P38650

SS
Gene name
Dync1h1 (Dhc1, Dnch1, Dnchc1, Dnec1, Dyhc, Map1c)
Protein name
Cytoplasmic dynein 1 heavy chain 1
Names
Cytoplasmic dynein heavy chain 1 , Dynein heavy chain, cytosolic , MAP 1C
Species
Rattus norvegicus (Rat)
KEGG Pathway
rno:29489
EC number
Protein Class

Descriptions

Cytoplasmic dynein (dynein hereafter) is an AAA+ motor responsible for nearly all motility and force generation towards the microtubule (MT) minus-end and involved in a wide variety of cellular functions, such as positioning of intracellular organelles, breakdown of the nuclear envelope and assembly of the mitotic spindle. The partial loss of dynein function has been implicated in a range of neurodegenerative and neurodevelopmental conditions, including spinal muscular atrophy, amyotrophic lateral sclerosis, Alzheimer's disease, and schizophrenia. <br>The core of the dynein complex is a homodimer of two heavy chains, the C-terminal motor domain of which is a catalytic ring of six AAA modules (AAA1-6). Dynein's MT binding domain is separated from the catalytic domain by a coiled-coil stalk. When dynein is not bound to its cargo, it forms two distinct conformations, the phi-particle, and open conformations, both of which move poorly along MTs. Formation of a dynein-dynactin-cargo adaptor complex aligns the dynein motor domains in a parallel conformation and activates processive motility along MTs. <br>Lissencephaly-1 (Lis-1) promotes the formation of the active complex with dynactin and also favors the recruitment of two dyneins to dynactin, resulting in increased velocity, higher force production and more effective competition against kinesin. Lis-1 binds to release dynein from its autoinhibited state and dissociates form motile complexes, indicating that its primary role is to orchestrate the assembly of the transport machinery.

Autoinhibitory domains (AIDs)

240-830 (Dynein Tail) SS

Target domain

1899-3093 (Motor domain)

Relief mechanism

Partner binding

Assay

1319-1717 (Dynein heavy chain linker) SS

Target domain

1899-3093 (Motor domain)

Relief mechanism

Partner binding

Assay

1866-4219 (Motor domain) SS

Target domain

1866-4219 (Motor domain in other dynein-1)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

0 structures for P38650

Entry ID Method Resolution Chain Position Source

No variants for P38650

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P38650

No associated diseases with P38650

15 regional properties for P38650

Type Name Position InterPro Accession
domain AAA+ ATPase domain 1899 - 2043 IPR003593-1
domain AAA+ ATPase domain 2214 - 2365 IPR003593-2
domain AAA+ ATPase domain 2585 - 2735 IPR003593-3
domain AAA+ ATPase domain 2927 - 3093 IPR003593-4
domain Dynein heavy chain region D6 P-loop domain 4035 - 4142 IPR004273
domain Dynein heavy chain, tail 240 - 830 IPR013594
domain Dynein heavy chain, linker 1320 - 1717 IPR013602
domain Dynein heavy chain, AAA module D4 2906 - 3184 IPR024317
domain Dynein heavy chain, coiled coil stalk 3199 - 3530 IPR024743
domain Dynein heavy chain, hydrolytic ATP-binding dynein motor region 1866 - 2229 IPR035699
domain Dynein heavy chain, ATP-binding dynein motor region 3559 - 3778 IPR035706
domain Dynein heavy chain, C-terminal domain 4332 - 4642 IPR041228
domain Dynein heavy chain, AAA 5 extension domain 2422 - 2547 IPR041466
domain Dynein heavy chain AAA lid domain 4175 - 4325 IPR041658
domain Dynein 2 heavy chain 1, cytoplasmic, ATPase lid domain 2749 - 2841 IPR054354

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm, cytoskeleton
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

