DYH5_RAT
ID DYH5_RAT Reviewed; 3470 AA.
AC M0R8U1;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Dynein axonemal heavy chain 5 {ECO:0000305};
DE AltName: Full=Axonemal beta dynein heavy chain 5;
DE AltName: Full=Ciliary dynein heavy chain 5;
DE Flags: Fragment;
GN Name=Dnah5 {ECO:0000312|RGD:1560828};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION.
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP SUBUNIT, AND INTERACTION WITH DNAL1.
RX PubMed=21496787; DOI=10.1016/j.ajhg.2011.03.018;
RA Mazor M., Alkrinawi S., Chalifa-Caspi V., Manor E., Sheffield V.C.,
RA Aviram M., Parvari R.;
RT "Primary ciliary dyskinesia caused by homozygous mutation in DNAL1,
RT encoding dynein light chain 1.";
RL Am. J. Hum. Genet. 88:599-607(2011).
CC -!- FUNCTION: Force generating protein of respiratory cilia. Produces force
CC towards the minus ends of microtubules. Dynein has ATPase activity; the
CC force-producing power stroke is thought to occur on release of ADP.
CC Required for structural and functional integrity of the cilia of
CC ependymal cells lining the brain ventricles.
CC {ECO:0000250|UniProtKB:Q8TE73}.
CC -!- SUBUNIT: Interacts with DNAL1 (PubMed:21496787). Consists of at least
CC two heavy chains and a number of intermediate and light chains.
CC {ECO:0000250|UniProtKB:Q8TE73, ECO:0000269|PubMed:21496787}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000250|UniProtKB:Q8TE73}.
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. {ECO:0000250|UniProtKB:Q8TE73}.
CC -!- SIMILARITY: Belongs to the dynein heavy chain family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AABR07008948; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AABR07008948; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; M0R8U1; -.
DR IntAct; M0R8U1; 1.
DR MINT; M0R8U1; -.
DR STRING; 10116.ENSRNOP00000065896; -.
DR PaxDb; M0R8U1; -.
DR RGD; 1560828; Dnah5.
DR VEuPathDB; HostDB:ENSRNOG00000048363; -.
DR eggNOG; KOG3595; Eukaryota.
DR HOGENOM; CLU_000038_9_1_1; -.
DR InParanoid; M0R8U1; -.
DR OMA; DRTIAQX; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000048363; Expressed in heart and 3 other tissues.
DR GO; GO:0097729; C:9+2 motile cilium; ISO:RGD.
DR GO; GO:0005858; C:axonemal dynein complex; ISO:RGD.
DR GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0030286; C:dynein complex; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0031514; C:motile cilium; ISS:UniProtKB.
DR GO; GO:0036157; C:outer dynein arm; ISO:RGD.
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; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; ISO:RGD.
DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0060271; P:cilium assembly; ISO:RGD.
DR GO; GO:0003341; P:cilium movement; ISO:RGD.
DR GO; GO:0007368; P:determination of left/right symmetry; ISO:RGD.
DR GO; GO:0003351; P:epithelial cilium movement involved in extracellular fluid movement; ISO:RGD.
DR GO; GO:0051649; P:establishment of localization in cell; ISO:RGD.
DR GO; GO:0030317; P:flagellated sperm motility; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0021670; P:lateral ventricle development; ISO:RGD.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0036158; P:outer dynein arm assembly; ISO:RGD.
DR Gene3D; 1.10.8.710; -; 1.
DR Gene3D; 1.20.140.100; -; 1.
DR Gene3D; 3.20.180.20; -; 1.
DR Gene3D; 3.40.50.300; -; 3.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR035699; AAA_6.
DR InterPro; IPR026983; DHC_fam.
DR InterPro; IPR041589; DNAH3_AAA_lid_1.
DR InterPro; IPR042222; Dynein_2_N.
DR InterPro; IPR043157; Dynein_AAA1S.
DR InterPro; IPR041466; Dynein_AAA5_ext.
DR InterPro; IPR024743; Dynein_HC_stalk.
DR InterPro; IPR024317; Dynein_heavy_chain_D4_dom.
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 Pfam; PF12774; AAA_6; 1.
DR Pfam; PF12780; AAA_8; 1.
DR Pfam; PF17857; AAA_lid_1; 1.
DR Pfam; PF08385; DHC_N1; 1.
DR Pfam; PF08393; DHC_N2; 1.
DR Pfam; PF17852; Dynein_AAA_lid; 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 projection; Cilium; Coiled coil; Cytoplasm; Cytoskeleton;
KW Dynein; Microtubule; Motor protein; Nucleotide-binding; Reference proteome;
KW Repeat.
