Q19020

SS
Gene name
dhc-1 (T21E12.4)
Protein name
Dynein heavy chain, cytoplasmic
Names
Dynein heavy chain, cytosolic , DYHC
Species
Caenorhabditis elegans
KEGG Pathway
cel:CELE_T21E12.4
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)

238-811 (Dynein Tail) SS

Target domain

1860-3038 (Motor domain)

Relief mechanism

Partner binding

Assay

1288-1685 (Dynein heavy chain linker) SS

Target domain

1860-3038 (Motor domain)

Relief mechanism

Partner binding

Assay

1827-4169 (Motor domain) SS

Target domain

1827-4169 (Motor domain in other dynein-1)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

0 structures for Q19020

Entry ID Method Resolution Chain Position Source

No variants for Q19020

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q19020

No associated diseases with Q19020

4 regional properties for Q19020

Type Name Position InterPro Accession
domain ACT domain 36 - 114 IPR002912
binding_site Aromatic amino acid hydroxylase, iron/copper binding site 281 - 292 IPR018301
domain Aromatic amino acid hydroxylase, C-terminal 106 - 452 IPR019774
domain Eukaryotic phenylalanine-4-hydroxylase, catalytic domain 119 - 424 IPR041912

Functions

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

10 GO annotations of cellular component

Name Definition
axon cytoplasm Any cytoplasm that is part of a axon.
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.
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.
kinetochore A multisubunit complex that is located at the centromeric region of DNA and provides an attachment point for the spindle microtubules.
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).
spindle The array of microtubules and associated molecules that forms between opposite poles of a eukaryotic cell during mitosis or meiosis and serves to move the duplicated chromosomes apart.
spindle pole Either of the ends of a spindle, where spindle microtubules are organized; usually contains a microtubule organizing center and accessory molecules, spindle microtubules and astral microtubules.
synapse The junction between an axon of one neuron and a dendrite of another neuron, a muscle fiber or a glial cell. As the axon approaches the synapse it enlarges into a specialized structure, the presynaptic terminal bouton, which contains mitochondria and synaptic vesicles. At the tip of the terminal bouton is the presynaptic membrane; facing it, and separated from it by a minute cleft (the synaptic cleft) is a specialized area of membrane on the receiving cell, known as the postsynaptic membrane. In response to the arrival of nerve impulses, the presynaptic terminal bouton secretes molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane.

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.

14 GO annotations of biological process

Name Definition
anterograde neuronal dense core vesicle transport The directed movement of substances in neuronal dense core vesicles along axonal microtubules towards the presynapse.
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 meiotic spindle orientation Any process that set the alignment of meiotic spindle relative to other cellular structures.
establishment of spindle localization The directed movement of the spindle to a specific location in the cell.
maintenance of centrosome location Any process in which a centrosome is maintained in a specific location within a cell and prevented from moving elsewhere.
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.
neuron remodeling The developmentally regulated remodeling of neuronal projections such as pruning to eliminate the extra dendrites and axons projections set up in early stages of nervous system development.
nuclear migration The directed movement of the nucleus to a specific location within a cell.
positive regulation of dense core granule transport Any process that activates or increases the frequency, rate or extent of dense core granule transport.
regulation of dendrite morphogenesis Any process that modulates the frequency, rate or extent of dendrite morphogenesis.
regulation of protein localization to synapse Any process that modulates the frequency, rate or extent of protein localization to synapse.
retrograde axonal transport The directed movement of organelles or molecules along microtubules from the cell periphery toward the cell body in nerve cell axons.
synaptic transmission, GABAergic The vesicular release of gamma-aminobutyric acid (GABA). from a presynapse, across a chemical synapse, the subsequent activation of GABA receptors at the postsynapse of a target cell (neuron, muscle, or secretory cell) and the effects of this activation on the postsynaptic membrane potential and ionic composition of the postsynaptic cytosol. This process encompasses both spontaneous and evoked release of neurotransmitter and all parts of synaptic vesicle exocytosis. Evoked transmission starts with the arrival of an action potential at the presynapse.
synaptic vesicle transport The directed movement of synaptic vesicles.

