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Protein

Dynein heavy chain 5, axonemal

Gene

Dnah5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Required for structural and functional integrity of the cilia of ependymal cells lining the brain ventricles.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1977 – 19848ATPSequence analysis
Nucleotide bindingi2259 – 22668ATPSequence analysis

GO - Molecular functioni

  • ATPase activity Source: InterPro
  • ATP binding Source: UniProtKB-KW
  • microtubule motor activity Source: MGI

GO - Biological processi

  • cilium assembly Source: MGI
  • cilium movement Source: MGI
  • determination of left/right symmetry Source: MGI
  • heart development Source: MGI
  • lateral ventricle development Source: MGI
  • outer dynein arm assembly Source: MGI
  • sperm motility Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Dynein heavy chain 5, axonemal
Alternative name(s):
Axonemal beta dynein heavy chain 5
Short name:
mDNAH5
Ciliary dynein heavy chain 5
Gene namesi
Name:Dnah5
Synonyms:Dnahc5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:107718. Dnah5.

Subcellular locationi

GO - Cellular componenti

  • axonemal dynein complex Source: MGI
  • axoneme Source: MGI
  • cytoplasm Source: UniProtKB-KW
  • microtubule Source: UniProtKB-KW
  • outer dynein arm Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasm, Cytoskeleton, Dynein, Microtubule

Pathology & Biotechi

Involvement in diseasei

Defects in Dnah5 are the cause of primary ciliary dyskinesia (PCD). PCD is characterized by recurrent respiratory infections, situs inversus and ciliary immotility and hydrocephalus.

Disruption phenotypei

Mice display defects in motility of the ependymal cells lining the brain ventricles and aqueduct. This results in impaired flow of cerebrospinal fluid through the cerebral aqueduct and gives rise to closure of the aqueduct and subsequent formation of triventricular hydrocephalus during early postnatal brain development.1 Publication

Keywords - Diseasei

Ciliopathy, Primary ciliary dyskinesia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 46214621Dynein heavy chain 5, axonemalPRO_0000114631Add
BLAST

Proteomic databases

EPDiQ8VHE6.
MaxQBiQ8VHE6.
PaxDbiQ8VHE6.
PeptideAtlasiQ8VHE6.
PRIDEiQ8VHE6.

PTM databases

iPTMnetiQ8VHE6.
PhosphoSiteiQ8VHE6.

Expressioni

Tissue specificityi

Strongly expressed in lung and kidney and weaker expression seen in brain, heart and testis. In the brain, expressed in ependymal cells lining the brain ventricles and the aqueduct.2 Publications

Developmental stagei

Embryos show a weak expression confined to the node from 7.0 to 8.25 dpc.1 Publication

Gene expression databases

BgeeiQ8VHE6.
CleanExiMM_DNAHC5.
GenevisibleiQ8VHE6. MM.

Interactioni

Subunit structurei

Consists of at least two heavy chains and a number of intermediate and light chains.

Protein-protein interaction databases

IntActiQ8VHE6. 2 interactions.
MINTiMINT-4093714.
STRINGi10090.ENSMUSP00000069751.

Structurei

3D structure databases

ProteinModelPortaliQ8VHE6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 19381938StemBy similarityAdd
BLAST
Regioni1939 – 2161223AAA 1By similarityAdd
BLAST
Regioni2221 – 2440220AAA 2By similarityAdd
BLAST
Regioni2547 – 2800254AAA 3By similarityAdd
BLAST
Regioni2913 – 3167255AAA 4By similarityAdd
BLAST
Regioni3182 – 3479298StalkBy similarityAdd
BLAST
Regioni3564 – 3794231AAA 5By similarityAdd
BLAST
Regioni4009 – 4223215AAA 6By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili260 – 30546Sequence analysisAdd
BLAST
Coiled coili803 – 82523Sequence analysisAdd
BLAST
Coiled coili1065 – 109430Sequence analysisAdd
BLAST
Coiled coili1433 – 146230Sequence analysisAdd
BLAST
Coiled coili3186 – 3299114Sequence analysisAdd
BLAST
Coiled coili3423 – 349068Sequence analysisAdd
BLAST
Coiled coili3729 – 381486Sequence analysisAdd
BLAST
Coiled coili4389 – 441729Sequence analysisAdd
BLAST

