DYHC2_CHLRE
ID DYHC2_CHLRE Reviewed; 4334 AA.
AC Q9SMH5; A8HYT6; Q9ZSS7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Cytoplasmic dynein 2 heavy chain 1;
DE AltName: Full=Cytoplasmic dynein heavy chain 1b;
DE Short=cDHC1b;
GN Name=DHC1B; Synonyms=DHC2; ORFNames=CHLREDRAFT_24009;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP INDUCTION.
RC STRAIN=21gr / CC-1690;
RX PubMed=10069812; DOI=10.1091/mbc.10.3.693;
RA Porter M.E., Bower R., Knott J.A., Byrd P., Dentler W.L.;
RT "Cytoplasmic dynein heavy chain 1b is required for flagellar assembly in
RT Chlamydomonas.";
RL Mol. Biol. Cell 10:693-712(1999).
RN [2]
RP SEQUENCE REVISION, FUNCTION, INTERACTION WITH D1BLIC, SUBCELLULAR LOCATION,
RP AND TOPOLOGY.
RC STRAIN=21gr / CC-1690;
RX PubMed=12802074; DOI=10.1091/mbc.e02-10-0682;
RA Perrone C.A., Tritschler D., Taulman P., Bower R., Yoder B.K., Porter M.E.;
RT "A novel dynein light intermediate chain colocalizes with the retrograde
RT motor for intraflagellar transport at sites of axoneme assembly in
RT chlamydomonas and mammalian cells.";
RL Mol. Biol. Cell 14:2041-2056(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503, and cw92;
RX PubMed=17932292; DOI=10.1126/science.1143609;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J.,
RA Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT "The Chlamydomonas genome reveals the evolution of key animal and plant
RT functions.";
RL Science 318:245-250(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 992-2189, FUNCTION, DISRUPTION PHENOTYPE,
RP SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=9971742; DOI=10.1083/jcb.144.3.473;
RA Pazour G.J., Dickert B.L., Witman G.B.;
RT "The DHC1b (DHC2) isoform of cytoplasmic dynein is required for flagellar
RT assembly.";
RL J. Cell Biol. 144:473-481(1999).
RN [5]
RP INTERACTION WITH D1BLIC, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=15269286; DOI=10.1091/mbc.e04-05-0377;
RA Hou Y., Pazour G.J., Witman G.B.;
RT "A dynein light intermediate chain, D1bLIC, is required for retrograde
RT intraflagellar transport.";
RL Mol. Biol. Cell 15:4382-4394(2004).
RN [6]
RP INTERACTION WITH D1BLIC; FAP133; FLA10 AND LC8.
RX PubMed=17895364; DOI=10.1242/jcs.012773;
RA Rompolas P., Pedersen L.B., Patel-King R.S., King S.M.;
RT "Chlamydomonas FAP133 is a dynein intermediate chain associated with the
RT retrograde intraflagellar transport motor.";
RL J. Cell Sci. 120:3653-3665(2007).
CC -!- FUNCTION: May function as a motor for intraflagellar retrograde
CC transport. Functions in flagellar biogenesis.
CC {ECO:0000269|PubMed:10069812, ECO:0000269|PubMed:12802074,
CC ECO:0000269|PubMed:9971742}.
CC -!- SUBUNIT: The cytoplasmic dynein complex 2 is probably composed by a
CC DHC1B homodimer and a number of D1BLIC light intermediate chains.
CC Interacts with FAP133, FLA10 and LC8. {ECO:0000269|PubMed:12802074,
CC ECO:0000269|PubMed:15269286, ECO:0000269|PubMed:17895364}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum basal body
CC {ECO:0000269|PubMed:12802074, ECO:0000269|PubMed:9971742}. Cell
CC projection, cilium, flagellum membrane {ECO:0000305}; Peripheral
CC membrane protein {ECO:0000305}; Cytoplasmic side. Cytoplasm
CC {ECO:0000269|PubMed:12802074, ECO:0000269|PubMed:9971742}.
CC -!- INDUCTION: Up-regulated during flagellum biogenesis.
CC {ECO:0000269|PubMed:10069812, ECO:0000269|PubMed:9971742}.
CC -!- DISRUPTION PHENOTYPE: Algae display short flagellar stumps filled with
CC aberrant microtubules, raft-like particles and other amorphous
CC material. {ECO:0000269|PubMed:10069812, ECO:0000269|PubMed:9971742}.
CC -!- SIMILARITY: Belongs to the dynein heavy chain family. {ECO:0000305}.
