ID A0A2Y9J6S6_ENHLU Unreviewed; 1868 AA.
AC A0A2Y9J6S6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Dedicator of cytokinesis protein 1 isoform X2 {ECO:0000313|RefSeq:XP_022355404.1};
GN Name=LOC111145075 {ECO:0000313|RefSeq:XP_022355404.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022355404.1};
RN [1] {ECO:0000313|RefSeq:XP_022355404.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022355404.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000256|PROSITE-
CC ProRule:PRU00983}.
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DR RefSeq; XP_022355404.1; XM_022499696.1.
DR Proteomes; UP000248482; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; 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:UP000248482};
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 425..609
FT /note="C2 DOCK-type"
FT /evidence="ECO:0000259|PROSITE:PS51650"
FT DOMAIN 1207..1617
FT /note="DOCKER"
FT /evidence="ECO:0000259|PROSITE:PS51651"
FT REGION 1612..1718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1730..1868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 185..212
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1633..1662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1676..1715
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1730..1761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1776..1795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1825..1856
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1868 AA; 215844 MW; E3F4332977E4614F 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 KRDKISFVCQ
IVRVGRMELR DNNTRKLTSG LRRPFGVAVM DVTDIINGKV DDEDKQHFIP FQPVAGENDF
LQTVINKVIA AKEVNHKGQG LWVTLKLLPG DIHQIRKEFP HLVDRTTAVA RKTGFPEIIM
PGDVRNDIYV TLVQGDFDKG SKTTAKNVEV TVSVYDEDGK RLEHVIFPGA GDEAISEYKS
VIYYQVKQPR WFETVKVAIP IEDVNRSHLR FTFRHRSSQD SKDKSEKIFA LAFVKLMRYD
GTTLRDGEHD LIVYKAEAKK LEDAATYLSL PSTKAELEEK AHSATGRSMQ SLGNCTISKD
SFQISTLVCS TKLTQNVDLL GLLKWRSNTS LLQQNLRQLM KVDGGEVVKF LQDTLDALFN
IMMENSESET FDTLVFDALV FIIGLIADRK FQHFNPVLET YIKKHFSATL AYTKLTKVLR
NYVDNAEKPG VSDQLYRAMK ALEYIFKFIV RSRVLFNQLY EDKGEADFME SLLQLFRSIS
DMMSSVSDQT VRVKGAALKY LPTIVNDVKL VFDPKELSKM FTDFILNVPM GLLTIQKLYC
LIEIIHSDLF TQHDCREILL PMMTDQLKYH LERQEDLEAC CQLLSTILEV LYRKDVGPTQ
RHVQIIMEKL LRTVNRTVIS MGRDSELIGN FVACMTAILR QMEDYHYAHL IKTFGKMRTD
VVDFLMETFI MFKNLIGKNV YPFDWVIMNM MQNKVFLRAI NQYADMLNKK FLDQANFELQ
LWNNYFHLAV AFLTQESLQL ENFSSAKRAK ILNKYGDMRR QIGFEIRDMW YNLGQHKIKF
IPEMVGPILE MTLIPETELR KATIPIFFDM MQCEFHSTRS FQMFENEIIT KLDHEVEGGR
GDEQYKVLFD KILLEHCRKH KYLAKTGETF VKLVVRLMER LLDYRTIMHD ENKENRMSCT
VNVLNFYKEI EREEMYIRYL YKLCDLHREC DNYTEAAYTL LLHAKLLKWS EDVCAAHLTQ
RDGYQATTQG QLKEQLYQEI IHYFDKGKMW EEAIALGKEL AEQYENEMFD YEQLSELLKK
QAQFYENIVK VIRPKPDYFA VGYYGQGFPT FLRGKVFIYR GKEYERREDF EARLLTQFPN
AEKMKTTSPP GDDIKNSPGQ YIQCFTVKPK LDLPPKFHRP VSEQIVSFYR VNEVQRFEYS
RPIRKGEKNP DNEFANMWIE RTIYTTAYKL PGILRWFEVK SVFMVEISPL ENAIETMQLT
NDKMNSMVQQ HLDDPSLPIN PLSMLLNGIV DPAVMGGFAN YEKAFFTERY LQEHPEAHEK
IEKLKDLIAW QIPFLAEGIR IHGDKVTEAL RPFHERMEAC FKQLKEKVEK QYGVRTMPSS
LDDRRGSRPR SMVRSFTMPS SSRPLSVASV SSLSSDSTPS RPGSDGFALE PLLPKKMHCR
SQDKLDKDDP EKEKKDKKKE KRNSKHQEMF DKEFKPTDVA MQQSEAVILS ETISPLRPQR
PKSQVINVTG SERRFSVSPS SPSSQPVPPP VTPRAKLSFS LQSSLELNGV SSMTGMDTAE
VPPPLPLKGS MADYGNLVEN QDLISSPTPP PPPPHQRHLP PPLPSKTPPP PPPKTTRKQT
SVDSGIVQ
//
