DOCK9_RAT
ID DOCK9_RAT Reviewed; 720 AA.
AC Q63603;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Dedicator of cytokinesis protein 9;
DE AltName: Full=Cdc42 guanine nucleotide exchange factor zizimin-1;
DE AltName: Full=Protein TRG;
DE Flags: Fragment;
GN Name=Dock9; Synonyms=Trg;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Fischer;
RA Pianese L., Porcellini A., Avvedimento V.E., D'Esposti F., Feliciello A.,
RA Monticelli A., Musti A.M., Tortora G., Varrone S., Cocozza S.;
RT "A novel thyroid transcript negatively regulated by tsh.";
RL Life Sci. Adv. (Mol. Biol.) 13:75-83(1994).
CC -!- FUNCTION: Guanine nucleotide-exchange factor (GEF) that activates CDC42
CC by exchanging bound GDP for free GTP. Overexpression induces filopodia
CC formation (By similarity). {ECO:0000250|UniProtKB:Q8BIK4,
CC ECO:0000250|UniProtKB:Q9BZ29}.
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 -!- DOMAIN: The DOCKER domain is necessary and sufficient for the GEF
CC activity. {ECO:0000250|UniProtKB:Q8BIK4}.
CC -!- MISCELLANEOUS: 'Zizim' means 'spike' in Hebrew.
CC -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA48220.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X68101; CAA48220.1; ALT_FRAME; mRNA.
DR PIR; I60486; I60486.
DR AlphaFoldDB; Q63603; -.
DR SMR; Q63603; -.
DR IntAct; Q63603; 1.
DR PRIDE; Q63603; -.
DR RGD; 629617; Dock9.
DR InParanoid; Q63603; -.
DR PhylomeDB; Q63603; -.
DR Proteomes; UP000002494; Unplaced.
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; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR Gene3D; 1.20.58.740; -; 1.
DR Gene3D; 1.25.40.410; -; 1.
DR InterPro; IPR026791; DOCK.
DR InterPro; IPR026796; DOCK9.
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 PANTHER; PTHR23317:SF77; PTHR23317:SF77; 1.
DR Pfam; PF06920; DHR-2; 1.
DR PROSITE; PS51651; DOCKER; 1.
PE 2: Evidence at transcript level;
KW Guanine-nucleotide releasing factor; Membrane; Reference proteome.
FT CHAIN <1..720
FT /note="Dedicator of cytokinesis protein 9"
FT /id="PRO_0000190001"
FT DOMAIN 186..638
FT /note="DOCKER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00984"
FT REGION 277..638
FT /note="Interaction with CDC42"
FT /evidence="ECO:0000250|UniProtKB:Q9BZ29"
FT NON_TER 1
SQ SEQUENCE 720 AA; 82455 MW; 650A4F4BD3DF816C CRC64;
KLSRGHSPLM KKVFDVYLCF LQKHQSEMAL KNVFTALRSL IYKFPSTFYE GRADMCASLC
YEVLKCCNSK LSSIRTEASQ LLYFLMRNNF DYTGKKSFVR THLQVIISLS QLIADVVGIG
GTRFQQSLSI INNCANSDRL IKHTSFSSDV KDLTKRIRTV LMATAQMKEH ENDPEMLVDL
QYSLAKSYAS TPELRKTWLD SMARIHVKNG DLSEAAMCYV HVTALVAEYL TRKEADLALQ
REPPVFPYSH TSCQRKSRGG MFRQGCTAFR VITPNIDEEA SMMEDVGMQD VHFNEDVLME
LLEQCADGLW KAERLRAGLL TSINSSSPSM KSGGTLETTH LYDTLHRPYS KVTEVITRAA
GSWDLLPGGL FGQGFFEDED GKEYIYKEPK LTPLSEISQR LLKLYSDKFG SENVKMIQDS
GKVNPKDLDS KFAYIQVTHV TPFFDEKELQ ERKTEFERCH NIRRFMFEMP FTQTGKRQGG
VEEQCKRRTI LTAIHCFPYV KKRIPVMYQH HTDLNPIEVA IDEMSKKVAE LHQLCSSAEV
DMIKLQLKLQ GSVSVQVNAG PLAYARAFLD DTNTKRYPDN KVKLLKEVFR QFVEACGQAL
AVNERLIKED QLEYQEEMKA NYREIRKELS DIIVPRICPG EDKRATKFPA HLQRHQRDTN
KHSGSRVDQF ILSCVTLPHE PHVGTCFVMC KLRTTFRANH WFCQAQEEAM GNGREKEPGL