DCK1_YEAST
ID DCK1_YEAST Reviewed; 1932 AA.
AC Q06409; D6VZ58;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=DOCK-like protein 1 {ECO:0000303|PubMed:25598154};
GN Name=DCK1 {ECO:0000303|PubMed:25598154}; OrderedLocusNames=YLR422W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP INTERACTION WITH LMO1, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND
RP FUNCTION.
RX PubMed=25598154; DOI=10.1111/mmi.12937;
RA Schmitz H.P., Jendretzki A., Wittland J., Wiechert J., Heinisch J.J.;
RT "Identification of Dck1 and Lmo1 as upstream regulators of the small GTPase
RT Rho5 in Saccharomyces cerevisiae.";
RL Mol. Microbiol. 96:306-324(2015).
CC -!- FUNCTION: Forms a transiant heterodimeric complex with LMO1, that acts
CC as a guanine nucleotide exchange factor exchange factor (GEF) for the
CC small GTPase RHO5 (PubMed:25598154). DCK1, LMO1 and RHO5 relocate to
CC mitochondria upon oxidative stress and trigger cell death
CC (PubMed:25598154). The DCK1/LMO1/RHO5 signaling module mediates
CC mitochondrial turnover under nitrogen starvation conditions via
CC mitophagy (PubMed:25598154). The DCK1/LMO1/RHO5 signaling module plays
CC also a function in cell wall integrity signaling (PubMed:25598154).
CC {ECO:0000269|PubMed:25598154}.
CC -!- SUBUNIT: Forms an active heterodimer with LMO1.
CC {ECO:0000269|PubMed:25598154}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC Mitochondrion {ECO:0000269|PubMed:25598154}. Note=Quickly relocates to
CC mitochondria under oxidative stress. {ECO:0000269|PubMed:25598154}.
CC -!- DISRUPTION PHENOTYPE: Leads to hyper-resistance to cell wall stress
CC agents such as calcofluor white and Congo red.
CC {ECO:0000269|PubMed:25598154}.
CC -!- MISCELLANEOUS: Present with 238 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000305}.
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DR EMBL; U20939; AAB67508.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09724.1; -; Genomic_DNA.
DR PIR; S53409; S53409.
DR RefSeq; NP_013526.1; NM_001182310.1.
DR AlphaFoldDB; Q06409; -.
DR BioGRID; 31681; 264.
DR DIP; DIP-6405N; -.
DR IntAct; Q06409; 2.
DR MINT; Q06409; -.
DR STRING; 4932.YLR422W; -.
DR iPTMnet; Q06409; -.
DR MaxQB; Q06409; -.
DR PaxDb; Q06409; -.
DR PRIDE; Q06409; -.
DR EnsemblFungi; YLR422W_mRNA; YLR422W; YLR422W.
DR GeneID; 851141; -.
DR KEGG; sce:YLR422W; -.
DR SGD; S000004414; DCK1.
DR VEuPathDB; FungiDB:YLR422W; -.
DR eggNOG; KOG1998; Eukaryota.
DR GeneTree; ENSGT00940000175868; -.
DR HOGENOM; CLU_238900_0_0_1; -.
DR InParanoid; Q06409; -.
DR OMA; TFPTLMN; -.
DR BioCyc; YEAST:G3O-32482-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-8980692; RHOA GTPase cycle.
DR Reactome; R-SCE-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:Q06409; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06409; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; IBA:GO_Central.
DR GO; GO:0000422; P:autophagy of mitochondrion; IMP:SGD.
DR GO; GO:0035556; P:intracellular signal transduction; IMP:SGD.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR Gene3D; 1.20.58.740; -; 1.
DR Gene3D; 1.25.40.410; -; 1.
DR InterPro; IPR026791; DOCK.
DR InterPro; IPR043161; DOCK_C_lobe_A.
DR InterPro; IPR043162; DOCK_C_lobe_C.
DR InterPro; IPR027357; DOCKER_dom.
DR PANTHER; PTHR45653; PTHR45653; 1.
DR Pfam; PF06920; DHR-2; 1.
DR PROSITE; PS51651; DOCKER; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Mitochondrion; Reference proteome.