Domaini

Dynein heavy chains probably consist of an N-terminal stem (which binds cargo and interacts with other dynein components), and the head or motor domain. The motor contains six tandemly-linked AAA domains in the head, which form a ring. A stalk-like structure (formed by two of the coiled coil domains) protrudes between AAA 4 and AAA 5 and terminates in a microtubule-binding site. A seventh domain may also contribute to this ring; it is not clear whether the N-terminus or the C-terminus forms this extra domain. There are four well-conserved and two non-conserved ATPase sites, one per AAA domain. Probably only one of these (within AAA 1) actually hydrolyzes ATP, the others may serve a regulatory function.

Sequence similaritiesi

Belongs to the dynein heavy chain family.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG3595. Eukaryota.
COG5245. LUCA.
GeneTreeiENSGT00760000118964.
HOGENOMiHOG000257779.
HOVERGENiHBG005543.
InParanoidiQ8VHE6.
KOiK10408.
OMAiARVHDIY.
OrthoDBiEOG73BVBP.
TreeFamiTF316836.

Family and domain databases

Gene3Di3.40.50.300. 5 hits.
InterProiIPR003593. AAA+_ATPase.
IPR011704. ATPase_dyneun-rel_AAA.
IPR026983. DHC_fam.
IPR024743. Dynein_HC_stalk.
IPR024317. Dynein_heavy_chain_D4_dom.
IPR004273. Dynein_heavy_dom.
IPR013594. Dynein_heavy_dom-1.
IPR013602. Dynein_heavy_dom-2.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10676. PTHR10676. 3 hits.
PfamiPF07728. AAA_5. 1 hit.
PF12780. AAA_8. 1 hit.
PF08385. DHC_N1. 1 hit.
PF08393. DHC_N2. 1 hit.
PF03028. Dynein_heavy. 1 hit.
PF12777. MT. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 3 hits.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 5 hits.

Sequencei

Sequence statusi: Complete.

