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 24-JAN-2024, entry version 161. 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, RC Pancreas, 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 348. DR DIP; DIP-32262N; -. DR IntAct; Q4ACU6; 437. DR MINT; Q4ACU6; -. DR STRING; 10090.ENSMUSP00000104932; -. DR GlyGen; Q4ACU6; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q4ACU6; -. DR PhosphoSitePlus; Q4ACU6; -. DR SwissPalm; Q4ACU6; -. DR jPOST; Q4ACU6; -. DR MaxQB; Q4ACU6; -. DR PaxDb; 10090-ENSMUSP00000104932; -. DR PeptideAtlas; 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; 193 antibodies from 20 providers. DR DNASU; 58234; -. DR Ensembl; ENSMUST00000109309.9; ENSMUSP00000104932.3; ENSMUSG00000022623.18. [Q4ACU6-1] DR Ensembl; ENSMUST00000230807.2; ENSMUSP00000155608.2; ENSMUSG00000022623.18. [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 AGR; MGI:1930016; -. 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; FERQGMP; -. DR OrthoDB; 2247290at2759; -. 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 76 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 199 other cell types or tissues. DR ExpressionAtlas; Q4ACU6; baseline and differential. 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: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:0005886; C:plasma membrane; 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:0003779; F:actin binding; IEA:UniProtKB-KW. DR GO; GO:0001664; F:G protein-coupled receptor binding; ISO:MGI. 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: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:0050804; P:modulation of chemical synaptic transmission; IDA:SynGO. 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:0099175; P:regulation of postsynapse 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 CDD; cd00992; PDZ_signaling; 1. DR CDD; cd09506; SAM_Shank1_2_3; 1. DR DisProt; DP02376; -. DR Gene3D; 2.30.42.10; -; 1. DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2. 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:SF4; SH3 AND MULTIPLE ANKYRIN REPEAT DOMAINS PROTEIN 3; 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; 5. 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; 4. DR PROSITE; PS50106; PDZ; 1. DR PROSITE; PS50105; SAM_DOMAIN; 1. DR PROSITE; PS50002; SH3; 1. DR Genevisible; Q4ACU6; MM. 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 //