Q9SMH3 (DYH1A_CHLRE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
1-alpha DHC
Dynein-1, subspecies f

Gene names

Name:	DHC1
Synonyms:	IDA1, PF9

Organism

Chlamydomonas reinhardtii (Chlamydomonas smithii)

Taxonomic identifier

3055 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Chlorophyta › Chlorophyceae › Chlamydomonadales › Chlamydomonadaceae › Chlamydomonas

Protein attributes

Sequence length	4625 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	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. Ref.4
Subcellular location	Cell projection › cilium › flagellum. Cytoplasm › cytoskeleton › flagellum axoneme.
Induction	By deflagellation.
Domain	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.
Disruption phenotype	Cells swim slowly with near normal beat frequencies but aberrant waveforms, and are unable to phototax. Ref.6
Sequence similarities	Belongs to the dynein heavy chain family.

Ontologies

Keywords
Biological process	Cilium biogenesis/degradation
Cellular component	Cell projection Cilium Cytoplasm Cytoskeleton Dynein Flagellum Microtubule
Domain	Coiled coil Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Motor protein
Gene Ontology (GO)
Biological_process	ATP catabolic process Inferred from electronic annotation. Source: GOC cell projection organization Inferred from electronic annotation. Source: UniProtKB-KW microtubule-based movement Inferred from electronic annotation. Source: InterPro
Cellular_component	cilium Inferred from electronic annotation. Source: UniProtKB-KW cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW dynein complex Inferred from electronic annotation. Source: UniProtKB-KW microtubule Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity Inferred from electronic annotation. Source: InterPro microtubule motor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 4625	4625	Dynein-1-alpha heavy chain, flagellar inner arm I1 complex		PRO_0000114646
Regions
	Nucleotide binding	960 – 967	8	ATP Potential
	Nucleotide binding	1958 – 1965	8	ATP Potential
	Nucleotide binding	2242 – 2249	8	ATP Potential
	Nucleotide binding	2588 – 2595	8	ATP Potential
	Nucleotide binding	2945 – 2952	8	ATP Potential
	Nucleotide binding	3680 – 3687	8	ATP Potential
	Region	1 – 1919	1919	Stem By similarity
	Region	1920 – 2141	222	AAA 1 By similarity
	Region	2201 – 2437	237	AAA 2 By similarity
	Region	2550 – 2800	251	AAA 3 By similarity
	Region	2906 – 3155	250	AAA 4 By similarity
	Region	3192 – 3494	303	Stalk By similarity
	Region	3542 – 3773	232	AAA 5 By similarity
	Region	3998 – 4216	219	AAA 6 By similarity
	Coiled coil	1227 – 1259	33	Potential
	Coiled coil	1339 – 1409	71	Potential
	Coiled coil	3192 – 3297	106	Potential
	Coiled coil	3400 – 3494	95	Potential
	Coiled coil	3701 – 3788	88	Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9SMH3 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 875F51048AF99340	FASTA	4,625	522,843