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
P38650 Dync1h1 Cytoplasmic dynein 1 heavy chain 1 Rattus norvegicus (Rat) SS
10 20 30 40 50 60
MDSGNESSII QPPNLKTAAE GDVKEYIVQV VTSHFGLSPR DQTTLDVELT AATTFITDFI
70 80 90 100 110 120
NEADKNVIVV DRVVAREQGD QPAGAESGGE ESAPATFQVH DGLFMTDRGQ AMMFVKQSNV
130 140 150 160 170 180
IEAEKKIATQ VSAFPLNGGS AWEQLHFLMS RLLNPYCKSF IGQSGRGERD GDKLAPTVQK
190 200 210 220 230 240
CFTEAEAALL HLQQNIDIPE INLVVNQHIL DAIEQAGKEN RRAKIEDLGD LVEDANFLNA
250 260 270 280 290 300
LQSGCNRWVK EIRKVTQLER DPSSGTSLQE MTFWLNLERA LLKISQKRDG EEVTLTLEAL
310 320 330 340 350 360
KCGKRFHATV GFDSDNGLKQ KLAVVQDYNT LMKEFPLSEL VSATDVPKLM HAVVGIFLHL
370 380 390 400 410 420
RKLRSTKYPL QRALRLVEAI SRDLNSQLLK VLSSYNLMRT PIAEFNEIMS QCQALFSKWD
430 440 450 460 470 480
DEYDKFIALL RDINKKKRDD PSKLSWKVTA VHKRLETRLM QILQFRKQHE QFRTVIERVL
490 500 510 520 530 540
RPVGNGSRER EQLMIDSSEG EKSPDEQVDI AYEFLKNVDF LDVDSPAWEN AFKRYEDQIG
550 560 570 580 590 600
VVETAITTRL KSQLESSRNS NEMFSIFSRY NALFIRPRIR GAIYEYQTRL INRVKEDINE
610 620 630 640 650 660
LQARFTKARG EQGVKIMQTV GLPPFSAKIM WIRNYERQLQ RYMKRVEDVL GKQWENHVDG
670 680 690 700 710 720
RQLKADGDNF KVKLNTQPMF DEWVESVQSQ NWTLPNKILT VDRVQVDGRM QLQLKINYHS
730 740 750 760 770 780
DSSVLYKEVS HLKSMGFRVP LKIVNWAHQA NQMRPSATSL IEAARTFASV NAALASVQGV
790 800 810 820 830 840
DSLLASYKKD IQNQLIEGAT LGWDSYKVDQ YQLKLAETVN TYQERCEELL NVVRIVNADL
850 860 870 880 890 900
NVLKSCRYDK ETIENLLTSI QKGVDQLSLG NYSNLAQWVN TLDRQIETIL ARRVEDAIRV
910 920 930 940 950 960
WTLVFSQSEE VEELRERQVV LPTVKNVVVD LCMTAQTLYI SPSTRETREK ILEQLYEWHS
970 980 990 1000 1010 1020
VCTAQMRISG KRFQMVMNEE IEPETYHNIL NVMPEGQACL EKAYDCVNGI MSDLEEYLSE
1030 1040 1050 1060 1070 1080
WLSYQSLWVL QAEQLFEMLG TSLSKWMKTL MEIRKGRLVF DTQDTRKVIF PVSVEYGKAQ
1090 1100 1110 1120 1130 1140
QKILFKYDYW HKEMLVKFGA VVGDEMQKFF NSVSKWRNVL ETQSVDGGST SDTIGLISFV
1150 1160 1170 1180 1190 1200
QSLKKQTKSG QDAVDLYRSS QRLLNQQRYQ FPAQWLYSEN VEGEWSAFTE ILSLRDASIQ
1210 1220 1230 1240 1250 1260
TQMMNLQTKF AQEDELVEKR TVETLTEWNK SKPVEGAQRP QEALNVITAF EAKLNKLTEE
1270 1280 1290 1300 1310 1320
RNKMRKARVA LDLSDSAHAP SEGDKLTVAT EELAAMKDVW KALQPVYTGI DEAKEKTWLS
1330 1340 1350 1360 1370 1380
VQPRKIRQSL DELMNQLKQL PVKCRTYKSY EHVKQMLHTY GKMNMLVAEL KSEALKERHW
1390 1400 1410 1420 1430 1440
HQMMKEMRVN WNLSDLTLGQ VWDADILRHE HTIKKILLVA QGEMALEEFL REMREYWQNY
1450 1460 1470 1480 1490 1500
EVELVNYQNK TRLIKGWDDL FNKLKEHQNS LSAMKLSPYY KQFEESAQSW DEKLNKINAM
1510 1520 1530 1540 1550 1560