Q8VHE6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFRIGRRQLW KQSVTRVLTQ RLKEEKEAKR ARLDGRHDYL FAIVASCLDL
60 70 80 90 100
NKPEVEDALL EGNQIERMDQ LFAVGGLRHL MFYYQDVEGA EAGHCGSSGG
110 120 130 140 150
VNPASGKMKK PKVFVTEGKD VALMGACVFF IRSDPSKAIT PENIHREVSF
160 170 180 190 200
NTLDTADGGL LNSVRRLLSD IFIPALRASS HGWGELEGLQ DASSIRQEFL
210 220 230 240 250
SSLEGFVGIL SGAQNSLKEK VNLQKCDIIE LKSLKEPTDY LALASNPETV
260 270 280 290 300
EKVECCMRVW IKQMEQILAE NSQLRKEADD VGPRAELEHW KQRLSRFNYL
310 320 330 340 350
LDQLKSPDVK AALALLAAAK SKLLKVWRDT DIRITDAANE AKDNVKYLYT
360 370 380 390 400
LEKCCDPLYS SDPVTMIDAI PTLINAIKMV YSISHYYNTS EKITSLFVKV
410 420 430 440 450
TNQMISACKA HITNNGTATI WSQPQEIVMQ KIAAVIKLKQ GYQSCFQETK
460 470 480 490 500
QKLKQNPSEK QFDFSEMYIF GKFETFHRRL AKIMDIFTTF KTYSVLQDSK
510 520 530 540 550
IEGLEDMATK YQDIVAAIKK KEYNFLDQRE MDFDQDYEEF CKRINELHND
560 570 580 590 600
LQRFMDITFE KIPSTRQALS TLKKFERLNI PNLGIEEKYQ IIFQNFATDI
610 620 630 640 650
DTISKLYTKQ KYDPPLARNQ PPIAGKILWA RQLFHRLEQP MQLFQQHPFV
660 670 680 690 700
LRTAEAKPVI RSYNRIAKVL LEFEVLYHRA WLQQIEEIHA GLEASLLVKA
710 720 730 740 750
PGTGELFVNF DPQILVLFRE TQCMSQLGLP VSPFAAALFQ KRDMFKKNFS
760 770 780 790 800
DMKMMLSEYE RVKLKMPPAI EQLMFPHLAR VDEALQPGLA VLTWTSLNIG
810 820 830 840 850
GYLENAFAKI KDLELLLDRV NDLIEFRIHA ILEEMSSMAL CQLPQDDPLT
860 870 880 890 900
CEEFLQMTKD LCVSGAQLLH FKSSLVEEAV NELINMLLDV DVPPEEAAEN
910 920 930 940 950
VCHENASPSG NTSGRREGHS EALASSFNAG ASSLPLTATA RKKKETEVLE
960 970 980 990 1000
EARELLSHFN HQNTDALLKV TRNTLEAIRR RIHFSHMINF RDSNDASKAK
1010 1020 1030 1040 1050
QNHLPIFRAS VTLAIPNIAM TPALEDIQQT LNKAVECIIS VPKGVRQWSS
1060 1070 1080 1090 1100
ELLSKRKMHE RKMAAVKNNE DSDSDAEVEE NELQETLEIA SINLPIPVQT
1110 1120 1130 1140 1150
QNYYKNISDN KEIVKLVSVL STVISSTKKE VITSMDRFKR YNHIWQKEKE
1160 1170 1180 1190 1200
DTIMTFIAQN PLLPEFESRI LYFQSLEQEI NAEPEYIRVG SIALYTADLK
1210 1220 1230 1240 1250
LSLTAETKAW MAVIGRHCNR KYRAEMENIL TVVEESQKKL SRPIKDLDDI
1260 1270 1280 1290 1300
RIAMAALKEI REQQISTDFQ VGPIEESYAL LNKYGLLVAK EEMDKVDTLR
1310 1320 1330 1340 1350
YAWEKLLARA SDVQNELGAL QPSFRKELIS TVEVFLQDCQ QFYLDYDLNG
1360 1370 1380 1390 1400
PMASGLKPQE ASGRLIIFQN QFDNIYRKYI TYTGGEELFG LPVTPYPQLL
1410 1420 1430 1440 1450
EIKRQLNLLQ KIYSLYNNVI ETVNSYQDTL WSDVNIEKIN NELLEFQNRC
1460 1470 1480 1490 1500
RKLPRALKDW QAFLDLKKTI DDFSECCPLL EYMASNAMVE RHWQRITALT
1510 1520 1530 1540 1550
GHSLDVGNET FKLRNIMEAP LLKYKEEIED ICISAVKERD IEQKLRQVIN
1560 1570 1580 1590 1600
EWDNKTLTFS GFKTRGELLL RGDSTSEVIA SMEDSLMLLG SLLSNRYNMP
1610 1620 1630 1640 1650
FKAQIQKWVQ CLSNSTDIIE NWMTVQNLWI YLEAVFVGGD IAKQLPKEAK
1660 1670 1680 1690 1700
RFSNIDKSWV KIMTRAHEIP NVVQCCVGDE TMGQLLPHLL DQLEICQKSL
