ID DOCK7_HUMAN Reviewed; 2140 AA. AC Q96N67; Q00M63; Q2PPY7; Q45RE8; Q45RE9; Q5T1B9; Q5T1C0; Q6ZV32; Q8TB82; AC Q96NG6; Q96NI0; Q9C092; DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 4. DT 27-MAR-2024, entry version 185. DE RecName: Full=Dedicator of cytokinesis protein 7; GN Name=DOCK7; Synonyms=KIAA1771; 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 [MRNA] (ISOFORM 2), INTERACTION WITH RAC1 AND RAC3, RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN DOCKER. RC TISSUE=Fetal brain; RX PubMed=16982419; DOI=10.1016/j.neuron.2006.07.020; RA Watabe-Uchida M., John K.A., Janas J.A., Newey S.E., Van Aelst L.; RT "The Rac activator DOCK7 regulates neuronal polarity through local RT phosphorylation of stathmin/Op18."; RL Neuron 51:727-739(2006). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7), NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 830-2140 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE RP SCALE MRNA] OF 1156-2140 (ISOFORM 2), AND NUCLEOTIDE SEQUENCE [LARGE SCALE RP MRNA] OF 585-2140 (ISOFORM 3). RC TISSUE=Brain, Mesangial cell, Thalamus, and Thymus; 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=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 109-2140 (ISOFORMS 3 AND 4). RC TISSUE=Brain; RA Yamauchi J., Miyamoto Y., Takashima S., Tanoue A.; RT "Molecular characterization of human Dock7."; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 830-2140 (ISOFORM 1), AND TISSUE RP SPECIFICITY. RC TISSUE=Brain; RX PubMed=11214970; DOI=10.1093/dnares/7.6.347; RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XIX. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 7:347-355(2000). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1332-2140 (ISOFORM 2). RC TISSUE=Ovary; 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 [8] RP NOMENCLATURE. RX PubMed=12432077; DOI=10.1242/jcs.00219; RA Cote J.-F., Vuori K.; RT "Identification of an evolutionarily conserved superfamily of DOCK180- RT related proteins with guanine nucleotide exchange activity."; RL J. Cell Sci. 115:4901-4913(2002). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [10] RP INTERACTION WITH TSC1, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=15963462; DOI=10.1016/j.bbrc.2005.05.175; RA Nellist M., Burgers P.C., van den Ouweland A.M.W., Halley D.J.J., RA Luider T.M.; RT "Phosphorylation and binding partner analysis of the TSC1-TSC2 complex."; RL Biochem. Biophys. Res. Commun. 333:818-826(2005). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1429 (ISOFORMS 2 AND 6), RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1398 (ISOFORMS 3 AND 4), AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-180; SER-182; RP SER-882; SER-888; SER-900; THR-907; SER-910; SER-1383 AND SER-1432, RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1421; SER-1425 AND SER-1429 RP (ISOFORMS 2 AND 6), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1390; RP SER-1394 AND SER-1398 (ISOFORMS 3 AND 4), AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180; SER-896; SER-900; RP SER-905; THR-907; THR-909; SER-910 AND SER-1438, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1962, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-180; SER-182 AND RP SER-1430, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1383, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180; SER-182; SER-452; RP