DOCK9_MOUSE
ID DOCK9_MOUSE Reviewed; 2055 AA.
AC Q8BIK4; Q921Y6;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-JUL-2003, sequence version 2.
DT 25-MAY-2022, entry version 146.
DE RecName: Full=Dedicator of cytokinesis protein 9;
DE AltName: Full=Cdc42 guanine nucleotide exchange factor zizimin-1;
DE Short=Zizimin-1 {ECO:0000303|PubMed:25729399};
GN Name=Dock9 {ECO:0000312|MGI:MGI:106321};
GN Synonyms=D14Wsu89e, Kiaa1058, Ziz1 {ECO:0000305};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 212-2055 (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-181; SER-444;
RP SER-453; SER-1270 AND SER-1273, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=22494997; DOI=10.1186/1742-4933-9-2;
RA Sakabe I., Asai A., Iijima J., Maruyama M.;
RT "Age-related guanine nucleotide exchange factor, mouse Zizimin2, induces
RT filopodia in bone marrow-derived dendritic cells.";
RL Immun. Ageing 9:2-2(2012).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=25729399; DOI=10.1186/s12979-015-0028-x;
RA Matsuda T., Yanase S., Takaoka A., Maruyama M.;
RT "The immunosenescence-related gene Zizimin2 is associated with early bone
RT marrow B cell development and marginal zone B cell formation.";
RL Immun. Ageing 12:1-1(2015).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND DOMAIN.
RX PubMed=25851601; DOI=10.1091/mbc.e14-08-1310;
RA Jaudon F., Raynaud F., Wehrle R., Bellanger J.M., Doulazmi M., Vodjdani G.,
RA Gasman S., Fagni L., Dusart I., Debant A., Schmidt S.;
RT "The RhoGEF DOCK10 is essential for dendritic spine morphogenesis.";
RL Mol. Biol. Cell 26:2112-2127(2015).
CC -!- FUNCTION: Guanine nucleotide-exchange factor (GEF) that activates CDC42
CC by exchanging bound GDP for free GTP (PubMed:25851601). Overexpression
CC induces filopodia formation (By similarity).
CC {ECO:0000250|UniProtKB:Q9BZ29, ECO:0000269|PubMed:25851601}.
CC -!- SUBUNIT: Homodimer. Interacts preferentially with nucleotide-depleted
CC CDC42 (By similarity). {ECO:0000250|UniProtKB:Q9BZ29}.
CC -!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000305}.
CC Note=Associated with membranes. {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BIK4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BIK4-2; Sequence=VSP_007712, VSP_007713, VSP_007714,
CC VSP_007715;
CC Name=3;
CC IsoId=Q8BIK4-3; Sequence=VSP_007711;
CC -!- TISSUE SPECIFICITY: Expressed in lung (PubMed:25729399,
CC PubMed:22494997). Also detected in Peyers patches, thymus, brain and
CC lymph nodes (PubMed:22494997). Expressed in Purkinje cells
CC (PubMed:25851601). {ECO:0000269|PubMed:22494997,
CC ECO:0000269|PubMed:25729399, ECO:0000269|PubMed:25851601}.
CC -!- DOMAIN: The DOCKER domain is necessary and sufficient for the GEF
CC activity. {ECO:0000269|PubMed:25851601}.
CC -!- MISCELLANEOUS: 'Zizim' means 'spike' in Hebrew. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000255|PROSITE-
CC ProRule:PRU00983}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH09134.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC65713.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK122431; BAC65713.1; ALT_INIT; mRNA.
DR EMBL; AK045750; BAC32480.1; -; mRNA.
DR EMBL; BC009134; AAH09134.1; ALT_INIT; mRNA.
DR EMBL; BC046250; AAH46250.1; -; mRNA.
DR CCDS; CCDS88728.1; -. [Q8BIK4-1]
DR AlphaFoldDB; Q8BIK4; -.
DR SMR; Q8BIK4; -.
DR STRING; 10090.ENSMUSP00000047881; -.
DR iPTMnet; Q8BIK4; -.
DR PhosphoSitePlus; Q8BIK4; -.
DR EPD; Q8BIK4; -.
