DOC11_MOUSE
ID DOC11_MOUSE Reviewed; 2073 AA.
AC A2AF47; Q5KTP7;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Dedicator of cytokinesis protein 11 {ECO:0000312|MGI:MGI:1923224};
DE AltName: Full=Activated Cdc42-associated guanine nucleotide exchange factor;
DE Short=ACG;
DE AltName: Full=Zizimin-2 {ECO:0000303|PubMed:25729399};
GN Name=Dock11 {ECO:0000312|MGI:MGI:1923224};
GN Synonyms=Ziz2 {ECO:0000303|PubMed:25729399};
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 [MRNA], INTERACTION WITH CDC42, TISSUE SPECIFICITY,
RP FUNCTION, AND DOMAIN.
RC TISSUE=Spleen;
RX PubMed=15710388; DOI=10.1016/j.febslet.2005.01.006;
RA Nishikimi A., Meller N., Uekawa N., Isobe K., Schwartz M.A., Maruyama M.;
RT "Zizimin2: a novel, DOCK180-related Cdc42 guanine nucleotide exchange
RT factor expressed predominantly in lymphocytes.";
RL FEBS Lett. 579:1039-1046(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CDC42, FUNCTION, AND
RP DOMAIN.
RX PubMed=16968698; DOI=10.1074/jbc.m606248200;
RA Lin Q., Yang W., Baird D., Feng Q., Cerione R.A.;
RT "Identification of a DOCK180-related guanine nucleotide exchange factor
RT that is capable of mediating a positive feedback activation of Cdc42.";
RL J. Biol. Chem. 281:35253-35262(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, Pancreas, Spleen, 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 [6]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION BY LPS.
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 [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND 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 [8]
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:15710388, PubMed:16968698,
CC PubMed:25851601). Required for marginal zone (MZ) B-cell development,
CC is associated with early bone marrow B-cell development, MZ B-cell
CC formation, MZ B-cell number and marginal metallophilic macrophages
CC morphology (PubMed:25729399). Facilitates filopodia formation through
CC the activation of CDC42 (PubMed:22494997).
CC {ECO:0000269|PubMed:15710388, ECO:0000269|PubMed:16968698,
CC ECO:0000269|PubMed:22494997, ECO:0000269|PubMed:25729399,
CC ECO:0000269|PubMed:25851601}.
CC -!- SUBUNIT: Interacts with CDC42. {ECO:0000269|PubMed:15710388,
CC ECO:0000269|PubMed:16968698}.
CC -!- TISSUE SPECIFICITY: Expressed in spleen, thymus, mesenteric lymph nodes
CC (MLN), bone marrow and peripheral blood lymphocytes. Enriched in B-
CC cells from germinal centers. Expressed in B-, T- and dendritic cells as
CC well as Purkinje cells (PubMed:22494997, PubMed:25851601).
CC {ECO:0000269|PubMed:15710388, ECO:0000269|PubMed:22494997,
CC ECO:0000269|PubMed:25729399, ECO:0000269|PubMed:25851601}.
CC -!- DEVELOPMENTAL STAGE: In spleen, expression is down-regulated in aged
CC mice. {ECO:0000269|PubMed:22494997}.
CC -!- INDUCTION: In dendritic cells, the expression is up-regulated by LPS
CC and anti-Fc-gamma receptor. {ECO:0000269|PubMed:22494997}.
CC -!- DOMAIN: The DOCKER domain is necessary for the GEF activity
CC (PubMed:25851601, PubMed:15710388). The DOCKER domain mediates
CC interaction with activated CDC42 in conjunction with residues 66-126
CC (PubMed:16968698). {ECO:0000269|PubMed:15710388,
CC ECO:0000269|PubMed:16968698, ECO:0000269|PubMed:25851601}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice are viable and fertile
CC (PubMed:25729399). They have higher percentage of early bone marrow B-
CC cells, but a reduced fraction of marginal zone B-cells. Their
CC percentage of thymic CD4(+) T-cells is increased and they show an
CC altered of morphologymarginal metallophilic macrophages
CC (PubMed:25729399). {ECO:0000269|PubMed:25729399}.
