DYHC2_CAEEL
ID DYHC2_CAEEL Reviewed; 4171 AA.
AC Q19542;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Cytoplasmic dynein 2 heavy chain 1;
DE AltName: Full=Abnormal chemotaxis protein 3;
GN Name=che-3 {ECO:0000312|WormBase:F18C12.1};
GN ORFNames=F18C12.1 {ECO:0000312|WormBase:F18C12.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION.
RX PubMed=10545497; DOI=10.1083/jcb.147.3.519;
RA Signor D., Wedaman K.P., Orozco J.T., Dwyer N.D., Bargmann C.I., Rose L.S.,
RA Scholey J.M.;
RT "Role of a class DHC1b dynein in retrograde transport of IFT motors and IFT
RT raft particles along cilia, but not dendrites, in chemosensory neurons of
RT living Caenorhabditis elegans.";
RL J. Cell Biol. 147:519-530(1999).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27515926; DOI=10.1038/srep31544;
RA Niwa S.;
RT "The nephronophthisis-related gene ift-139 is required for ciliogenesis in
RT Caenorhabditis elegans.";
RL Sci. Rep. 6:31544-31544(2016).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ARG-295; ARG-1384;
RP ARG-1693 AND LYS-2935.
RX PubMed=28479320; DOI=10.1016/j.cub.2017.04.015;
RA Yi P., Li W.J., Dong M.Q., Ou G.;
RT "Dynein-driven retrograde intraflagellar transport is triphasic in C.
RT elegans sensory cilia.";
RL Curr. Biol. 27:1448-1461(2017).
CC -!- FUNCTION: Functions as a motor for intraflagellar retrograde transport
CC in chemosensory neurons (PubMed:10545497, PubMed:28479320). Functions
CC in cilia biogenesis (PubMed:10545497, PubMed:27515926).
CC {ECO:0000269|PubMed:10545497, ECO:0000269|PubMed:27515926,
CC ECO:0000269|PubMed:28479320}.
CC -!- SUBUNIT: The cytoplasmic dynein complex 2 is probably composed by a
CC heavy chain che-3 homodimer and a number of light intermediate chains.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Shorter phasmid cilia with an irregular
CC morphology. {ECO:0000269|PubMed:27515926, ECO:0000269|PubMed:28479320}.
CC -!- SIMILARITY: Belongs to the dynein heavy chain family. {ECO:0000305}.
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DR EMBL; Z75536; CAA99830.2; -; Genomic_DNA.
DR PIR; T21085; T21085.
DR RefSeq; NP_492221.2; NM_059820.2.
DR SMR; Q19542; -.
DR BioGRID; 38027; 5.
DR STRING; 6239.F18C12.1; -.
DR PaxDb; Q19542; -.
DR PeptideAtlas; Q19542; -.
DR PRIDE; Q19542; -.
DR EnsemblMetazoa; F18C12.1.1; F18C12.1.1; WBGene00000485.
DR GeneID; 172593; -.
DR KEGG; cel:CELE_F18C12.1; -.
DR UCSC; F18C12.1; c. elegans.
DR CTD; 172593; -.
DR WormBase; F18C12.1; CE32386; WBGene00000485; che-3.
DR eggNOG; KOG3595; Eukaryota.
DR GeneTree; ENSGT00940000154620; -.
DR HOGENOM; CLU_000038_7_2_1; -.
DR InParanoid; Q19542; -.
DR OMA; PFMLIGP; -.
DR OrthoDB; 26380at2759; -.
DR PhylomeDB; Q19542; -.
DR Reactome; R-CEL-5620924; Intraflagellar transport.
DR PRO; PR:Q19542; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00000485; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005930; C:axoneme; IBA:GO_Central.
DR GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IBA:GO_Central.
DR GO; GO:0030286; C:dynein complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0031514; C:motile cilium; IBA:GO_Central.
DR GO; GO:0097730; C:non-motile cilium; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0045505; F:dynein intermediate chain binding; IBA:GO_Central.
