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Database: UniProt
Entry: A0A2K5M3M7_CERAT
LinkDB: A0A2K5M3M7_CERAT
Original site: A0A2K5M3M7_CERAT 
ID   A0A2K5M3M7_CERAT        Unreviewed;      1927 AA.
AC   A0A2K5M3M7;
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:ENSCATP00000019782.1};
GN   Name=DOCK4 {ECO:0000313|Ensembl:ENSCATP00000019782.1};
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:ENSCATP00000019782.1, ECO:0000313|Proteomes:UP000233060};
RN   [1] {ECO:0000313|Ensembl:ENSCATP00000019782.1}
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   Ensembl; ENSCATT00000043966.1; ENSCATP00000019782.1; ENSCATG00000033543.1.
DR   GeneTree; ENSGT00940000155659; -.
DR   Proteomes; UP000233060; Unplaced.
DR   Bgee; ENSCATG00000033543; Expressed in lung and 12 other cell types or tissues.
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:UniProtKB-KW.
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          1191..1597
FT                   /note="DOCKER"
FT                   /evidence="ECO:0000259|PROSITE:PS51651"
FT   REGION          1649..1730
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1743..1789
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1811..1927
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1467..1494
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1649..1700
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1703..1717
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1761..1789
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1811..1837
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1880..1896
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1927 AA;  221050 MW;  3838DAE652D2CE1F 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
     QDVTGEFVAC LLSLLRQMTD RHYQQLLDSF NTKEELRDFL LQIFTVFRIL IRPEMFPKDW
     TVMRLVANNV IITTVLYLSD ALRKNFLNEN FDYKIWDSYF YLAVIFINQL CLQLEMFTPS
     KKKKVLEKYG DMRVTMGCEI FSMWQNLGEH KLHFIPALIG PFLEVTLIPQ PDLRNVMIPI
     FHDMMDWEQR RSGNFKQVEA KLIDKLDSLM SEGKGDETYR ELFNSIIPLF GPYPSLLKKI
     ERETWRESGV SLIATVTRLM ERLLDYRDCM KMGEVDGKKI GCTVSLLNFY KTELNKEEMY
     IRYIHKLYDL HLKAQNFTEA AYTLLLYDEL LEWSDRPLRE FLTYPMQTEW QRKEHLHLTI
     IQNFDRGKCW ENGIILCRKI AEQYESYYDY RNLSKMRMME ASLYDKIMDQ QRLEPEFFRV
     GFYGKKFPFF LRNKEFVCRG HDYERLEAFQ QRMLNEFPHA IAMQHANQPD ETIFQAEAQY
     LQIYAVTPIP ESQEVLQREG VPDNIKSFYK VNHIWKFRYD RPFHKGTKDK ENEFKSLWVE
     RTSLYLVQSL PGISRWFEVE KREVVEMSPL ENAIEVLENK NQQLKTLISQ CQTRQMQNIN
     PLTMCLNGVI DAAVNGGVSR YQEAFFVKEY ILSHPEDGEK IARLRELMLE QAQILEFGLA
     VHEKFVPQDM RPLHKKLVDQ FFVMKSSLGI QEFSACMQAS PVHFPNGSPR VCRNSAPASV
     SPDGTRVIPR RSPLSYPAVN RYSSSSLSSQ ASAEVSNITG QSESSDEVFN MQPSPSTSSL
     SSTHSASPNV TSSAPSSARA SPLLSDKHKH SRENSCLSPR ERPCSAIYPT PVEPSQRMLF
     NHIGDGALPR SDPNLSAPEK ASPARHTTSV SPSPAGRSPL KGSVQSFTPS PVEYHSPGLI
     SNSPVLSGSY SSGISSLSRC STSETSGFEN QVNEQSVPLP VPVPVPVYGG EEPVRKESKT
     PPPYSVYERT LRRPVPLPHS LSIPVTPEPP ALPPKPLAAR SSHLENGARR TDPGPRPRPL
     PRKVSQL
//
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