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Database: UniProt
Entry: A0A2K5M3L4_CERAT
LinkDB: A0A2K5M3L4_CERAT
Original site: A0A2K5M3L4_CERAT 
ID   A0A2K5M3L4_CERAT        Unreviewed;      2003 AA.
AC   A0A2K5M3L4;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Dedicator of cytokinesis 4 {ECO:0000313|Ensembl:ENSCATP00000019772.1};
GN   Name=DOCK4 {ECO:0000313|Ensembl:ENSCATP00000019772.1};
OS   Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Cercocebus.
OX   NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000019772.1, ECO:0000313|Proteomes:UP000233060};
RN   [1] {ECO:0000313|Ensembl:ENSCATP00000019772.1}
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; 9531.ENSCATP00000019772; -.
DR   Ensembl; ENSCATT00000043956.1; ENSCATP00000019772.1; ENSCATG00000033543.1.
DR   GeneTree; ENSGT00940000155659; -.
DR   OMA; MRDFGHS; -.
DR   Proteomes; UP000233060; Unplaced.
DR   Bgee; ENSCATG00000033543; Expressed in lung and 12 other cell types or tissues.
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:0032420; C:stereocilium; 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:UP000233060};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          1..59
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          393..566
FT                   /note="C2 DOCK-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51650"
FT   DOMAIN          1227..1633
FT                   /note="DOCKER"
FT                   /evidence="ECO:0000259|PROSITE:PS51651"
FT   REGION          1685..1766
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1779..2003
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1503..1530
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1685..1736
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1739..1753
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1794..1813
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1834..1911
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1956..1972
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2003 AA;  229182 MW;  95CBB2A8463D87D2 CRC64;
     SWVGFIASFR GTVPYGLSLE IGDTVQILEK CDGWYRGFAL KNPNIKGIFP SSYVHLKNAC
     VKNKGQFEMV IPTEDSVITE MTSTLRDWGT MWKQLYVRNE GDLFHRLWHI MNEILDLRRQ
     VLVGHLTHDR MKDVKRHITA RLDWGNEQLG LDLVPRKEYA MVDPEDISIT ELYRLMEHRH
     RKKDTPVQAS SHHLFVQMKS LMCSNLGEEL EVIFSLFDSK ENRPISERFF LRLNRNGLPK
     APDKPERHCS LFVDLGSSEL KKDIYITVHI IRIGRMGAGE KKNACSVQYR RPFGCAVLSI
     ADLLTGETKD DLILKVYMCN TESEWYQIHE NIIKKLNARY NLTGSNAGLA VSLQLLHGDI
     EQIRREYSSV FSHGVSITRK LGFSNIIMPG EMRNDLYITI ERGEFEKGGK SVARNVEVTM
     FIVDSSGQTL KDFISFGSGE PPASEYHSFV LYHNNSPRWS ELLKLPIPVD KFRGAHIRFE
     FRHCSTKEKG EKKLFGFSFV PLMQEDGRTL PDGTHELIVH KCEENTNLQD TTRYLKLPFS
     KGIFLGNNNQ AMKATKESFC ITSFLCSTKL TQNGDMLDLL KWRTHPDKIT GCLSKLKEID
     GSEIVKFLQD TLDTLFGILD ENSQKYGSKV FDSLVHIINL LQDSKFHHFK PVMDTYIESH
     FAGALAYRDL IKVLKWYVDR ITEAERQEHI QEVLKAQEYI FKYIVQSRRL FSLATGGQNE
     EEFRCCIQEL LMSVRFFLSQ ESKGSGALSQ SQAVFLSSFP AVYSELLKLF DVREVANLVQ
     DTLGSLPTIL HVDDSLQAIK LQCIGKTVES QLYTNPDSRY ILLPVVLHHL HIHLQEQKDL
     IMCARILSNV FCLIKKNSSE KSVLEEIDVI VASLLDILLR TILEITSRPQ PSSSAMRFQF
     QDVTRTGFLN KESLHDSSTL STFSFCADTY GKVPMTGRHT GEFVACLLSL LRQMTDRHYQ
     QLLDSFNTKE ELRDFLLQIF TVFRILIRPE MFPKDWTVMR LVANNVIITT VLYLSDALRK
     NFLNENFDYK IWDSYFYLAV IFINQLCLQL EMFTPSKKKK VLEKYGDMRV TMGCEIFSMW
     QNLGEHKLHF IPALIGPFLE VTLIPQPDLR NVMIPIFHDM MDWEQRRSGN FKQVEAKLID
     KLDSLMSEGK GDETYRELFN SIIPLFGPYP SLLKKIERET WRESGVSLIA TVTRLMERLL
     DYRDCMKMGE VDGKKIGCTV SLLNFYKTEL NKEEMYIRYI HKLYDLHLKA QNFTEAAYTL
     LLYDELLEWS DRPLREFLTY PMQTEWQRKE HLHLTIIQNF DRGKCWENGI ILCRKIAEQY
     ESYYDYRNLS KMRMMEASLY DKIMDQQRLE PEFFRVGFYG KKFPFFLRNK EFVCRGHDYE
     RLEAFQQRML NEFPHAIAMQ HANQPDETIF QAEAQYLQIY AVTPIPESQE VLQREGVPDN
     IKSFYKVNHI WKFRYDRPFH KGTKDKENEF KSLWVERTSL YLVQSLPGIS RWFEVEKREV
     VEMSPLENAI EVLENKNQQL KTLISQCQTR QMQNINPLTM CLNGVIDAAV NGGVSRYQEA
     FFVKEYILSH PEDGEKIARL RELMLEQAQI LEFGLAVHEK FVPQDMRPLH KKLVDQFFVM
     KSSLGIQEFS ACMQASPVHF PNGSPRVCRN SAPASVSPDG TRVIPRRSPL SYPAVNRYSS
     SSLSSQASAE VSNITGQSES SDEVFNMQPS PSTSSLSSTH SASPNVTSSA PSSARASPLL
     SDKHKHSREN SCLSPRERPC SAIYPTPVEP SQRMLFNHIG DGALPRSDPN LSAPEKAVNP
     TPSSWSLDSG KEAKNMSDSG KLISPPVPPR PTQTASPARH TTSVSPSPAG RSPLKGSVQS
     FTPSPVEYHS PGLISNSPVL SGSYSSGISS LSRCSTSETS GFENQVNEQS VPLPVPVPVP
     VPVYGGEEPV RKESKTPPPY SVYERTLRRP VPLPHSLSIP VTPEPPALPP KPLAARSSHL
     ENGARRTDPG PRPRPLPRKV SQL
//
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