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Q9SMH3

- DYH1A_CHLRE

UniProt

Q9SMH3 - DYH1A_CHLRE

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Protein

Dynein-1-alpha heavy chain, flagellar inner arm I1 complex

Gene

DHC1

Organism
Chlamydomonas reinhardtii (Chlamydomonas smithii)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Force generating protein of eukaryotic cilia and flagella. 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 assembly of the I1 inner arm complex and its targeting to the appropriate axoneme location. Also required for phototaxis.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi960 – 9678ATPSequence Analysis
Nucleotide bindingi1958 – 19658ATPSequence Analysis
Nucleotide bindingi2242 – 22498ATPSequence Analysis
Nucleotide bindingi2588 – 25958ATPSequence Analysis
Nucleotide bindingi2945 – 29528ATPSequence Analysis
Nucleotide bindingi3680 – 36878ATPSequence Analysis

GO - Molecular functioni

  1. ATPase activity Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. microtubule motor activity Source: InterPro

GO - Biological processi

  1. cell projection organization Source: UniProtKB-KW
  2. microtubule-based movement Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Keywords - Biological processi

Cilium biogenesis/degradation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Dynein-1-alpha heavy chain, flagellar inner arm I1 complex
Alternative name(s):
1-alpha DHC
Dynein-1, subspecies f
Gene namesi
Name:DHC1
Synonyms:IDA1, PF9
OrganismiChlamydomonas reinhardtii (Chlamydomonas smithii)
Taxonomic identifieri3055 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeChlorophytaChlorophyceaeChlamydomonadalesChlamydomonadaceaeChlamydomonas

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. dynein complex Source: UniProtKB-KW
  3. microtubule Source: UniProtKB-KW
  4. motile cilium Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Disruption phenotypei

Cells swim slowly with near normal beat frequencies but aberrant waveforms, and are unable to phototax.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 46254625Dynein-1-alpha heavy chain, flagellar inner arm I1 complexPRO_0000114646Add
BLAST

Proteomic databases

PRIDEiQ9SMH3.

Expressioni

Inductioni

By deflagellation.

Interactioni

Subunit structurei

The I1 inner arm complex (also known as the f dynein complex) is a two-headed isoform composed of two heavy chains (1-alpha and 1-beta), three intermediate chains and three light chains. I1 occupies a specific position proximal to the first radial spoke and repeats every 96 nm along the length of the axoneme.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ9SMH3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 19191919StemBy similarityAdd
BLAST
Regioni1920 – 2141222AAA 1By similarityAdd
BLAST
Regioni2201 – 2437237AAA 2By similarityAdd
BLAST
Regioni2550 – 2800251AAA 3By similarityAdd
BLAST
Regioni2906 – 3155250AAA 4By similarityAdd
BLAST
Regioni3192 – 3494303StalkBy similarityAdd
BLAST
Regioni3542 – 3773232AAA 5By similarityAdd
BLAST
Regioni3998 – 4216219AAA 6By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1227 – 125933Sequence AnalysisAdd
BLAST
Coiled coili1339 – 140971Sequence AnalysisAdd
BLAST
Coiled coili3192 – 3297106Sequence AnalysisAdd
BLAST
Coiled coili3400 – 349495Sequence AnalysisAdd
BLAST
Coiled coili3701 – 378888Sequence 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.
A construct expressing the first 1249 amino acids but lacking the motor domain is able to assemble I1 complexes and target them to their correct location on the axoneme, although motility is not normal. Phototaxis is also restored.

Sequence similaritiesi

Belongs to the dynein heavy chain family.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiCOG5245.

Family and domain databases

Gene3Di3.40.50.300. 4 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. 1 hit.
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. 4 hits.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 6 hits.

Sequencei

Sequence statusi: Complete.