DR MaxQB; Q8BIK4; -.
DR PaxDb; Q8BIK4; -.
DR PeptideAtlas; Q8BIK4; -.
DR PRIDE; Q8BIK4; -.
DR ProteomicsDB; 279465; -. [Q8BIK4-1]
DR ProteomicsDB; 279466; -. [Q8BIK4-2]
DR ProteomicsDB; 279467; -. [Q8BIK4-3]
DR UCSC; uc007val.1; mouse. [Q8BIK4-3]
DR UCSC; uc011zqg.1; mouse. [Q8BIK4-1]
DR MGI; MGI:106321; Dock9.
DR eggNOG; KOG1997; Eukaryota.
DR InParanoid; Q8BIK4; -.
DR PhylomeDB; Q8BIK4; -.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR ChiTaRS; Dock9; mouse.
DR PRO; PR:Q8BIK4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8BIK4; protein.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd08697; C2_Dock-D; 1.
DR Gene3D; 1.20.58.740; -; 1.
DR Gene3D; 1.25.40.410; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR037809; C2_Dock-D.
DR InterPro; IPR027007; C2_DOCK-type_domain.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR026791; DOCK.
DR InterPro; IPR026796; DOCK9.
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; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR23317; PTHR23317; 1.
DR PANTHER; PTHR23317:SF77; PTHR23317:SF77; 1.
DR Pfam; PF06920; DHR-2; 1.
DR Pfam; PF14429; DOCK-C2; 1.
DR Pfam; PF11878; DUF3398; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51650; C2_DOCK; 1.
DR PROSITE; PS51651; DOCKER; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Guanine-nucleotide releasing factor; Membrane;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..2055
FT /note="Dedicator of cytokinesis protein 9"
FT /id="PRO_0000190000"
FT DOMAIN 185..292
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 649..827
FT /note="C2 DOCK-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00983"
FT DOMAIN 1614..2055
FT /note="DOCKER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00984"
FT REGION 301..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1253..1291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1679..2055
FT /note="Interaction with CDC42"
FT /evidence="ECO:0000250|UniProtKB:Q9BZ29"
FT COMPBIAS 301..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 936
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZ29"
FT MOD_RES 1244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZ29"
FT MOD_RES 1250
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZ29"
FT MOD_RES 1264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZ29"
FT MOD_RES 1270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..1366
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007711"
FT VAR_SEQ 1364
FT /note="R -> RNQEGLGPIGHDRKSQTLPVSRNR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007712"
FT VAR_SEQ 1661
FT /note="K -> KEADLALQREPPAFPYSHSTCQRKSWG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007713"
FT VAR_SEQ 1777..1790
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007714"
