DYHC_TRIGR
ID DYHC_TRIGR Reviewed; 4466 AA.
AC P23098;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Dynein beta chain, ciliary;
OS Tripneustes gratilla (Hawaian sea urchin) (Echinus gratilla).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC Euechinoidea; Echinacea; Temnopleuroida; Toxopneustidae; Tripneustes.
OX NCBI_TaxID=7673;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 162-172; 1193-1204;
RP 3240-3259 AND 3325-3339.
RC TISSUE=Blastula, and Sperm;
RX PubMed=1830927; DOI=10.1038/352640a0;
RA Gibbons I.R., Gibbons B.H., Mocz G., Asai D.J.;
RT "Multiple nucleotide-binding sites in the sequence of dynein beta heavy
RT chain.";
RL Nature 352:640-643(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1833761; DOI=10.1073/pnas.88.19.8563;
RA Gibbons I.R., Asai D.J., Ching N.S., Dolecki G.J., Mocz G.,
RA Phillipson C.A., Ren H., Tang W.Y., Gibbons B.H.;
RT "A PCR procedure to determine the sequence of large polypeptides by rapid
RT walking through a cDNA library.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:8563-8567(1991).
RN [3]
RP 3D-STRUCTURE MODELING.
RX PubMed=11250194; DOI=10.1016/s0969-2126(00)00557-8;
RA Mocz G., Gibbons I.R.;
RT "Model for the motor component of dynein heavy chain based on homology to
RT the AAA family of oligomeric ATPases.";
RL Structure 9:93-103(2001).
CC -!- FUNCTION: Force generating protein of eukaryotic cilia and flagella.
CC Produces force towards the minus ends of microtubules. Dynein has
CC ATPase activity; the force-producing power stroke is thought to occur
CC on release of ADP.
CC -!- SUBUNIT: Consists of at least two heavy chains (alpha and beta), three
CC intermediate chains and several light chains.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum. Cytoplasm,
CC cytoskeleton, flagellum axoneme.
CC -!- DOMAIN: Dynein heavy chains probably consist of an N-terminal stem
CC (which binds cargo and interacts with other dynein components), and the
CC head or motor domain. The motor contains six tandemly-linked AAA
CC domains in the head, which form a ring. A stalk-like structure (formed
CC by two of the coiled coil domains) protrudes between AAA 4 and AAA 5
CC and terminates in a microtubule-binding site. A seventh domain may also
CC contribute to this ring; it is not clear whether the N-terminus or the
CC C-terminus forms this extra domain. There are four well-conserved and
CC two non-conserved ATPase sites, one per AAA domain. Probably only one
CC of these (within AAA 1) actually hydrolyzes ATP, the others may serve a
CC regulatory function.
CC -!- SIMILARITY: Belongs to the dynein heavy chain family. {ECO:0000305}.
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DR EMBL; X59603; CAA42170.1; -; mRNA.
DR PIR; S17653; S17653.
DR SMR; P23098; -.
DR PRIDE; P23098; -.
DR GO; GO:0097729; C:9+2 motile cilium; IEA:UniProt.
DR GO; GO:0005858; C:axonemal dynein complex; IEA:InterPro.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0045505; F:dynein intermediate chain binding; IEA:InterPro.
DR GO; GO:0051959; F:dynein light intermediate chain binding; IEA:InterPro.
DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; IEA:InterPro.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0003341; P:cilium movement; IEA:InterPro.
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; IPR041589; DNAH3_AAA_lid_1.
DR InterPro; IPR030443; DNAH9-like.
DR InterPro; IPR042222; Dynein_2_N.
DR InterPro; IPR043157; Dynein_AAA1S.
DR InterPro; IPR041466; Dynein_AAA5_ext.
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:SF257; PTHR10676:SF257; 1.
DR Pfam; PF12774; AAA_6; 1.
DR Pfam; PF12780; AAA_8; 1.
DR Pfam; PF12781; AAA_9; 1.
DR Pfam; PF17857; AAA_lid_1; 1.
DR Pfam; PF18198; AAA_lid_11; 1.
DR Pfam; PF08385; DHC_N1; 1.
DR Pfam; PF08393; DHC_N2; 1.
