ID G3SE25_GORGO Unreviewed; 1605 AA.
AC G3SE25;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=SH3 and multiple ankyrin repeat domains 3 {ECO:0000313|Ensembl:ENSGGOP00000026355.2};
GN Name=SHANK3 {ECO:0000313|Ensembl:ENSGGOP00000026355.2};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000026355.2, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000026355.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000026355.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000026355.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Postsynaptic density
CC {ECO:0000256|ARBA:ARBA00034105}.
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DR EMBL; CABD030121886; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030121887; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030121888; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030121889; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030121890; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030121891; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 9593.ENSGGOP00000026355; -.
DR Ensembl; ENSGGOT00000030890.2; ENSGGOP00000026355.2; ENSGGOG00000011582.3.
DR GeneTree; ENSGT00940000153561; -.
DR InParanoid; G3SE25; -.
DR OMA; FERQGMP; -.
DR Proteomes; UP000001519; Chromosome 22.
DR Bgee; ENSGGOG00000011582; Expressed in cerebellum and 5 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; IBA:GO_Central.
DR GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
DR GO; GO:0098919; F:structural constituent of postsynaptic density; IEA:Ensembl.
DR GO; GO:0030160; F:synaptic receptor adaptor activity; IBA:GO_Central.
DR GO; GO:0097113; P:AMPA glutamate receptor clustering; IEA:Ensembl.
DR GO; GO:0008306; P:associative learning; IEA:Ensembl.
DR GO; GO:0048854; P:brain morphogenesis; IEA:Ensembl.
DR GO; GO:0060997; P:dendritic spine morphogenesis; IEA:Ensembl.
DR GO; GO:0001838; P:embryonic epithelial tube formation; IEA:Ensembl.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0014009; P:glial cell proliferation; IEA:Ensembl.
DR GO; GO:0097117; P:guanylate kinase-associated protein clustering; IEA:Ensembl.
DR GO; GO:0040011; P:locomotion; IEA:Ensembl.
DR GO; GO:0035641; P:locomotory exploration behavior; IEA:Ensembl.
DR GO; GO:0060292; P:long-term synaptic depression; IEA:Ensembl.
DR GO; GO:0060291; P:long-term synaptic potentiation; IEA:Ensembl.
DR GO; GO:0000165; P:MAPK cascade; IEA:Ensembl.
DR GO; GO:0007613; P:memory; IEA:Ensembl.
DR GO; GO:0032232; P:negative regulation of actin filament bundle assembly; IEA:Ensembl.
DR GO; GO:0045794; P:negative regulation of cell volume; IEA:Ensembl.
DR GO; GO:0061351; P:neural precursor cell proliferation; IEA:Ensembl.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
DR GO; GO:0097114; P:NMDA glutamate receptor clustering; IEA:Ensembl.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; IEA:Ensembl.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IEA:Ensembl.
DR GO; GO:1900451; P:positive regulation of glutamate receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0048170; P:positive regulation of long-term neuronal synaptic plasticity; IEA:Ensembl.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IEA:Ensembl.
DR GO; GO:0051835; P:positive regulation of synapse structural plasticity; IEA:Ensembl.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IEA:Ensembl.
DR GO; GO:0097107; P:postsynaptic density assembly; IEA:Ensembl.
DR GO; GO:1904717; P:regulation of AMPA glutamate receptor clustering; IEA:Ensembl.
DR GO; GO:2000822; P:regulation of behavioral fear response; IEA:Ensembl.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; IEA:Ensembl.
DR GO; GO:2000821; P:regulation of grooming behavior; IEA:Ensembl.
DR GO; GO:1900452; P:regulation of long-term synaptic depression; IEA:Ensembl.
DR GO; GO:0097396; P:response to interleukin-17; IEA:Ensembl.
DR GO; GO:0035176; P:social behavior; IEA:Ensembl.
DR GO; GO:0021773; P:striatal medium spiny neuron differentiation; IEA:Ensembl.
