Intramolecular interaction with the ANK repeats"
FT /evidence="ECO:0000250"
FT REGION 354..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..684
FT /note="Required for interaction with ABI1"
FT /evidence="ECO:0000250"
FT REGION 760..1460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1475..1524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1546..1584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1627..1663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1494..1514
FT /evidence="ECO:0000255"
FT MOTIF 1410..1416
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 402..418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..464
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..792
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..846
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1321..1343
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1367..1400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1433..1452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1495..1509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1638..1652
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 122
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLU4"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 555
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 694
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 781
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 790
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 801
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 890
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 897
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 912
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BYB0"
FT MOD_RES 930
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLU4"
FT MOD_RES 965
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 995
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1130
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1134
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1159
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BYB0"
FT MOD_RES 1166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1234
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1253
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BYB0"
FT MOD_RES 1420
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLU4"
FT MOD_RES 1510
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1521
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1529
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1539
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1634
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1636
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1638
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BYB0"
FT VAR_SEQ 1..890
FT /note="Missing (in isoform 10)"
FT /evidence="ECO:0000305"
FT /id="VSP_053606"
FT VAR_SEQ 1..675
FT /note="MDGPGASAVVVRVGIPDLQQTKCLRLDPTAPVWAAKQRVLCALNHSLQDALN
FT YGLFQPPSRGRAGKFLDEERLLQDYPPNLDTPLPYLEFRYKRRVYAQNLIDDKQFAKLH
FT TKANLKKFMDYVQLHSTDKVARLLDKGLDPNFHDPDSGECPLSLAAQLDNATDLLKVLR
FT NGGAHLDFRTRDGLTAVHCATRQRNAGALTTLLDLGASPDYKDSRGLTPLYHSALGGGD
FT ALCCELLLHDHAQLGTTDENGWQEIHQACRFGHVQHLEHLLFYGANMGAQNASGNTALH
FT ICALYNQESCARVLLFRGANKDVRNYNSQTAFQVAIIAGNFELAEVIKTHKDSDVVPFR
FT ETPSYAKRRRLAGPSGLASPRPLQRSASDINLKGDQPAASPGPTLRSLPHQLLLQRLQE
FT EKDRDRDGELENDISGPSAGRGGHNKISPSGPGGSGPAPGPGPASPAPPAPPPRGPKRK
FT LYSAVPGRKFIAVKAHSPQGEGEIPLHRGEAVKVLSIGEGGFWEGTVKGRTGWFPADCV
FT EEVQMRQYDTRHETREDRTKRLFRHYTVGSYDSLTSHSDYVIDDKVAILQKRDHEGFGF
FT VLRGAKAETPIEEFTPTPAFPALQYLESVDVEGVAWRAGLRTGDFLIEVNGVNVVKVGH
FT KQVVGLIRQGGNRLVMKVVSVTRKPEEDGARRR -> MKKFASSRSLNKILAQCDSSSR
FT EYEEVQAVERKWHLHLATPRRLLLDRRAKASLFFA (in isoform 8 and
FT isoform 9)"
FT /evidence="ECO:0000305"
FT /id="VSP_053607"
FT VAR_SEQ 1..589
FT /note="MDGPGASAVVVRVGIPDLQQTKCLRLDPTAPVWAAKQRVLCALNHSLQDALN
FT YGLFQPPSRGRAGKFLDEERLLQDYPPNLDTPLPYLEFRYKRRVYAQNLIDDKQFAKLH
FT TKANLKKFMDYVQLHSTDKVARLLDKGLDPNFHDPDSGECPLSLAAQLDNATDLLKVLR
FT NGGAHLDFRTRDGLTAVHCATRQRNAGALTTLLDLGASPDYKDSRGLTPLYHSALGGGD
FT ALCCELLLHDHAQLGTTDENGWQEIHQACRFGHVQHLEHLLFYGANMGAQNASGNTALH
FT ICALYNQESCARVLLFRGANKDVRNYNSQTAFQVAIIAGNFELAEVIKTHKDSDVVPFR
FT ETPSYAKRRRLAGPSGLASPRPLQRSASDINLKGDQPAASPGPTLRSLPHQLLLQRLQE
FT EKDRDRDGELENDISGPSAGRGGHNKISPSGPGGSGPAPGPGPASPAPPAPPPRGPKRK
FT LYSAVPGRKFIAVKAHSPQGEGEIPLHRGEAVKVLSIGEGGFWEGTVKGRTGWFPADCV
FT EEVQMRQYDTRHETREDRTKRLFRHYTVGSYDSLTSHSDYVIDDKVAILQKRDHEGFGF
FT VLRGAK -> MLVNAFYLALPA (in isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_053608"
FT VAR_SEQ 1..536
FT /note="MDGPGASAVVVRVGIPDLQQTKCLRLDPTAPVWAAKQRVLCALNHSLQDALN
FT YGLFQPPSRGRAGKFLDEERLLQDYPPNLDTPLPYLEFRYKRRVYAQNLIDDKQFAKLH
FT TKANLKKFMDYVQLHSTDKVARLLDKGLDPNFHDPDSGECPLSLAAQLDNATDLLKVLR
FT NGGAHLDFRTRDGLTAVHCATRQRNAGALTTLLDLGASPDYKDSRGLTPLYHSALGGGD
FT ALCCELLLHDHAQLGTTDENGWQEIHQACRFGHVQHLEHLLFYGANMGAQNASGNTALH
FT ICALYNQESCARVLLFRGANKDVRNYNSQTAFQVAIIAGNFELAEVIKTHKDSDVVPFR
FT ETPSYAKRRRLAGPSGLASPRPLQRSASDINLKGDQPAASPGPTLRSLPHQLLLQRLQE
FT EKDRDRDGELENDISGPSAGRGGHNKISPSGPGGSGPAPGPGPASPAPPAPPPRGPKRK
FT LYSAVPGRKFIAVKAHSPQGEGEIPLHRGEAVKVLSIGEGGFWEGTVKGRTGWFPADCV
FT EEVQMRQYDTRH -> MLPA (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_053609"
FT VAR_SEQ 1..528
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:24164323"
FT /id="VSP_053610"
FT VAR_SEQ 1..433
FT /note="MDGPGASAVVVRVGIPDLQQTKCLRLDPTAPVWAAKQRVLCALNHSLQDALN