	10 20 30 40 50 60 MDRRLEWVKE KACLGLGVEP NLFEAAIANP ESRARVTAFL DGTVTSSALL FALEEATIYV 70 80 90 100 110 120 EEYQEVLAEE QAPEAEDGEG EEHDGQEPGE AGGEGAEGST APGDSGDGQP EDAPAAAAEA 130 140 150 160 170 180 NGANPEDEAA APADGAADGA AGEGGEEGDG AEGDEPPAPP APKYVRRVIS VPKVVSKLNV 190 200 210 220 230 240 ALGSLPEELS VFPVFYFILN RSGHVAAEEL DSAVEFGLLS EGPSLRILEQ MLSSVFVPIL 250 260 270 280 290 300 VQMSGGDVAS GGVLMQSMTD NSHRELLGNM QKFHSQVTQA LQQLTGDVTL QLPDFPLEDM 310 320 330 340 350 360 DRAAADTDLV MQLEQYMAEW SQVLASVLQR ESQKHPTGKG PLAEIEFWRE RNAVLSSLYE 370 380 390 400 410 420 QLNLPQVKRM ILVVEKGSDD RNLMAGFKSQ LGELTKLATE ARDNVKFLTT LERHFKNIAT 430 440 450 460 470 480 GPLGGILDTL PPMMNALRMV WIISRHYSDD QRMGSLFQRI AREIGDRVEA AVDLRHIFRM 490 500 510 520 530 540 TSADAVELLK VCKSVLEHWL QTYMAMREKI ELSGRDARWE FPKQLLFART NYMAEICTDL 550 560 570 580 590 600 IEMVEIVDDF FRFLGPELKT VTGDTAGIDR VVHRVVAMYE PIESISFNVF DYGNQHEWKA 610 620 630 640 650 660 AKQQFYADNE DIKEATRELI DTSFRKLRSA EGACELLQSF KSIKSKGAIQ KQVMNKFNDI 670 680 690 700 710 720 LEQFAREIEQ TADIFERNKD APPVTKNQPP VAGAIKWVRS LLERLKRTMA KLLSTEEEII 730 740 750 760 770 780 RTTELGQAVE SKFKSFARSV MLTEKKWFSS WSDSINGVAM QHLKQTIFRR SAATNRVEVN 790 800 810 820 830 840 FHPDLVRLIR ETRYLDRMGF PIPEIALNVA LQEDKFLQWL EGLNSMLFKY YESIDQLTPV 850 860 870 880 890 900 ERELMERKLE ELESCLQPGF TILNWNSLGI TEFIGTCDKA IATFQQLVKQ VQKNSGIIEQ 910 920 930 940 950 960 VVYAIAGAQL VTEPEEGAEV MDLQEFYEDI ERQRLAALES LVKKYRTISP LLGKIEEVVA 970 980 990 1000 1010 1020 GTNSGKSPAL SSYYSFWERA IFNALNTMVL CAMTKLQDMI EQRSKHAEGG RKPPLFKVTV 1030 1040 1050 1060 1070 1080 SLQSVDVVVQ PPMTEVNKAL GRLVRSLVES TKAFVRWMDG TCVETPEQRG ATDDDEPIVF 1090 1100 1110 1120 1130 1140 TFYWDVAANP QVIKTMLNLN QSIQRAITSV NKYAESWRRH QALWKTDKNS VLDKFKARDP 1150 1160 1170 1180 1190 1200 SAAQFEDKLS KYAKMATEIS AQAKDFDQDF IRVSCHALAS SVCDEAQAWV RAIAQTMREL 1210 1220 1230 1240 1250 1260 DAVTESQLRD KIAKYQTALH RPPDTLEELK QVLNTVNTIR GESMVMELRY ADLEERYRTR 1270 1280 1290 1300 1310 1320 LLYATNPEEE SQCAHELASA SQVRALWTEL LNEAEAVDWS LEETKKKFSE TTRSQVSDFA 1330 1340 1350 1360 1370 1380 AITAELWEKF RTTGPGLPTV ELASGLDELH KYESNLADAL RQREQLVLAE KLFGMEITAY 1390 1400 1410 1420 1430 1440 PELAQLESEI RKLAQVYGVY AEHAEAVRQY GGQLWSELDV GKMMAGTEAI LTKLRKLKSL 1450 1460 1470 1480 1490 1500 KLLPVYELVE KEIQGFYNSL PLMKELKSEA LRKRHWTRLM EVTGQEFDMD PKTFTLGNMF 1510 1520 1530 1540 1550 1560 AMQLHKYAEE IGKITNAAVK ELTIESEIRK LADVWREQRF ELGKYMKGPE DRGWVLRSTE 1570 1580 1590 1600 1610 1620 DILVLLEDMG LNLQSMMASP FVRPFLTEVR AWEQKLSLIG ECIEVWMHVQ RKWMYLESIF 1630 1640 1650 1660 1670 1680 VGSDDIRHQL PAEAKRFDNI DRQWQKIMND TAKNTVVLDA CMADGRLDLL KSLSEQLEVC 1690 1700 1710 1720 1730 1740 QKSLSEYLDT KRCAFPRFYF ISDDELLSIL GTSDPTSVQE HMLKLFDNCA ALVFGRGNKT 1750 1760 1770 1780 1790 1800 ITGMVSSEKE GFEFRNVVPI EGAVELWMTN VEAEMRKTLY QITKEGIFFY