Q9SMH3-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MDRRLEWVKE KACLGLGVEP NLFEAAIANP ESRARVTAFL DGTVTSSALL
60 70 80 90 100
FALEEATIYV EEYQEVLAEE QAPEAEDGEG EEHDGQEPGE AGGEGAEGST
110 120 130 140 150
APGDSGDGQP EDAPAAAAEA NGANPEDEAA APADGAADGA AGEGGEEGDG
160 170 180 190 200
AEGDEPPAPP APKYVRRVIS VPKVVSKLNV ALGSLPEELS VFPVFYFILN
210 220 230 240 250
RSGHVAAEEL DSAVEFGLLS EGPSLRILEQ MLSSVFVPIL VQMSGGDVAS
260 270 280 290 300
GGVLMQSMTD NSHRELLGNM QKFHSQVTQA LQQLTGDVTL QLPDFPLEDM
310 320 330 340 350
DRAAADTDLV MQLEQYMAEW SQVLASVLQR ESQKHPTGKG PLAEIEFWRE
360 370 380 390 400
RNAVLSSLYE QLNLPQVKRM ILVVEKGSDD RNLMAGFKSQ LGELTKLATE
410 420 430 440 450
ARDNVKFLTT LERHFKNIAT GPLGGILDTL PPMMNALRMV WIISRHYSDD
460 470 480 490 500
QRMGSLFQRI AREIGDRVEA AVDLRHIFRM TSADAVELLK VCKSVLEHWL
510 520 530 540 550
QTYMAMREKI ELSGRDARWE FPKQLLFART NYMAEICTDL IEMVEIVDDF
560 570 580 590 600
FRFLGPELKT VTGDTAGIDR VVHRVVAMYE PIESISFNVF DYGNQHEWKA
610 620 630 640 650
AKQQFYADNE DIKEATRELI DTSFRKLRSA EGACELLQSF KSIKSKGAIQ
660 670 680 690 700
KQVMNKFNDI LEQFAREIEQ TADIFERNKD APPVTKNQPP VAGAIKWVRS
710 720 730 740 750
LLERLKRTMA KLLSTEEEII RTTELGQAVE SKFKSFARSV MLTEKKWFSS
760 770 780 790 800
WSDSINGVAM QHLKQTIFRR SAATNRVEVN FHPDLVRLIR ETRYLDRMGF
810 820 830 840 850
PIPEIALNVA LQEDKFLQWL EGLNSMLFKY YESIDQLTPV ERELMERKLE
860 870 880 890 900
ELESCLQPGF TILNWNSLGI TEFIGTCDKA IATFQQLVKQ VQKNSGIIEQ
910 920 930 940 950
VVYAIAGAQL VTEPEEGAEV MDLQEFYEDI ERQRLAALES LVKKYRTISP
960 970 980 990 1000
LLGKIEEVVA GTNSGKSPAL SSYYSFWERA IFNALNTMVL CAMTKLQDMI
1010 1020 1030 1040 1050
EQRSKHAEGG RKPPLFKVTV SLQSVDVVVQ PPMTEVNKAL GRLVRSLVES
1060 1070 1080 1090 1100
TKAFVRWMDG TCVETPEQRG ATDDDEPIVF TFYWDVAANP QVIKTMLNLN
1110 1120 1130 1140 1150
QSIQRAITSV NKYAESWRRH QALWKTDKNS VLDKFKARDP SAAQFEDKLS
1160 1170 1180 1190 1200
KYAKMATEIS AQAKDFDQDF IRVSCHALAS SVCDEAQAWV RAIAQTMREL
1210 1220 1230 1240 1250
DAVTESQLRD KIAKYQTALH RPPDTLEELK QVLNTVNTIR GESMVMELRY
1260 1270 1280 1290 1300
ADLEERYRTR LLYATNPEEE SQCAHELASA SQVRALWTEL LNEAEAVDWS
1310 1320 1330 1340 1350
LEETKKKFSE TTRSQVSDFA AITAELWEKF RTTGPGLPTV ELASGLDELH
1360 1370 1380 1390 1400
KYESNLADAL RQREQLVLAE KLFGMEITAY PELAQLESEI RKLAQVYGVY
1410 1420 1430 1440 1450
AEHAEAVRQY GGQLWSELDV GKMMAGTEAI LTKLRKLKSL KLLPVYELVE
1460 1470 1480 1490 1500
KEIQGFYNSL PLMKELKSEA LRKRHWTRLM EVTGQEFDMD PKTFTLGNMF
1510 1520 1530 1540 1550
AMQLHKYAEE IGKITNAAVK ELTIESEIRK LADVWREQRF ELGKYMKGPE
1560 1570 1580 1590 1600
DRGWVLRSTE DILVLLEDMG LNLQSMMASP FVRPFLTEVR AWEQKLSLIG
1610 1620 1630 1640 1650