FDVWIDVQRR WVYLEGLFSG SAEISTLLPF ESSRFATITT DVLALMKKVA ASPRILDVVN
1570 1580 1590 1600 1610 1620
MQGAQRLLER LADMLAKIQK ALGEYLERER SSFPRFYFVG DEDLLEIMGN SKDITRIQKH
1630 1640 1650 1660 1670 1680
LKKMFAGITA IDINEEDRSI TAFHSREGEK VDLVKIVSTK DVRINDWLQA LEAEMKHTLA
1690 1700 1710 1720 1730 1740
RQLAASLTHF SKMNIQTMTT DDYVEWLDKF PAQVITLTAE IWWCDEMEKT LADGKGAENV
1750 1760 1770 1780 1790 1800
EQAVVKTLEL LADSVLKEQP PIRRKKMEAL ITELVHKRDT CRKLVSMKIR AANDFGWLQC
1810 1820 1830 1840 1850 1860
MRFYFDPKQV DPVRCCVVKM ANSQFFYGFE YLGIQERLVR TPLTDRCYLT MTQALHSRLG
1870 1880 1890 1900 1910 1920
GSPFGPAGTG KTESVKALGH QLGRFVLVFN CDETFDFQAM GRILVGLCQV GAWGCFDEFN
1930 1940 1950 1960 1970 1980
RLEERMLSAV SQQIQTIQEA VRAGGDMSVD LVGKRLNVNS NIGIFITMNP GYSGRSNLPD
1990 2000 2010 2020 2030 2040
NLKQLFRSLA MTQPDRQLIA QVMLFSQGFR TAETLANKIV PLFILCKEQL SDQCHYDFGL
2050 2060 2070 2080 2090 2100
RALKYVLVSA GNIKRDKLDK MGSAALEDVA EQQMLIQSVC ETLVPKLVNE DIALLFSLLS
2110 2120 2130 2140 2150 2160
DVFPGIHYTA NQMRELRQQL STVCDEHLLI YSDVQGEMGS MWLDKVLQLY QITNLNHGLM
2170 2180 2190 2200 2210 2220
LVGSSGSGKT MAWKVLLKAL ERWENVEGVA HVIDAKAMSK DSLYGVMDPN TREWTDGLFT
2230 2240 2250 2260 2270 2280
SVIRKIIDNV RGEADRRQWI IFDGDVDPEW VENLNSVLDD NKLLTLPNGE RLSIPPNVRI
2290 2300 2310 2320 2330 2340
IFEVADLKYA TLATVSRCGM VWFSEEVVTS EMLFERYLSI IRRVPLDSDS AISFSSSSAP
2350 2360 2370 2380 2390 2400
VNLIGEDAKP TRSIEIQRTA ALALQTHFSP DGIVPGSLKY AVSELEHIMP PTPQRLLSSF
2410 2420 2430 2440 2450 2460
FSMMSYSIRK IVSHDEGLID DSVEIDQIQS FVLRSMLTNL VWAFSGDGKW KSREMMSDFI
2470 2480 2490 2500 2510 2520
RQATTISLPP NQQACLIDYE VQLSGDWQPW LSKVPTMEIE SHRVAAADLV VPTIDTVRHE
2530 2540 2550 2560 2570 2580
MLLAAWLAEH KPLVLCGPPG SGKTMTLLAA LRSQQEMEVV NVNFSSSTTP ELLLRTFDHY
2590 2600 2610 2620 2630 2640
CEYRRTPNGV VLAPVQLSQW LVIFCDEINL PAPDKYGTQR VISFLRQLVE LNGFYRTSDH
2650 2660 2670 2680 2690 2700
SWVSLERIQF VGACNPPTDP GRHPMTSRFL RHVPIVYVDY PGQTSLQQIY GTFNRAMLKM
2710 2720 2730 2740 2750 2760
TPAVRGLADQ LTNAMVDVYL ASQEHFTQDD QPHYVYSPRE LTRWVRGISE AITPLESLSA
2770 2780 2790 2800 2810 2820
EQLVRLWAHE AIRLFQDRLV TEEEREWTDK LVDTTAERYF GNACRLDEAL KRPLLYSCWL
2830 2840 2850 2860 2870 2880
SRNYVPVTRE ELQDYVSARL KGFYEEELDV KLVLFDQMLD HVLRIDRIYR QSQGHLLLIG
2890 2900 2910 2920 2930 2940
TAGAGKTTLS RFVAWLNGLS VFQLKVHSKY TAADFDEDMR TVLRRAGCRN EKLCFIMDES
2950 2960 2970 2980 2990 3000
NMLDTGFLER LNTLLANGEV PGLFEGDEHT TLMTQIKEGA QRQGLILDSH DELYKWFTQQ
3010 3020 3030 3040 3050 3060