AKTPRTKWIS 1810 1820 1830 1840 1850 1860 ENLGMVTLVG SQIWWTWETE DVFRRVRDGN KHSMKEFAAK LTGQLSELTS MVRSDLSNEV 1870 1880 1890 1900 1910 1920 RKKVNTLIII DVHARDIIDT YVRDSIVDAR EFAWESQLRF YWDRQQDDIL IRQCTGLFKY 1930 1940 1950 1960 1970 1980 GYEYMGLNGR LVITALTDRC YMTLTTALTY RLGGAPAGPA GTGKTETTKD LAKSMALLCV 1990 2000 2010 2020 2030 2040 VFNCGEGLDY KAMGSIFSGL VQCGAWGCFD EFNRIEAEVL SVVSSQIKNI QEALKNDLTR 2050 2060 2070 2080 2090 2100 FQFEGKEISI DPRTGIFITM NPGYAGRTEL PDNLKALFRP VTMVVPDLEQ ICEIMLFSEG 2110 2120 2130 2140 2150 2160 FDSAKVLAKK MTVLYKLSRE QLSKQHHYDF GLRALKSVLV MAGSLKRGAP DMSEQLVLMR 2170 2180 2190 2200 2210 2220 ALRDMNLPKF IFDDVPLFLG LINDLFPGMD CPRVRYPQFN DVVEADLADQ GFKVLTEPSE 2230 2240 2250 2260 2270 2280 QVDKVVQLYE VMMTRHTTMV VGQTGGGKTV ILNTLARAQT KLGKKTHLYT INPKAISVAE 2290 2300 2310 2320 2330 2340 LYGVLDKDTR DWTDGLLSNI FREMNKPLPA ERDEARYLVF DGDVDAVWVE NMNSVMDDNK 2350 2360 2370 2380 2390 2400 LLTLPNGERI RLQNHCKLLF EVFDLQYASP ATISRCGMVY VDSRNLGYKP YIYTWLNSRA 2410 2420 2430 2440 2450 2460 KQAEVDILRG LFEKYAVPSV DWILEGIDGE ELVRRPKQAV PVTNLNMITQ LCNLLNATIT 2470 2480 2490 2500 2510 2520 DHPRMSDPQI LEAIFIFCTI WSLGAAIVQR PESPDRDRFD AFVKHIASMG LVDGERVAAT 2530 2540 2550 2560 2570 2580 QLPARSLYEY CFDTNEGVWK SWRSYLQPYE PPADGAFAKI LVPTVDVVRS TWLLNTVVAA 2590 2600 2610 2620 2630 2640 GKPCLFVGES GTAKSVTIAN YLAHLDSTIN IVLNVNFSSR TSSLDVQRAI EDSTEKRTKD 2650 2660 2670 2680 2690 2700 TYGPPMGKRL LMFIDDLNMP RVDTYGTQQP IALLKLFIER KGLYDRGKEL SWKNMKDVQV 2710 2720 2730 2740 2750 2760 VGAMGPPGGA RNPVDPRFIS LFSVFEIQFP SNENLRTIYQ AILSRHLAKL PTDEIRDQLG 2770 2780 2790 2800 2810 2820 ERLTDVTLEL YNFIIDKLPP TPSRFHYIFN LRDLSRIYEG LLLTVGDVFK TPEQFLRLWR 2830 2840 2850 2860 2870 2880 NECLRVLHDR LISTDDKRVM TERLEALVQQ KFPNLAAHTL ASPVLFGDFK NVINELQGEG 2890 2900 2910 2920 2930 2940 EVAPRMYDDL GDYNSIKPLF EDVMTNFYNR KRKPMNLVFF EDALEHLTRI HRTLRLPQGN 2950 2960 2970 2980 2990 3000 CLLVGVGGSG KQSLSKLAAF TAGCEVFEIT LTRGYDELAF REDLKRLYAM LGSDNKRVMF 3010 3020 3030 3040 3050 3060 LFTDAHVADE GFLELINNML TSGMVPALYD GAEKDGLIGS VRAEVEKKGL LATKESCWSY 3070 3080 3090 3100 3110 3120 YVDKCRNNLH VVLAMSPVGE TLRSRCRNFP GMVNNTVIDW FEPWPEQALT SVASVFLAEE 3130 3140 3150 3160 3170 3180 ALPEALRPQI VEHMVTVHQS VRTFSTRFLE ELRRYNYVTP KNYLDFINNY KRALATNRRT 3190 3200 3210 3220 3230 3240 IEDTVTRLSG GLEKLIQAAV EVDAMQKELS QAQVVVAQAT KECNELLEVI STNTVDVETK 3250 3260 3270 3280 3290 3300 AKAAAIKEAQ LKVDSEQIAI EKAEAEAALE EAIPALEEAA AALQDLSKDH ITEIRSYAKP 3310 3320 3330 3340 3350 3360 PEQVQKVCEC VVILRNIKDV SWLGAKSMMA DGNFLRSLVE FDKDSLTDKQ VKKVKEYFKD 3370 3380 3390 3400 3410 3420 PKAPLTYDSL RAISTAGAGL LKWVLAMVNY NNVARTVEPK RKKVAESEKN LRIAQKDLAS 3430 3440 3450 3460 3470 3480 TKLELQSLND QLGKLRTQFE EKTAEQQDLK AKADLMERRL IAASKLIAGL GSERERWTRD 3490 3500 3510 3520 3530 3540 IADLESRRDR LIGDCLLTSS FLSYTGAFTA TYRHAMVYEM WQDDVKARGV PVTQPFRLEA 3550 3560 3570 3580 3590 3600 LLTSDVETTG WASEGLPSDE