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P38650 (DYHC1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytoplasmic dynein 1 heavy chain 1
Alternative name(s):
Cytoplasmic dynein heavy chain 1
Dynein heavy chain, cytosolic
MAP 1C
Gene names
Name:Dync1h1
Synonyms:Dhc1, Dnch1, Dnchc1, Dnec1, Dyhc, Map1c
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length4644 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP.

Subunit structure

Homodimer. The cytoplasmic dynein 1 complex consists of two catalytic heavy chains (HCs) and a number of non-catalytic subunits presented by intermediate chains (ICs), light intermediate chains (LICs) and light chains (LCs); the composition seems to vary in respect to the IC, LIC and LC composition. The heavy chain homodimer serves as a scaffold for the probable homodimeric assembly of the respective non-catalytic subunits. The ICs and LICs bind directly to the HC dimer and dynein LCs assemble on the IC dimer. Interacts with DYNC1LI1; DYNC1LI1 and DYNC1LI2 bind mutually exclusive to DYNC1H1. Interacts with DYNC1LI2; DYNC1LI1 and DYNC1LI2 bind mutually exclusive to DYNC1H1. Interacts with DYNC1I2. Ref.3 Ref.4

Subcellular location

Cytoplasmcytoskeleton.

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.

Sequence similarities

Belongs to the dynein heavy chain family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 46444643Cytoplasmic dynein 1 heavy chain 1
PRO_0000114629

Regions

Nucleotide binding1904 – 19118ATP Potential
Nucleotide binding2222 – 22298ATP Potential
Nucleotide binding2593 – 26008ATP Potential
Nucleotide binding2935 – 29428ATP Potential
Region2 – 18651864Stem By similarity
Region446 – 701256Interaction with DYNC1I2
Region649 – 800152Interaction with DYNC1LI2
Region1866 – 2097232AAA 1 By similarity
Region2178 – 2450273AAA 2 By similarity
Region2554 – 2803250AAA 3 By similarity
Region2897 – 3166270AAA 4 By similarity
Region3187 – 3498312Stalk By similarity
Region3551 – 3780230AAA 5 By similarity
Region4003 – 4219217AAA 6 By similarity
Coiled coil48 – 6922 Potential
Coiled coil179 – 20022 Potential
Coiled coil453 – 47624 Potential
Coiled coil541 – 56424 Potential
Coiled coil1169 – 120133 Potential
Coiled coil1229 – 125022 Potential
Coiled coil1355 – 137117 Potential
Coiled coil3187 – 327387 Potential
Coiled coil3394 – 3498105 Potential
Coiled coil3735 – 379864 Potential

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue11231N6-acetyllysine By similarity
Modified residue34781N6-acetyllysine By similarity
Modified residue42811N6-acetyllysine By similarity

Experimental info

Sequence conflict1024 – 10252SR → MP in AAA41103. Ref.2
Sequence conflict17721N → D in AAA41103. Ref.2
Sequence conflict20981P → A in AAA41103. Ref.2
Sequence conflict21391F → V in AAA41103. Ref.2
Sequence conflict21751D → A in AAA41103. Ref.2
Sequence conflict21851K → Q in AAA41103. Ref.2
Sequence conflict23661L → V in AAA41103. Ref.2
Sequence conflict23821T → S in AAA41103. Ref.2
Sequence conflict24631G → A in AAA41103. Ref.2
Sequence conflict32191A → D in AAA41103. Ref.2
Sequence conflict41311R → K in AAA41103. Ref.2
Sequence conflict43661F → S in AAA41103. Ref.2
Sequence conflict45111A → G in AAA41103. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P38650 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 8C6ABDBEDF875D82

FASTA4,644532,252
        10         20         30         40         50         60 
MSETGGGEDG SAGLEVSAVQ NVADVSVLQK HLRKLVPLLL EDGGDAPAAL EAALEEKSAL 

        70         80         90        100        110        120 
EQMRKFLSDP QVHTVLVERS TLKEDVGDEG EEEKEFISYN INIDIHYGVK SNSLAFIKRA 

       130        140        150        160        170        180 
PVIDADKPVS SQLRVLTLSE DSPYETLHSF ISNAVAPFFK SYIRESGKAD RDGDKMAPSV 