DR GO; GO:0051959; F:dynein light intermediate chain binding; ISS:WormBase.
DR GO; GO:0003777; F:microtubule motor activity; ISS:WormBase.
DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0007635; P:chemosensory behavior; IMP:WormBase.
DR GO; GO:0060271; P:cilium assembly; IGI:UniProtKB.
DR GO; GO:0043053; P:dauer entry; IGI:UniProtKB.
DR GO; GO:0035721; P:intraciliary retrograde transport; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IGI:WormBase.
DR GO; GO:1905515; P:non-motile cilium assembly; IMP:WormBase.
DR GO; GO:0061066; P:positive regulation of dauer larval development; IMP:WormBase.
DR GO; GO:0008104; P:protein localization; IMP:WormBase.
DR Gene3D; 1.10.8.710; -; 1.
DR Gene3D; 1.10.8.720; -; 1.
DR Gene3D; 1.20.140.100; -; 1.
DR Gene3D; 3.10.490.20; -; 1.
DR Gene3D; 3.20.180.20; -; 1.
DR Gene3D; 3.40.50.300; -; 5.
DR InterPro; IPR035699; AAA_6.
DR InterPro; IPR035706; AAA_9.
DR InterPro; IPR041658; AAA_lid_11.
DR InterPro; IPR042219; AAA_lid_11_sf.
DR InterPro; IPR026983; DHC_fam.
DR InterPro; IPR026815; DYNC2H1.
DR InterPro; IPR042222; Dynein_2_N.
DR InterPro; IPR043157; Dynein_AAA1S.
DR InterPro; IPR041228; Dynein_C.
DR InterPro; IPR043160; Dynein_C_barrel.
DR InterPro; IPR024743; Dynein_HC_stalk.
DR InterPro; IPR024317; Dynein_heavy_chain_D4_dom.
DR InterPro; IPR004273; Dynein_heavy_D6_P-loop.
DR InterPro; IPR013602; Dynein_heavy_linker.
DR InterPro; IPR013594; Dynein_heavy_tail.
DR InterPro; IPR042228; Dynein_linker_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10676; PTHR10676; 1.
DR PANTHER; PTHR10676:SF352; PTHR10676:SF352; 1.
DR Pfam; PF12774; AAA_6; 1.
DR Pfam; PF12780; AAA_8; 1.
DR Pfam; PF12781; AAA_9; 1.
DR Pfam; PF18198; AAA_lid_11; 1.
DR Pfam; PF08385; DHC_N1; 1.
DR Pfam; PF08393; DHC_N2; 1.
DR Pfam; PF18199; Dynein_C; 1.
DR Pfam; PF03028; Dynein_heavy; 1.
DR Pfam; PF12777; MT; 1.
DR SUPFAM; SSF52540; SSF52540; 4.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Developmental protein; Dynein; Membrane; Microtubule; Motor protein;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..4171
FT /note="Cytoplasmic dynein 2 heavy chain 1"
FT /id="PRO_0000318748"
FT REGION 1..1598
FT /note="Stem"
FT /evidence="ECO:0000250"
FT REGION 1599..1823
FT /note="AAA 1"
FT /evidence="ECO:0000250"
FT REGION 1883..2100
FT /note="AAA 2"
FT /evidence="ECO:0000250"
FT REGION 2184..2432
FT /note="AAA 3"
FT /evidence="ECO:0000250"
FT REGION 2527..2767
FT /note="AAA 4"
FT /evidence="ECO:0000250"
FT REGION 2776..3064
FT /note="Stalk"
FT /evidence="ECO:0000250"
FT REGION 3140..3367
FT /note="AAA 5"
FT /evidence="ECO:0000250"
FT REGION 3575..3784
FT /note="AAA 6"
FT /evidence="ECO:0000250"
FT COILED 164..203
FT /evidence="ECO:0000255"
FT COILED 629..693
FT /evidence="ECO:0000255"
FT COILED 829..861
FT /evidence="ECO:0000255"
FT COILED 927..1048
FT /evidence="ECO:0000255"
FT COILED 1354..1383
FT /evidence="ECO:0000255"
FT COILED 2790..2877
FT /evidence="ECO:0000255"
FT COILED 2999..3059
FT /evidence="ECO:0000255"
FT COILED 3308..3336
FT /evidence="ECO:0000255"
FT BINDING 115..122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 1637..1644
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 1921..1928
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2226..2233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2565..2572
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 295
FT /note="R->C: Shorter cilium, and severely reduced speed and
FT reduced frequency of intraflagellar retrograde transport of
FT mutant protein."