CC -!- MISCELLANEOUS: 'Zizim' means 'spike' in Hebrew. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000255|PROSITE-
CC ProRule:PRU00983}.
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DR EMBL; AB116935; BAD83670.1; -; mRNA.
DR EMBL; AL672023; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL672038; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS40923.1; -.
DR RefSeq; NP_001009947.2; NM_001009947.3.
DR AlphaFoldDB; A2AF47; -.
DR SMR; A2AF47; -.
DR BioGRID; 217880; 18.
DR IntAct; A2AF47; 2.
DR MINT; A2AF47; -.
DR STRING; 10090.ENSMUSP00000033419; -.
DR iPTMnet; A2AF47; -.
DR PhosphoSitePlus; A2AF47; -.
DR EPD; A2AF47; -.
DR jPOST; A2AF47; -.
DR MaxQB; A2AF47; -.
DR PaxDb; A2AF47; -.
DR PeptideAtlas; A2AF47; -.
DR PRIDE; A2AF47; -.
DR ProteomicsDB; 279794; -.
DR Antibodypedia; 29701; 52 antibodies from 17 providers.
DR Ensembl; ENSMUST00000033419; ENSMUSP00000033419; ENSMUSG00000031093.
DR GeneID; 75974; -.
DR KEGG; mmu:75974; -.
DR UCSC; uc009sxi.1; mouse.
DR CTD; 139818; -.
DR MGI; MGI:1923224; Dock11.
DR VEuPathDB; HostDB:ENSMUSG00000031093; -.
DR eggNOG; KOG1997; Eukaryota.
DR GeneTree; ENSGT00940000155658; -.
DR InParanoid; A2AF47; -.
DR OMA; QTVCNHE; -.
DR OrthoDB; 20156at2759; -.
DR PhylomeDB; A2AF47; -.
DR TreeFam; TF313629; -.
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 BioGRID-ORCS; 75974; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Dock11; mouse.
DR PRO; PR:A2AF47; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; A2AF47; protein.
DR Bgee; ENSMUSG00000031093; Expressed in manus and 221 other tissues.
DR ExpressionAtlas; A2AF47; baseline and differential.
DR Genevisible; A2AF47; MM.
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:0001782; P:B cell homeostasis; IMP:UniProtKB.
DR GO; GO:0002315; P:marginal zone B cell differentiation; IMP:UniProtKB.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IMP:UniProtKB.
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; 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 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 Guanine-nucleotide releasing factor; Phosphoprotein; Reference proteome.
FT CHAIN 1..2073
FT /note="Dedicator of cytokinesis protein 11"
FT /id="PRO_0000299559"
FT DOMAIN 165..272
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 640..818
FT /note="C2 DOCK-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00983"
FT DOMAIN 1609..2036
FT /note="DOCKER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00984"
FT REGION 1227..1267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1251..1267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSL3"
FT MOD_RES 16
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSL3"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSL3"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSL3"