       190        200        210        220        230        240 
EKKIAELEMG LLHLQQNIEI PEISLPIHPI ITNVAKQCYE RGEKPKVTDF GDKVEDPTFL 

       250        260        270        280        290        300 
NQLQSGVNRW IREIQKVTKL DRDPASGTAL QEISFWLNLE RALYRIQEKR ESPEVLLTLD 

       310        320        330        340        350        360 
ILKHGKRFHA TVSFDTDTGL KQALETVNDY NPLMKDFPLN DLLSATELDK IRQALVAIFT 

       370        380        390        400        410        420 
HLRKIRNTKY PIQRALRLVE AISRDLSSQL LKVLGTRKLM HVAYEEFEKV MVACFEVFQT 

       430        440        450        460        470        480 
WDDEYEKLQV LLRDIVKRKR EENLKMVWRI NPAHRKLQAR LDQMRKFRRQ HEQLRAVIVR 

       490        500        510        520        530        540 
VLRPQVTAVA QQNQGEAPEP QDMKVAEVLF DAADANAIEE VNLAYENVKE VDGLDVSKEG 

       550        560        570        580        590        600 
TEAWEAAMKR YDERIDRVET RITARLRDQL GTAKNANEMF RIFSRFNALF VRPHIRGAIR 

       610        620        630        640        650        660 
EYQTQLIQRV KDDIESLHDK FKVQYPQSQA CKMSHVRDLP PVSGSIIWAK QIDRQLTAYM 

       670        680        690        700        710        720 
KRVEDVLGKG WENHVEGQKL KQDGDSFRMK LNTQEIFDDW ARKVQQRNLG VSGRIFTIES 

       730        740        750        760        770        780 
ARVRGRSGNV LKLKVNFLPE IITLSKEVRN LKWLGFRVPL AIVNKAHQAN QLYPFAISLI 

       790        800        810        820        830        840 
ESVRTYERTC EKVEERNTIS LLVAGLKKEV QALIAEGIAL VWESYKLDPY VQRLAETVFN 

       850        860        870        880        890        900 
FQEKVDDLLI IEEKIDLEVR SLETCMYDHK TFSEILNRVQ KAVDDLNLHS YSNLPIWVNK 

       910        920        930        940        950        960 
LDMEIERILG VRLQAGLRAW TQVLLGQAED KAEVDMDTDA PQVSHKPGGE PKIKNVVHEL 

       970        980        990       1000       1010       1020 
RITNQVIYLN PPIEECRYKL YQEMFAWKMI VLSLPRIQSQ RYQVGVHYEL TEEEKFYRNA 

      1030       1040       1050       1060       1070       1080 
LTRSRDGPVA LEESYSAVMG IVTEVEQYVK VWLQYQCLWD MQAENIYNRL GEDLSKWQAL 

      1090       1100       1110       1120       1130       1140 
LVQIRRARGT FDNAETKKEF GPVVIDYGKV QSKVNLKYDS WHKEVLSKFG QMLGSNMTEF 

      1150       1160       1170       1180       1190       1200 
HSQISKSRQE LEQHSVDTAS TSDAVTFITY VQSLKRKIKQ FEKQVELYRN GQRLLEKQRF 

      1210       1220       1230       1240       1250       1260 
QFPPSWLYID NIEGEWGAFN DIMRRKDSAI QQQVANLQMK IVQEDRAVES RTTDLLTDWE 

      1270       1280       1290       1300       1310       1320 
KTKPVTGNLR PEEALQALTI YEGKFGRLKD DREKCAKAKE ALELTDTGLL SGSEERVQVA 

      1330       1340       1350       1360       1370       1380 
LEELQDLKGV WSELSKVWEQ IDQMKEQPWV SVQPRKLRQN LDGLLNQLKN FPARLRQYAS 

      1390       1400       1410       1420       1430       1440 
YEFVQRLLKG YMKINMLVIE LKSEALKDRH WKQLMKRLHV NWVVSELTLG QIWDVDLQKN 

      1450       1460       1470       1480       1490       1500 
EAIVKDVLLV AQGEMALEEF LKQIREVWNT YELDLVNYQN KCRLIRGWDD LFNKVKEHIN 

      1510       1520       1530       1540       1550       1560 
SVSAMKLSPY YKVFEEDALS WEDKLNRIMA LFDVWIDVQR RWVYLEGIFT GSADIKHLLP 

