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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
 
 
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