ECIEVWMHVQ RKWMYLESIF VGSDDIRHQL PAEAKRFDNI DRQWQKIMND
1660 1670 1680 1690 1700
TAKNTVVLDA CMADGRLDLL KSLSEQLEVC QKSLSEYLDT KRCAFPRFYF
1710 1720 1730 1740 1750
ISDDELLSIL GTSDPTSVQE HMLKLFDNCA ALVFGRGNKT ITGMVSSEKE
1760 1770 1780 1790 1800
GFEFRNVVPI EGAVELWMTN VEAEMRKTLY QITKEGIFFY AKTPRTKWIS
1810 1820 1830 1840 1850
ENLGMVTLVG SQIWWTWETE DVFRRVRDGN KHSMKEFAAK LTGQLSELTS
1860 1870 1880 1890 1900
MVRSDLSNEV RKKVNTLIII DVHARDIIDT YVRDSIVDAR EFAWESQLRF
1910 1920 1930 1940 1950
YWDRQQDDIL IRQCTGLFKY GYEYMGLNGR LVITALTDRC YMTLTTALTY
1960 1970 1980 1990 2000
RLGGAPAGPA GTGKTETTKD LAKSMALLCV VFNCGEGLDY KAMGSIFSGL
2010 2020 2030 2040 2050
VQCGAWGCFD EFNRIEAEVL SVVSSQIKNI QEALKNDLTR FQFEGKEISI
2060 2070 2080 2090 2100
DPRTGIFITM NPGYAGRTEL PDNLKALFRP VTMVVPDLEQ ICEIMLFSEG
2110 2120 2130 2140 2150
FDSAKVLAKK MTVLYKLSRE QLSKQHHYDF GLRALKSVLV MAGSLKRGAP
2160 2170 2180 2190 2200
DMSEQLVLMR ALRDMNLPKF IFDDVPLFLG LINDLFPGMD CPRVRYPQFN
2210 2220 2230 2240 2250
DVVEADLADQ GFKVLTEPSE QVDKVVQLYE VMMTRHTTMV VGQTGGGKTV
2260 2270 2280 2290 2300
ILNTLARAQT KLGKKTHLYT INPKAISVAE LYGVLDKDTR DWTDGLLSNI
2310 2320 2330 2340 2350
FREMNKPLPA ERDEARYLVF DGDVDAVWVE NMNSVMDDNK LLTLPNGERI
2360 2370 2380 2390 2400
RLQNHCKLLF EVFDLQYASP ATISRCGMVY VDSRNLGYKP YIYTWLNSRA
2410 2420 2430 2440 2450
KQAEVDILRG LFEKYAVPSV DWILEGIDGE ELVRRPKQAV PVTNLNMITQ
2460 2470 2480 2490 2500
LCNLLNATIT DHPRMSDPQI LEAIFIFCTI WSLGAAIVQR PESPDRDRFD
2510 2520 2530 2540 2550
AFVKHIASMG LVDGERVAAT QLPARSLYEY CFDTNEGVWK SWRSYLQPYE
2560 2570 2580 2590 2600
PPADGAFAKI LVPTVDVVRS TWLLNTVVAA GKPCLFVGES GTAKSVTIAN
2610 2620 2630 2640 2650
YLAHLDSTIN IVLNVNFSSR TSSLDVQRAI EDSTEKRTKD TYGPPMGKRL
2660 2670 2680 2690 2700
LMFIDDLNMP RVDTYGTQQP IALLKLFIER KGLYDRGKEL SWKNMKDVQV
2710 2720 2730 2740 2750
VGAMGPPGGA RNPVDPRFIS LFSVFEIQFP SNENLRTIYQ AILSRHLAKL
2760 2770 2780 2790 2800
PTDEIRDQLG ERLTDVTLEL YNFIIDKLPP TPSRFHYIFN LRDLSRIYEG
2810 2820 2830 2840 2850
LLLTVGDVFK TPEQFLRLWR NECLRVLHDR LISTDDKRVM TERLEALVQQ
2860 2870 2880 2890 2900
KFPNLAAHTL ASPVLFGDFK NVINELQGEG EVAPRMYDDL GDYNSIKPLF
2910 2920 2930 2940 2950
EDVMTNFYNR KRKPMNLVFF EDALEHLTRI HRTLRLPQGN CLLVGVGGSG
2960 2970 2980 2990 3000
KQSLSKLAAF TAGCEVFEIT LTRGYDELAF REDLKRLYAM LGSDNKRVMF
3010 3020 3030 3040 3050
LFTDAHVADE GFLELINNML TSGMVPALYD GAEKDGLIGS VRAEVEKKGL
3060 3070 3080 3090 3100
LATKESCWSY YVDKCRNNLH VVLAMSPVGE TLRSRCRNFP GMVNNTVIDW
3110 3120 3130 3140 3150
FEPWPEQALT SVASVFLAEE ALPEALRPQI VEHMVTVHQS VRTFSTRFLE
3160 3170 3180 3190 3200
ELRRYNYVTP KNYLDFINNY KRALATNRRT IEDTVTRLSG GLEKLIQAAV