      1570       1580       1590       1600       1610       1620 
VETQRFQSIS TEFLALMKKV SKSPLVMDVL NIQGVQRSLE RLADLLGKIQ KALGEYLERE 

      1630       1640       1650       1660       1670       1680 
RSSFPRFYFV GDEDLLEIIG NSKNVAKLQK HFKKMFAGVS SIILNEDSSV VLGISSREGE 

      1690       1700       1710       1720       1730       1740 
EVMFKTPVSI TEHPKINEWL TLVEKEMRVT LAKLLAESVT EVEIFGKATS IDPNTYITWI 

      1750       1760       1770       1780       1790       1800 
DKYQAQLVVL SAQIAWSENV ENALSNVGGG GNVGPLQSVL SNVEVTLNVL ADSVLMEQPP 

      1810       1820       1830       1840       1850       1860 
LRRRKLEHLI TELVHQRDVT RSLIKSKIDN AKSFEWLSQM RFYFDPKQTD VLQQLSIQMA 

      1870       1880       1890       1900       1910       1920 
NAKFNYGFEY LGVQDKLVQT PLTDRCYLTM TQALEARLGG SPFGPAGTGK TESVKALGHQ 

      1930       1940       1950       1960       1970       1980 
LGRFVLVFNC DETFDFQAMG RIFVGLCQVG AWGCFDEFNR LEERMLSAVS QQVQCIQEAL 

      1990       2000       2010       2020       2030       2040 
REHSNPNYDK TSAPITCELL NKQVKVSPDM AIFITMNPGY AGRSNLPDNL KKLFRSLAMT 

      2050       2060       2070       2080       2090       2100 
KPDRQLIAQV MLYSQGFRTA EVLANKIVPF FKLCDEQLSS QSHYDFGLRA LKSVLVSPGN 

      2110       2120       2130       2140       2150       2160 
VKRERIQKIK REKEERGEAV DEGEIAENLP EQEILIQSFC ETMVPKLVAE DIPLLFSLLS 

      2170       2180       2190       2200       2210       2220 
DVFPGVQYHR GEMTDLREEL KKVCKEMYLT YGDGEEVGGM WVEKVLQLYQ ITQINHGLMM 

      2230       2240       2250       2260       2270       2280 
VGPSGSGKSM AWRVLLKALE RLEGVEGVAH IIDPKAISKD HLYGTLDPNT REWTDGLFTH 

      2290       2300       2310       2320       2330       2340 
VLRKIIDNVR GELQKRQWIV FDGDVDPEWV ENLNSVLDDN KLLTLPNGER LSLPPNVRIM 

      2350       2360       2370       2380       2390       2400 
FEVQDLKYAT LATVSRCGMV WFSEDLLSTD MIFNNFLARL RTIPLDEGED EAQRRRKGKE 

      2410       2420       2430       2440       2450       2460 
DEGEEAASPM LQIQRDAATI MQPYFTSNGL VTKALEHAFK LEHIMDLTRL RCLGSLFSML 

      2470       2480       2490       2500       2510       2520 
HQGCRNVAQY NANHPDFPMQ IEQLERYIQR YLVYAILWSL SGDSRLKMRA ELGEYIRRIT 

      2530       2540       2550       2560       2570       2580 
TVPLPTAPNI PIIDYEVSIS GEWSPWQAKV PQIEVETHKV AAPDVVVPTL DTVRHEALLY 

      2590       2600       2610       2620       2630       2640 
TWLAEHKPLV LCGPPGSGKT MTLFSALRAL PDMEVVGLNF SSATTPELLL KTFDHYCEYR 

      2650       2660       2670       2680       2690       2700 
RTPNGVVLAP VQLGKWLVLF CDEINLPDMD KYGTQRVISF IRQMVEHGGF YRTSDQTWVK 

      2710       2720       2730       2740       2750       2760 
LERIQFVGAC NPPTDPGRKP LSHRFLRHVP VVYVDYPGPA SLTQIYGTFN RAMLRLIPSL 

      2770       2780       2790       2800       2810       2820 
RTYAEPLTAA MVEFYTMSQE RFTQDTQPHY IYSPREMTRW VRGIFEALRP LETLPVEGLI 