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DR EMBL; AJ132478; CAB56748.2; -; Genomic_DNA.
DR EMBL; DS496110; EDP08405.1; -; Genomic_DNA.
DR EMBL; AF096277; AAC99457.1; -; mRNA.
DR PIR; T34340; T34340.
DR SMR; Q9SMH5; -.
DR STRING; 3055.EDP08405; -.
DR PaxDb; Q9SMH5; -.
DR PRIDE; Q9SMH5; -.
DR eggNOG; KOG3595; Eukaryota.
DR HOGENOM; CLU_000038_7_2_1; -.
DR InParanoid; Q9SMH5; -.
DR OrthoDB; 26380at2759; -.
DR GO; GO:0097014; C:ciliary plasm; IDA:BHF-UCL.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IDA:BHF-UCL.
DR GO; GO:0030286; C:dynein complex; IDA:BHF-UCL.
DR GO; GO:0030990; C:intraciliary transport particle; IDA:BHF-UCL.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0031514; C:motile cilium; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003774; F:cytoskeletal motor activity; TAS:BHF-UCL.
DR GO; GO:0045503; F:dynein light chain binding; IPI:GO_Central.
DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; IEA:InterPro.
DR GO; GO:0072594; P:establishment of protein localization to organelle; IMP:BHF-UCL.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0044458; P:motile cilium assembly; IMP:BHF-UCL.
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; IPR003593; AAA+_ATPase.
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; 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 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 SMART; SM00382; AAA; 3.
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; Flagellum; Membrane; Microtubule;
KW Motor protein; Nucleotide-binding.
FT CHAIN 1..4334
FT /note="Cytoplasmic dynein 2 heavy chain 1"
FT /id="PRO_0000318747"
FT REGION 1..1704
FT /note="Stem"
FT /evidence="ECO:0000250"
FT REGION 1705..1929
FT /note="AAA 1"
FT /evidence="ECO:0000250"
FT REGION 1996..2211
FT /note="AAA 2"
FT /evidence="ECO:0000250"
FT REGION 2299..2544
FT /note="AAA 3"
FT /evidence="ECO:0000250"
FT REGION 2641..2882
FT /note="AAA 4"
FT /evidence="ECO:0000250"
FT REGION 2897..3185
FT /note="Stalk"
FT /evidence="ECO:0000250"
FT REGION 3260..3492
FT /note="AAA 5"
FT /evidence="ECO:0000250"
FT REGION 3701..3917
FT /note="AAA 6"
FT /evidence="ECO:0000250"
FT COILED 1026..1097
FT /evidence="ECO:0000255"
FT COILED 2930..2998
FT /evidence="ECO:0000255"
FT COILED 3120..3199
FT /evidence="ECO:0000255"
FT BINDING 150..157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 1743..1750
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2034..2041
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2334..2341
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2679..2686