FT CHAIN 1..3470
FT /note="Dynein axonemal heavy chain 5"
FT /id="PRO_0000441779"
FT REGION 1..1938
FT /note="Stem"
FT /evidence="ECO:0000250"
FT REGION 899..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1939..2161
FT /note="AAA 1"
FT /evidence="ECO:0000250"
FT REGION 2221..2440
FT /note="AAA 2"
FT /evidence="ECO:0000250"
FT REGION 2547..2800
FT /note="AAA 3"
FT /evidence="ECO:0000250"
FT REGION 2913..3167
FT /note="AAA 4"
FT /evidence="ECO:0000250"
FT COILED 3207..3241
FT /evidence="ECO:0000255"
FT COILED 3434..3468
FT /evidence="ECO:0000255"
FT BINDING 1977..1984
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2259..2266
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT NON_TER 3470
SQ SEQUENCE 3470 AA; 395933 MW; BC2B495A5A3F7BC6 CRC64;
MFRIGRRQLW KQSVTRVLTQ RLKEEKEAKR ARLDGRHDYL FAIVASCLDL NKPEVEDALL
EGNQIERIDQ LFAVGGLRHL MFYYQDVEGA EAGQFGSSGG VNPASGKMKK PKVFVTEGKD
VALMGACVFF TRADPSKAIT AENIHREVSF NTLDTADGGL LNSVRRLLSD IFIPALRASS
HGWGELEGLQ DASSIQQEFL SSLEGFVGIL SGAQNSLKEK VNLQKCDIVE LKSLKEPMDY
LALASNPETV EKVECCMRVW IKQMEQILAE NNQLRKEADD VGPRAELEHW KKRLSKFNYL
LDQLKSPDVK AVLAMLAAAK SKLLKVWRDA DIRVTDAANE AKDNVKYLYT LEKCCDPLYS
SDPVTMVDAI PTLINAIKMI YSISHYYNTS ERITSLFVKV TNQMISACKA HITNNGTATI
WSQPQDIVMQ KIAAAIKLKQ GYQCCFQETK QKLKQNPSEK QFDFSEMYIF GKFETFHQRL
AKIMDIFTTF KTYSVLQDSK IEGLEDMVTK YQDVVAGIKK KEYNFLDQRK MDFDQDYDEF
CKQTNELHSE LQRFMDTTFE KIQSTRQALS TLKKFERLNI PNLGIEAKYQ IVFQNFGTDI
DMISKLYTKQ KYDPPLARDQ PPIAGKILWA RQLFHRLEQP MQLFQQHPFV LRTVEAKPVI
RSYNRIAKVL LEFEVLYHRA WLQQIEEIHV GLEASLLVKA PGTGQLFVNF DPQILILFRE
TQCMSQMGLP VSPFAAALFE KRDMYKKNFS DMKMMLSEYQ RVKLKMPPAI EQLMLPHLAR
VDEALQPGLA VLTWTSLNIG TYLENAFEKI KDLELLLDRI NDLIEFRIHA ILEEMSSVAL
CQLPQDDPLT CEEFLQMTKD LCVNGAQKLH FKSSLVEEAV NELINMLLDV DVLPEEASEK
VRHENASPNG DTSGGGEGCA EALASSFNAG TSSLPLTTIA RKKKEMEVLE EARELLSYFN
HQNTDALLKV TRNTLEAIRR RIHFSHMINF RDSKGASKVK QNHLPIFRAS VTLAIPNISM
TPALEDIQQT LNKAVECIIS VPKGVRQWSS ELLSKRKMRE RKMAAVQSNE DSDSDTEVEE
SELQETLELA SVNLPIPVQT QNYYKNISDN KEIVKLVSVL STVISSTKKE VITSMDRFKC
YNHIWQKEKE DTIMTFIAQN PLLSEFESRI LYFQSLEQEI NAEPEYICVG SIALYTADLK
FSLTAETKAW MMVLGRHCNR KYRSEMENIF TVVEEFQKKL NRPIKDLDDI RIAMAALKEI
REQQISTDFQ VGPIEESYAL LNKYGLLVAK EEMDKVDTLR YAWEKLLARA SDVQNELGAL
QPSFRKELIS TVEVFLQDCQ QFYLDYDLNG PMVSGLKPQE ASDRLIIFQN QFDNIYRKYI