14 GO annotations of cellular component

Name Definition
axon The long process of a neuron that conducts nerve impulses, usually away from the cell body to the terminals and varicosities, which are sites of storage and release of neurotransmitter.
axon cytoplasm Any cytoplasm that is part of a axon.
axonemal dynein complex A dynein complex found in eukaryotic cilia and flagella; the motor domain heads interact with adjacent microtubules to generate a sliding force which is converted to a bending motion.
cell cortex The region of a cell that lies just beneath the plasma membrane and often, but not always, contains a network of actin filaments and associated proteins.
centrosome A structure comprised of a core structure (in most organisms, a pair of centrioles) and peripheral material from which a microtubule-based structure, such as a spindle apparatus, is organized. Centrosomes occur close to the nucleus during interphase in many eukaryotic cells, though in animal cells it changes continually during the cell-division cycle.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytoplasmic dynein complex Any dynein complex with a homodimeric dynein heavy chain core that catalyzes movement along a microtubule. Cytoplasmic dynein complexes participate in many cytoplasmic transport activities in eukaryotes, such as mRNA localization, intermediate filament transport, nuclear envelope breakdown, apoptosis, transport of centrosomal proteins, mitotic spindle assembly, virus transport, kinetochore functions, and movement of signaling and spindle checkpoint proteins. Some complexes participate in intraflagellar transport. Subunits associated with the dynein heavy chain mediate association between dynein heavy chain and cargoes, and may include light chains and light intermediate chains.
cytoplasmic microtubule Any microtubule in the cytoplasm of a cell.
dynein complex Any of several large complexes that contain two or three dynein heavy chains and several light chains, and have microtubule motor activity.
filopodium Thin, stiff, actin-based protrusion extended by the leading edge of a motile cell such as a crawling fibroblast or amoeba, or an axonal or dendritic growth cone, or a dendritic shaft.
manchette A tubular array of microtubules that extends from the perinuclear ring surrounding the spermatid nucleus to the flagellar axoneme. The manchette may also contain F-actin filaments.
microtubule Any of the long, generally straight, hollow tubes of internal diameter 12-15 nm and external diameter 24 nm found in a wide variety of eukaryotic cells; each consists (usually) of 13 protofilaments of polymeric tubulin, staggered in such a manner that the tubulin monomers are arranged in a helical pattern on the microtubular surface, and with the alpha/beta axes of the tubulin subunits parallel to the long axis of the tubule; exist in equilibrium with pool of tubulin monomers and can be rapidly assembled or disassembled in response to physiological stimuli; concerned with force generation, e.g. in the spindle.
neuronal cell body The portion of a neuron that includes the nucleus, but excludes cell projections such as axons and dendrites.
nuclear envelope The double lipid bilayer enclosing the nucleus and separating its contents from the rest of the cytoplasm; includes the intermembrane space, a gap of width 20-40 nm (also called the perinuclear space).

5 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP hydrolysis activity Catalysis of the reaction
dynein intermediate chain binding Binding to an intermediate chain of the dynein complex.
dynein light intermediate chain binding Binding to a light intermediate chain of the dynein complex.
minus-end-directed microtubule motor activity A motor activity that generates movement along a microtubule toward the minus end, driven by ATP hydrolysis.

16 GO annotations of biological process

Name Definition
cell division The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells.
cellular response to 3,3',5-triiodo-L-thyronine Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a 3,3',5-triiodo-L-thyronine stimulus.
cellular response to nerve growth factor stimulus A process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a nerve growth factor stimulus.
cytoplasmic microtubule organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of structures formed of microtubules and associated proteins in the cytoplasm of a cell.
establishment of spindle localization The directed movement of the spindle to a specific location in the cell.
mitotic spindle organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the microtubule spindle during a mitotic cell cycle.
nuclear migration The directed movement of the nucleus to a specific location within a cell.
P-body assembly The aggregation, arrangement and bonding together of proteins and RNA molecules to form a cytoplasmic mRNA processing body.
positive regulation of cold-induced thermogenesis Any process that activates or increases the frequency, rate or extent of cold-induced thermogenesis.
positive regulation of intracellular transport Any process that activates or increases the frequency, rate or extent of the directed movement of substances within cells.
positive regulation of spindle assembly Any process that activates or increases the frequency, rate or extent of spindle assembly.
regulation of metaphase plate congression Any process that modulates the rate, frequency, or extent of metaphase plate congression, the alignment of chromosomes at the metaphase plate, a plane halfway between the poles of the spindle.
regulation of mitotic spindle organization Any process that modulates the rate, frequency or extent of the assembly, arrangement of constituent parts, or disassembly of the microtubule spindle during a mitotic cell cycle.
retrograde axonal transport The directed movement of organelles or molecules along microtubules from the cell periphery toward the cell body in nerve cell axons.
spermatid development The process whose specific outcome is the progression of a spermatid over time, from its formation to the mature structure.
stress granule assembly The aggregation, arrangement and bonding together of proteins and RNA molecules to form a stress granule.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P36022 DYN1 Dynein heavy chain, cytoplasmic Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) EV
P37276 Dhc64C Dynein heavy chain, cytoplasmic Drosophila melanogaster (Fruit fly) SS
Q14204 DYNC1H1 Cytoplasmic dynein 1 heavy chain 1 Homo sapiens (Human) EV
Q9JHU4 Dync1h1 Cytoplasmic dynein 1 heavy chain 1 Mus musculus (Mouse) SS
Q19020 dhc-1 Dynein heavy chain, cytoplasmic Caenorhabditis elegans SS
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