      2830       2840       2850       2860       2870       2880 
RIWAHEALRL FQDRLVEDEE RRWTDENIDM VALKHFPNID KEKAMSRPIL YSNWLSKDYI 

      2890       2900       2910       2920       2930       2940 
PVDQEELRDY VKARLKVFYE EELDVPLVLF NEVLDHVLRI DRIFRQPQGH LLLIGVSGAG 

      2950       2960       2970       2980       2990       3000 
KTTLSRFVAW MNGLSVYQIK VHRKYTGEDF DEDLRTVLRR SGCKNEKIAF IMDESNVLDS 

      3010       3020       3030       3040       3050       3060 
GFLERMNTLL ANGEVPGLFE GDEYATLMTQ CKEGAQKEGL MLDSHEELYK WFTSQVIRNL 

      3070       3080       3090       3100       3110       3120 
HVVFTMNPSS EGLKDRAATS PALFNRCVLN WFGDWSTEAL YQVGKEFTSK MDLEKPNYIV 

      3130       3140       3150       3160       3170       3180 
PDYMPVVYDK LPQPPTHREA IVNSCVFVHQ TLHQANARLA KRGGRTMAIT PRHYLDFINH 

      3190       3200       3210       3220       3230       3240 
YANLFHEKRS ELEEQQMHLN VGLRKIKETV DQVEELRRAL RIKSQELEVK NAAANDKLKK 

      3250       3260       3270       3280       3290       3300 
MVKDQQEAEK KKVMSQEIQE QLHKQQEVIA DKQMSVKEDL DKVEPAVIEA QNAVKSIKKQ 

      3310       3320       3330       3340       3350       3360 
HLVEVRSMAN PPAAVKLALE SICLLLGEST TDWKQIRSII MRENFIPTIV NFSAEEISDA 

      3370       3380       3390       3400       3410       3420 
IREKMKKNYM SNPSYNYEIV NRASLACGPM VKWAIAQLNY ADMLKRVEPL RNELQKLEDD 

      3430       3440       3450       3460       3470       3480 
AKDNQQKANE VEQMIRDLEA SIARYKEEYA VLISEAQAIK ADLAAVEAKV NRSTALLKSL 

      3490       3500       3510       3520       3530       3540 
SAERERWEKT SETFKNQMST IAGDCLLSAA FIAYAGYFDQ QMRQNLFTTW SHHLQQANIQ 

      3550       3560       3570       3580       3590       3600 
FRTDIARTEY LSNADERLRW QASSLPADDL CTENAIMLKR FNRYPLIIDP SGQATEFIMN 

      3610       3620       3630       3640       3650       3660 
EYKDRKITRT SFLDDAFRKN LESALRFGNP LLVQDVESYD PVLNPVLNRE VRRTGGRVLI 

      3670       3680       3690       3700       3710       3720 
TLGDQDIDLS PSFVIFLSTR DPTVEFPPDL CSRVTFVNFT VTRSSLQSQC LNEVLKAERP 

      3730       3740       3750       3760       3770       3780 
DVDEKRSDLL KLQGEFQLRL RQLEKSLLQA LNEVKGRILD DDTIITTLEN LKREAAEVTR 

      3790       3800       3810       3820       3830       3840 
KVEETDIVMQ EVETVSQQYL PLSTACSSIY FTMESLKQVH FLYQYSLQFF LDIYHNVLYE 

      3850       3860       3870       3880       3890       3900 
NPNLKGATDH TQRLSVITKD LFQVAFNRVA RGMLHQDHIT FAMLLARIKL KGTMGEPTYD 

      3910       3920       3930       3940       3950       3960 
AEFQHFLRGK EIVLSAGSTP KVQGLTVEQA EAVARLSCLP AFKDLIAKVQ ADEQFGIWLE 

      3970       3980       3990       4000       4010       4020 
SSSPEQTVPY LWTEETPATP IGQAIHRLLL IQAFRPDRLL AMAHMFVSTN LGESFMSIME 

      4030       4040       4050       4060       4070       4080 
QPLDLTHIVG TEVKPNTPVL MCSVPGYDAS GHVEDLAAEQ NTQITSIAIG SAEGFNQADK 

      4090       4100       4110       4120       4130       4140 
AINTAVKSGR WVMLKNVHLA PGWLMQLEKK LHSLQPHACF RLFLTMEINP RVPVNLLRAG 