DR GO; GO:0071625; P:vocalization behavior; IEA:Ensembl.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd09506; SAM_Shank1_2_3; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 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; 3.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT REPEAT 122..155
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 156..188
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 223..255
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 256..288
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 432..491
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 521..615
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1542..1605
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 381..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 820..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 987..1019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1064..1145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1160..1409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1424..1473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1495..1532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..742
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..796
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1276..1297
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1316..1349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1444..1458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1605 AA; 172012 MW; 264FCC5D3CDC25B6 CRC64;
DPAAPVWAAK QRVLCALNHS LQDALNYGLF QPPSRGRAGK FLDEERLLQE YPPNLDTPLP
YLEFRYKRRV YAQNLIDDKQ FAKLHTKANL KKFMDYVQLH STDKVARLLD KGLDPNFHDP
DSGECPLSLA AQLDNATDLL KVLKNGGAHL DFRTRDGLTA VHCATRQRNA AALTTLLDLG
ASPDYKDSRG LTPLYHSALG GGDALCCELL LHDHAQLGTT DENGWQEIHQ ACRFGHVQHL
EHLLFYGADM GAQNASGNTA LHICALYNQE SCARVLLFRG ANRDVRNYNS QTSFQVAIIA
GNFELAEVIK THKDSDVVPF RETPSYAKRR RLAGPSGLAS PRPLQRSASD INLKGEAQPA
ASPGPSLRSL PHQLLLQRLQ EEKDRDRDAD QESNISGPLA GRGVGGRPSL PPAALLVPEA
PAPSPRKLYS AVPGRKFIAV KAHSPQGEGE IPLHRGEAVK VLSIGEGGFW EGTVKGRTGW
FPADCVEEVQ MRQHDTRPGE QGLPHSSLLS FISDYVIDDK VAVLQKRDHE GFGFVLRGAK
AETPIEEFTP TPAFPALQYL ESVDVEGVAW RAGLRTGDFL IEVNGVNVVK VGHKQVVALI
RQGGNRLVMK VVSVTRKPEE DGARRRAPPP PKRAPSTTLT LRSKSMTAEL EELGEWRGWQ
WRWTQMLAAA AEPTLRPDIA DADSRAATVK QRPTSRRITP AEISSLFERQ GLPGPEKLPG
SLRKGIPRTK SVGEDEKLAS LLEGRFPRST SMQDPVREGR GIPPPPQTAP PPPPAPYYFD
SGPPPAFSPP PPPGRAYDTV RSSFKPGLEA RLGAGAAGLY EPGAALGPLP YPERQKRARS
MIILQDSAPE SGDAPRPPPA ATPPERPKRR PRPPGPDSPY ANLGAFSASL FAPSKPQRRK
SPLVKQLQVE DAQERAALAV GSPGPGGGSF AREPSPTHRG PRPGGLDYGA GDGPGLAFGG
PGPAKDRRLE ERRRSTVFLS VGAIEGSAPS ADLPSLQPSR SIDERLLGTG PTAGRDLLLP
SPVSALKPLV SGPSLGPSGS TFIHPLTGKP LDPSSPLALA LAARERALAS QAPSRSPTPV
HSPDADRPGP LFVDVQARDP ERGPLASPAF SPRSPAWIPV PARREAEKVP REERKSPEDK
KSMILSVLDT SLQRPAGLIV VHATSNGQEP SRLGGAEEER PGTPELAPAP MQSAAVAEPL
PSPRAQPPGG TPADAGPGQG SSEEEPELVF AVNLPPAQLS SSDEETREEL ARIGLVPPPE
EFANGVLLAT PLAGPGPSPT TVPSPASGKP SSEPPPAPES AADSGVEEAD TRSSSDPHLE
TTSTISTVSS MSTLSSESGE LTDTHTSFAD GHTFLLEKPP VPPKPKLKSP LGKGPVTFRD
PLLKQSSDSE LMAQQHHAAS AGLASAAGPA RPRYLFQRRS KLWGDPVESR GLPGPEDDKP
TVISELSSRL QQLNKDTRSL GEEPVGGLGS LLDPAKKSPI AAARLFSSLG ELSSISAQRS
PGGPGGGASY SVRPSGRYPV ARRAPSPVKP ASLERQKPLQ LWSKFDVGDW LESIHLGEHR
DRFEDHEIEG AHLPALTKDD FVELGVTRVG HRMNIERALR QLDGS
//