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Database: UniProt
Entry: A0A2K5VSV1_MACFA
LinkDB: A0A2K5VSV1_MACFA
Original site: A0A2K5VSV1_MACFA 
ID   A0A2K5VSV1_MACFA        Unreviewed;      1941 AA.
AC   A0A2K5VSV1;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Dedicator of cytokinesis 4 {ECO:0000313|Ensembl:ENSMFAP00000027911.2};
GN   Name=DOCK4 {ECO:0000313|Ensembl:ENSMFAP00000027911.2};
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000027911.2, ECO:0000313|Proteomes:UP000233100};
RN   [1] {ECO:0000313|Ensembl:ENSMFAP00000027911.2, ECO:0000313|Proteomes:UP000233100}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSMFAP00000027911.2}
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; ENSMFAT00000002097.2; ENSMFAP00000027911.2; ENSMFAG00000044248.2.
DR   VEuPathDB; HostDB:ENSMFAG00000044248; -.
DR   GeneTree; ENSGT00940000155659; -.
DR   Proteomes; UP000233100; Chromosome 3.
DR   Bgee; ENSMFAG00000044248; Expressed in lung and 13 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; IPR016024; ARM-type_fold.
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   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48371; ARM repeat; 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:UP000233100};
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..574
FT                   /note="C2 DOCK-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51650"
FT   DOMAIN          1199..1605
FT                   /note="DOCKER"
FT                   /evidence="ECO:0000259|PROSITE:PS51651"
FT   REGION          1657..1738
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1751..1797
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1819..1941
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1475..1502
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1657..1708
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1711..1725
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1769..1797
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1819..1845
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1847..1861
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1894..1910
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1941 AA;  222693 MW;  2197D1A771499E97 CRC64;
     MWIPTEHEKY GVVIASFRGT VPYGLSLEIG DTVQILEKCD GWYRGFALKN PNIKGIFPSS
     YVHLKNACVK NKGQFEMVIP TEDSVITEMT STLRDWGTMW KQLYVRNEGD LFHRLWHIMN
     EILDLRRQVL VGHLTHDRMK DVKRHITARL DWGNEQLGLD LVPRKEYAMV DPEDISITEL
     YRLMEHRHRK KDTPVQASSH HLFVQMKSLM CSNLGEELEV IFSLFDSKEN RPISERFFLR
     LNRNGLPKAP DKPERQCSLF VDLGSSELRK DIYITVHIIR IGRMGAGEKK NACSVQYRRP
     FGCAVLSIAD LLTGETKDDL ILKVYMCNTE SEWYQIHENI IKKLNARYNL TGSNAGLAVS
     LQLLHGDIEQ IRREYSSVFS HGVSITRKLG FSNIIMPGEM RNDLYITIER GEFEKGGKSV
     ARNVEVTMFI VDSSGQTLKD FISFGSGEPP ASEYHSFVLY HNNSPRWSEL LKLPIPVDKF
     RGAHIRFEFR HCSTKEKGEK KLFGFSFVPL MQEDGRTLPD GTHELIVHKC EENTNLQDTT
     RYLKLPFSKG IFLGNNNQAM KATKESFCIT SFLCSTKLTQ NGDMLDLLKW RTHPDKITGC
     LSKLKEIDGS EIVKFLQDTL DTLFGILDEN SQKYGSKVFD SLVHIINLLQ DSKFHHFKPV
     MDTYIESHFA GALAYRDLIK VLKWYVDRIT EAERQEHIQE VLKAQEYIFK YIVQSRRLFS
     LATGGQNEEE FRRCIQELLM SVRFFLSQES KGSGALSQSQ AVFLSSFPAV YSELLKLFDV
     REVANLVQDT LGSLPTILHV DDSLQAIKLQ CIGKTVESQL YTNPDSRYIL LPVVLHHLHI
     HLQEQKDLIM CARILSNVFC LIKKNSSEKS VLEEIDVIVA SLLDILLRTI LEITSRPQPS
     SSAMRFQFQD VTGEFVACLL SLLRQMTDRH YQQLLDSFNT KEELRDFLLQ IFTVFRILIR
     PEMFPKDWTV MRLVANNVII TTVLYLSDAL RKNFLNENFD YKIWDSYFYL AVIFINQLCL
     QLEMFTPSKK KKVLEKYGDM RVTMGCEIFS MWQNLGEHKL HFIPALIGPF LEVTLIPQPD
     LRNVMIPIFH DMMDWEQRRS GNFKQVEAKL IDKLDSLMSE GKGDETYREL FNSIIPLFGP
     YPSLLKKIER ETWRESGVSL IATVTRLMER LLDYRDCMKM GEVDGKKIGC TVSLLNFYKT
     ELNKEEMYIR YIHKLYDLHL KAQNFTEAAY TLLLYDELLE WSDRPLREFL TYPMQTEWQR
     KEHLHLTIIQ NFDRGKCWEN GIILCRKIAE QYESYYDYRN LSKMRMMEAS LYDKIMDQQR
     LEPEFFRVGF YGKKFPFFLR NKEFVCRGHD YERLEAFQQR MLNEFPHAIA MQHANQPDET
     IFQAEAQYLQ IYAVTPIPES QEVLQREGVP DNIKSFYKVN HIWKFRYDRP FHKGTKDKEN
     EFKSLWVERT SLYLVQSLPG ISRWFEVEKR EVVEMSPLEN AIEVLENKNQ QLKTLISQCQ
     TRQMQNINPL TMCLNGVIDA AVNGGVSRYQ EAFFVKEYIL SHPEDGEKIA RLRELMLEQA
     QILEFGLAVH EKFVPQDMRP LHKKLVDQFF VMKSSLGIQE FSACMQASPV HFPNGSPRVC
     RNSAPASVSP DGTRVIPRRS PLSYPAVNRY SSSSLSSQAS AEVSNITGQS ESSDEVFNMQ
     PSPSTSSLSS THSASPNVTS SAPSSARASP LLSDKHKHSR ENSCLSPRER PCSAIYPTPV
     EPSQRMLFNH IGDGALPRSD PNLSAPEKAS PARHTTSVSP SPAGRSPLKG SVQSFTPSPV
     EYHSPGLISN SPVLSGSYSS GISSLSRCST SETSGFENQV NEQSVPLPVP VPVPVPVPVP
     SYGGEEPVRK ESKTPPPYSV YERTLRRPVP LPHSLSIPVT PEPPALPPKP LAARSSHLEN
     GARRTDPGPR PRPLPRKVSQ L
//
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