ARHG9_HUMAN
ID ARHG9_HUMAN Reviewed; 516 AA.
AC O43307; A8K1S8; B4DHC7; F8W7P8; Q5JSL6;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Rho guanine nucleotide exchange factor 9;
DE AltName: Full=Collybistin;
DE AltName: Full=PEM-2 homolog;
DE AltName: Full=Rac/Cdc42 guanine nucleotide exchange factor 9;
GN Name=ARHGEF9; Synonyms=ARHDH9, KIAA0424;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9455477; DOI=10.1093/dnares/4.5.307;
RA Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VIII. 78
RT new cDNA clones from brain which code for large proteins in vitro.";
RL DNA Res. 4:307-313(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10559246; DOI=10.1074/jbc.274.47.33587;
RA Reid T., Bathoorn A., Ahmadian M.R., Collard J.G.;
RT "Identification and characterization of hPEM-2, a guanine nucleotide
RT exchange factor specific for Cdc42.";
RL J. Biol. Chem. 274:33587-33593(1999).
RN [6]
RP STRUCTURE BY NMR OF 7-75.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the SH3 domain from Rho guanine nucleotide exchange
RT factor 9.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [7]
RP VARIANT DEE8 ALA-55, CHARACTERIZATION OF VARIANT DEE8 ALA-55, AND
RP ALTERNATIVE SPLICING.
RX PubMed=15215304; DOI=10.1523/jneurosci.1184-04.2004;
RA Harvey K., Duguid I.C., Alldred M.J., Beatty S.E., Ward H., Keep N.H.,
RA Lingenfelter S.E., Pearce B.R., Lundgren J., Owen M.J., Smart T.G.,
RA Luescher B., Rees M.I., Harvey R.J.;
RT "The GDP-GTP exchange factor collybistin: an essential determinant of
RT neuronal gephyrin clustering.";
RL J. Neurosci. 24:5816-5826(2004).
RN [8]
RP VARIANT DEE8 HIS-290.
RX PubMed=22612257; DOI=10.1111/j.1528-1167.2012.03516.x;
RA Lemke J.R., Riesch E., Scheurenbrand T., Schubach M., Wilhelm C.,
RA Steiner I., Hansen J., Courage C., Gallati S., Buerki S., Strozzi S.,
RA Simonetti B.G., Grunt S., Steinlin M., Alber M., Wolff M., Klopstock T.,
RA Prott E.C., Lorenz R., Spaich C., Rona S., Lakshminarasimhan M., Kroell J.,
RA Dorn T., Kraemer G., Synofzik M., Becker F., Weber Y.G., Lerche H.,
RA Boehm D., Biskup S.;
RT "Targeted next generation sequencing as a diagnostic tool in epileptic
RT disorders.";
RL Epilepsia 53:1387-1398(2012).
RN [9]
RP VARIANT LYS-401.
RX PubMed=23033978; DOI=10.1056/nejmoa1206524;
RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C.,
RA del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G.,
RA Veltman J.A., Vissers L.E.;
RT "Diagnostic exome sequencing in persons with severe intellectual
RT disability.";
RL N. Engl. J. Med. 367:1921-1929(2012).
RN [10]
RP VARIANT DEE8 HIS-290.
RX PubMed=25678704; DOI=10.1074/jbc.m114.633024;
RA Papadopoulos T., Schemm R., Grubmueller H., Brose N.;
RT "Lipid binding defects and perturbed synaptogenic activity of a
RT collybistinR290H mutant that causes epilepsy and intellectual disability.";
RL J. Biol. Chem. 290:8256-8270(2015).
CC -!- FUNCTION: Acts as guanine nucleotide exchange factor (GEF) for CDC42.
CC Promotes formation of GPHN clusters (By similarity).
CC {ECO:0000250|UniProtKB:Q9QX73, ECO:0000269|PubMed:10559246}.
CC -!- SUBUNIT: Interacts with GPHN. {ECO:0000250|UniProtKB:Q9QX73}.
CC -!- INTERACTION:
CC O43307; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-3447299, EBI-6658203;
CC O43307; Q9NW38: FANCL; NbExp=3; IntAct=EBI-3447299, EBI-2339898;
CC O43307; Q92993: KAT5; NbExp=3; IntAct=EBI-3447299, EBI-399080;
CC O43307; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-3447299, EBI-11742507;
CC O43307; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-3447299, EBI-9090795;
CC O43307; Q9NU19: TBC1D22B; NbExp=3; IntAct=EBI-3447299, EBI-8787464;
CC O43307; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-3447299, EBI-10241197;
CC O43307; Q14119: VEZF1; NbExp=3; IntAct=EBI-3447299, EBI-11980193;
CC O43307; P61981: YWHAG; NbExp=3; IntAct=EBI-3447299, EBI-359832;
CC O43307; Q86VK4-3: ZNF410; NbExp=3; IntAct=EBI-3447299, EBI-11741890;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10559246}.