FT VAR_SEQ 2054..2055
FT /note="MG -> ICPLEEKTSVLPNSLHIFNAISGTPTSTVVQGLTSSSSVV (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007715"
FT CONFLICT 441
FT /note="A -> T (in Ref. 3; AAH46250)"
FT /evidence="ECO:0000305"
FT CONFLICT 1288
FT /note="Missing (in Ref. 3; AAH46250)"
FT /evidence="ECO:0000305"
FT CONFLICT 1602
FT /note="P -> R (in Ref. 1; BAC65713)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2055 AA; 235312 MW; D2AC9C53F6177A66 CRC64;
MGCTTSVILF KGIRTVFERN CAYMCKQPGE SNALEYTAYN WSKEDSELSI AFCLAKPKLI
EPLDYENVIV QKKTQILNDC LREMLLFPYD DFQTAILRRQ GRYLRSTVPA NAEEEAQSLF
VTECIKTYNS DWHLVTYKYE DYSGEFRQLP NKVPKLDKLP VHVYEVDEEA DKDEDAASLG
SQKGGITKHG WLYKGNMNSA ISVTMRSFKR RFFHLIQLGD GSYNLNFYKD EKISKEPKGS
IFLDSCMGVI QNNRVRRFAF ELKMQDKSSY LLAADSEAEM EEWVTVLNKI LQLNFEAAMQ
EKRNGDPHED DEQSKLEGSG SGLDSYLPEL AKSTREAEIK LKSESRVKLF YLDPDTQKLD
FSSAEPEVKP FEEKFGKRIL VKCNDLSFNL QCCVAENEEG PTTNVEPFFV TLSLFDIKYN
RKISADFHVD LNHFSVRQML APTSPALMNG GQSPPAFQDA LHTAMQYPKQ GIFSVTCPHP
DIFLVARIEK VLQGSITHCA EPYMRSSDSS KVAQKVLKNA KQACQRLGQY RMPFAWAART
LFKDTSGNLD KNARFSAIYR QDSNKLSNDD MLKLLADFRK PEKMAKLPVI LGNLDITIDS
VSCDFPNYLN SSYIPMRQFE TCSKSPITFE VEEFVPCIPK HTQPYTVYSN HLYVYPKYLK
YDSQKSFAKA RNIAICIEFK DSDEEDSQPL KCIYGRPGGP VFTRSALAAV LHHQQNPEFY
DEIKIELPAQ LHERHHLLFT FFHVSCDNST KGSTKKKDAV ETQVGFSWLP LLKDGRVLTS
EQHIPVSANL PSGYLGYQEL GMGRHYGPEV KWVEGGKPLL KISTHLVSTV YTQDQHLHNF
FQYCQKTESG AQASGSELVK YLKSLHAMEG HVMIAFLPTI LNQLFRVLTR ATQEEVAVNV
TRVIIHVVAQ CHEEGLESHL RSYVKFAYKA EPYVASEYKT VHEELTKSMT TILKPSADFL
TSNKLLKYSW FFFDVLIKSM AQHLIENNKV KLLRNQRFPA SYHHAVETVV NMLMPHITQK
FRDNPEASKN ANHSLAVFIK RCFTFMDRGF VFKQINNYIS CFAPGDPKTL FEYKFEFLRV
VCNHEHYIPL NLPMPFGKGR IQRYQDLQLD YSLTDEFCRN HFLVGLLLRE VGTALQEFRE
VRVIAISMLK NLLIKHSFDD RYNSRSHQAR IATLYLPLFG LLIENVQRIN VRDVSPFPVN
PGSIVKDEAL AVPAGNPLMT PQKGNTLDHS LHKDLLGAIS GIASPYTAST PNINSVRNAD
SRGSLISTDS GNSLPDRNPE KSNSLDKQQQ SGMLGNSVVR CDKLDQSEIK SLLMCFLYVL
KSMSDDALFT YWNKASTAEL MDFFTISEVC LHQFQYMGKR YIARTGMMHA RLQQLGSLDN
SVTFNHSYGH SEADVVHQSL LEANIATEVC LTALDTLSLF TLAFKNQLLA DHGHNPLMKK
VFDVYLCFLQ KHQSEMALKN VFTALRSLIY KFPSAFYEGR ADMCASLCYE VLKCCNSKLS
SIRTEASQLL YFLMRNNFDY TGKKSFVRTH LQVIISVSQL IADVVGIGGT RFQQSLSIIN
NCANSDRIIK HTSFSSDVKD LTKRIRTVLM ATAQMKEHEN DPEMLVDLQY SLAKSYASTP
ELRKTWLDSM ARIHVKNGDL SEAAMCYVHV TALVAEYLTR KGMFRQGCTA FRVITPNIDE
EASMMEDVGM QDVHFNEDVL MELLEQCADG LWKAERYELI ADIYKLIIPI YEKRRDFERL
AHLYDTLHRA YSKVTEVMHS GRRLLGTYFR VAFFGQAAQY QFTDSETDVE GFFEDEDGKE
YIYKEPKLTP LSEISQRLLK LYSDKFGSEN VKMIQDSGKV NPKDLDSKFA YIQVTHVTPF
FDEKELQERR TEFERCHNIR RFMFEMPFTQ TGKRQGGVEE QCKRRTILTA IHCFPYVKKR
IPVMYQHHTD LNPIEVAIDE MSKKVAELRQ LCSSAEVDMI KLQLKLQGSV SVQVNAGPLA
YARAFLDDTN TKRYPDNKVK LLKEVFRQFV EACGQALAVN ERLIKEDQLE YQEEMKANYR
EMAKELSDIM REQMG