FT /evidence="ECO:0000269|PubMed:28479320"
FT MUTAGEN 1384
FT /note="R->C: Reduced frequency of intraflagellar retrograde
FT transport of mutant protein."
FT /evidence="ECO:0000269|PubMed:28479320"
FT MUTAGEN 1693
FT /note="R->C: Shorter cilium, and reduced speed and
FT frequency of intraflagellar retrograde transport of mutant
FT protein."
FT /evidence="ECO:0000269|PubMed:28479320"
FT MUTAGEN 2935
FT /note="K->Q: Reduced binding to microtubules. Severely
FT truncated cilium. Accumulates in truncated cilium and does
FT not undergo intraflagellar retrograde transport."
FT /evidence="ECO:0000269|PubMed:28479320"
SQ SEQUENCE 4171 AA; 473818 MW; D45B5ADE572D06BC CRC64;
MSSDSKDQRK TYFLRVASYL LGLNIVEEKL KSTEPLEIFL DSNTNLLVFS RSEQKLELSN
KMKSSAPSAN VFRVVFYKTQ SVPLNNDNFK SVVNVISANG TLNHVFLKSV QNVFGKELTE
GNNMQLIAAV NELEESLLAT VEMSGGGSLH DEIRSWKGQT GKPANDYNEA FKQLQLLVET
MEERSIDELS ELVECFEDTC DELWNCGTPY PQNRMKMLIE YGASYLCETI TFKIDDSAIW
RNDKVADQLR SAIDVCDQML IIVRLLTAQT WKRNVEHTWE GDAMEMKFLN GFKDRLDEIL
SLKSLGGQLE ELLEERGVRE ETEKTIETAM RGMAPLAYNP FTEPNWKSRL LVSERSIEGT
IDRTLPILKQ RLAPANGDSQ SIVLSLEKLK SFLCRSNIKE KLQHEREMFL NRLVSMLSQK
NQEFNEKSLQ VDAKNFQFLT EVAARIVWIR QQTSQMESIR SLSKMMLNNI SNYSAFASKL
DEFIEKLQYA EKECFDDWCR ETVGLIDNKN ETINLETTGK IMYLEASNRE LNVNYSDRLL
RLLKEVRQLI SLGFNIPSKI MSCANNGEKY YRFGVILKQI AHFYNTIDQQ MIPSQQSLML
EEAIAFEKLV IPRKDASNSA SKVTWNDPKQ LEEFIVQLQS AEQKLSNRNR RLRNVHMELI
EMVEKLMDLN IVKQNNEWKE IILKIRSKMK EEEIVHGAVK NNMKPWLIHW DFQLYKALLI
QYEWGIESIQ SQLSTISVSL VFADQKIQLR PTIEEIRSKY YKELCRFLRI PDKFRGVQED
ENSTKFYAQM IERSMHLLPT VYEKAEQLMM KVETCDAIFV DWLVISQVDL EELIEENLKT
AADWESQFKI LKGKAREAER LPHELKFECI LVSTAGVKSA IEDAIQRLYD ALSWTLRHSI
STTSQSISTF LSQAIEVLNT VPQSIDEIAE ANAKHVIFAE NNRRLKEEWK VMEEQLTLLR
