DOCK7_HUMAN
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 03-AUG-2022, entry version 176.
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; 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};
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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 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; 190.
DR CORUM; Q96N67; -.
DR ELM; Q96N67; -.
DR IntAct; Q96N67; 89.
DR MINT; Q96N67; -.
DR STRING; 9606.ENSP00000251157; -.
DR GlyGen; Q96N67; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96N67; -.
DR MetOSite; Q96N67; -.
DR PhosphoSitePlus; 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; Q96N67; -.
DR PeptideAtlas; Q96N67; -.
DR PRIDE; 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 Antibodypedia; 1929; 119 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 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; DLNDGHH; -.
DR OrthoDB; 20156at2759; -.
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; 68 hits in 1078 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 183 other tissues.
DR ExpressionAtlas; Q96N67; baseline and differential.
DR Genevisible; Q96N67; HS.
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:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
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 Gene3D; 1.20.58.740; -; 1.
DR Gene3D; 1.25.40.410; -; 1.
DR Gene3D; 2.60.40.150; -; 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 PANTHER; PTHR23317; PTHR23317; 1.
DR Pfam; PF06920; DHR-2; 1.
DR Pfam; PF14429; DOCK-C2; 1.
DR Pfam; PF11878; DUF3398; 1.
DR PROSITE; PS51650; C2_DOCK; 1.
DR PROSITE; PS51651; DOCKER; 1.
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
