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   27-MAR-2024, entry version 124.
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; 10090-ENSMUSP00000033419; -.
DR   PeptideAtlas; A2AF47; -.
DR   ProteomicsDB; 279794; -.
DR   Pumba; A2AF47; -.
DR   Antibodypedia; 29701; 67 antibodies from 17 providers.
DR   Ensembl; ENSMUST00000033419.13; ENSMUSP00000033419.6; ENSMUSG00000031093.15.
DR   GeneID; 75974; -.
DR   KEGG; mmu:75974; -.
DR   UCSC; uc009sxi.1; mouse.
DR   AGR; MGI:1923224; -.
DR   CTD; 139818; -.
DR   MGI; MGI:1923224; Dock11.
DR   VEuPathDB; HostDB:ENSMUSG00000031093; -.
DR   eggNOG; KOG1997; Eukaryota.
DR   GeneTree; ENSGT00940000155658; -.
DR   InParanoid; A2AF47; -.
DR   OMA; YDHYIPL; -.
DR   OrthoDB; 5480873at2759; -.
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 76 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 224 other cell types or tissues.
DR   ExpressionAtlas; A2AF47; baseline and differential.
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   CDD; cd11700; DHR2_DOCK11; 1.
DR   CDD; cd13267; PH_DOCK-D; 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   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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; IPR046769; DOCKER_Lobe_A.
DR   InterPro; IPR046770; DOCKER_Lobe_B.
DR   InterPro; IPR046773; DOCKER_Lobe_C.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR23317; DEDICATOR OF CYTOKINESIS DOCK; 1.
DR   PANTHER; PTHR23317:SF81; DEDICATOR OF CYTOKINESIS PROTEIN 11; 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   Pfam; PF00169; PH; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS51650; C2_DOCK; 1.
DR   PROSITE; PS51651; DOCKER; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   Genevisible; A2AF47; MM.
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
//