1710 1720 1730 1740 1750
TGYLEKKRLC FPRFFFVSDP ALLEILGQAS DSHTIQAHLL NVFDNIKTVK
1760 1770 1780 1790 1800
FHDKIYDRIL SISSREGETI ELDKPVMAEG NVEVWLNSLL EESQSSLHLV
1810 1820 1830 1840 1850
IRQAAANIQE PGFQLIEFLS SFPAQVGLLG IQMLWTRDSE EALRNAKFDK
1860 1870 1880 1890 1900
KIMQKTNQAF LELLNMLIEI TTKDLSSMER VKYETLITIH VHQRDIFDDL
1910 1920 1930 1940 1950
CHMHVKSPTD FEWLKQCRFY FKEDSDKTMI HITDVAFIYQ NEFLGCTDRL
1960 1970 1980 1990 2000
VITPLTDRCY ITLAQALGMS MGGAPAGPAG TGKTETTKDM GRCLGKYVVV
2010 2020 2030 2040 2050
FNCSDQMDFR GLGRIFKGLA QSGSWGCFDE FNRIDLPVLS VAAQQISIIL
2060 2070 2080 2090 2100
TCKKEHKKSF IFTDGDNVTM NPEFGLFLTM NPGYAGRQEL PENLKINFRS
2110 2120 2130 2140 2150
VAMMVPDRQI IIRVKLASCG FIDNVVLARK FFTLYQLCEE QLSKQVHYDF
2160 2170 2180 2190 2200
GLRNILSVLR TLGAAKRASP TDTESTIVMR VLRDMNLSKL IDEDEPLFLS
2210 2220 2230 2240 2250
LIEDLFPNIL LDKAGYPELE TAISKQVEEA GLINHPPWKL KVIQLFETQR
2260 2270 2280 2290 2300
VRHGMMTLGP SGSGKTTCIH TLMKAMTDCG KPHREMRMNP KAITAPQMFG
2310 2320 2330 2340 2350
RLDVATNDWT DGIFSTLWRK TLKAKKGEHI WIVLDGPVDA IWIENLNSVL
2360 2370 2380 2390 2400
DDNKTLTLAN GDRIPMAPNC KIVFEPHNID NASPATVSRN GMVFMSSSVL
2410 2420 2430 2440 2450
DWSPILEGFL KRRSPQEAEI LRQLYAETFP DLYRFSIQNL EFKMEVLEAF
2460 2470 2480 2490 2500
VITQSTHMLQ GLIPPKEQAG EVDPEHLGRL FVFAMMWSVG AVLELEGRRR
2510 2520 2530 2540 2550
MELWLRSREG PTLHLPQLTD AGDTMFDYYV APNGTWRHWS LCTPEYVYPP
2560 2570 2580 2590 2600
DTTPEYGSIL VPNVDNVRTD FLIKTIAKQG KAVLLIGEQG TAKTVIIKGF
2610 2620 2630 2640 2650
MSKFDPESHM VKNLNFSSAT TPVMFQRTIE SYVDKRMGTT YGPPAGKKMA
2660 2670 2680 2690 2700
VFIDDLNMPV INEWGDQVTN EIVRQLMEQS GFYNLEKPGE FTSIVDIQFL
2710 2720 2730 2740 2750
AAMIHPGGGR NDIPQRLKRQ FSIFNCTLPS DASMDKIFGV IGAGYYCAQR
2760 2770 2780 2790 2800
GFSEEVQDAL IKLVPLTRRL WQMTKLKMLP TPAKFHYVFN LRDLSRIWQG
2810 2820 2830 2840 2850
MLNITSEVIK DTDELLRLWK HECKRVIADR FSMSSDVTWF DKAVVSLVEE
2860 2870 2880 2890 2900
EFGEEKAPVV DCGVDAYFVD FLRDAPEATG ETPEEADAEM PKLYEPIASL
2910 2920 2930 2940 2950
NHLRERLSVF LQLYNESIRG TGMDMVFFID AMVHLVKISR VIRTPRGNAL
2960 2970 2980 2990 3000
LVGVGGSGKQ SLTRLASFIA GYTSFQITLT RSYNTSNLME DLKVLYRTAG
3010 3020 3030 3040 3050
QQGKGITFIF TDNEIKEESF LEYMNNVLSS GEVSNLFARD EIDEINSDLT
3060 3070 3080 3090 3100
PIMKKEHPRR PPTNDNLYEY FMSRVRGNLH IVLCFSPVGE KFRNRALKFP
3110 3120 3130 3140 3150
ALISGCTIDW FSRWPKDALV AVSEHFLSSY TIDCTAEIKK ELVQCMGSFQ
3160 3170 3180 3190 3200
DGVAEKCADY FQRFRRSTHV TPKSYLSFIQ GYKFIYEEKH MEVQSLANRM
3210 3220 3230 3240 3250
NTGLEKLKEA SESVAALSKE LAGKEKELQV ANEKADTVLK EVTMKAQAAE
3260 3270 3280 3290 3300
KVKAEVQKVK DKAQAIVDSI SKDKAIAEEK LEAAKPALEE AEAALQTIKP
3310 3320 3330 3340 3350
SDIATVRTLG RPPHLIMRIM DCVLLLFQRR VNAVKIDVDK GCTMPSWQES
3360 3370 3380 3390 3400
