ID A0A3P8YGY0_ESOLU Unreviewed; 1965 AA.
AC A0A3P8YGY0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Dedicator of cytokinesis 4 {ECO:0000313|Ensembl:ENSELUP00000015842.2};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000015842.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000015842.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000015842.2}
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 Ensembl; ENSELUT00000025111.2; ENSELUP00000015842.2; ENSELUG00000016080.2.
DR GeneTree; ENSGT00940000155659; -.
DR Proteomes; UP000265140; LG23.
DR Bgee; ENSELUG00000016080; Expressed in brain and 14 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; 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 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 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; 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 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 PROSITE; PS51650; C2_DOCK; 1.
DR PROSITE; PS51651; DOCKER; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000265140};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 434..607
FT /note="C2 DOCK-type"
FT /evidence="ECO:0000259|PROSITE:PS51650"
FT DOMAIN 1232..1638
FT /note="DOCKER"
FT /evidence="ECO:0000259|PROSITE:PS51651"
FT REGION 1680..1811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1856..1965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1680..1743
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1744..1758
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1776..1790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1908..1927
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1965 AA; 225299 MW; 9ABA76E16EF4E6F8 CRC64;
MRVALRFNYS EKRDFSDFRA AVHTCLVVAS YQILTCVCVC VCVWFYVCSK ACVLFVFPVL
ASFRGTVQHG LPLEIGDTVH CFILFPQGIF PCSYIYLKNA HIKNKGQFET VIPMEDSVIT
EMTSTLRDWG AMWKRLYVKN EGDLFHRLWH VMNEILDLRR QVLVGHLTND RMRDVKHHIT
ARLDWGNEQL CLDLVPRREF SMVDPDEISV TELFKLMEHR HRKKETPVPA STHHLFVHMK
SLMSFSLGEE LEVFFHIYDS RENRPLSERF FVRLNKNGVP KSPEKTERQC TLFVDLGSSD
LRKDVYIVVH IIRIGRMGAG EKKNLCSVQY RRPFGCAVVS IADLLTADSK DDHLLKVYAC
NTESEWHQIH ESIIRKISSR YNLAGSNTGL AVSLQLLHGD IEQLRREYMV LFTRGVSITK
KLGFSDIIMP GDMRNDLYIT LEKGEFEKGG KSVARNVEIT VYVLDIDGQV MKVSYVAAGS
GEPGGDEYHS FVLYHNNSPR WAEQIKLPIP VDMFRGSHVR FEFRHCSTKD KGEKKLFGYS
FVPLMQEDGR TLPDGTHELI IHKCEENANL QDSARYLKLP FSKANLPGNN QAVKGVKESF
WITSFLCSTK LTQNGDMLDL LKWRAHPERI NDSLSKLKEI DGSEIVKFLQ DTLDTLFGIL
DESSQRYGLK VFDCLVHIIN LLQDSKFQHF KPVMDTYIES HFAGALSYRD LIKVLKWYVD
RIIDAEHQDH IQQVLKASEY IFKYIVQSRR LFALATGGQN EEEFRCCVHE LFMSIRFFLS
QENKGTSPVT QTQAVFLRTF PAVYGELLKI FTVKEVAGFV KETLGSLPAT AHAECPLEAV
KLQCMAKTVE SQLYVNPDSR CTLLPVVLRL LQAHMQEQRD LVMCAHILTS MLSLIRKDDS
EPAVSEEVDL IVESLLGLLL QTILEITNRP QPAGTNMRLQ FQDVTGEFVA CLLALLRQMT
DKHYQQLLQA FTSKDDLRDF LLQIFTVFRI LIRPEMFPKD WTVMRLVTNN VIITTVLYLS
DALRKNFLNE KFDYKVWDSY FYLSVIFINQ PCLQLESFSP SKRKKILEKY GDMRVMMGCE
IFSMWQNLGE HKLNFIPAMI GPFLEVTLVP QPDLRNVMIP IFHDMMDWEQ RRSGNFKQVE
AKLIDKLDSL MSEGKGDETY RELFNSIIPL FGPYPSLLKK IERETWRESG ISLIATVTRL
MERLLDYRDC MKLGEVDGKK IGCTVSLLNF YKTELNKEEM YIRYIHKLYD LHLKAQNYTE
ASYTLLLYDE LLEWSERPLR EFLNYPMQSE WQRKEYLHLT IVQNFDRGKC WENGIILCRE
LADQYDSYYD YRNLSKMRMM EASLYDKIMD QQRLEPEFFR VGFYGKKFPF FLRNKEFVCR
GHDYERLEAF QQRMLNEFPH AIAMQHVNQP DQTIYQAEAQ YLQIYAVSPI PESQDVLQRD
GVPDNIKSFY KVNHIWRFRY DRPFHKGTKD KENEFKSLWV ERTTLTLVQS LPGISRWFEV
DKRELVEVSP LENAIEVIEN KNLQLRTLIT QCQSRQMQNI NPLTMCLNGV IDAAVNGGLA
RYQEAFFVKD YVMNHPEDGE KIGRLRELMF EQAHILEYGL AVHEKFVPQD MKPLHKKLVD
QFHVMKSSLG IQEFPAYVRA SPVHFNGSPR NSCRNSVPNI LSLDGARVVA RRSPLTYPSV
NRYSSSSLSS QASNEVSNIT GQSESSDEVF NMQPSPSTSS LSSNHSASPN VTSSAPSSAR
GSPQLQDKHK HSRENSCLSP RERPVSAIFP TPLDPAQKAS PNQIGDTILP RSDPNLSAPD
KGKTGVSCSC SSMPPFTPSP TECQSAGLVS NSPVLSGSYS SGISSLSRCS VSEASGTEAT
AGDHPAHLAA TMPNSVSSGS DELIRRENKT PPPYSVYERT NPRRPVPLPH SLSIPPNSDP
PALPPKPHQI RTSSMKLDQA SDSRRADGVP HVPRPRPLPR KVSQL
//