FT YGLFQPPSRGRAGKFLDEERLLQDYPPNLDTPLPYLEFRYKRRVYAQNLIDDKQFAKLH
FT TKANLKKFMDYVQLHSTDKVARLLDKGLDPNFHDPDSGECPLSLAAQLDNATDLLKVLR
FT NGGAHLDFRTRDGLTAVHCATRQRNAGALTTLLDLGASPDYKDSRGLTPLYHSALGGGD
FT ALCCELLLHDHAQLGTTDENGWQEIHQACRFGHVQHLEHLLFYGANMGAQNASGNTALH
FT ICALYNQESCARVLLFRGANKDVRNYNSQTAFQVAIIAGNFELAEVIKTHKDSDVVPFR
FT ETPSYAKRRRLAGPSGLASPRPLQRSASDINLKGDQPAASPGPTLRSLPHQLLLQRLQE
FT EKDRDRDGELENDISGPSAGRGGHNKI -> MEAPGAGFACPLPPGIASVTYVFVY
FT (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:24164323"
FT /id="VSP_053611"
FT VAR_SEQ 1..89
FT /note="MDGPGASAVVVRVGIPDLQQTKCLRLDPTAPVWAAKQRVLCALNHSLQDALN
FT YGLFQPPSRGRAGKFLDEERLLQDYPPNLDTPLPYLE -> MGLCGSLLPTFSLSEQ
FT (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_053612"
FT VAR_SEQ 703..710
FT /note="Missing (in isoform 2 and isoform 9)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_053613"
FT VAR_SEQ 784..790
FT /note="EDEKLAS -> SSAASVS (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_053614"
FT VAR_SEQ 791..1730
FT /note="Missing (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_053615"
FT STRAND 9..15
FT /evidence="ECO:0007829|PDB:6KYK"
FT TURN 16..19
FT /evidence="ECO:0007829|PDB:6KYK"
FT STRAND 20..26
FT /evidence="ECO:0007829|PDB:6KYK"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:6KYK"
FT HELIX 32..42
FT /evidence="ECO:0007829|PDB:6KYK"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:6KYK"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:6KYK"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:6KYK"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:6KYH"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:6KYK"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:6KYK"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:6KYK"
FT HELIX 104..110
FT /evidence="ECO:0007829|PDB:6KYK"
FT HELIX 113..124
FT /evidence="ECO:0007829|PDB:6KYK"
FT HELIX 128..137
FT /evidence="ECO:0007829|PDB:6KYK"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:6KYK"
FT HELIX 152..158
FT /evidence="ECO:0007829|PDB:6KYK"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:6KYH"
FT HELIX 163..171
FT /evidence="ECO:0007829|PDB:6KYK"
FT HELIX 186..192
FT /evidence="ECO:0007829|PDB:6KYK"
FT HELIX 196..204
FT /evidence="ECO:0007829|PDB:6KYK"
FT HELIX 219..226
FT /evidence="ECO:0007829|PDB:6KYK"
FT HELIX 231..238
FT /evidence="ECO:0007829|PDB:6KYK"
FT HELIX 253..260
FT /evidence="ECO:0007829|PDB:6KYK"
FT HELIX 263..271
FT /evidence="ECO:0007829|PDB:6KYK"
FT HELIX 286..292
FT /evidence="ECO:0007829|PDB:6KYK"
FT HELIX 296..304
FT /evidence="ECO:0007829|PDB:6KYK"
FT HELIX 319..326
FT /evidence="ECO:0007829|PDB:6KYK"
FT HELIX 329..337
FT /evidence="ECO:0007829|PDB:6KYK"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:6KYK"