LKLMTAGNFL QNLQQFPKDT INEEVIEFLN PYFEMSDYNI ETAKRVCGNV
3410 3420 3430 3440 3450
AGLCSWTKAM ASFFSINKEV LPLKANLIVQ ENRHILAMQD LQKAQAELDA
3460 3470 3480 3490 3500
KQAELDVVQA EYEQAMAEKQ TLLEDADRCR HKMQTASTLI SGLAGEKERW
3510 3520 3530 3540 3550
TEQSKEFAAQ TKRLVGDVLL ATAFLSYSGP FNQEFRDLLL HDWKKEMKAR
3560 3570 3580 3590 3600
KIPFGNGLNL NEMLIDAPTI SEWNLQGLPN DDLSIQNGII VTKASRYPLL
3610 3620 3630 3640 3650
IDPQTQGKIW IKNKESQNEL QITSLNHKYF RNHLEDSLSL GRPLLIEDVG
3660 3670 3680 3690 3700
EELDPALDNV LEKNFIKTGS TFKVKVGDKE VDVMDGFKLY ITTKLPNPAY
3710 3720 3730 3740 3750
TPEISARTSI IDFTVTVKGL EDQLLGRVIL TEKQELEKER THLLEDVTAN
3760 3770 3780 3790 3800
KRRMKELEDN LLYRLTSTQG SLVEDESLII VLSNTKKTAE EVTQKLEISG
3810 3820 3830 3840 3850
ETEIQINSAR EEYRPVATRG SILYFLITEM RLVNEMYQTS LRQFLGLFDL
3860 3870 3880 3890 3900
SLARSVKSPI TSKRIANIIE HMTYEVFKYA ARGLYEEHKF LFTLLLTLKI
3910 3920 3930 3940 3950
DIQRNLVKHE EFLTLIKGGA SLDLKACPPK PSKWILDMTW LNLVELSKLK
3960 3970 3980 3990 4000
QFSDILDQIS RNEKMWRVWF DKENPEEEPL PNAYDKSLDC FRRLLLIRSW
4010 4020 4030 4040 4050
CPDRTIAQAR KYIMDSMGEN YAEGVILDLE KTWEESDPRT PLICLLSMGS
4060 4070 4080 4090 4100
DPTDSIIALG KRLKIETRYV SMGQGQEVHA RKLLHQTMAN GGWVLLQNCH
4110 4120 4130 4140 4150
LGLDFLDELM DVVTETETVH DTFRLWITTE VHKQFPITLL QMSIKFANEP
4160 4170 4180 4190 4200
PQGLRAGLRR TYGGVSQDLL DVSVGAQWKP MLYAVAFLHS TVQERRKFGP
4210 4220 4230 4240 4250
LGWNIPYEFN QADFNATVQF IQNHLDDMDV KKGVSWTTVR YMIGEIQYGG
4260 4270 4280 4290 4300
RVTDDYDKRL LNTFAKVWFS ENMFGPDFTF YQGYNIPKCS TVDGYLQYIQ
4310 4320 4330 4340 4350
SLPAYDSPEV FGLHPNADIT YQSKLAKDVL DTILGIQPKD SSGGGDETRE
4360 4370 4380 4390 4400
AVVARLADDM LEKLPEDYSP FEVKERLQKM GPFQPMNIFL RQEIDRMQRV
4410 4420 4430 4440 4450
LSLVRSTLTE LKLAVDGTII MSENLRDALD CMFDARIPAR WKKASWVSST
4460 4470 4480 4490 4500
LGFWFTELLE RNCQFTSWVS NGRPHCFWMT GFFNPQGFLT AMRQEITRAN
4510 4520 4530 4540 4550
KGWALDNMVL CNEVTKFMKD DISAPPTEGV YVYGLYLEGA GWDKRNMKLI
4560 4570 4580 4590 4600
ESKPKVLFEL MPVIRIFAEN NTARDPRLYC CPIYKKPVRT DLNYIAAVDL
4610 4620
KTAQAPEHWV LRGVALLCDV K
Length:4,621
Mass (Da):527,558
Last modified:July 27, 2011 - v2
Checksum:iCC6F243FF149B214
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti892 – 8921V → A in AAL69993 (PubMed:11912187).Curated
Sequence conflicti898 – 8981A → S in AAL69993 (PubMed:11912187).Curated
Sequence conflicti3854 – 38585RSVKS → SLSRA in AAL69993 (PubMed:11912187).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF466704 mRNA. Translation: AAL69993.1.
AC131997 Genomic DNA. No translation available.
AC154880 Genomic DNA. No translation available.
AK052643 mRNA. Translation: BAC35077.2.
CCDSiCCDS27404.1.
RefSeqiNP_579943.3. NM_133365.3.
UniGeneiMm.248464.