THR-907; SER-929; SER-964; SER-1383; SER-1432; SER-1438 AND SER-2129, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [21] RP INVOLVEMENT IN DEE23. RX PubMed=24814191; DOI=10.1016/j.ajhg.2014.04.012; RA Perrault I., Hamdan F.F., Rio M., Capo-Chichi J.M., Boddaert N., RA Decarie J.C., Maranda B., Nabbout R., Sylvain M., Lortie A., Roux P.P., RA Rossignol E., Gerard X., Barcia G., Berquin P., Munnich A., Rouleau G.A., RA Kaplan J., Rozet J.M., Michaud J.L.; RT "Mutations in DOCK7 in individuals with epileptic encephalopathy and RT cortical blindness."; RL Am. J. Hum. Genet. 94:891-897(2014). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-888, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [23] RP METHYLATION [LARGE SCALE ANALYSIS] AT LYS-381, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; 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 [24] RP INTERACTION WITH NOD2. RX PubMed=27812135; DOI=10.1371/journal.pone.0165420; RA Thiebaut R., Esmiol S., Lecine P., Mahfouz B., Hermant A., Nicoletti C., RA Parnis S., Perroy J., Borg J.P., Pascoe L., Hugot J.P., Ollendorff V.; RT "Characterization and Genetic Analyses of New Genes Coding for NOD2 RT Interacting Proteins."; RL PLoS ONE 11:E0165420-E0165420(2016). RN [25] RP FUNCTION, AND IDENTIFICATION IN DISP COMPLEX. RX PubMed=29467281; DOI=10.15252/embr.201744884; RA O'Loughlin T., Masters T.A., Buss F.; RT "The MYO6 interactome reveals adaptor complexes coordinating early endosome RT and cytoskeletal dynamics."; RL EMBO Rep. 19:0-0(2018). CC -!- FUNCTION: Functions as a guanine nucleotide exchange factor (GEF), CC which activates Rac1 and Rac3 Rho small GTPases by exchanging bound GDP CC for free GTP. Does not have a GEF activity for CDC42. Required for CC STMN1 'Ser-15' phosphorylation during axon formation and consequently CC for neuronal polarization (PubMed:16982419). As part of the DISP CC complex, may regulate the association of septins with actin and thereby CC regulate the actin cytoskeleton (PubMed:29467281). Has a role in CC pigmentation (By similarity). Involved in the regulation of cortical CC neurogenesis through the control of radial glial cells (RGCs) CC proliferation versus differentiation; negatively regulates the basal- CC to-apical interkinetic nuclear migration of RGCs by antagonizing the CC microtubule growth-promoting function of TACC3 (By similarity). CC {ECO:0000250|UniProtKB:Q8R1A4, ECO:0000269|PubMed:16982419, CC ECO:0000269|PubMed:29467281}. CC -!- SUBUNIT: Component of the DOCK7-induced septin displacement/DISP CC complex, at least composed of DOCK7, LRCH3 and MYO6 (PubMed:29467281). CC Interacts with TSC1. Interacts with nucleotide-free RAC1 and RAC3. CC Interacts with TACC3 and CRY1 (By similarity). Interacts with NOD2 CC (PubMed:27812135). {ECO:0000250|UniProtKB:Q8R1A4, CC ECO:0000269|PubMed:15963462, ECO:0000269|PubMed:16982419, CC ECO:0000269|PubMed:27812135, ECO:0000269|PubMed:29467281}. CC -!- INTERACTION: CC Q96N67; Q9Y2L9: LRCH1; NbExp=2; IntAct=EBI-2433703, EBI-2797324; CC Q96N67; Q96II8: LRCH3; NbExp=9; IntAct=EBI-2433703, EBI-8795942; CC Q96N67; O75427: LRCH4; NbExp=2; IntAct=EBI-2433703, EBI-718707; CC Q96N67; Q6ZNJ1: NBEAL2; NbExp=8; IntAct=EBI-2433703, EBI-2862306; CC Q96N67; O15027: SEC16A; NbExp=3; IntAct=EBI-2433703, EBI-357515; CC -!- SUBCELLULAR LOCATION: Cell projection, axon CC {ECO:0000269|PubMed:16982419}. Note=Enriched in the developing axons of CC hippocampal neurons. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Name=1; CC IsoId=Q96N67-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96N67-2; Sequence=VSP_022240, VSP_007707; CC Name=3; CC IsoId=Q96N67-3; Sequence=VSP_012440, VSP_022240; CC Name=4; CC IsoId=Q96N67-4; Sequence=VSP_012440, VSP_022240, VSP_007707; CC Name=5; CC IsoId=Q96N67-5; Sequence=VSP_012440; CC Name=6; CC IsoId=Q96N67-6; Sequence=VSP_022240; CC Name=7; CC IsoId=Q96N67-7; Sequence=VSP_054534, VSP_054535; CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11214970}. CC -!- DOMAIN: The DOCKER domain mediates GEF activity. CC {ECO:0000269|PubMed:16982419}. CC -!- DISEASE: Developmental and epileptic encephalopathy 23 (DEE23) CC [MIM:615859]: A severe disease characterized by early-onset intractable CC epilepsy, dysmorphic features, intellectual disability, and cortical CC blindness. Brain imaging shows an abnormally marked pontobulbar sulcus CC with mild pontine hypoplasia, white matter abnormalities, and atrophy CC in the occipital lobe. {ECO:0000269|PubMed:24814191}. Note=The disease CC is caused by variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000255|PROSITE- CC ProRule:PRU00983}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH16392.2; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=ABC33725.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAB70933.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB71042.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAC86032.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; DQ341187; ABC68221.1; -; mRNA. DR EMBL; AK055401; BAB70917.1; -; mRNA. DR EMBL; AK055493; BAB70933.1; ALT_INIT; mRNA. DR EMBL; AK055905; BAB71042.1; ALT_FRAME; mRNA. DR EMBL; AK125049; BAC86032.1; ALT_INIT; mRNA. DR EMBL; AK292640; BAF85329.1; -; mRNA. DR EMBL; AC096946; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC103923; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL138847; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL451044; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471059; EAX06582.1; -; Genomic_DNA. DR EMBL; DQ309763; ABC33725.1; ALT_FRAME; mRNA. DR EMBL; DQ118679; AAZ38451.1; -; mRNA. DR EMBL; DQ118680; AAZ38452.1; -; mRNA. DR EMBL; AB051558; BAB21862.1; -; mRNA. DR EMBL; BC016392; AAH16392.2; ALT_FRAME; mRNA. DR CCDS; CCDS30734.1; -. [Q96N67-5] DR CCDS; CCDS60156.1; -. [Q96N67-2] DR CCDS; CCDS60157.1; -. [Q96N67-7] DR CCDS; CCDS81335.1; -. [Q96N67-4] DR CCDS; CCDS81336.1; -. [Q96N67-3] DR CCDS; CCDS81338.1; -. [Q96N67-6] DR CCDS; CCDS90964.1; -. [Q96N67-1] DR RefSeq; NP_001258928.1; NM_001271999.1. [Q96N67-2] DR RefSeq; NP_001258929.1; NM_001272000.1. [Q96N67-3] DR RefSeq; NP_001258930.1; NM_001272001.1. [Q96N67-4] DR RefSeq; NP_001258931.1; NM_001272002.1. [Q96N67-7] DR RefSeq; NP_001317543.1; NM_001330614.1. [Q96N67-6] DR RefSeq; NP_212132.2; NM_033407.3. [Q96N67-5] DR RefSeq; XP_011540628.1; XM_011542326.2. DR PDB; 6AJ4; X-ray; 3.26 A; A/C/E/G=1832-2114. DR PDB; 6AJL; X-ray; 3.23 A; A/C/E/G=1832-2114. DR PDBsum; 6AJ4; -. DR PDBsum; 6AJL; -. DR AlphaFoldDB; Q96N67; -. DR SMR; Q96N67; -. DR BioGRID; 124527; 262. DR ComplexPortal; CPX-7725; DISP septin regulator complex. DR CORUM; Q96N67; -. DR ELM; Q96N67; -. DR IntAct; Q96N67; 98. DR MINT; Q96N67; -. DR STRING; 9606.ENSP00000251157; -. DR GlyCosmos; Q96N67; 1 site, 1 glycan. DR