ID A0A2K6QLJ9_RHIRO Unreviewed; 2000 AA.
AC A0A2K6QLJ9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Dedicator of cytokinesis 4 {ECO:0000313|Ensembl:ENSRROP00000029651.1};
GN Name=DOCK4 {ECO:0000313|Ensembl:ENSRROP00000029651.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000029651.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000029651.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000256|PROSITE-
CC ProRule:PRU00983}.
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DR STRING; 61622.ENSRROP00000029651; -.
DR Ensembl; ENSRROT00000054054.1; ENSRROP00000029651.1; ENSRROG00000038597.1.
DR GeneTree; ENSGT00940000155659; -.
DR OMA; MRDFGHS; -.
DR Proteomes; UP000233200; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IEA:Ensembl.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0060326; P:cell chemotaxis; IEA:Ensembl.
DR GO; GO:1904694; P:negative regulation of vascular associated smooth muscle contraction; IEA:Ensembl.
DR GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; IEA:Ensembl.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd08695; C2_Dock-B; 1.
DR CDD; cd11705; DHR2_DOCK4; 1.
DR CDD; cd12049; SH3_DOCK4_B; 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; 1.20.1270.350; Dedicator of cytokinesis N-terminal subdomain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR037811; C2_Dock-B.
DR InterPro; IPR027007; C2_DOCK-type_domain.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037014; DHR2_DOCK4.
DR InterPro; IPR026791; DOCK.
DR InterPro; IPR035769; DOCK4_SH3.
DR InterPro; IPR043161; DOCK_C_lobe_A.
DR InterPro; IPR043162; DOCK_C_lobe_C.
DR InterPro; IPR032376; DOCK_N.
DR InterPro; IPR042455; DOCK_N_sub1.
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; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR45653; DEDICATOR OF CYTOKINESIS; 1.
DR PANTHER; PTHR45653:SF7; DEDICATOR OF CYTOKINESIS PROTEIN 4; 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; PF16172; DOCK_N; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51650; C2_DOCK; 1.
DR PROSITE; PS51651; DOCKER; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000233200};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 1..56
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 390..563
FT /note="C2 DOCK-type"
FT /evidence="ECO:0000259|PROSITE:PS51650"
FT DOMAIN 1224..1630
FT /note="DOCKER"
FT /evidence="ECO:0000259|PROSITE:PS51651"
FT REGION 1682..1763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1776..2000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1500..1527
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1682..1733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1736..1750
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1791..1810
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1831..1908
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1953..1969
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2000 AA; 228889 MW; 24722A02A2DE0F74 CRC64;
PLIASFRGTV PYGLSLEIGD TVQILEKCDG WYRGFALKNP NIKGIFPSSY VHLKNACVKN
KGQFEMVIPT EDSVITEMTS TLRDWGTMWK QLYVRNEGDL FHRLWHIMNE ILDLRRQVLV
GHLTHDRMKD VKRHITARLD WGNEQLGLDL VPRKEYAMVD PEDISITELY RLMEHRHRKK
DTPVQASSHH LFVQMKSLMC SNLGEELEVI FSLFDSKENR PISERFFLRL NRNGLPKAPD
KPERHCSLFV DLGSSELRKD VYITVHIIRI GRMGAGEKKN ACSVQYRRPF GCAVLSIADL
LTGETKDDLI LKVYMCNTES EWYQIHENII KKLNARYNLT GSNAGLAVSL QLLHGDIEQI
RREYSSVFSH GVSITRKLGF SNIIMPGEMR NDLYITIERG EFEKGGKSVA RNVEVTMFIV
DSSGQTLKDF ISFGSGEPPA SEYHSFVLYH NNSPRWSELL KLPIPVDKFR GAHIRFEFRH
CSTKEKGEKK LFGFSFVPLM QEDGRTLPDG THELIVHKCE ENTNLQDTTR YLKLPFSKGI
FLGNNNQAMK ATKESFCITS FLCSTKLTQN GDMLDLLKWR THPDKITGCL SKLKEIDGSE
IVKFLQDTLD TLFGILDENS QKYGSKVFDS LVHIINLLQD SKFHHFKPVM DTYIESHFAG
ALAYRDLIKV LKWYVDRITE AERQEHIQEV LKAQEYIFKY IVQSRRLFSL ATGGQNEEEF
RCCIQELLMS VRFFLSQESK GSGALSQSQA VFLSSFPAVY SELLKLFDVR EVANLVQDTL
GSLPTILHVD DSLQAIKLQC IGKTVESQLY TNPDSRYILL PVVLHHLHIH LQEQKDLIMC
ARILSNVFCL IKKNSSEKSV LEEIDVIVAS LLDILLRTIL EITSRPQPSS SAMRFQFQDV
TRTGFLNRES LHDSSTLSTF SFCADTYGKL PMTGRHTGEF VACLLSLLRQ MTDRHYQQLL
DSFNTKEELR DFLLQIFTVF RILIRPEMFP KDWTVMRLVA NNVIITTVLY LSDALRKNFL
NENFDYKIWD SYFYLAVIFI NQLCLQLEMF TPSKKKKVLE KYGDMRVTMG CEIFSMWQNL
GEHKLHFIPA LIGPFLEVTL IPQPDLRNVM IPIFHDMMDW EQRRSGNFKQ VEAKLIDKLD
SLMSEGKGDE TYRELFNSII PLFGPYPSLL KKIERETWRE SGVSLIATVT RLMERLLDYR
DCMKMGEVDG KKIGCTVSLL NFYKTELNKE EMYIRYIHKL YDLHLKAQNF TEAAYTLLLY
DELLEWSDRP LREFLTYPMQ TEWQRKEHLH LTIIQNFDRG KCWENGIILC RKIAEQYESY
YDYRNLSKMR MMEASLYDKI MDQQRLEPEF FRVGFYGKKF PFFLRNKEFV CRGHDYERLE
AFQQRMLNEF PHAIAMQHAN QPDETIFQAE AQYLQIYAVT PIPESQEVLQ REGVPDNIKS
FYKVNHIWKF RYDRPFHKGT KDKENEFKSL WVERTSLYLV QSLPGISRWF EVEKREVVEM
SPLENAIEVL ENKNQQLKTL ISQCQTRQMQ NINPLTMCLN GVIDAAVNGG VSRYQEAFFV
KEYILSHPED GEKIARLREL MLEQAQILEF GLAVHEKFVP QDMRPLHKKL VDQFFVMKSS
LGIQEFSACM QASPVHFPNG SPRVCRNSAP ASVSPDGTRV IPRRSPLSYP AVNRYSSSSL
SSQASAEVSN ITGQSESSDE VFNMQPSPST SSLSSTHSAS PNVTSSAPSS ARASPLLSDK
HKHSRENSCL SPRDRPCSAI YPTPVEPSQR MLFNHIGDGA LPRSDPNLSA PEKAVNPTPS
SWSLDSGKEA KNMSDSGKLI SPPVPPRPTQ TASPARHTTS VSPSPAGRSP LKGSVQSFTP
SPVEYHSPGL ISNSPVLSGS YSSGISSLSR CSTSETSGFE NQVNEQSVPL PVPVPVPMPV
YGGEEPVRKE SKTPPPYSVY ERTLRRPVPL PHSLSIPVTP EPPALPPKPL AARSSHLENG
ARRTDPGPRP RPLPRKVSQL
//