TYTGGEELFG LPVTQYPQLL EIKKQLNLLQ KIYSLYNNVI ETVNSYQDTL WSEVNIEKIN
SELLEFQNRC RKLPRALKDW QAFLDMKKTI DDFSECCPLL EYMASNAMVE RHWQRITTLT
GHSLDVGNET FKLRNIMEVP LLKYKEEIED ICISAVKERD IEQKLKQVIN EWDNKTLTFS
SFKTRGELLL RGDSTSEVIA SMEDSLMLLG SLLSNRYNMP FKAQIQNWVQ CLSNSTDIIE
NWMTVQNLWI YLEAVFVGGD IAKQLPKEAK RFSNIDKSWV KIMTRAHEIP NVVQCCVGDE
TMGQLLPHLL DQLEICQKSL TGYLEKKRLC FPRFFFVSDP ALLEILGQAS DSHTIQAHLL
NVFDNIKTVK FHDKIYDRIL SISSREGETI ELDKPVMAEG NVEVWLNSLL EESQSSLHLV
IRQAAANIQE SGFQLIEFLS SFPAQVGLLG IQMLWTRDSE EALQNAKFDK KIMQKTNQSF
LELLNMLIEM TTKDLSSMER VKYETLITIH VHQRDIFDDL CHMHVKSPTD FEWLKQCRFY
FKEDSDKTMI HITDVAFTYQ NEFLGCTDRL VITPLTDRCY ITLAQALGMS MGGAPAGPAG
TGKTETTKDM GRCLGKYVVV FNCSDQMDFR GLGRIFKGLA QSGSWGCFDE FNRIDLPVLS
VAAQQISIIL TCKKEHKKSF IFTDGDNVTM NPEFGLFLTM NPGYAGRQEL PENLKINFRS
VAMMVPDRQI IIRVKLASCG FIDNVVLARK FFTLYQLCEE QLSKQVHYDF GLRNILSVLR
TLGAAKRASH TDTESTIVMR VLRDMNLSKL IDEDEPLFLS LIEDLFPNIL LDKAGYPELE
TAISKQVEEA GLINHPPWKL KVIQLFETQR VRHGMMTLGP SGSGKTSCIH TLMKAMTDCG
KPHREMRMNP KAITAPQMFG RLDVATNDWT DGIFSTLWRK TLKAKKGEHI WIVLDGPVDA
IWIENLNSVL DDNKTLTLAN GDRIPMAPNC KIVFEPHNID NASPATVSRN GMVFMSSSVL
DWSPILEGFL KRRSPQEAEI LRQLYAETFP DLYRFSIQNL EFKMEILEAF VITQSTHMLQ
GLIPTKEQAG DVDPEHLGRL FVFAMMWSVG AVLELEGRRR MELWLRSREG PTLHLPQLTD
PGDTMFDYYV APDGTWRHWS MCIPEYVYPP DTTPEYGSIL VPNVDNVRTD FLIKTIAKQG
KAVLLIGEQG TAKTVIIKGF MSKFDPESHT VKNLNFSSAT TPLMFQRTIE SYVDKRMGTT
YGPPAGKKMA VFIDDLNMPV INEWGDQVTN EIVRQLMEQN GFYNLEKPGE FTSIVDIQFL
AAMIHPGGGR NDIPQRLKRQ FSIFNCTLPS DASMDKIFGV IGEGYYCAQR GFSKEVQDAV
IKLVPLTRRL WQMTKLKMLP TPAKFHYVFN LRDLSRIWQG MLNITSEVIK DTDELLRLWK
HECKRVIADR FSMSSDVTWF DKAVVSLVEE EFGEEKTPVV DCGVDAYFVD FLRDAPEATG
ETPEETDAEM PKLYEPIASL NHLQERLSVF LQLYNESIRG TGMDMVFFRD AMVHLVKISR
VIRTPRGNAL LVGVGGSGKQ SLTRLASFIA GYTSFQITLT RSYNTSNLME DLKVLYRTAG
QQGKGITFIF TDNEIKEESF LEYMNNVLSS GEVSNLFARD EIDEINSDLT SIMKKEHPKR
PPTNDNLYEY FMSRVRGNLH IVLCFSPVGE KFRNRALKFP ALISGCTIDW FSRWPKDALV
AVSEHFLSSY NIDCTAEIKK ELVQCMGSFQ DGVAEKCADY FQRFRRSTHV TPKSYLSFIQ
GYKFIYEEKH VEVQSLANRM NTGLEKLKEA SESVAALSQE LAVKEKELQV ANEKADMVLK
EVTMKAQAAE KVKAEVQKVK DKAQAIVDSI SKDKAIAEEK LEAAKPALEE AEAALQTIKP
SDIATVRTLG RPPHLIMRIM DCVLLLFHRR VNAVKIDLDK SCTVPSWQES LKLMTAGNFL
QNLQQFPKDT INEEVIEFLS PYFEMSDYNI ETAKRVCGNV AGLCSWTKAM ASFFSINKEV
LPLKANLIVQ ENRHALAMQD LQKAQAELDD KQAELDVVQA EYEQAMTEKQ