DR Pfam; PF17852; Dynein_AAA_lid; 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 projection; Cilium; Cilium biogenesis/degradation;
KW Coiled coil; Cytoplasm; Cytoskeleton; Direct protein sequencing; Dynein;
KW Flagellum; Microtubule; Motor protein; Nucleotide-binding; Repeat.
FT CHAIN 1..4466
FT /note="Dynein beta chain, ciliary"
FT /id="PRO_0000114645"
FT REGION 1..1813
FT /note="Stem"
FT /evidence="ECO:0000305"
FT REGION 1814..2035
FT /note="AAA 1"
FT /evidence="ECO:0000305"
FT REGION 2095..2316
FT /note="AAA 2"
FT /evidence="ECO:0000305"
FT REGION 2422..2669
FT /note="AAA 3"
FT /evidence="ECO:0000305"
FT REGION 2767..3016
FT /note="AAA 4"
FT /evidence="ECO:0000305"
FT REGION 3033..3325
FT /note="Stalk"
FT /evidence="ECO:0000305"
FT REGION 3409..3636
FT /note="AAA 5"
FT /evidence="ECO:0000305"
FT REGION 3846..4072
FT /note="AAA 6"
FT /evidence="ECO:0000305"
FT COILED 733..805
FT /evidence="ECO:0000255"
FT COILED 1036..1056
FT /evidence="ECO:0000255"
FT COILED 1306..1337
FT /evidence="ECO:0000255"
FT COILED 1443..1468
FT /evidence="ECO:0000255"
FT COILED 3033..3092
FT /evidence="ECO:0000255"
FT COILED 3263..3325
FT /evidence="ECO:0000255"
FT COILED 3573..3642
FT /evidence="ECO:0000255"
FT BINDING 154..161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 1852..1859
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2133..2140
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2460..2467
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2805..2812
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VARIANT 611..615
FT /note="Missing"
FT VARIANT 3357
FT /note="P -> LLTGNFFCCFMTA"
SQ SEQUENCE 4466 AA; 511782 MW; 2A695BF8F336911E CRC64;
MADVVDPRLE FISEYILKSY KLKPDKWAKC INVEENKILM LEFLEKADNP QLVFTVNAAG
LITPSYEFPS ALKNTKAIYF IKKGREPVGK DNIKTTLVYG DLSYTPLEQL SALVDEILVP
LLANPRNHEQ WPVVVSQDVL RHVHNLKSSV YVVAGQVKGK TLLPLPVGSE KVETAAESEE
KDDSYDRSLV HAIESVIIDW THQIRDVLKR DSAQPLLEGL NPGPMVEINF WKAKCENLDC
IFQQLRDPKV RKMKELLERT QSSYLPSFNN IERDVEAALT EAQDINCYLK PLIYQVESLD
ELEFPDMTPR LAPILHTVCL IWSNSDYYNT APRIIVLLQE ICNLLIDLCR TFLDPSEIFK
LEPEESLEKV RGALAVLKAW RDLYDEHRAK LKDYFKDGRE VKGWEFASPL VFTRMDNFTS
RIETIQSLFE TNVEFSKLEK TEMGSMKGRM LSQQVEKIHE EFQECAKVFT ERPYDGLDPQ