SVAGTGMEQI DNLEQTWDRF ELMLDGHQSM IKDQVEVLKS NVETSVKGMK DEAEKLKARW
EQFKPRNDAL QGDREEMLKA IQFIKEKRVQ WQQLSDGREK IEKECGQFGL EPPKMDIIDE
IDEDIKQFED NWLIYEMFNN ELDTMSQEEW IVFRSKTYLF DEFLQKWMEK LKGTGSQTHM
SVRLMKDVEH FKEVSSALKF CRGDVLSADH WHEMFRFLGL PRGTTIEKLK FADLLSVSKN
IIENTDQLKQ LNSRAQGEVA IRDAIQELTL WAAQTEFTLA DYKHSNGQNL KIIKEWKESI
NSLKDSQALL QSLKSSPYYS QFTDKTAVWE TRLADLDVFL AQMNEIQRKW IYLEPIFGRG
ALPSEASRFS RVDSEYRAIL NDVSKDARLV SLCSRQSLKK SLEQIVDQLN RCQKALNQFL
EQKRTAFPRF YFIGDDDLLE ILGQSTNPQV IQTHMKKLFQ GINRVQFSST GETIISMVSS
EGETVPLSKA VRIVPQVESW LQELSDEMRR TLKDLTAQAV ADAQPSLAKY PSQVLCLAEE
VKFSASIENN LNGSSDLNSF KSQLLEKLKA YTNMKVDDKV SDLKLKSLIL DLIHHIDVVD
QLLTNQAKSI NSWTWQRQLR FYLVNGGIVL RQVSSEFEYT YEYQGNYAKL VHTPLTDKCY
LTLTQAMYMG LGGNPYGPAG TGKTESVKAL AALMGRQVLV FNCDEGIDVT SMGRIFTGIV
ECGAWGCFDE FNRLDSTVLS AVSMQIQTIQ GAIKSRAGSC TFGGKNVQVN PNSAIFVTLN
PAGKGYGGRQ KMPDNLKQLF RAVVMGKPDN ELISSTILYS EGFVDATALA RKIVSVFQLS
RQMLSKQQHY DWGLRALKVV LGGCGALRRT QTNKNETDLV VQALLLNTLS KLTFSDSERF
NSLIDDIFSN VTKEMTKFEE LVEPLGVAAQ EMGIKLGDKQ MEKVFQLYEQ MRQRIGVVVV
GAAGSGKSTI WKILQRSLIL TKKPLKVTQF NPKAVNRSKL LGNMDMDTRE WSDGIITMAA
REVTKDTSVH HWIVCDGDID PEWVEALNSV LDDNRLLTMP SGERIQFGSN VNFLFETDSL
QFASPATVSR MGMIYISEED VTPKDIVASW LVKTTEDLHA DMPSWIEEHF WRCLKWVRSH
KISGITSFAI LKNGLTHLKA SKTKTQFLVL LFNGFLPTVT PENRQEFAKG VVFQGMSVPD
PKNICYDERI DGIMSYTDDV SQNVTKEEVE REDLRPFVQT ADTQRYSDII GSWLQSGNRE
SFLITGTTGC GKQQLLKHCF QNDPESQLAS LYCSAQSSSS HLLQLIQQNC VQASNPTGRV
WRPKDRPNMI LFLKGINLPA PDKYGTNELL ALLQQLLTYQ GFFDHNLEWV SIENIQFVGS
MNPIGDGAAV SISNRLFSLL RCVSLNTTDS SQLTSIYRTY LTPILEEVGE RNSEIIANRM
VDIYNKVQSN FRPTDSVVFL FSPRDLTNWV VSLLRHELDQ GKLEAVICFE ARRIFADRLP
TENDKLKFEE ILRNVIPISQ ANETVIFKEK VYVTTGTVVP GESNTGLPLT PINMSDFNQL
LAKSINRFAF EIANFNCPLT SQLAFFCACI DRVLTGPGGH LFLPGRPGFG RRDSVRLVAH