CC Postsynaptic density {ECO:0000250|UniProtKB:Q3UTH8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=CB3(SH3+);
CC IsoId=O43307-1; Sequence=Displayed;
CC Name=2; Synonyms=CB3(SH3-);
CC IsoId=O43307-2; Sequence=VSP_042920, VSP_042921;
CC Name=3;
CC IsoId=O43307-3; Sequence=VSP_044555;
CC -!- TISSUE SPECIFICITY: Detected in brain. Detected at low levels in heart.
CC {ECO:0000269|PubMed:10559246}.
CC -!- DISEASE: Developmental and epileptic encephalopathy 8 (DEE8)
CC [MIM:300607]: A disorder characterized by hyperekplexia and early
CC infantile epileptic encephalopathy. Neurologic features include
CC exaggerated startle response, seizures, impaired psychomotor
CC development, and intellectual disability. Seizures can be provoked by
CC tactile stimulation or extreme emotion. {ECO:0000269|PubMed:15215304,
CC ECO:0000269|PubMed:22612257, ECO:0000269|PubMed:25678704}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA24854.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB007884; BAA24854.2; ALT_INIT; mRNA.
DR EMBL; AK289993; BAF82682.1; -; mRNA.
DR EMBL; AK295033; BAG58088.1; -; mRNA.
DR EMBL; AL451106; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL391277; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355142; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC056892; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC117406; AAI17407.1; -; mRNA.
DR CCDS; CCDS35315.1; -. [O43307-1]
DR CCDS; CCDS55429.1; -. [O43307-3]
DR CCDS; CCDS55430.1; -. [O43307-2]
DR RefSeq; NP_001166950.1; NM_001173479.1. [O43307-2]
DR RefSeq; NP_001166951.1; NM_001173480.1. [O43307-3]
DR RefSeq; NP_056000.1; NM_015185.2. [O43307-1]
DR RefSeq; XP_016884855.1; XM_017029366.1.
DR RefSeq; XP_016884862.1; XM_017029373.1.
DR PDB; 2YSQ; NMR; -; A=7-75.
DR PDBsum; 2YSQ; -.
DR AlphaFoldDB; O43307; -.
DR BMRB; O43307; -.
DR SMR; O43307; -.
DR BioGRID; 116834; 26.
DR IntAct; O43307; 24.
DR STRING; 9606.ENSP00000253401; -.
DR iPTMnet; O43307; -.
DR PhosphoSitePlus; O43307; -.
DR BioMuta; ARHGEF9; -.
DR EPD; O43307; -.
DR jPOST; O43307; -.
DR MassIVE; O43307; -.
DR MaxQB; O43307; -.
DR PaxDb; O43307; -.
DR PeptideAtlas; O43307; -.
DR PRIDE; O43307; -.
DR ProteomicsDB; 29986; -.
DR ProteomicsDB; 48882; -. [O43307-1]
DR ProteomicsDB; 48883; -. [O43307-2]
DR Antibodypedia; 27024; 188 antibodies from 30 providers.
DR DNASU; 23229; -.
DR Ensembl; ENST00000253401.10; ENSP00000253401.6; ENSG00000131089.17. [O43307-1]
DR Ensembl; ENST00000623517.3; ENSP00000485369.1; ENSG00000131089.17. [O43307-2]
DR Ensembl; ENST00000624843.3; ENSP00000485626.1; ENSG00000131089.17. [O43307-3]
DR Ensembl; ENST00000671907.1; ENSP00000500829.1; ENSG00000131089.17. [O43307-1]
DR GeneID; 23229; -.
DR KEGG; hsa:23229; -.
DR UCSC; uc004dvj.3; human. [O43307-1]
DR CTD; 23229; -.
DR DisGeNET; 23229; -.
DR GeneCards; ARHGEF9; -.
DR HGNC; HGNC:14561; ARHGEF9.
DR HPA; ENSG00000131089; Tissue enhanced (retina).
DR MalaCards; ARHGEF9; -.
DR MIM; 300429; gene.
DR MIM; 300607; phenotype.
DR neXtProt; NX_O43307; -.
DR OpenTargets; ENSG00000131089; -.
DR Orphanet; 163985; Hyperekplexia-epilepsy syndrome.
DR PharmGKB; PA24978; -.
DR VEuPathDB; HostDB:ENSG00000131089; -.
DR eggNOG; KOG3519; Eukaryota.
DR GeneTree; ENSGT00940000154103; -.