Genome annotation databases

EnsembliENSMUST00000067048; ENSMUSP00000069751; ENSMUSG00000022262.
GeneIDi110082.
KEGGimmu:110082.
UCSCiuc007vjy.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF466704 mRNA. Translation: AAL69993.1.
AC131997 Genomic DNA. No translation available.
AC154880 Genomic DNA. No translation available.
AK052643 mRNA. Translation: BAC35077.2.
CCDSiCCDS27404.1.
RefSeqiNP_579943.3. NM_133365.3.
UniGeneiMm.248464.

3D structure databases

ProteinModelPortaliQ8VHE6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8VHE6. 2 interactions.
MINTiMINT-4093714.
STRINGi10090.ENSMUSP00000069751.

PTM databases

iPTMnetiQ8VHE6.
PhosphoSiteiQ8VHE6.

Proteomic databases

EPDiQ8VHE6.
MaxQBiQ8VHE6.
PaxDbiQ8VHE6.
PeptideAtlasiQ8VHE6.
PRIDEiQ8VHE6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000067048; ENSMUSP00000069751; ENSMUSG00000022262.
GeneIDi110082.
KEGGimmu:110082.
UCSCiuc007vjy.1. mouse.

Organism-specific databases

CTDi1767.
MGIiMGI:107718. Dnah5.

Phylogenomic databases

eggNOGiKOG3595. Eukaryota.
COG5245. LUCA.
GeneTreeiENSGT00760000118964.
HOGENOMiHOG000257779.
HOVERGENiHBG005543.
InParanoidiQ8VHE6.
KOiK10408.
OMAiARVHDIY.
OrthoDBiEOG73BVBP.
TreeFamiTF316836.

Miscellaneous databases

PROiQ8VHE6.
SOURCEiSearch...

Gene expression databases

BgeeiQ8VHE6.
CleanExiMM_DNAHC5.
GenevisibleiQ8VHE6. MM.

Family and domain databases

Gene3Di3.40.50.300. 5 hits.
InterProiIPR003593. AAA+_ATPase.
IPR011704. ATPase_dyneun-rel_AAA.
IPR026983. DHC_fam.
IPR024743. Dynein_HC_stalk.
IPR024317. Dynein_heavy_chain_D4_dom.
IPR004273. Dynein_heavy_dom.
IPR013594. Dynein_heavy_dom-1.
IPR013602. Dynein_heavy_dom-2.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10676. PTHR10676. 3 hits.
PfamiPF07728. AAA_5. 1 hit.
PF12780. AAA_8. 1 hit.
PF08385. DHC_N1. 1 hit.
PF08393. DHC_N2. 1 hit.
PF03028. Dynein_heavy. 1 hit.
PF12777. MT. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 3 hits.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 5 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Loss of function of axonemal dynein Mdnah5 causes primary ciliary dyskinesia and hydrocephalus."
    Ibanez-Tallon I., Gorokhova S., Heintz N.
    Hum. Mol. Genet. 11:715-721(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DISEASE.
    Strain: C57BL/6J X CBA/J.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2481-3749.
    Strain: C57BL/6J.
    Tissue: Kidney.
  4. Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  5. "Dysfunction of axonemal dynein heavy chain Mdnah5 inhibits ependymal flow and reveals a novel mechanism for hydrocephalus formation."
    Ibanez-Tallon I., Pagenstecher A., Fliegauf M., Olbrich H., Kispert A., Ketelsen U.-P., North A., Heintz N., Omran H.
    Hum. Mol. Genet. 13:2133-2141(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Lung.

Entry informationi

Entry nameiDYH5_MOUSE
AccessioniPrimary (citable) accession number: Q8VHE6
Secondary accession number(s): E9QKD7, Q8BWG1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: July 27, 2011
Last modified: July 6, 2016
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.