ID A0A1S3FMZ9_DIPOR Unreviewed; 1869 AA.
AC A0A1S3FMZ9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Dedicator of cytokinesis protein 1 isoform X2 {ECO:0000313|RefSeq:XP_012877399.1};
GN Name=Dock1 {ECO:0000313|RefSeq:XP_012877399.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012877399.1};
RN [1] {ECO:0000313|RefSeq:XP_012877399.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012877399.1};
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_012877399.1; XM_013021945.1.
DR STRING; 10020.ENSDORP00000003224; -.
DR GeneID; 105989761; -.
DR CTD; 1793; -.
DR OrthoDB; 8258at2759; -.
DR Proteomes; UP000081671; 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 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:UP000081671};
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..1869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 1736..1751
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1776..1790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1826..1857
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1869 AA; 215106 MW; 64916B41CA106B1E CRC64;
MTRWVPTKRE EKYGVAFYNY DARGADELSL QIGDTVHILE TYEGWYRGYT LRKKSKKGIF
PASYIHLKEA IVEGKGQHET VIPGDLPLIQ EVTTTLREWA AIWRQLYVQD NREMFRSVRH
MIYDLIEWRS QILSGTLPQD ELKELKKKVT AKIDYGNRIL DLDLVVRDED GNILDPELTS
TISLFRAHKV ASKQVEERLQ EEKSQKQNLD INRQAKFAAT PSLALFVNLK NVVCKIGEDA
EVLMSLYDPT ESKFISENYL VRWSSSGLPK DIDRLHNLRA VFTDLGSKDL KREKISFVCQ
IVRVGRMELR DSNTRKLTSG LRRPFGVAVM DVTDIINGKV DDEDKQHFIP FQPVAGENDF
LQTVINKVIA AKEVNHKGQG LWVTLKLLPG DVHQIRKEFP HLVDRTTAVA RKTGFPEIIM
PGDVRNDIYV TLVQGDFDKG NKTTAKNVEV TVSVYDEDGK RLEHVIFPGA GDEAISEYKS
VIYYQVKQPR WFETVKVAIP IEDVNRSHLR FTFRHRSSQD SKDKSEKIFA LAFVKLMRYD
GTTLRDGEHD LIVYKAEAKK LEDAATYLSL PSTKAELEEK GHSATGKSMQ SLGNCTISKD
SFQISTLVCS TKLTQNVDLL GLLKWRSNTN LLQQNLRQLM KVDGGEVVKF LQDTLDALFN
IMMENSESET FDTLVFDALV FIIGLIADRK FQHFNPVLET YIKKHFSATL AYTKLTKVLR
TYVDGAEKPG INEQLYKAMK ALEYIFKFIV RSRILFNQLY EDKGEADFVE SLLQLFRSIN
DMMSSMSDQT VRVKGAALKY LPTIVNDVKL VFDPKELSKM FTDFILNVPT GLLTIQKLYC
LIEIVHSDLF TQHDCREILL PMMTEQLKYH LERQEDLEAC CQLLSNILEV LYKKDVGPTQ
RHVQIIMEKL LRTVNRTVIS MGRDSELIGN FVACMTAILR QMEDYHYAHL IKTFGKMRTD
VVDFLMETFI MFKNLIGKNV YPFDWVIMNM MQNKVFLRAI NQYADMLNKK FLDQANFELQ
LWNNYFHLAV AFLTQDSLQL ENFSSAKRGK ILNKYGDMRR QIGFEIRDMW YNLGQHKIKF
IPEMVGPILE MTLIPETELR KATIPIFFDM MQCEFHSTRS FQMFENEIVT KLDHEVEGGR
GDEQYKVLFD KILLEHCRKH KYLAKTGETF VKLVVRLMER LLDYRTIMND ENKENRMSCT
VNVLNFYKEI EREEMYIRYL YKLCDLHKEC DNYTEAAYTL LLHAKLLKWS EDVCAAHLTQ
RDGYQATTQG QLKEQLYQEI IHYFDKGKMW EEAIALGKEL AEQYETEMFD YEQLSELLKK
QAQFYENIVK VIRPKPDYFA VGYYGQGFPT FLRGKVFIYR GKEYERREDF EARLLTQFPN
AEKMKTTSPP GDDIKNSPGQ YIQCFTVKPK LDLPPKFHRP VSEQIVSFYR VNEVQRFEYS
RPIRKGEKNP DNEFANMWIE RTIYTTAYKL PGILRWFEVK SVFMVEISPL ENAIETMQLT
NDKISSMVQQ HLDDPGLPIN PLSMLLNGIV DPAVMGGFAN YEKAFFTDRY LQEHPEAHGQ
IEKLKDLIAW QIPFLAEGIR IHGDKVTEAL RPFHERMEAC FKQLREKVEK QYGIRTMPSS
LDDRRGSRPR SMVRSFTMPS TSRPLSVASV SSLSSDSTPS RPGSDGFALE PLLPKKMHSR
SQDKLDKDDA EKEKKDKKKE KRNSKHQEIF DKEFKPADGS LQPSEAVILS ETISPLRPQR
PKSQVLNVMG SERRFSVSPA PPGSQHTPPP VTPRAKLSFS VQSGLELNGV TGGGTSVDAA
DVPPPLPLKG STADYGNLME TQDLGGSPTP PPPPPPPHQR PPPLPSKTPP PPPPKTTRKQ
TSVDSGIVQ
//