DR HOGENOM; CLU_008436_2_1_1; -.
DR InParanoid; O43307; -.
DR OrthoDB; 428887at2759; -.
DR PhylomeDB; O43307; -.
DR TreeFam; TF316832; -.
DR PathwayCommons; O43307; -.
DR Reactome; R-HSA-193648; NRAGE signals death through JNK.
DR Reactome; R-HSA-416482; G alpha (12/13) signalling events.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013406; RHOQ GTPase cycle.
DR Reactome; R-HSA-977443; GABA receptor activation.
DR SignaLink; O43307; -.
DR SIGNOR; O43307; -.
DR BioGRID-ORCS; 23229; 11 hits in 694 CRISPR screens.
DR ChiTaRS; ARHGEF9; human.
DR EvolutionaryTrace; O43307; -.
DR GeneWiki; ARHGEF9; -.
DR GenomeRNAi; 23229; -.
DR Pharos; O43307; Tbio.
DR PRO; PR:O43307; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; O43307; protein.
DR Bgee; ENSG00000131089; Expressed in Brodmann (1909) area 46 and 181 other tissues.
DR ExpressionAtlas; O43307; baseline and differential.
DR Genevisible; O43307; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0098982; C:GABA-ergic synapse; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0099572; C:postsynaptic specialization; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0099150; P:regulation of postsynaptic specialization assembly; IBA:GO_Central.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd11975; SH3_ARHGEF9; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR035728; ARHGEF9_SH3.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Disease variant; Epilepsy;
KW Guanine-nucleotide releasing factor; Phosphoprotein; Reference proteome;
KW SH3 domain; Synapse.
FT CHAIN 1..516
FT /note="Rho guanine nucleotide exchange factor 9"
FT /id="PRO_0000253895"
FT DOMAIN 8..67
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 103..287
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 318..425
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 100..110
FT /note="Interaction with GPHN"
FT /evidence="ECO:0000250"
FT REGION 453..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UTH8"
FT VAR_SEQ 1..102
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044555"
FT VAR_SEQ 1..10
FT /note="MTLLITGDSI -> MQWIRGGSGM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042920"
FT VAR_SEQ 11..63
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042921"
FT VARIANT 55
FT /note="G -> A (in DEE8; affects dendritic gephrin
FT clustering and trafficking of GABA-A receptors to synapses;
FT dbSNP:rs121918361)"
FT /evidence="ECO:0000269|PubMed:15215304"
FT /id="VAR_028752"
FT VARIANT 290
FT /note="R -> H (in DEE8)"
FT /evidence="ECO:0000269|PubMed:22612257,
FT ECO:0000269|PubMed:25678704"
FT /id="VAR_072742"
FT VARIANT 401
FT /note="E -> K (probable disease-associated variant found in
FT a patient with moderate intellectual disability, speech
FT delay and sleep disturbances)"
FT /evidence="ECO:0000269|PubMed:23033978"
FT /id="VAR_069370"
FT CONFLICT 109
FT /note="N -> D (in Ref. 2; BAF82682)"
FT /evidence="ECO:0000305"
FT STRAND 11..17
FT /evidence="ECO:0007829|PDB:2YSQ"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:2YSQ"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:2YSQ"
FT STRAND 42..49
FT /evidence="ECO:0007829|PDB:2YSQ"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:2YSQ"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:2YSQ"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:2YSQ"
SQ SEQUENCE 516 AA; 60982 MW; AAEE17366B46B707 CRC64;
MTLLITGDSI VSAEAVWDHV TMANRELAFK AGDVIKVLDA SNKDWWWGQI DDEEGWFPAS
FVRLWVNQED EVEEGPSDVQ NGHLDPNSDC LCLGRPLQNR DQMRANVINE IMSTERHYIK
HLKDICEGYL KQCRKRRDMF SDEQLKVIFG NIEDIYRFQM GFVRDLEKQY NNDDPHLSEI
GPCFLEHQDG FWIYSEYCNN HLDACMELSK LMKDSRYQHF FEACRLLQQM IDIAIDGFLL
TPVQKICKYP LQLAELLKYT AQDHSDYRYV AAALAVMRNV TQQINERKRR LENIDKIAQW
QASVLDWEGE DILDRSSELI YTGEMAWIYQ PYGRNQQRVF FLFDHQMVLC KKDLIRRDIL
YYKGRIDMDK YEVVDIEDGR DDDFNVSMKN AFKLHNKETE EIHLFFAKKL EEKIRWLRAF
REERKMVQED EKIGFEISEN QKRQAAMTVR KVPKQKGVNS ARSVPPSYPP PQDPLNHGQY
LVPDGIAQSQ VFEFTEPKRS QSPFWQNFSR LTPFKK