3210 3220 3230 3240 3250
EVDAMQKELS QAQVVVAQAT KECNELLEVI STNTVDVETK AKAAAIKEAQ
3260 3270 3280 3290 3300
LKVDSEQIAI EKAEAEAALE EAIPALEEAA AALQDLSKDH ITEIRSYAKP
3310 3320 3330 3340 3350
PEQVQKVCEC VVILRNIKDV SWLGAKSMMA DGNFLRSLVE FDKDSLTDKQ
3360 3370 3380 3390 3400
VKKVKEYFKD PKAPLTYDSL RAISTAGAGL LKWVLAMVNY NNVARTVEPK
3410 3420 3430 3440 3450
RKKVAESEKN LRIAQKDLAS TKLELQSLND QLGKLRTQFE EKTAEQQDLK
3460 3470 3480 3490 3500
AKADLMERRL IAASKLIAGL GSERERWTRD IADLESRRDR LIGDCLLTSS
3510 3520 3530 3540 3550
FLSYTGAFTA TYRHAMVYEM WQDDVKARGV PVTQPFRLEA LLTSDVETTG
3560 3570 3580 3590 3600
WASEGLPSDE LSIQNGILTV RANRWPLCID PQMQAVNWIK SREGKMLEGK
3610 3620 3630 3640 3650
VKTFNDSDFL KQLELSIQYG FPFLFENLDE YIDPVIDPVL EKNLVPGDGK
3660 3670 3680 3690 3700
FVIKLGDKEV EWDSNFRLYM TSKLSNPHYG PEISGKTMII NYGVTQQGLT
3710 3720 3730 3740 3750
EQLLNVTLRH ERSDLEEARE ALIKQMSENK ATLQALEDTL LRELSNAQGN
3760 3770 3780 3790 3800
ILDNSELIAT LESAKLKAVE IAEKLEASKV TAAEIEETRV RYSPAAKRGA
3810 3820 3830 3840 3850
ILFFVIAGLS AITNMYEYSL ASFLVVFNGS LHSSRRDASI EGRLRNIIDT
3860 3870 3880 3890 3900
LTYDVYAYTC LGLFERHKLM FSFQMTCKIL EGDTPLDPQL LDFFLKGNLS
3910 3920 3930 3940 3950
LEKAARRKPF DWFPDAGWQD LMRLVELGQK KIGADGRMHA LGSLANDVES
3960 3970 3980 3990 4000
DEAAWRTWYD LEAPEEAELP CGYQSFLSDF EKLCLMRCLR MDRVTVGITR
4010 4020 4030 4040 4050
FVIGVMGEKY VQPPVLEYRS IYKQSTETTP IVFVLSPGAD PAFDVFKLGE
4060 4070 4080 4090 4100
EMGFRPGAKL KYMALGQGMG PKAQELIETG ATRGLWIMLQ NCHLLPTWLK
4110 4120 4130 4140 4150
TLEKILEKIT KPHADFRLWL TTELTDRFPL GVLQRSLKVV TEPPNGLKLN
4160 4170 4180 4190 4200
MRQSYSKITE EVLADCPHQA FRPLVYVLGF FHAVVQERRK YGKLGWNVPY
4210 4220 4230 4240 4250
DFNETDFRIS MALISTYLTK AWDAQDDLIP WGTLRYLIGE AMYGGRVSDS
4260 4270 4280 4290 4300
YDRRILTTYL DEYLGDFLFD TFQPFRFYAC KDYEIAIPQT GSRDTYLKAV
4310 4320 4330 4340 4350
EALPLVQSPE AFGLNANADI SYYTSATKAI WTDLVDLQPR TGGGGGGVAR
4360 4370 4380 4390 4400
EEFIGGVARD IAAKIPEPFD LPQLRKELGT PSPTQVVLLQ ELERWNSVLG
4410 4420 4430 4440 4450
VMVSSLRDLQ RALSGEIGFS SRLEELASSL YNGKLPAMWA RLNPATEKAL
4460 4470 4480 4490 4500
GAWMLWFGRR YRQYKDWTEH GEPKVIWLSG LHIPETYIAA LVQAACRDKG
4510 4520 4530 4540 4550
WPLDKSTLYT KVTKFTDPYQ VSERPKYGCY MSGLYLEGAA WDLEASQLRK
4560 4570 4580 4590 4600
QDPKVLVNEL PILQVIPIEA NKLKLANTFR APVYVTQARR NAMGVGLVFD
4610 4620
ADLASAEHSS HWVLQGVALV LNIDQ
Length:4,625
Mass (Da):522,843
Last modified:May 1, 2000 - v1
Checksum:i875F51048AF99340
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ243806 Genomic DNA. Translation: CAB56598.1.
U61364 Genomic DNA. Translation: AAC49514.1.
PIRiS72239.