GlyGen; Q96N67; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q96N67; -. DR MetOSite; Q96N67; -. DR PhosphoSitePlus; Q96N67; -. DR SwissPalm; Q96N67; -. DR BioMuta; DOCK7; -. DR DMDM; 122065170; -. DR CPTAC; CPTAC-1729; -. DR CPTAC; CPTAC-1730; -. DR CPTAC; CPTAC-1731; -. DR CPTAC; CPTAC-1732; -. DR EPD; Q96N67; -. DR jPOST; Q96N67; -. DR MassIVE; Q96N67; -. DR MaxQB; Q96N67; -. DR PaxDb; 9606-ENSP00000251157; -. DR PeptideAtlas; Q96N67; -. DR ProteomicsDB; 77473; -. [Q96N67-1] DR ProteomicsDB; 77474; -. [Q96N67-2] DR ProteomicsDB; 77475; -. [Q96N67-3] DR ProteomicsDB; 77476; -. [Q96N67-4] DR ProteomicsDB; 77477; -. [Q96N67-5] DR ProteomicsDB; 77478; -. [Q96N67-6] DR ProteomicsDB; 77516; -. DR Pumba; Q96N67; -. DR Antibodypedia; 1929; 141 antibodies from 20 providers. DR DNASU; 85440; -. DR Ensembl; ENST00000251157.10; ENSP00000251157.6; ENSG00000116641.18. [Q96N67-6] DR Ensembl; ENST00000340370.10; ENSP00000340742.5; ENSG00000116641.18. [Q96N67-5] DR Ensembl; ENST00000404627.3; ENSP00000384446.2; ENSG00000116641.18. [Q96N67-7] DR Ensembl; ENST00000454575.6; ENSP00000413583.2; ENSG00000116641.18. [Q96N67-2] DR Ensembl; ENST00000634264.1; ENSP00000489284.1; ENSG00000116641.18. [Q96N67-3] DR Ensembl; ENST00000635123.1; ENSP00000489499.1; ENSG00000116641.18. [Q96N67-4] DR Ensembl; ENST00000635253.2; ENSP00000489124.1; ENSG00000116641.18. [Q96N67-1] DR GeneID; 85440; -. DR KEGG; hsa:85440; -. DR MANE-Select; ENST00000635253.2; ENSP00000489124.1; NM_001367561.1; NP_001354490.1. DR UCSC; uc001dap.5; human. [Q96N67-1] DR AGR; HGNC:19190; -. DR CTD; 85440; -. DR DisGeNET; 85440; -. DR GeneCards; DOCK7; -. DR HGNC; HGNC:19190; DOCK7. DR HPA; ENSG00000116641; Low tissue specificity. DR MalaCards; DOCK7; -. DR MIM; 615730; gene. DR MIM; 615859; phenotype. DR neXtProt; NX_Q96N67; -. DR OpenTargets; ENSG00000116641; -. DR Orphanet; 411986; Early-onset epileptic encephalopathy-cortical blindness-intellectual disability-facial dysmorphism syndrome. DR PharmGKB; PA134872825; -. DR VEuPathDB; HostDB:ENSG00000116641; -. DR eggNOG; KOG1997; Eukaryota. DR GeneTree; ENSGT00940000155661; -. DR HOGENOM; CLU_000624_0_0_1; -. DR InParanoid; Q96N67; -. DR OMA; FPHQFND; -. DR OrthoDB; 5480873at2759; -. DR PhylomeDB; Q96N67; -. DR TreeFam; TF313629; -. DR PathwayCommons; Q96N67; -. DR Reactome; R-HSA-8875555; MET activates RAP1 and RAC1. DR Reactome; R-HSA-9013148; CDC42 GTPase cycle. DR Reactome; R-HSA-9013149; RAC1 GTPase cycle. DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production. DR SignaLink; Q96N67; -. DR SIGNOR; Q96N67; -. DR BioGRID-ORCS; 85440; 73 hits in 1157 CRISPR screens. DR ChiTaRS; DOCK7; human. DR GeneWiki; Dock7; -. DR GenomeRNAi; 85440; -. DR Pharos; Q96N67; Tbio. DR PRO; PR:Q96N67; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q96N67; Protein. DR Bgee; ENSG00000116641; Expressed in ventricular zone and 185 other cell types or tissues. DR ExpressionAtlas; Q96N67; baseline and differential. DR GO; GO:0030424; C:axon; TAS:BHF-UCL. DR GO; GO:0045178; C:basal part of cell; TAS:BHF-UCL. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0030426; C:growth cone; TAS:BHF-UCL. DR GO; GO:0043005; C:neuron projection; TAS:BHF-UCL. DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central. DR GO; GO:0031267; F:small GTPase binding; IDA:BHF-UCL. DR GO; GO:0090630; P:activation of GTPase activity; IDA:BHF-UCL. DR GO; GO:0007409; P:axonogenesis; IMP:BHF-UCL. DR GO; GO:0045200; P:establishment of neuroblast polarity; IMP:BHF-UCL. DR GO; GO:0022027; P:interkinetic nuclear migration; ISS:UniProtKB. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:BHF-UCL. DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab. DR GO; GO:0031175; P:neuron projection development; IMP:BHF-UCL. DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:BHF-UCL. DR GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; IMP:BHF-UCL. DR GO; GO:0050767; P:regulation of neurogenesis; ISS:UniProtKB. DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro. DR CDD; cd08696; C2_Dock-C; 1. DR CDD; cd11703; DHR2_DOCK7; 1. DR Gene3D; 1.20.58.740; -; 1. DR Gene3D; 1.25.40.410; -; 1. DR Gene3D; 2.60.40.150; C2 domain; 1. DR InterPro; IPR037808; C2_Dock-C. DR InterPro; IPR027007; C2_DOCK-type_domain. DR InterPro; IPR035892; C2_domain_sf. DR InterPro; IPR026791; DOCK. DR InterPro; IPR021816; DOCK_C/D_N. DR InterPro; IPR043161; DOCK_C_lobe_A. DR InterPro; IPR043162; DOCK_C_lobe_C. DR InterPro; IPR027357; DOCKER_dom. DR InterPro; IPR046769; DOCKER_Lobe_A. DR InterPro; IPR046770; DOCKER_Lobe_B. DR InterPro; IPR046773; DOCKER_Lobe_C. DR PANTHER; PTHR23317; DEDICATOR OF CYTOKINESIS DOCK; 1. DR PANTHER; PTHR23317:SF78; DEDICATOR OF CYTOKINESIS PROTEIN 7; 1. DR Pfam; PF06920; DHR-2_Lobe_A; 1. DR Pfam; PF20422; DHR-2_Lobe_B; 1. DR Pfam; PF20421; DHR-2_Lobe_C; 1. DR Pfam; PF14429; DOCK-C2; 1. DR Pfam; PF11878; DOCK_C-D_N; 1. DR PROSITE; PS51650; C2_DOCK; 1. DR PROSITE; PS51651; DOCKER; 1. DR Genevisible; Q96N67; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cell projection; KW Coiled coil; Developmental protein; Differentiation; Epilepsy; KW Guanine-nucleotide releasing factor; Methylation; Neurogenesis; KW Phosphoprotein; Reference proteome. FT CHAIN 1..2140 FT /note="Dedicator of cytokinesis protein 7" FT /id="PRO_0000189995" FT DOMAIN 561..727 FT /note="C2 DOCK-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00983" FT DOMAIN 1678..2114 FT /note="DOCKER" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00984" FT REGION 138..183 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 888..971 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 365..395 FT /evidence="ECO:0000255" FT COILED 2086..2112 FT /evidence="ECO:0000255" FT COMPBIAS 144..158 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 888..914 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 944..971 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 30 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 180 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 182 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 381 FT /note="N6-methyllysine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 450 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q8R1A4" FT MOD_RES 452 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 862 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8R1A4" FT MOD_RES 864 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8R1A4" FT MOD_RES 882 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 888 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:24275569" FT MOD_RES 896 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 900 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332" FT MOD_RES 905 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 907 