LSIQNGILTV RANRWPLCID PQMQAVNWIK SREGKMLEGK 3610 3620 3630 3640 3650 3660 VKTFNDSDFL KQLELSIQYG FPFLFENLDE YIDPVIDPVL EKNLVPGDGK FVIKLGDKEV 3670 3680 3690 3700 3710 3720 EWDSNFRLYM TSKLSNPHYG PEISGKTMII NYGVTQQGLT EQLLNVTLRH ERSDLEEARE 3730 3740 3750 3760 3770 3780 ALIKQMSENK ATLQALEDTL LRELSNAQGN ILDNSELIAT LESAKLKAVE IAEKLEASKV 3790 3800 3810 3820 3830 3840 TAAEIEETRV RYSPAAKRGA ILFFVIAGLS AITNMYEYSL ASFLVVFNGS LHSSRRDASI 3850 3860 3870 3880 3890 3900 EGRLRNIIDT LTYDVYAYTC LGLFERHKLM FSFQMTCKIL EGDTPLDPQL LDFFLKGNLS 3910 3920 3930 3940 3950 3960 LEKAARRKPF DWFPDAGWQD LMRLVELGQK KIGADGRMHA LGSLANDVES DEAAWRTWYD 3970 3980 3990 4000 4010 4020 LEAPEEAELP CGYQSFLSDF EKLCLMRCLR MDRVTVGITR FVIGVMGEKY VQPPVLEYRS 4030 4040 4050 4060 4070 4080 IYKQSTETTP IVFVLSPGAD PAFDVFKLGE EMGFRPGAKL KYMALGQGMG PKAQELIETG 4090 4100 4110 4120 4130 4140 ATRGLWIMLQ NCHLLPTWLK TLEKILEKIT KPHADFRLWL TTELTDRFPL GVLQRSLKVV 4150 4160 4170 4180 4190 4200 TEPPNGLKLN MRQSYSKITE EVLADCPHQA FRPLVYVLGF FHAVVQERRK YGKLGWNVPY 4210 4220 4230 4240 4250 4260 DFNETDFRIS MALISTYLTK AWDAQDDLIP WGTLRYLIGE AMYGGRVSDS YDRRILTTYL 4270 4280 4290 4300 4310 4320 DEYLGDFLFD TFQPFRFYAC KDYEIAIPQT GSRDTYLKAV EALPLVQSPE AFGLNANADI 4330 4340 4350 4360 4370 4380 SYYTSATKAI WTDLVDLQPR TGGGGGGVAR EEFIGGVARD IAAKIPEPFD LPQLRKELGT 4390 4400 4410 4420 4430 4440 PSPTQVVLLQ ELERWNSVLG VMVSSLRDLQ RALSGEIGFS SRLEELASSL YNGKLPAMWA 4450 4460 4470 4480 4490 4500 RLNPATEKAL GAWMLWFGRR YRQYKDWTEH GEPKVIWLSG LHIPETYIAA LVQAACRDKG 4510 4520 4530 4540 4550 4560 WPLDKSTLYT KVTKFTDPYQ VSERPKYGCY MSGLYLEGAA WDLEASQLRK QDPKVLVNEL 4570 4580 4590 4600 4610 4620 PILQVIPIEA NKLKLANTFR APVYVTQARR NAMGVGLVFD ADLASAEHSS HWVLQGVALV LNIDQ

References

[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.

Web resources

Protein Spotlight

The kink behind the wriggle - Issue 34 of May 2003

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ243806 Genomic DNA. Translation: CAB56598.1. U61364 Genomic DNA. Translation: AAC49514.1.
PIR	S72239.
3D structure databases
ProteinModelPortal	Q9SMH3.
ModBase	Search...
Proteomic databases
PRIDE	Q9SMH3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	COG5245.
Family and domain databases
InterPro	IPR003593. AAA+_ATPase. IPR011704. ATPase_dyneun-rel_AAA. IPR026982. DHC1. 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. [Graphical view]
PANTHER	PTHR10676. PTHR10676. 1 hit. PTHR10676:SF135. PTHR10676:SF135. 1 hit.
Pfam	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]
SMART	SM00382. AAA. 4 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DYH1A_CHLRE

Accession

Primary (citable) accession number: Q9SMH3
Secondary accession number(s): Q96388

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 9, 2003
Last sequence update:	May 1, 2000
Last modified:	April 3, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program