Cross-referencesi

Web resourcesi

Protein Spotlight

The kink behind the wriggle - Issue 34 of May 2003

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ243806 Genomic DNA. Translation: CAB56598.1 .
U61364 Genomic DNA. Translation: AAC49514.1 .
PIRi S72239.

3D structure databases

ProteinModelPortali Q9SMH3.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q9SMH3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG5245.

Family and domain databases

Gene3Di 3.40.50.300. 4 hits.
InterProi IPR003593. 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 ]
PANTHERi PTHR10676. PTHR10676. 1 hit.
Pfami PF07728. 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 ]
SMARTi SM00382. AAA. 4 hits.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 6 hits.
ProtoNeti Search...

Publicationsi

  1. "Domains in the 1-alpha dynein heavy chain required for inner arm assembly and flagellar motility in Chlamydomonas."
    Myster S.H., Knott J.A., Wysocki K.M., O'Toole E.T., Porter M.E.
    J. Cell Biol. 146:801-818(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, MUTAGENESIS.
    Strain: 21gr / CC-1690.
  2. "The dynein gene family in Chlamydomonas reinhardtii."
    Porter M.E., Knott J.A., Myster S.H., Farlow S.J.
    Genetics 144:569-585(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1914-2064.
    Strain: 137c / CC-125.
  3. "High-pressure liquid chromatography fractionation of Chlamydomonas dynein extracts and characterization of inner-arm dynein subunits."
    Goodenough U.W., Gebhart B., Mermall V., Mitchell D.R., Heuser J.E.
    J. Mol. Biol. 194:481-494(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: DYNEIN COMPLEX ELECTRON MICROSCOPY.
    Strain: CC-620.
  4. "Three distinct inner dynein arms in Chlamydomonas flagella: molecular composition and location in the axoneme."
    Piperno G., Ramanis Z., Smith E.F., Sale W.S.
    J. Cell Biol. 110:379-389(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  5. "Phosphoregulation of an inner dynein arm complex in Chlamydomonas reinhardtii is altered in phototactic mutant strains."
    King S.J., Dutcher S.K.
    J. Cell Biol. 136:177-191(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: REQUIREMENT OF I1 DYNEIN COMPLEX FOR PHOTOTAXIS.
  6. "The Chlamydomonas Dhc1 gene encodes a dynein heavy chain subunit required for assembly of the I1 inner arm complex."
    Myster S.H., Knott J.A., O'Toole E.T., Porter M.E.
    Mol. Biol. Cell 8:607-620(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: ISOLATION, DISRUPTION PHENOTYPE.
    Strain: 21gr / CC-1690.

Entry informationi

Entry nameiDYH1A_CHLRE
AccessioniPrimary (citable) accession number: Q9SMH3
Secondary accession number(s): Q96388
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3