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 2005
FT /note="C -> L (in Ref. 4; AAC99457)"
FT /evidence="ECO:0000305"
FT CONFLICT 3762
FT /note="Missing (in Ref. 3; EDP08405)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 4334 AA; 481652 MW; E2DA5EAE0E8605B0 CRC64;
MSSDSRKTFV VTTIACAIAP AGQQDQYAAY LGQDENGAIA SFLDSTQNTL QAGVSGLGTG
QLQLKLSNAA EFPEGCEFSV VLSKLRAGPI RTEDVPAGVA VATVAHSPLS SLYHTLKDVY
SPLIKSQTAE GVPVLDKRLS ELLAQVQAGL GTAVRKGVPA SAQEVADPNQ APLQEVVTPL
DEINFWAELT NSPNAGPIKS SALQVSSALE PLRQSFEQLS SDAPEGEGGS IGWEGAKELV
DLTTNALRAA WPVKLPIGGW AMGQKRADNF LRVVGAALAT YVQRRVDRLA AAGRGDLWSA
PFGEVRAVLV GASGLMTRWV QESTALVEDW RLGVDTGGHD WEGAAFADAY VRSFQERLEE
IYNMREMVDE LAKLVGREEA GSLGVQQVFA PFQGLQALQV SDFNTHVWKA AHEDFERRMG
PIEQRISQKL KELFASVIIP SLTSAIGPGR GGDRAAAGGS LIQPQQVFAE IKRYSSLMGR
KNIASALQSE KETLAKQVDR HLDSVQAEFD AHRDSATGGA KVAPVGRVTA SIVERIMWCM
QTLQKLGKVS EVLKHMLRGG VAGDEGSGGA ALRNTLGVVS ELQKEVEIFR KEQYSAWEEW
MSEELGEMAN WKNSKLMTFD SQNSHVKTHF NDQLVLLLRE VRQLQSLGFG VRKDILNEVE
IANKFYRYGM VLKQRANFYN NIATEMVQCQ KPMMLKDALD FEKVLMNPKD AQGKEITWRN
AAALDGYVRR LNEVADRLAE KNRTLRKWHS VLSDKVVTLA GTDLVRHKDK WAAGVKEMRE
IFGRLEAEGY SRESQQVWRQ HWDFQLYKAL EVQYLSGLEM INKTLPEVEV KMVFRQHRLQ
YDPPLEELRI RHVKDLLNTF LGLPLRMKGV SDLSERPGFF RPIVDANPTG IARVYAAAES
LFTQLADELK KYQDWMVLGT LDLDEFADAN LLEVSDWELN FRMLKAASRD AEKLPNEIRI
ECYKVSLAPV KGSIDEHMKK LQDTLVASLR RKTVAEKDQI EDFMKNGREL FTRQANTVED
IGLAGQEAKG LTAKLAEVQA ARRRIDEKNK LLRQMAGGGR DAAFAVVDLT EVNNSWDAFT
NQLQQFDAHL EEQKGNLAVQ ISRQLEEFKG KVAGMNSRWQ ELKPKSGPSG NPAVVLAKIQ
EYANAIKELR EESAKLYKEA EAFKIDVPDF ELMTEMETDV MATKAHWDRY ADFLRERDEM
ANRDWLSMRD QVWKIEDFLA KWTKATAGKS DDPIAVILTQ EIDNYTLCLP HLKSCLRGAG
WEDTHWNQLF GLLGMKTSGP AAVSKETVTL THFLEKADLV VKHADVIKSL DAQAQGEAVI
RKALTELKMW GMAREFTFTE STQSVAGRQR RTPLIKEWRD AMTEVGDNQS LVASLKQSSY
YNMFKDEVSS WENKLSFLQE GLTLLNQIQR KWVYLEPIFG RGALPSQQQR FRNVDEEFRR
TMTSLESTKK VVTFADIPGI RDKLPQMAQQ LDVCQRALAD FLEEKRSQFP RFYFLGDDDL
LEILGQARNP AVIQSHLKKL FAGIQKVKFS QDQSTIQAMQ SMEGEVVDLA PTVRITEQIE
TWLGDLTRSM KNTLQQQNEV LCAGRMNDEF RAAASQCLQL KEAVAFTEKA EVALKAGSSG
LAKLVTEMRA QLMKLTGSDF TGHHLLQLKK QALVLDFIHY CDVAEYLAKD KIGGTTEWGW
TRQLRYYHRA EGSVKVAMAE ATFDYTWEYQ GNAAKLVYTP LTDKCYLTLT QGMALGYGGN
PYGPAGTGKT ESVKALGQAL ARQVLVFNCD EEFDFKSMGR IFVGLVKCGA WGCFDEFNRL
DEEVLSAVSQ QIQTIQLALK EGAKTMMFMD KTVEVDKNAG IFVTLNPAGK GYGGRSKLPD
NLKQLFRSIA MTVPNNELIA EVLLLSEGFN HAKDLARKLV SLFSLSRELL SPQQHYDWGL
RALKTVLGIA GRELRDARKA GQNVDAEIEA EIIIRSVAAT KLPTLTFDDN SRFKALINDL
FPGAKLTDAR NEALEKALAE AAAACKMELT QQQIDRMLQL HLACEQRIGV IIVGPSGSGK