      4150       4160       4170       4180       4190       4200 
RIFVFEPPPG VKANMLRTFS SIPVSRMCKS PNERARLYFL LAWFHAVIQE RLRYAPLGWS 

      4210       4220       4230       4240       4250       4260 
KKYEFGESDL RSACDTVDTW LDDTAKGRQN ISPDKIPWSA LKTLMAQSIY GGRVDNEFDQ 

      4270       4280       4290       4300       4310       4320 
RLLNTFLERL FTTRSFDSEF KLACKVDGHK DIQMPDGIRR EEFVQWVELL PDAQTPSWLG 

      4330       4340       4350       4360       4370       4380 
LPNNAERVLL TTQGVDMISK MLKMQMLEDE DDLAYAETEK KTRTDFTSDG RPAWMRTLHT 

      4390       4400       4410       4420       4430       4440 
TASNWLHLIP QTLSPLKRTV ENIKDPLFRF FEREVKMGAK LLQDVRQDLA DVVQVCEGKK 

      4450       4460       4470       4480       4490       4500 
KQTNYLRTLI NELVKGILPR SWSHYTVPAG MTVIQWVSDF SERIKQLQNI SQAAAAGGAK 

      4510       4520       4530       4540       4550       4560 
ELKNIHVCLG ALFVPEAYIT ATRQYVAQAN SWSLEELCLE VNVTASQSTT LDACSFGVTG 

      4570       4580       4590       4600       4610       4620 
LKLQGATCSN NKLSLSNAIS TVLPLTQLRW GKQTSAEKKA SVVTLPVYLN FTRADLIFTV 

      4630       4640 
DFEIATKEDP RSFYERGVAV LCTE 

« Hide

References

[1]"The primary structure of rat brain (cytoplasmic) dynein heavy chain, a cytoplasmic motor enzyme."
Zhang Z., Tanaka Y., Nonaka S., Aizawa H., Kawasaki H., Nakata T., Hirokawa N.
Proc. Natl. Acad. Sci. U.S.A. 90:7928-7932(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Brain.
[2]"Molecular cloning of the retrograde transport motor cytoplasmic dynein (MAP 1C)."
Mikami A., Paschal B.M., Mazumdar M., Vallee R.B.
Neuron 10:787-796(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Brain.
[3]"HMW-2, the Sertoli cell cytoplasmic dynein from rat testis, is a dimer composed of nearly identical subunits."
Neely M.D., Erickson H.P., Boekelheide K.
J. Biol. Chem. 265:8691-8698(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[4]"Distinct but overlapping sites within the cytoplasmic dynein heavy chain for dimerization and for intermediate chain and light intermediate chain binding."
Tynan S.H., Gee M.A., Vallee R.B.
J. Biol. Chem. 275:32769-32774(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DYNC1LI1; DYNC1LI2 AND DYNC1I2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D13896 mRNA. Translation: BAA02996.1.
L08505 mRNA. Translation: AAA41103.1.
PIRA38905.
RefSeqNP_062099.3. NM_019226.3.
UniGeneRn.11027.

3D structure databases

ProteinModelPortalP38650.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid248131. 6 interactions.
IntActP38650. 4 interactions.
MINTMINT-4564742.

Chemistry

BindingDBP38650.
ChEMBLCHEMBL3694.

Proteomic databases

PaxDbP38650.
PRIDEP38650.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID29489.
KEGGrno:29489.
UCSCRGD:2511. rat.

Organism-specific databases

CTD1778.
RGD2511. Dync1h1.

Phylogenomic databases

eggNOGCOG5245.
HOGENOMHOG000176055.
HOVERGENHBG096595.
InParanoidP38650.
KOK10413.
PhylomeDBP38650.

Gene expression databases

GenevestigatorP38650.

Family and domain databases

Gene3D3.40.50.300. 5 hits.
InterProIPR003593. 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]
PANTHERPTHR10676. PTHR10676. 1 hit.
PfamPF07728. 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]
SMARTSM00382. AAA. 4 hits.
[Graphical view]
SUPFAMSSF52540. SSF52540. 5 hits.
ProtoNetSearch...

Other

NextBio609363.
PROP38650.

Entry information

Entry nameDYHC1_RAT
AccessionPrimary (citable) accession number: P38650
Secondary accession number(s): Q63178
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 11, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families