FT CHAIN 1..1932
FT /note="DOCK-like protein 1"
FT /id="PRO_0000247776"
FT DOMAIN 1410..1824
FT /note="DOCKER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00984"
FT REGION 1908..1932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1908..1922
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1932 AA; 221563 MW; 1E9CE4AE6F8D3F94 CRC64;
MSQQDSQRWL PTDRLIYGVL VKSFLPLQRY PELVYENSNY ANVYVGAEVY VFEESVDKKW
CRAYQCLRPF PEEFISNMNS ANDVLPDVKP KVVIFPRKYV HFEAEKAVST MPFFKAPSAE
DFKPLISKEC ESRSFCDSLY VSSTDDISTG KPRKTPRPPF PFFRYQKRSF KDEMGPILSL
ISSHVYSMYS IGEFSIYRKM IKLYYDLDTI RFRLSMNLTT EAEKINLIRA ATSLRTKIAK
FLSSTYRKNK LIANSTPRNP DPYGFEGIFA RDIDTGELLS YEIDKLRTLV SSSMLCGLTN
NFPTVPVVES DDESSSNGLF GTVRSSILVN LKDLAWDPSI SDPKYQDLSI CVYLRTKDEV
LTESFTMTKS SNMESALDEI PAMLFKNILE TIVHKNKVYL VVVLKETIAI TTETAPEISS
YNISTEESSS HSPFSPFNSS TENKIDHVKK GLAAGVINIS PVFKFYNGLS VANKAQRFNL
YLYSSDSSDS QNFNSSKDAD LGWGGLINKI IKDSSEGVSV NPRAVSLSVT VKEIIGKQEA
EKVLSTSLVP IRSIPTYFYD TMFSQAERIY LNLGRVSLYG LPAADTNIEN VTVQISCRNK
AVKFCKNKLE ERSGDWKFVS VRPNESIGES IRIEGVENMN EDETLRVLVY LNGFLMAKSN
IHIKKKNEII EYRKGTVFQI MSSKSVPLIH LELEASYFGR RYNINPAITN FLVLQTKNVE
FDQQLKEHYS VTLKQLNNVS FKDLLKHFDT ILAHYLLLLE SVNEATDKKG PSSSLPNIVF
SEFVKFLNLM LTHQENSRYW FNRLYKKVMS KELECPNVAP ILIKHMTTIF DRSHSSWTRT
GTAICRTILY IIVLAIGSSH SDEMPNFSHF FRSLHKFLML ADEPIMADQI LLIESIPSML
ETMTNHCKVE DLVRFAIGLF ECCQEKEMNQ KMYSRPLSVR EEEYLNTKFN CLLKLINKKV
LQNYLTNTES VDKLRLQFLS KTLEWLLTPY TPGDDKCFHV ESLRLVNSVF ITIIEDYKFD
MLQRNLIRLL PYLCKSFVHL RRYCKKARLM RPRRVFTMLF PREIPCNYIP VDSIVNDEVV
VEVLLELAII ICEITKIASS RFPSYQSFSE IINLCDKDTL FQSNFYSRQI TNENVYTITK
TVFLFFKQDW FPGMKWLGVS ALLGRSSLIL LSLCKDYIIE NNSPSPSKES EKRVDMRLWA
EYVKVILLVS NHKSASLTKL AITPRKAVYL ISGDLKKISA YILNECWDAL ATGHYNITYA
KKYGLGALSD CQFELFVHNQ FLIREIFIFA FHRHIDATRI CCKILWGLGL NFWRIFGSLQ
PAVNACIPEL FSAYQIGKLR LNDYELERFV SCLFFMMHVP DSDTFFPACM DFLRDLLGFL
HIVNEIYKIP NQEEFDDDRT ARHIEMFEYL LEANRPELFH KMIYDLFIHF IQKKDFVQAA
LSLELLAGTY AWDSNDTLEA ISFPPLPEQS SFERKEYLLK ESARNFSRGQ KPEKALAVYK
DLIKAYDEIN YDLNGLAFVH DQIAGIYTRL QSIDRLVPTY FKVSFMGFGF PKSLRNKSFV
FEGLPFEHIT SMHDRLLRSY HGSNIVHSQE EVDMLLMNPP MGKYIHVASV EPCLSISDNY
NSSDKKSSIN NKVRMYIENR DLRTFSNSRR LPGAKGVTDL WVEEYTYHTM NTFPTLMNRS
EIVKVTKSKL SPLENAIRSL QVKIQELYGL ENMCNKTLKD HGDVNDLFTE LSTNITGTIS
APVNGGISQY KAFLEPSTSK QFSTDDLGRL TLAFDELVAV LGRCLTLHAE LLPSKDLKPS
HDLLVRLFEE NFAEEIERYS RTLSEANRSR NNMITARIIS HKNPNKKASF SGRDHHTSGS
NHSQFVLEHS DSFGPNSLLF GKYLTRTLSH SSTTSSLDKS GIVSGTSSTF LAGSQPNTNT
DSQHKHDYSH SG