CQEFLDDYEE FEKKVFDLDR RLGSILCQGF DDCCGLEAVF KMLDCYGPLL DRPVIRNDFE
CKYPVVLMLY DLELDQAKEI YDEHMRVEEN DGNAPLNKNM PDVAGQLKWS AQLRDRISKP
MGSLKHMEHP TGVRRILESE DAKVVFQKYE EMINLLNKYE QKVFENWTKG VDEVCKTNLD
QSLITRDEST KLIKINFDPK LVAVLREVKY LQIRGEESIP ESAASIYEKH ETLRKYVANL
DLTQAWYNKV RNTVLEVEFP LIEGQLADLD TRLKQAESEL NWTSDSVWEY IQETRDQVHD
LEKRVQQTKD NVDRIKKIMA EWTKQPLFER KELKKESLLA LDDRQDRLKK RYAEISTAGE
KIHSLIKENL GLFKADASSD IWKAYVDYVD DMVIDGFFNC IHCTLSYLLE NTDPRHCAAP
LFEARLELQV PDMIFNPSLD YGVADGFYDL VEMLISDTYK MASLVSRLAE HNGQEHYQAD
LEGMDDLSDV RNDLMDRVQT IMTKAQEYRN SFDNYAYLYV DDRKEFMRQF LLYNHVLTTE
EIEAHAEDGV PECPPTLDQF KEQVDTYEKI YSEADEIEPE QVFDAWFRVD SKPFKAALLN
IIKKWSFMFK QHLIDHVTNS LSELQEFIKV GNSGLTKTVE EGDYNGLVEC MGHLMAVKER
QAATDEMFEP IKQTIELLKT YDQEMSEEVH TQLQELPEQW NNTKKIAITV KQQVAPLQAN
EVAIIRRKCT SFDVRQHEFR ERFRKEAPFI FTFEGPYQCL DRCHSEIYEM EEHMANLQES
AGLFEVNMPD YKQLKACRRE VRLLKALWDL IMIVRTSIED WKTTPWLEIN VEQMEMDCKK
FAKDIRSLDK EMRAWDAYNG LDATVKNMLT SLRAVSELQN PAIRERHWQQ LMAATKVKFT
MDKETTLSDL LALNLHNFED EVRNIVDKAV KEMGMEKVLK ELNTTWSSMD FEYEPHSRTG
ISLLKSNEEL IETLEDNQVQ LQNLMTSKHI AHFLEEVSGW QKKLSTTDSV ITIWFEVQRT
WSHLESIFIG SEDIRNQLPE DSKRFDGIDT DFKELASEME KTPNVVEATN RARLYDRLEA
IQGSLVVCEK ALAEYLETKR LAFPRFYFVS SADLLDILSQ GNNPSQVQRH LSKLFDNMAK
LKFKQDDEGN DTKLALGMYS KEGEYVDFDK ECECTGQVEV WLNRVMDAMR STVRSQFADA
VVSYEEKPRE QWLYDYPAQV ALATTQVWWT TEVNISFARL EEGHENSMKD YNKKQIQQLN
TLIGLLIGKL TKGDRQKIMT ICTIDVHARD VVAMMVLKKV DNAQAFQWLS QLRHRWADDD
KHCYANICDA QFKYSYEYLG NTPRLVITPL TDRCYITLTQ SLHLVMSGAP AGPAGTGKTE
TTKDLGRALG IMVYVFNCSE QMDYKSCGNI YKGLSQTGAW GCFDEFNRIS VEVLSVVAVQ
VKCVQDAIRD KKERFNFMGE EISLIPSVGI FITMNPGYAG RTELPENLKA LFRPCAMVVP
DFELICEIML VAEGFLDARL LARKFITLYT LCKELLSKQD HYDWGLRAIK SVLVVAGSLK
RGDPQRPEDQ VLMRALRDFN VPKIVSDDTP VFMGLIGDLF PALDVPRRRD MDFEKVVKQS
TLDLKLQAED SFVLKVVQLE ELLAVRHSVF VIGNAGTGKS QVLKVLNKTY SNMKRKPVLV
DLNPKAVTND ELFGIINPAT REWKDGLFSV IMRDMSNITH DGPKWIVLDG DIDPMWIESL
NTVMDDNKVL TLASNERIPL TPSMRLLFEI SHLKTATPAT VSRAGILYIN PSDLGWNPIV
TSWIDTREVQ SERANLTILF DKYLPTLLDT LRVRFKKIIP IPEQSMVQML CYLLECLLTP
ENTPADCPKE LYELYFVFAS IWAFGGSMFQ DQLVDYRVEF SKWWITEFKT IKFPNQGTVF
DYFIDQESKK FLPWSEKVPV FELDPEIPMQ AVLVHTNETT RVRFFMDLLM ERGRPVMLVG