FT MOD_RES 248
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSL3"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSL3"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSL3"
FT MOD_RES 1240
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSL3"
FT CONFLICT 1608
FT /note="A -> T (in Ref. 1; BAD83670)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2073 AA; 237771 MW; 2907066969A6A8F8 CRC64;
MAEVRKFTKR LSKPGTAAEL RQSVSEAVRG SVVLEKAKLV EPLDYENVIT QRKTQIYSDP
LRDLLMFPME DISISVIGRQ RRTVQSTVPE DAEKRAQSLF VKECIKTYST DWHVVNYKYE
DFSGDFRMLP CKSLRPEKIP NHVFEIDEDC EKDEDSSSLC SQKGGVIKQG WLHKANVNST
ITVTMKVFKR RYFYLTQLPD GSYILNSYKD EKNSKESKGC IYLDACIDVV QCPKMRRHAF
ELKMLDKYSH YLAAETEQEM EEWLIMLKKI IQINTDSLVQ EKKDTVEAIQ EEETSSQGKA
ENIMASLERS MHPELMKYGR ETEQLNKLSR GDGRQNLFSF DSEVQRLDFS GIEPDVKPFE
EKCNKRFMVN CHDLTFNILG HIGDNAKGPP TNVEPFFINL ALFDVKNNCK ISADFHVDLN
PPSVREMLWG TSTQLSNDGN AKGFSPESLI HGIAESQLCY IKQGIFSVTN PHPEIFLVVR
IEKVLQGNIT HCAEPYIKNS DPIKTAQKVH RTAKQVCSRL GQYRMPFAWA ARPIFKDVQG
SLDLDGRFSP LYKQDSSKLS NEDILKLLSE YKKPEKTKLQ IIPGQLSITV ECVPVDLPNC
ITSSYVPLKP FEKNCQNITV EVEEFVPEMT KYCYPFTIYK NHLYVYPLQL KYDSQKSFAK
ARNIAVCVEF RDSDESDASA LKCIYGKPAG SVFTTNAYAV VSHHNQNPEF YDEIKIELPI
HLHQKHHLLF TFYHVSCEIN TKGTTKKQDT VETPVGFAWV PLLKDGRVIT LEQQLPVSAN
LPPGYLNVND AESRRQSNAD IKWVDGAKPL LKIKTHLEST IYTQDLHVHK FFHHCQLIQS
GSKEVPGELI KYLKCLHAME IQVMIQFLPV ILMQLFRVLT NMTHEDDVPI NCTMVLLHIV
SKCHEEGLES YLRSFIKYSF RPEKPSTLQA QLIHETLATT MIAILKQSAD FLAINKLLKY
SWFFFEIIAK SMATYLLEEN KIKLPRGQRF PEAYHHVLHS LLLAIIPHVT IRYAEIPDES
RNGNYSLASF LKRCLTLMDR GFVFNLINDY ISGFSPKDPK VLAEYKFEFL QTICNHEHYI
PLNLPMAFAK PKLQRVQDSN LEYSLSDEYC KHHFLVGLLL RETSIALQDN YEIRYTAISV
IKNLLIKHAF DTRYQHKNQQ AKIAQLYLPF VGLLLENIQR LAGRDTLYSC AAMPSSASRD
EFPCGFVSPT NRGSLASDKD TAYGSFQNGH GIKREDSRGS LIPEGATGFP DPGSTSENTR
QSSSRSSVSQ YNRLDQYEIR NLLMCYLYIV KMISEDTLLT YWNKVSPQEL INILVLLEVC
LFHFRYMGKR NIARVHDAWL SKHFGIDRKS QTMPALRNRS GVMQARLQHL SSLESSFTLN
HSSATTEADI FHQALLEGNT ATEVSLTVLD TISFFTQCFK NQLLNNDGHN PLMKKVFDIH
LAFLKNGQSE VSLKHVFASL RSFISKFPSA FFKGRVNMCA AFCYEVLKCC TSKISSTRNE
ASALLYLLMR NNFEYTKRKT FLRTHLQIII AVSQLIADVA LSGGSRFQES LFIINNFANS
DRPMKATAFP TEVKDLTKRI RTVLMATAQM KEHEKDPEML IDLQYSLAKS YASTPELRKT
WLDSMAKIHI KNGDFSEAAM CYVHVAALVA EFLHRKKLFP SGCSAFKKIT PNIDEEGAMK
EDAGMMDVHY SEEVLLELLE QCVDGLWKAE RYEVISEISK LIIPIYEKRR EFEKLTQVYR
TLHGAYTKIL EVMHTKKRLL GTFFRVAFYG QSFFEEEDGK EYIYKEPKLT GLSEISLRLV
KLYGEKFGTE NVKIIQDSDK VNAKELDPKF AHIQVTYVKP YFDDKELTER KTEFERNHNI
NRFVFEAPYT LSGKKQGCIE EQCKRRTILT TSNSFPYVKK RIPINCEQQV NLKPIDVATD
EIKDKTAELH KLCSSVDVDM IQLQLKLQGC VSVQVNAGPL AYARAFLNES QANKYPPKKV
NELKDMFRKF IQACSIALEL NERLIKEDQI EYHEGLKSNF RDMVKELSDI IHEQILQEDT
MHSPWMNNTL HVFCAISGTS SNRGYGSPRY AEV
