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Database: UniProt
Entry: A0A2K6G299_PROCO
LinkDB: A0A2K6G299_PROCO
Original site: A0A2K6G299_PROCO 
ID   A0A2K6G299_PROCO        Unreviewed;      1883 AA.
AC   A0A2K6G299;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Dedicator of cytokinesis 1 {ECO:0000313|Ensembl:ENSPCOP00000020346.1};
GN   Name=DOCK1 {ECO:0000313|Ensembl:ENSPCOP00000020346.1};
OS   Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS   coquereli).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC   Indriidae; Propithecus.
OX   NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000020346.1, ECO:0000313|Proteomes:UP000233160};
RN   [1] {ECO:0000313|Ensembl:ENSPCOP00000020346.1}
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   RefSeq; XP_012510818.1; XM_012655364.1.
DR   STRING; 379532.ENSPCOP00000020346; -.
DR   Ensembl; ENSPCOT00000030999.1; ENSPCOP00000020346.1; ENSPCOG00000022132.1.
DR   GeneID; 105819174; -.
DR   KEGG; pcoq:105819174; -.
DR   CTD; 1793; -.
DR   GeneTree; ENSGT00940000154974; -.
DR   OMA; LWDNQAF; -.
DR   OrthoDB; 8258at2759; -.
DR   Proteomes; UP000233160; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0016477; P:cell migration; IEA:Ensembl.
DR   GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   CDD; cd08694; C2_Dock-A; 1.
DR   CDD; cd11707; DHR2_DOCK1; 1.
DR   CDD; cd12051; SH3_DOCK1_5_A; 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; IPR027007; C2_DOCK-type_domain.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR026791; DOCK.
DR   InterPro; IPR047025; DOCK1_5_SH3.
DR   InterPro; IPR047026; DOCK1_C2.
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:SF1; DEDICATOR OF CYTOKINESIS PROTEIN 1; 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; PF00018; SH3_1; 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:UP000233160};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          9..70
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          446..630
FT                   /note="C2 DOCK-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51650"
FT   DOMAIN          1228..1638
FT                   /note="DOCKER"
FT                   /evidence="ECO:0000259|PROSITE:PS51651"
FT   REGION          1636..1737
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1772..1792
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1810..1883
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          185..212
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1654..1683
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1697..1736
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1841..1871
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1883 AA;  217413 MW;  311BEC91BAD931DF CRC64;
     MTRWVPTKRE EKYGVAFYNY DARGADELSL QIGDTVHILE TYEGWYRGYT LRKKSKKGIF
     PASYIHLKEA IVEGKGQHET VIPGDLPLIQ EVTTTLREWS TIWRQLYVQD NREMFRSVRH
     MIYDLIEWRS QILSGTLPQD ELKELKKKVT AKIDYGNRIL DLDLVVRDED GNILDPELTS
     TISLFRAHEI ASKQVEERLQ EEKSQKQNID INRQAKFAAT PSLALFVNLK NVVCKIGEDA
     EVLMSLYDPV ESKFISENYL VRWSSSGLPK DIDRLHNLRA VFTDLGSKDL KREKISFVCQ
     IVRVGRMELR DNNTRKLTSG LRRPFGVAVM DVTDIINGKV DDEDKQHFIP FQPLALDDAV
     RHKPLNMSSR FSPRVAGEND FLQTVINKVI AAKEVNHKGQ GLWVTLKLLP GDIHQIRKEF
     PHLVDRTTAV ARKTGFPEII MPGDVRNDIY VTLVQGDFDK GSKTTAKNVE VTVSVYDEDG
     KRLEHVIFPG AGDEAISEYK SVIYYQVKQP RWFETVKVAI PIEDVNRSHL RFTFRHRSSQ
     DSKDKSEKIF ALAFVKLMRY DGTTLRDGEH DLIVYKAEVK KLEDAGTYLS LPSTKAELEE
     KGHSATGKGM QSLGSCTISK DSFQISTLVC STKLTQNVDL LGLLKWRSNT NLLQQNLRQL
     MKVDGGEVVK FLQDTLDALF NIMMENSESE TFDTLVFDAL VFIIGLIADR KFQHFNPVLE
     TYIKKHFSAT LAYTKLTKVL RNYVDNAEKP GINDQLYKAM KALEYIFKFI VRSRILFNQL
     YENKGEADFV DSLLQLFRSI NDMMSSLSDQ TVRVKGAALK YLPTIVNDVK LVFDPKELSK
     MFTDFILNVP VGLLTIQKLY CLIEIVHSDL FTQHDCREIL LPMMTDQLKY HLERQEDLEA
     CCQLLSNVLE VLYRKDVGPT QRHVQIIMEK LLRTVNRTVI SMGRDSELIG NFVACMTAIL
     RQMEDYHYAH LIKTFGKMRT DVVDFLMETF IMFKNLIGKN VYPFDWVIMN MMQNKVFLRA
     INQYADMLNK KFLDQANFEL QLWNNYFHLA VAFLTQESLQ LENFSSAKRA KILNKYGDMR
     RQIGFEIRDM WYNLGQHKIK FIPEMVGPIL EMTLIPETEL RKATIPIFFD MMQCEFHSTR
     SFQMFENEII TKLDHEVEGG RGDEQYKVLF DKILLEHCRK HKYLAKTGET FVKLVVRLME
     RLLDYRTIMH DENKENRMSC TVNVLNFYKE IEREEMYIRY LYKLCDLHKE CDNYTEAAYT
     LLLHAKLLKW SEDVCAAHLT QRDGYQATTQ GQLKEQLYQE IIHYFDKGKM WEEAIALGKE
     LAEQYENEMF DYEQLSELLK KQAQFYENIV KVVRPKPDYF AVGYYGQGLP TFLRGKVFIY
     RGKEYERRED FEARLLTQFP NAEKMKTTSP PGDDIKNSPG QHIQCFTVKP KLDLPPKFHR
     PVSEQIVSFY RVNEVQRFEY SRPIRKGEKN PDNEFANMWI ERTVYTTAYK LPGILRWFEV
     KSVFMVEISP LENAIETMQL TNDKIDSMVQ QHLDDPSLPV NPLSMLLNGI VDPAVMGGFA
     NYEKAFFTDR YLQEHPEAHE KIEKLKDLIA WQIPFLAEGI RIHGEKVTEA LRPFHERMEA
     CFKQLKEKVE KQYGIRTVPS SLDDRRGSRP RSMVRSFTMP SSSRPLSVAS VSSLSSDSTP
     SRPGSDGFAL EPLLPKKMHS RSQDKLDKDD LDKEKKDKKK EKRNSKHQEI FDKEFKPTDI
     SLQQSEAVIL SETISPLRPQ RPKSQVINVI GSERRFSVSP SSQQTPPPVT PRAKLNFSLQ
     SSLELNGMTG VDVADVPPPL PLKGSTADYG NLMENQDLMG SSTPPPPPPH QKHLPPPLPS
     KTPPPPPPKT TRKQTSVDSG IVQ
//
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