FT STRAND 544..552
FT /evidence="ECO:0007829|PDB:5IZU"
FT STRAND 555..560
FT /evidence="ECO:0007829|PDB:5IZU"
FT STRAND 564..574
FT /evidence="ECO:0007829|PDB:3O5N"
FT STRAND 577..579
FT /evidence="ECO:0007829|PDB:5IZU"
FT STRAND 582..586
FT /evidence="ECO:0007829|PDB:3O5N"
FT STRAND 601..603
FT /evidence="ECO:0007829|PDB:3O5N"
FT STRAND 608..612
FT /evidence="ECO:0007829|PDB:3O5N"
FT STRAND 614..617
FT /evidence="ECO:0007829|PDB:3O5N"
FT HELIX 618..621
FT /evidence="ECO:0007829|PDB:3O5N"
FT STRAND 628..632
FT /evidence="ECO:0007829|PDB:3O5N"
FT HELIX 643..651
FT /evidence="ECO:0007829|PDB:3O5N"
FT TURN 652..654
FT /evidence="ECO:0007829|PDB:3O5N"
FT STRAND 655..665
FT /evidence="ECO:0007829|PDB:3O5N"
SQ SEQUENCE 1730 AA; 185397 MW; 1343F857BE3EECD8 CRC64;
MDGPGASAVV VRVGIPDLQQ TKCLRLDPTA PVWAAKQRVL CALNHSLQDA LNYGLFQPPS
RGRAGKFLDE ERLLQDYPPN LDTPLPYLEF RYKRRVYAQN LIDDKQFAKL HTKANLKKFM
DYVQLHSTDK VARLLDKGLD PNFHDPDSGE CPLSLAAQLD NATDLLKVLR NGGAHLDFRT
RDGLTAVHCA TRQRNAGALT TLLDLGASPD YKDSRGLTPL YHSALGGGDA LCCELLLHDH
AQLGTTDENG WQEIHQACRF GHVQHLEHLL FYGANMGAQN ASGNTALHIC ALYNQESCAR
VLLFRGANKD VRNYNSQTAF QVAIIAGNFE LAEVIKTHKD SDVVPFRETP SYAKRRRLAG
PSGLASPRPL QRSASDINLK GDQPAASPGP TLRSLPHQLL LQRLQEEKDR DRDGELENDI
SGPSAGRGGH NKISPSGPGG SGPAPGPGPA SPAPPAPPPR GPKRKLYSAV PGRKFIAVKA
HSPQGEGEIP LHRGEAVKVL SIGEGGFWEG TVKGRTGWFP ADCVEEVQMR QYDTRHETRE
DRTKRLFRHY TVGSYDSLTS HSDYVIDDKV AILQKRDHEG FGFVLRGAKA ETPIEEFTPT
PAFPALQYLE SVDVEGVAWR AGLRTGDFLI EVNGVNVVKV GHKQVVGLIR QGGNRLVMKV
VSVTRKPEED GARRRAPPPP KRAPSTTLTL RSKSMTAELE ELASIRRRKG EKLDEILAVA
AEPTLRPDIA DADSRAATVK QRPTSRRITP AEISSLFERQ GLPGPEKLPG SLRKGIPRTK
SVGEDEKLAS LLEGRFPRST SMQDTVREGR GIPPPPQTAP PPPPAPYYFD SGPPPTFSPP
PPPGRAYDTV RSSFKPGLEA RLGAGAAGLY DPSTPLGPLP YPERQKRARS MIILQDSAPE
VGDVPRPAPA ATPPERPKRR PRPSGPDSPY ANLGAFSASL FAPSKPQRRK SPLVKQLQVE
DAQERAALAV GSPGPVGGSF AREPSPTHRG PRPGSLDYSS GEGLGLTFGG PSPGPVKERR
LEERRRSTVF LSVGAIEGSP PSADLPSLQP SRSIDERLLG TGATTGRDLL LPSPVSALKP
LVGGPSLGPS GSTFIHPLTG KPLDPSSPLA LALAARERAL ASQTPSRSPT PVHSPDADRP
GPLFVDVQTR DSERGPLASP AFSPRSPAWI PVPARREAEK PPREERKSPE DKKSMILSVL
DTSLQRPAGL IVVHATSNGQ EPSRLGAEEE RPGTPELAPA PMQAAAVAEP MPSPRAQPPG
SIPADPGPGQ GSSEEEPELV FAVNLPPAQL SSSDEETREE LARIGLVPPP EEFANGILLT
TPPPGPGPLP TTVPSPASGK PSSELPPAPE SAADSGVEEA DTRSSSDPHL ETTSTISTVS
SMSTLSSESG ELTDTHTSFA DGHTFLLEKP PVPPKPKLKS PLGKGPVTFR DPLLKQSSDS
ELMAQQHHAA STGLASAAGP ARPRYLFQRR SKLWGDPVES RGLPGPEDDK PTVISELSSR
LQQLNKDTRS LGEEPVGGLG SLLDPAKKSP IAAARLFSSL GELSTISAQR SPGGPGGGAS
YSVRPSGRYP VARRAPSPVK PASLERVEGL GAGVGGAGRP FGLTPPTILK SSSLSIPHEP
KEVRFVVRSV SARSRSPSPS PLPSPSPGSG PSAGPRRPFQ QKPLQLWSKF DVGDWLESIH
LGEHRDRFED HEIEGAHLPA LTKEDFVELG VTRVGHRMNI ERALRQLDGS