NAGLGKSVLV GDKLSNLGED SMVANVPFNY YTTSEMLQRV LEKPLEKKAG RNYGPPGTKK
LVYFIDDMNM PEVDTYGTVQ PHTLIRQHMD YKHWYDRQKL TLKEIHKCQY VSCMNPTAGS
FTINSRLQRH FCVFALSFPG QDALSTIYNS ILSQHLANIS VSNALQKLSP TVVSATLDLH
KKVAQSFLPT AIKFHYVFNL RDLSNVFQGL LYSGPDLLKA PIDFARLWMH ECQRVYGDKM
INDQDIEAFE KLVLEYAKKF FEDVDEEALK AKPNIHCHFA TGIGDPKYMQ VPNWPELNKI
LVEALDTYNE INAVMNLVLF EDAMQHVCRI NRILESPRGN ALLVGVGGSG KQSLARLASY
ISSLEVFQIT LRKGYGIPDL KLDLATVCMK AGLKNIGTVF LMTDAQVSDE KFLVLINDLL
ASGEIPDLFA DDEVENIIGG VRNEVKGMGL QDTRENCWKF FIDRLRRQLK TVLCFSPVGT
TLRVRSRKFP AVVNCTSIDW FHEWPQEALV SVSMRFLDEV ELLKGDIKKS IAEFMAYVHV
SVNESSKLYL TNERRYNYTT PKSFLEQIKL YESLLSMKSK ELTAKMERLE NGLTKLQSTA
QQVDDLKAKL ASQEVELAQK NEDADKLIQV VGVETEKVSK EKAIADDEEK KVAIINEEVS
KKAKDCSEDL AKAEPALLAA QEALNTLNKN NLTELKSFGS PPSAVLKVAA AVMVLLAPNG
KIPKDRSWKA AKVVMNKVDA FLDSLINYDK ENIHENCLKS IKEYLNDPEF EPEYIKGKSL
AAGGLCSWVV NIVKFYNVYC DVEPKRIALQ KANDELKAAQ DKLALIKAKI AELDANLAEL
TAQFEKATSD KLKCQQEAEA TSRTITLANR LVGGLASENV RWGEAVANFK IQEKTLPGDV
LLITAFVSYI GCFTKTYRVD LQERMWLPFL KSQKDPIPIT EGLDVLSMLT DDADIAVWNN
EGLPSDRMST ENATILSNCQ RWPLMIDPQL QGIKWIKQKY GDDLRVIRIG QRGYLDTIEN
AISSGDTVLI ENMEESIDPV LDPVLGRNTI KKGRYIKIGD KEVEYNPDFR LILQTKLANP
HYKPEMQAQT TLINFTVTRD GLEDQLLANV VAQERPDLEK LKSDLTKQQN DFKIILKELE
DNLLSRLSSA EGNFLGDTAL VENLETTKRT AAEISVKVEE AKVTEVKINE ARELYRPAAA
RASLLYFILN DLNKINPIYQ FSLKAFNTVF SLPIARAEPC EDVKERVVNL IDCITYSVFI
YTTRGLFEAD KLIFTTQVAF QVLLMKKEIA QNELDFLLRF PIQVGLTSPV DFLTNSAWGA
IKSLSAMEDF RNLDRDIEGS AKRWKKFVES ECPEKEKFPQ EWKNKSALQK LCMMRALRAD
RMSYAVRNFI EEKLGSKYVE GRQVEFAKSY EETDPATPVF FILSPGVDPL KDVEALGKKL
GFTFDNNNFH NVSLGQGQEI VAEQCMDLAA KEGHWVILQN IHLVAKWLST LEKKLEQYSV
GSHDSYRVYM SAEPAGSPEA HIIPQGILES SIKITNEPPT GMFANLHKAL YNFNQDTLEM
CAREAEFKVI LFALCYFHAV VCERQKFGPQ GWNRSYPFNT GDLTISVNVL YNYLEANSKV
PWQDLRYLFG EIMYGGHITD DWDRRLCRTY LEEYMAPEML DGELYLAPGF PVPPNSDYKG
YHQYIDEILP PESPYLYGLH PNAEIGFLTT ESDNLFKIVL ELQPRDAGGG GGGGSSREEK
IKSLLDEIVE KLPEEFNMME IMAKVEDRTP YVVVAFQECE RMNMLTSEIR RSLKELDLGL
KGELTITPDM EDLSNALFLD QIPATWVKRA YPSLFGLTSW YADLLQRIKE LEQWTADFAL
PNVVWLGGFF NPQSFLTAIM QSMARKNEWP LDKMCLQCDV TKKNKEDFSS APREGSYVHG
LFMEGARWDT QTNMIADARL KELAPNMPVI FIKAIPVDKQ DTRNIYECPV YKTKQRGPTF
VWTFNLKSKE KAAKWTLAGV ALLLQV