STLWELLEKA YERLGRKPIV YKMNPKAMPR QQLLGSMNMD TREWSDGVLT AAARKVVKEP
LEQRSWIICD GDVDPEWIES LNSVLDDNRL LTMPNGERIQ FANNVNFIFE CHSLEFASPA
TVSRCGMLFM SDEAMEVERM LQRWLKVQAT DNGDPGQMQS WMNDFFDKAF QWALSHPRAV
ETTKGGILDS GLSHLKLGPG SKQEFMAGLC RGLGSNMNPD IRNQFYNDMA RMSGEGGIMD
VGVATDPLIV LGDELRERGM DEADGGLVVT PEVTQNLLMM APWFKNRDPF LVVGPEGCGK
GALLDYCFKR IMGVQVAVVN CSAQTSAANV VQKLVQVCGK PVTTTSGKAL RPPDNTRVIL
YLKDLNLPRP DKYNTCQLIS FLQQLIAHHG YYDENLDFIR VERVQIVGSM TPPGSVGRHA
LSTRFTALVR IVTMGYPDRE NLATIYTNMA QRVLANSKTA SSVSPAALSK AMLEVYSSVR
ERFTPNDYPH YEFNARELSD WINGIQRYSL EGGLTLVQAI AHEGLRVFRD RLVGDHQEQF
TSMLYGTLTS LLGYKPDATP WYTSTLGASA EERISGDLTK IKMLRWEQDT FAELVAEKLK
GYEREHKELN LLLFPEVLER VSRFDRVLSQ QGGSLLLCGN SGVGRRSLML LLAYMHNMDF
ITPKMTKNYD LKSFRNDLKE VLRRAGVEAK PVMLFLEDHQ LVNNAFLELV NSLLSGGEVP
GLFTPEELAK ELAPLDKARD EDPLYTGPSN SYAFFSYRIR RNLHIVVSMD PSNEMFRSRC
EANPALFTRC SVQWLEGWSV KGLQQIAAAR LTELVESSPE LMKLGRDKLI NHMIHIHASS
GSQTTREYLA LVSLYGQIYN RKRTQVLEQQ NFLKGGLGKL AEAAVTVDTL SAEAEKQRVV
LKAKQAEADE ALVHIQDSML KAADRRKEVE VLKKRTAIEE VEMKERRVKV EEELSEVQPL
IDAARKAVGN IKKDNIAEIR SLKMPPDAIR DVLEGVLMVL GQQDTSWNNM KTFLGKGSVK
DDIINYDAHK ITPEIRARCA KLLAAKGNSF EDAVIRRVSV AAAPMAQWFK ANLEFSKVLE
RVSPLESELH RLQSSLEESQ RLIKQYEEEL VQLDAAVASL KAEFSKKTSE AETLKISVDK
AESVLSSARQ LLDGLRGEKV RWEITVGTLG EQLKELPLSS LLAAAFITYL PSHPEEHRLK
VTKDWCAYLG AAEFDVTRFL SSESEMLKWK AEGLPADGLS AQNAVVILNS TSRSPLIIDP
STQASEWLKS HLRVTGQNVE VTTMADQRFT TTLELAVRFG KTLVVAEVDK VEPILYPLLR
MDLDRQGPRF VVQIGDKATD YNDTFRLFLV TRNPDPYLPP DARSLLAVTN FTVTRSGLEG
QLLGLTLQKE RPELEEQKST MLRQEDECKV ALAELERNLL QTLATSTGNI LENKDLLDKL
NETKTRSATV EKALTESKTL QASLDQQREV YRPIAARGSV MYFLLADLQA LNQMYTFSLS
VFLNLFKKAL DRDTPPGGDV TARIALLAES LLELVFAYVS RSLFNADRLT FGMHMARHLQ
PSLFPEAQWA FFLGKPVPDS ASPPPKPSWV REEQAGAFSA LAAAFPQLVA AAELADSALW
AQWASGATDA LPGKIAGGKV NPFQQLLLVK AFRPDRLQSA MSSFICGTLN IKSVSPPPFS
LKALIEGETR PDEPVLFITT PGADPSQELS EYAAQTMGKE RWYFEVAMGQ GQAEKAVTLL
RECAKNGDWL VLKNVHLAVS WLPSLEKELL MLQKHDNFRI FLTSEPHPKF PSTLLEMSLK
VTFEAPPGMK KNLQRTYEAW SAEYLASGPP IRAQLLFVLA WFHAVVQERR TYIPQGWTKF
YEFSFADLRS GMDVITLATR AGTAPQWPLL LGLLDDAIYG GRLDNPFDSQ VLLTFLRRLF
SAETVGAAGG KVRPLPGSKV VVPTTNHRAD YVSIISALPD VDTPGLFCMP DNIDRTAQQV
NSARVISQLK AMSLRADAAG GFNRAQWQAQ LGPLLRLWDQ LMSGASALKA AMKDIRARGT
TDKGGAPIEN FVALERYKGA SLVALIDRTL GAIARVLKGT DTLSSGVQSS GAALLADVIP
GSWDAAWEGP EAPMDYCRAV VAKALAIEGH WARCQQPGGG GLLDGSGGAG PLELSSVFHP
GTFLNALRQQ SARTLGCSMD MLKAVTSWET AKLKAAAGGA PVALLGGLIM QGATFDGSRL
SPVAAEAPAF RAVPAMSMAW LHKDSPMAYA SYMEAPLYMT SDRSKLLARV QLPVSGPEEM
DGWVLAGLSL FLSV
