ID A0A3Q2UZS6_HAPBU Unreviewed; 1984 AA.
AC A0A3Q2UZS6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Dedicator of cytokinesis 4 {ECO:0000313|Ensembl:ENSHBUP00000003857.1};
OS Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000003857.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000003857.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000256|PROSITE-
CC ProRule:PRU00983}.
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DR RefSeq; XP_005915685.1; XM_005915623.2.
DR STRING; 8153.ENSHBUP00000003857; -.
DR Ensembl; ENSHBUT00000009668.1; ENSHBUP00000003857.1; ENSHBUG00000005422.1.
DR GeneID; 102297049; -.
DR CTD; 654774; -.
DR GeneTree; ENSGT00940000155659; -.
DR OrthoDB; 8258at2759; -.
DR Proteomes; UP000264840; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
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; 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; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000264840};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 6..67
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 401..573
FT /note="C2 DOCK-type"
FT /evidence="ECO:0000259|PROSITE:PS51650"
FT DOMAIN 1201..1607
FT /note="DOCKER"
FT /evidence="ECO:0000259|PROSITE:PS51651"
FT REGION 1614..1984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1614..1628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1646..1713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1716..1730
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1814..1877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1934..1953
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1984 AA; 227474 MW; 0990B28F3A6BA4E2 CRC64;
MWIPTEHEKY GVVLASFRGT IQHGLPLEIG DTVQILEKCE GWYRGFILKN PNVKGIFPSS
YIHLKNAHVK NKGQFETVIP DEDSVITEMT STLRDWGAMW KQLYVKNEGD LFHRLWHVMN
EILDLRRQVL VGHLTHDRLR DVKQHITARL DWGNEQLGLD LVPRREFSMV DPDEISVTEL
YRLMEHRHRK KETSTPASTH HLFVHVKSLM SANLGEELEV FFHIYDGREN RPLSERFFVR
LNKSGLPKSP EKTERQCTLF VDLGSSDLRK DVYIVVHIIR IGRMGAGEKK NQCNVQYRRP
FGCAVVSIAD LLTADSKDDH LLKVYACNTE SEWSQIHENI IKKANSRYNL SGSNTGLAVA
LQLLHGDIDQ LRREYMVLFT RGVSITRKLG FSDVIMPGEM RNDLYITLEK GEFEKGGKSV
ARNVEITVYV LDIDGQILKG HVAAGSGEPS VDEYHSLVLY HNNSPRWGDQ IKLPIPVDMF
RGSHVRFEFR HCSTKDKGEK KLFGYSFVPL MQEDGRTLPD GTHELIIHKC EENTSLADCS
RYLKQPFSKP NLPSNNQTLK GTKESFWITS FLCSTKLTQN GDMLDLLKWR AHPERINDSL
SKLKEIDGSE IVKFLQDTLD TLFGILDESS QRYGLKVFDS LVHIINLLQD SKFQHFKPVM
DTYIESHFAG ALSYRDLIKV LKWYVDRIVD AEHQDHIQQV LKASEYIFKY IIQSRRLFSL
ATGGQNEEEF RVCIHELFMS IRFFLSQENK GTTPVAQTQA VFLRTFPAIY GELLKIFTVR
EVAGFVRETL GSLPTTVHPD CPLEAVKLQC IAKTVESQLY INPDSRCILL PVVLRVLQAH
MQEQRDLVMC AQILSSMLSL IKKEENGTAE LVVSEEVELI VESLLGVLLR TILEISNRPQ
PAGTSMRLQF QDVTGEFVAC LLALLRQMSD KHYQKLLQAF SSKDDLRDFL LHIFTVFRIL
IRPEMFPKDW TVMRLVTNNV IITTVLYLSD ALRKNFLNDK FDYKVWDSYF YLSVIFINQP
CLQLESFSPS KRKKILEKYG DMRVMMGCEI FSMWQNLGEH KLNFIPAMIG PFLEVTLVPQ
PDLRNVMIPI FHDMMDWEQR RSGNFKQVEA KLIDKLDSLM SEGKGDETYR ELFNSIIPLF
GPYPSLLKKI ERETWRESGI SLIATVTRLM ERLLDYRDCM KLGEVDGKKI GCTVSLLNFY
KTELNKEEMY IRYIHKLYDL HLKAQNYTEA SYTLLLYDEL LEWSDRPLRE FLNYPMQSEW
QRKEYLHLTI IQNFDRGKCW ENGIILCREL ADQYESYYDY RNLSKMRMME ASLYDKIMDQ
QRLEPEFFRV GFYGKKFPFF LRNKEFVCRG HDYERLEAFQ QRMLNEFPHA IAMQHVNQPD
QTIYQADAQY LQIYAVTPIP DSQDVLQRDG VPDNIKSFYK FNHIWRFRYD RPFHKGTKDK
ENEFKSLWVE RTTLTLIQSL PGISRWFEVE KRELVEVSPL ENAIEVIENK NLQLRTLISQ
CQSRQMQNIN PLTMCLNGVI DAAVNGGLAR YQEAFFVKDY IMNHPEDGEK IGRLRELMFE
QAHILEYGLA VHEKFVPQDM RPLHKKLVDQ FHLMKSSLGI QEFPAYVRAS PVHFTNGSPR
TCRNSVPSII SPDGGRGVAR RSFQRRTSYP AVNRYSSSSL SSQASNEVSN ITGQSESSDE
VFNMQPSPST SSLSSNHSAS PNVTSSAPSS ARGSPQMAEK HKHSRENACL SPRERPVSAI
FPNPLDPAQR APAHQIGDTT LPRSDPNLSA PDKVRPAPSS WSLDSVKERM PHSSDSGGRM
LCPPVPPRPP YSGSSAKNMR SQSPVPTSRS PQKTTVPPFT PSPTECQSAS LVSNSPVLSG
SYSSGISSLS RCSVSEASGT ELPAGDHPPH QLPPPTTLPN SVSSSSDEPI RRENKTPPPY
SVYERNNPRR PVPLPHSLSI PPQTDPPALP PKPHQLRTGS MKLDGTADPR VPRPRPLPRK
VSQL
//