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163" FT MOD_RES 909 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 910 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332" FT MOD_RES 929 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 964 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1383 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 1430 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 1432 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1434 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8R1A4" FT MOD_RES 1438 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1962 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 2129 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 601..632 FT /note="VIFGKSSCSEFSKEAYTAVVYHNRSPDFHEEI -> SPSCTHPIPTVRPLPL FT WCYHSIFSLLSWDFIT (in isoform 7)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054534" FT VAR_SEQ 633..2140 FT /note="Missing (in isoform 7)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054535" FT VAR_SEQ 923..953 FT /note="Missing (in isoform 3, isoform 4 and isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.5" FT /id="VSP_012440" FT VAR_SEQ 1419..1427 FT /note="Missing (in isoform 2, isoform 3, isoform 4 and FT isoform 6)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16982419, FT ECO:0000303|Ref.5" FT /id="VSP_022240" FT VAR_SEQ 1832..1836 FT /note="STGWE -> DGK (in isoform 2 and isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16982419, FT ECO:0000303|Ref.5" FT /id="VSP_007707" FT VARIANT 824 FT /note="I -> T (in dbSNP:rs35400360)" FT /id="VAR_057524" FT CONFLICT 750 FT /note="H -> R (in Ref. 2; BAC86032)" FT /evidence="ECO:0000305" FT CONFLICT 1440 FT /note="E -> G (in Ref. 2; BAC86032)" FT /evidence="ECO:0000305" FT CONFLICT 1520 FT /note="S -> N (in Ref. 2; BAB70933)" FT /evidence="ECO:0000305" FT CONFLICT 1521 FT /note="A -> V (in Ref. 2; BAC86032)" FT /evidence="ECO:0000305" FT CONFLICT 1639 FT /note="P -> L (in Ref. 2; BAC86032)" FT /evidence="ECO:0000305" FT CONFLICT 1859 FT /note="E -> K (in Ref. 2; BAB70933)" FT /evidence="ECO:0000305" FT CONFLICT 1908 FT /note="K -> T (in Ref. 2; BAB71042)" FT /evidence="ECO:0000305" FT STRAND 1841..1849 FT /evidence="ECO:0007829|PDB:6AJL" FT HELIX 1850..1855 FT /evidence="ECO:0007829|PDB:6AJL" FT STRAND 1858..1864 FT /evidence="ECO:0007829|PDB:6AJL" FT HELIX 1870..1885 FT /evidence="ECO:0007829|PDB:6AJL" FT HELIX 1887..1889 FT /evidence="ECO:0007829|PDB:6AJL" FT STRAND 1890..1893 FT /evidence="ECO:0007829|PDB:6AJL" FT STRAND 1908..1918 FT /evidence="ECO:0007829|PDB:6AJL" FT HELIX 1922..1930 FT /evidence="ECO:0007829|PDB:6AJL" FT STRAND 1938..1947 FT /evidence="ECO:0007829|PDB:6AJL" FT STRAND 1951..1953 FT /evidence="ECO:0007829|PDB:6AJ4" FT TURN 1957..1959 FT /evidence="ECO:0007829|PDB:6AJL" FT STRAND 1961..1974 FT /evidence="ECO:0007829|PDB:6AJL" FT STRAND 1976..1990 FT /evidence="ECO:0007829|PDB:6AJL" FT HELIX 1992..2011 FT /evidence="ECO:0007829|PDB:6AJL" FT HELIX 2018..2029 FT /evidence="ECO:0007829|PDB:6AJL" FT STRAND 2032..2034 FT /evidence="ECO:0007829|PDB:6AJL" FT HELIX 2038..2044 FT /evidence="ECO:0007829|PDB:6AJL" FT STRAND 2045..2047 FT /evidence="ECO:0007829|PDB:6AJL" FT HELIX 2052..2082 FT /evidence="ECO:0007829|PDB:6AJL" FT HELIX 2085..2087 FT /evidence="ECO:0007829|PDB:6AJL" FT HELIX 2088..2109 FT /evidence="ECO:0007829|PDB:6AJL" FT MOD_RES Q96N67-2:1421 