MHNIQVFSPP VTANFSAKQF DNELKNAITQ AVTNNEHVVL ILEDHQLRKN IFLQAINSLL
ASGNVPGLFT QQELDGLVAL VSEAANQASF TGALQQFLAH RIRSLVHVVL ILEVEANDFK
INITENPAIL KHCNVIFADR FDRNSLVEIP KIQMESQGIT TTDAILTGFN DVLVNLPEHL
SIQPIKYRQF VENFFQLLGY KRLTLSVRLE RLKGGVSKLN EARDEVAKMQ KKAGKKSKLL
AEKQAEADEA LKAITESMSG AEDQKLSMEQ LKAATEKENV RIEEQKAKID EQLKEVQPLI
DEARRAVGSI KSESLSEIRS LRAPPEAVRD ILQAVLLFMG ILDTSWEAMR KFLSKSGVKD
DIMNFDANRI TNEIHKKVTA LVKQKSNSFE EANAKRASAA AAPLAAWVKA NLEYSKILEK
IAPLEGEKNK LVKNLKKAEK QMENLSKGLQ SVDEVVGELK RKFEVLMKEA TQIKVDLDRE
QDTIRIAGTL VESLSGEFER WKIQIETFGE EQSKMELCSL ITSAFITYLG GCSEKDRKSL
LKSMCKMFNM PPTFKPLSFA SLETEQLNWK TKGLPADQLS LENGSILFTS CHAPLIIDRS
GQVSLFLSKF LEKSETFKAA QPDLMTQIEL AIRFGKTIII DDIVEFDSAL IPILRKDLSS
QGPRQVISFG GKSIDFNPDF KIYFCTRDEK VDIRPNSYVQ LNIVNFTTTI SALSAQLLDV
AIHLEKPELE ERSSSLLRDA ELKKLELEGL EQLLLQQLAS SQGNLLENTA LLDSLNKSKE
SAEIITKSIV ESEQLHKELT TQKDIYVPLS LFTSSLFFSF SNLQFHNPMY NYSVNTIMHL
FGKTIKSCED KSSTRVETLA RQMQLTVFYH ISRGIFRQDR LMFAVAFINA TMPKMFQPKE
WELFTGVLVD ESTDLSALRV QWISPDRLQS LARIRTHLPS LFNNFQIQDD ATWNEFSKTL
QCENAFPKNV ELKMTHFQKV LFIQAVKPER LYNCLMDFVL KTLNIPSINP PAFELKHIFQ
ESESTEPILF ILADGADPSQ ELSEFASSMN VPYHSISMGQ GQEIAAYEAI RESASKGEWL
CLNNLHLMLQ AVPSIFKHLS LTTPHENFRL WLTTEGDARF PSMMLQQSLK ITFEPPPGVR
NNLLRTYTQI DRSTKNVITC QSIFVLAWLH ALLQERRTFI PQGWTKFYEF GASDVRVAKS
FVEQLTANKA DWEFVRGILK FVIYGGRIEN DFDFKVLDSY LNVLFCDEKI NGRAGSQLVK
GIDLLATTNV QEYIGHISKS VPSVDEPYLF GLPENIKYSW QIVEADRTIS SIRTLALGDT
KNALSDQSDK ISQIVSLWKK LCQSDDLPKR ELPTAIRSAD PISEVLCLET INALSLIKQL
HRSIGHVAKS MKTPSLASPA VQKTIQSLVF QQTPDEWDSM WAGPSDPADY LNVVVKKTRG
TLQLFESSKS SSLLSSPIDF SDLFYPNIFL NALRQTTSRQ IKIPLDQLIL SSAWTPSQLP
AKQCVQVQGL LLQGATFDSF LRETTVSSAA YSQAPIVFLA WTSESSSTIT GEQIQVPVYS
SSERSDLICS VNMPCRGADQ WNIAAVALFL R