VMRNLHVVFT MNPSGSGLRE RASTSPALFN RCVLNWFGDW SENALYQVGS ELTRTMDLDR
3070 3080 3090 3100 3110 3120
TDYEGSVRLT PSCELVPSQP TYRDAVVNTL CLVHKTVQKF NEMETKKGHR VMACTPRHFL
3130 3140 3150 3160 3170 3180
DFIKQFMSLF HEKRSDLEEE KIHLNIGLNK ISETEEQVKE LQKSLKLKSN ELQEKKEAAN
3190 3200 3210 3220 3230 3240
LKLKEMLGDQ QKAEEEKKFS EQLQKELAEQ LKQMAEKKTF VENDLAQVEP AVAEAQTAVQ
3250 3260 3270 3280 3290 3300
GIKKSQLVEV KSMSSPPVTV KLTLEAICIL LGENVGTDWK AIRQVMMKDD FMTRILQFDT
3310 3320 3330 3340 3350 3360
ELLTPEILKQ MEKYIQNPDW EFDKVNRASV ACGPMVKWAR AQLLYSTMLH KVEPLRNELK
3370 3380 3390 3400 3410 3420
RLEQEAAKKT QEGKVVDVRI TELEESIGKY KEEYAQLIGQ AENIKQDLLS VQEKVNRSTE
3430 3440 3450 3460 3470 3480
LLSSLRSERD RWSSGSAGFS QQMDSLVGDA LLSSAFLAYA GYYDQMLRDE IFHKWFNHVV
3490 3500 3510 3520 3530 3540
NAGLHFRHDL ARIEYLSTVD DRLQWQLNSL PVDDLCTENA IMLHRFNRYP LIIDPSGQAV
3550 3560 3570 3580 3590 3600
EYIMKQFAGK NIQKTSFLDE SFRKNLESAL RFGNSLLVQD VEAYDPILNP VLNREVKRAG
3610 3620 3630 3640 3650 3660
GRVLITIGDQ DIDLSPSFQI FMITRDSTVE FSPDICSRVT FVNFTVTSSS LASQCLNQVL
3670 3680 3690 3700 3710 3720
RSERPDVDKK RNDLLKLQGE FAVRLRHLEK ALLAALNESK GKILDDNSVI ETLEKLKNEA
3730 3740 3750 3760 3770 3780
AEVAQKSAET DKVMAEVDAV SAQYQRLSTA CSHIYHTLQQ LNEIHFLYHY SLDFLVEIFT
3790 3800 3810 3820 3830 3840
HVLKTPELSS TTDYAKRLRI ITTSLFQTVF RRVSRGMLHT DKVLLALLLM RIHIRSNPSA
3850 3860 3870 3880 3890 3900
PAYEQHFDLL LGRSDFVAKN DEADSTIPGG LDFLTVENKK SIAKARKVVG FENVFAHLQH
3910 3920 3930 3940 3950 3960
NSAAVTSWLT NDNPESNVPV VWDDADGKLS PLCIAMNSLI VVHALRPDRL MASAHRVVST
3970 3980 3990 4000 4010 4020
AFDDHFMQQD KVVDILSIVD NEVSPSEPVL LCSATGYDAS GKIEDLAVET NRQLTSIAIG
4030 4040 4050 4060 4070 4080
SAEGFNQADS ALGTATKSGR WVLLKNVHLA PSWLAQLEKR LHSMKPHAQF RLFLTAEIHP
4090 4100 4110 4120 4130 4140
KLPSSILRAS RVVVFEPATG LKANLLRSLS SIPPQRLTKA PTERSRLYLL VCWLHALVQE
4150 4160 4170 4180 4190 4200
RLRYTPLGWS TAYEFSDADL RVACDTLDAA VDAVAQGRPN VEPERLPWTT LRTLLSQCIY
4210 4220 4230 4240 4250 4260
GGKIDNQFDQ VLLDCVLENL FTAKSFEQDH VLIPKYDGDD SLFTPNMSKK DQMIGWVEEL
4270 4280 4290 4300 4310 4320
KNEQLPAWLG LPNNAEKVLL TKRGESMLRN MLKVTDEELA FNEDGKEEVK PQWMAQLGEL
4330 4340 4350 4360 4370 4380
AKQWLQLLPK EIVKMRRTVE NIKDPLFRFF EREVNLGSQL LKDIRRDLNE ISAVCRAEKK
4390 4400 4410 4420 4430 4440
QNNETRALAA SLQKGEVPTG WKRYTVPREV TVMDWMTDLN ERLKQLIRIG GADNLKRETF
4450 4460 4470 4480 4490 4500
WLGGTFSPEA YITATRQQVA QANTWSLEQL NLHIHIGRTD STDVFRISGI DIRGAKSVGG
4510 4520 4530 4540 4550 4560
NKLELCELVK SECDIVEFSW KQDVADGTRL PLYLYGDRRQ LISPLAFHLS SATVFYQRGV
ALVANSTL