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES Q96N67-2:1425 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES Q96N67-2:1429 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332, FT ECO:0007744|PubMed:18669648" FT MOD_RES Q96N67-3:1390 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES Q96N67-3:1394 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES Q96N67-3:1398 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332, FT ECO:0007744|PubMed:18669648" FT MOD_RES Q96N67-4:1390 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES Q96N67-4:1394 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES Q96N67-4:1398 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332, FT ECO:0007744|PubMed:18669648" FT MOD_RES Q96N67-6:1421 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES Q96N67-6:1425 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES Q96N67-6:1429 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332, FT ECO:0007744|PubMed:18669648" SQ SEQUENCE 2140 AA; 242561 MW; A14857DCB9C3AE6E CRC64; MAERRAFAQK ISRTVAAEVR KQISGQYSGS PQLLKNLNIV GNISHHTTVP LTEAVDPVDL EDYLITHPLA VDSGPLRDLI EFPPDDIEVV YSPRDCRTLV SAVPEESEMD PHVRDCIRSY TEDWAIVIRK YHKLGTGFNP NTLDKQKERQ KGLPKQVFES DEAPDGNSYQ DDQDDLKRRS MSIDDTPRGS WACSIFDLKN SLPDALLPNL LDRTPNEEID RQNDDQRKSN RHKELFALHP SPDEEEPIER LSVPDIPKEH FGQRLLVKCL SLKFEIEIEP IFASLALYDV KEKKKISENF YFDLNSEQMK GLLRPHVPPA AITTLARSAI FSITYPSQDV FLVIKLEKVL QQGDIGECAE PYMIFKEADA TKNKEKLEKL KSQADQFCQR LGKYRMPFAW TAIHLMNIVS SAGSLERDST EVEISTGERK GSWSERRNSS IVGRRSLERT TSGDDACNLT SFRPATLTVT NFFKQEGDRL SDEDLYKFLA DMRRPSSVLR RLRPITAQLK IDISPAPENP HYCLTPELLQ VKLYPDSRVR PTREILEFPA RDVYVPNTTY RNLLYIYPQS LNFANRQGSA RNITVKVQFM YGEDPSNAMP VIFGKSSCSE FSKEAYTAVV YHNRSPDFHE EIKVKLPATL TDHHHLLFTF YHVSCQQKQN TPLETPVGYT WIPMLQNGRL KTGQFCLPVS LEKPPQAYSV LSPEVPLPGM KWVDNHKGVF NVEVVAVSSI HTQDPYLDKF FALVNALDEH LFPVRIGDMR IMENNLENEL KSSISALNSS QLEPVVRFLH LLLDKLILLV IRPPVIAGQI VNLGQASFEA MASIINRLHK NLEGNHDQHG RNSLLASYIH YVFRLPNTYP NSSSPGPGGL GGSVHYATMA RSAVRPASLN LNRSRSLSNS NPDISGTPTS PDDEVRSIIG SKGLDRSNSW VNTGGPKAAP WGSNPSPSAE STQAMDRSCN RMSSHTETSS FLQTLTGRLP TKKLFHEELA LQWVVCSGSV RESALQQAWF FFELMVKSMV HHLYFNDKLE APRKSRFPER FMDDIAALVS TIASDIVSRF QKDTEMVERL NTSLAFFLND LLSVMDRGFV FSLIKSCYKQ VSSKLYSLPN PSVLVSLRLD FLRIICSHEH YVTLNLPCSL LTPPASPSPS VSSATSQSSG FSTNVQDQKI ANMFELSVPF RQQHYLAGLV LTELAVILDP DAEGLFGLHK KVINMVHNLL SSHDSDPRYS DPQIKARVAM LYLPLIGIIM ETVPQLYDFT ETHNQRGRPI CIATDDYESE SGSMISQTVA MAIAGTSVPQ LTRPGSFLLT STSGRQHTTF SAESSRSLLI CLLWVLKNAD ETVLQKWFTD LSVLQLNRLL DLLYLCVSCF EYKGKKVFER MNSLTFKKSK DMRAKLEEAI LGSIGARQEM VRRSRGQLGT YTIASPPERS PSGSAFGSQE NLRWRKDMTH WRQNTEKLDK SRAEIEHEAL IDGNLATEAN LIILDTLEIV VQTVSVTESK ESILGGVLKV LLHSMACNQS AVYLQHCFAT QRALVSKFPE LLFEEETEQC ADLCLRLLRH CSSSIGTIRS HASASLYLLM RQNFEIGNNF ARVKMQVTMS LSSLVGTSQN FNEEFLRRSL KTILTYAEED LELRETTFPD QVQDLVFNLH MILSDTVKMK EHQEDPEMLI DLMYRIAKGY QTSPDLRLTW LQNMAGKHSE RSNHAEAAQC LVHSAALVAE YLSMLEDRKY LPVGCVTFQN ISSNVLEESA VSDDVVSPDE EGICSGKYFT ESGLVGLLEQ AAASFSMAGM YEAVNEVYKV LIPIHEANRD AKKLSTIHGK LQEAFSKIVH QSTGWERMFG TYFRVGFYGT KFGDLDEQEF VYKEPAITKL AEISHRLEGF YGERFGEDVV EVIKDSNPVD KCKLDPNKAY IQITYVEPYF DTYEMKDRIT YFDKNYNLRR FMYCTPFTLD GRAHGELHEQ FKRKTILTTS HAFPYIKTRV NVTHKEEIIL TPIEVAIEDM QKKTQELAFA THQDPADPKM LQMVLQGSVG TTVNQGPLEV AQVFLSEIPS DPKLFRHHNK LRLCFKDFTK RCEDALRKNK SLIGPDQKEY QRELERNYHR LKEALQPLIN RKIPQLYKAV LPVTCHRDSF SRMSLRKMDL //