ID A0A3Q7TVY1_VULVU Unreviewed; 2139 AA.
AC A0A3Q7TVY1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Dedicator of cytokinesis protein 9 isoform X15 {ECO:0000313|RefSeq:XP_025859455.1};
GN Name=DOCK9 {ECO:0000313|RefSeq:XP_025859455.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025859455.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025859455.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025859455.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025859455.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000256|PROSITE-
CC ProRule:PRU00983}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_025859455.1; XM_026003670.1.
DR Proteomes; UP000286640; Unplaced.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd08697; C2_Dock-D; 1.
DR CDD; cd11698; DHR2_DOCK9; 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:SF77; DEDICATOR OF CYTOKINESIS PROTEIN 9; 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.
PE 3: Inferred from homology;
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000286640}.
FT DOMAIN 185..292
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 651..829
FT /note="C2 DOCK-type"
FT /evidence="ECO:0000259|PROSITE:PS51650"
FT DOMAIN 1623..2101
FT /note="DOCKER"
FT /evidence="ECO:0000259|PROSITE:PS51651"
FT REGION 301..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1267..1309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2139 AA; 244091 MW; 13BA2BB6D722EB8A CRC64;
MGCTTSVILF KGIRTVFERN CAYMCKQQGE NNALEYTAYH WTKEDSELLI SSCLAKPKLI
EPLDYENVIV QKKTQILNDC LREMLLFPYD DFQTATLRRQ GRYMCSTVPA DAEEEAQSLF
VTECIKTYNS DWHLVNYKFE DYSGEFRQLP NKVAKLDKLP VHVYEVDEEV DKDEDAASLG
SQKGGITKHG WLYKGNMNSA ISVTMRSFKR RFFHLLQLGD GSYNLNFYKD EKISKEPKGS
IFLDSCMGVV QNNKVRRFAF ELKMQDKSSY LLAADSEAEM EEWITILNKI LQLNFEAAMQ
EKRNGDSHED DEQSKFEGSG SGLDSYLPEL AKSTREAEIK LKSESRVKLF YLDPDAQKLD
FTSAEPEVKP FEEKFGKRIL VKCNDLSFNL QCCVAENEEG PTTNVEPFFV TLSLFDIKYN
RKISADFHVD LNHFSVRQML ATTSPALMNG GRPSSPVLQD ILQEAAMQYP KQGIFSVTCP
HPDIFLVARI EKVLQGSITH GAEPYMKSSD SSKVAQKVLK NAKQACQRLG QYRMPFAWAA
RTLFKDTSGN LDKNARFSAL YRQDSNKLSN DDMLKFLADF RKPEKMAKLP VILGNLDITI
DNVSSDFPNY VNSSYIPMKQ FETCSKTPIT FEVEEFVPCI PKHTQPYTIY NNHLYVYPKY
LKYDSQKSFA KARNIAICIE FKDSDEEDSQ PLKCIYGRPG GPVFTRSAFA AVLHHHQNPE
FYDEIKIELP TQLHGKHHLL FTFFHVSCDS SSKGSTKKKD VVETQVGYSW LPLLKDGRVV
TSEQHVPVSA NLPSGYLGYQ ELGMGRHYGP EIKWVEGSKP LLKVSTHLVS TVYTQDQHLH
NFFQYCQKTE SGAQALGSEL VKYLKSLHAM EGHVMIAFLP TILNQLFRVL TRATQEEVAV
NVTRVIIHVV AQCHEEGLES HLRSYVKYAY KAEPYIASEY KTVHEELTKA MTTILKPSAD
FLTSNKLLKY SWFFFDVLIK SMAQHLIENS KVKLLRNQRF PASYHHAVET VVNMLMPHIT
QKFRDNPEAS KNANHSLAVF IKRCFTFMDR GFVFKQINNY ISCFAPGDPK TLFEYKFEFL
RVVCNHEHYI PLNLPMPFGK GRIQRYQAFL SPTVESNDTP VDLQLDYSLT DEFCRNHFLV
GLLLREVGTA LQECREVRLI AISVLKNLLI KHSFDDRYAS RSHQARIATL YLPLFGLLIE
NVQRINVRDV SPFPVNPGST VKEESLLLPA ANPLVTPQKP GIALDNSLHK DLFGAISGIA
SPYTTSTPNI NSVRNADSRG SLISTDSGNS LPERNTEKSN SLDKHQQSGT LGNSVVRCDK
LDQSEIKSLL MCFLYILKSM SDDALFTYWN KASTSELMDF FTISEVCLHQ FQYMGKRYIA
SVRKISSVLG ISVDNGYGHS DADVLHQSLL EANIATEVCL TALDTLSLFT LAFKNQLLAD
HGHNPLMKKV FDVYLCFLQK HQSETALKNV FTALRSFIYK FPSTFYEGRA DMCAALCYEI
LKCCNSKLSS IRTEASQLLY FLMRNNFDYT GKKSFVRTHL QVIISVSQLI ADVVGIGGTR
FQQSLSIINN CANSDRLIKH TTFSSDVKDL TKRIRTVLMA TAQMKEHEND PEMLVDLQYS
LAKSYASTPE LRKTWLDSMA RIHVKNGDLS EAAMCYVHVT ALVAEYLTRK EADIALRPEL
PLFPYSHSTC QRRRRGGMFR QGCTAFRVIT PNIDEEASMM EDVGMQDVHF NEVSASAGVG
LQFDVLMELL EQCADGLWKA ERYELIADIY KLIIPIYEKR RDFERLAHLY DTLHRAYSKV
TEVMHSGRRL LGTYFRVAFF GQAAQYQFTD SETDVEGFFE DEDGKEYIYK EPKLTPLSEI
SQRLLKLYSD KFGSENVKMI QDSGKVNPKD LDSKYAYIQV THVIPFFDEK ELQERKTEFE
RSHNIRRFMF EMPFTQTGKR QGGVEEQCKR RTILTAIHCF PYVKKRIPVM YQHHTDLNPI
EVAIDEMSKK VAELRQLCSS AEVDMIKLQL KLQGSVSVQV NAGPLAYARA FLDDTNTKRY
PDNKVKLLKE VFRQFVEACG QALAVNERLI KEDQLEYQEE MKANYREMAK ELSEIMHEQI
CPLEEKTSVL PNSLHIFNAI SGTPTSTMVH GMTSSSSVV
//