ID I3MDW3_ICTTR Unreviewed; 4615 AA.
AC I3MDW3;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 24-JAN-2024, entry version 73.
DE SubName: Full=Dynein cytoplasmic 1 heavy chain 1 {ECO:0000313|Ensembl:ENSSTOP00000008629.3};
GN Name=DYNC1H1 {ECO:0000313|Ensembl:ENSSTOP00000008629.3};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000008629.3, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000008629.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the dynein heavy chain family.
CC {ECO:0000256|ARBA:ARBA00008887}.
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DR EMBL; AGTP01111535; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01111536; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 43179.ENSSTOP00000008629; -.
DR Ensembl; ENSSTOT00000009619.3; ENSSTOP00000008629.3; ENSSTOG00000009558.3.
DR eggNOG; KOG3595; Eukaryota.
DR GeneTree; ENSGT00940000156103; -.
DR HOGENOM; CLU_000038_1_2_1; -.
DR InParanoid; I3MDW3; -.
DR TreeFam; TF335573; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IEA:Ensembl.
DR GO; GO:0030175; C:filopodium; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0045505; F:dynein intermediate chain binding; IEA:InterPro.
DR GO; GO:0051959; F:dynein light intermediate chain binding; IEA:Ensembl.
DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; IEA:Ensembl.
DR GO; GO:0051293; P:establishment of spindle localization; IEA:Ensembl.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0033962; P:P-body assembly; IEA:Ensembl.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IEA:Ensembl.
DR GO; GO:0032388; P:positive regulation of intracellular transport; IEA:Ensembl.
DR GO; GO:1905832; P:positive regulation of spindle assembly; IEA:Ensembl.
DR GO; GO:0090235; P:regulation of metaphase plate congression; IEA:Ensembl.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; IEA:Ensembl.
DR GO; GO:0034063; P:stress granule assembly; IEA:Ensembl.
DR CDD; cd00009; AAA; 2.
DR Gene3D; 1.10.287.2620; -; 1.
DR Gene3D; 1.10.472.130; -; 1.
DR Gene3D; 1.10.8.1220; -; 1.
DR Gene3D; 1.10.8.710; -; 1.
DR Gene3D; 1.20.1270.280; -; 1.
DR Gene3D; 1.20.58.1120; -; 1.
DR Gene3D; 1.20.920.20; -; 2.
DR Gene3D; 1.20.920.30; -; 1.
DR Gene3D; 1.20.920.60; -; 1.
DR Gene3D; 3.10.490.20; -; 1.
DR Gene3D; 6.10.140.1060; -; 1.
DR Gene3D; 1.20.140.100; Dynein heavy chain, N-terminal domain 2; 1.
DR Gene3D; 3.20.180.20; Dynein heavy chain, N-terminal domain 2; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 5.
DR Gene3D; 1.10.8.720; Region D6 of dynein motor; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR035699; AAA_6.
DR InterPro; IPR035706; AAA_9.
DR InterPro; IPR041658; AAA_lid_11.
DR InterPro; IPR042219; AAA_lid_11_sf.
DR InterPro; IPR026983; DHC_fam.
DR InterPro; IPR042222; Dynein_2_N.
DR InterPro; IPR043157; Dynein_AAA1S.
DR InterPro; IPR041466; Dynein_AAA5_ext.
DR InterPro; IPR041228; Dynein_C.
DR InterPro; IPR043160; Dynein_C_barrel.
DR InterPro; IPR024743; Dynein_HC_stalk.
DR InterPro; IPR024317; Dynein_heavy_chain_D4_dom.
DR InterPro; IPR004273; Dynein_heavy_D6_P-loop.
DR InterPro; IPR013602; Dynein_heavy_linker.
DR InterPro; IPR013594; Dynein_heavy_tail.
DR InterPro; IPR042228; Dynein_linker_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR45703; DYNEIN HEAVY CHAIN; 1.
DR PANTHER; PTHR45703:SF23; DYNEIN HEAVY CHAIN, CYTOPLASMIC; 1.
DR Pfam; PF12774; AAA_6; 1.
DR Pfam; PF12775; AAA_7; 1.
DR Pfam; PF12780; AAA_8; 1.
DR Pfam; PF12781; AAA_9; 1.
DR Pfam; PF18198; AAA_lid_11; 1.
DR Pfam; PF08385; DHC_N1; 1.
DR Pfam; PF08393; DHC_N2; 1.
DR Pfam; PF17852; Dynein_AAA_lid; 1.
DR Pfam; PF18199; Dynein_C; 1.
DR Pfam; PF03028; Dynein_heavy; 1.
DR Pfam; PF12777; MT; 1.
DR SMART; SM00382; AAA; 4.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Dynein {ECO:0000256|ARBA:ARBA00023017};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1870..2014
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 2185..2336
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 2556..2706
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 2898..3064
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2359..2380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1155..1182
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 3174..3222
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 3371..3468
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2359..2377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 4615 AA; 529149 MW; 31306A3FAA81FE6D CRC64;
LRFHPGGQAR SASAGLTVRR LGPRPDGGEA PAALEAALEE KSALEQMRKF LSDPQVHTVL
VERSTLKEDV GDEGEEEKEF ISYNINIDIH YGVKSNSLAF IKRTPVIDAD KPVSSQLRVL
TLSEDSPYET LHSFISNAVA PFFKSYIRES GKADRDGDKM APSVEKKIAE LEMGLLHLQQ
NIEIPEISLP IHPIITNVAK QCYERGEKPK VTDFGDKVED PTFLNQLQSG VNRWIREIQK
VTKLDRDPAS GTALQEISFW LNLERALYRI QEKRESPEVL LTLDILKHGK RFHATVSFDT
DTGLKQALET VNDYNPLMKD FPLNDLLSAT ELDKIRQALV AIFTHLRKIR NTKYPIQRAL
RLVEAISRDL SSQLLKVLGT RKLMHVAYEE FEKVMVACFE VFQTWDDEYE KLQVLLRDIV
KRKREENLKM VWRINPAHRK LQARLDQMRK FRRQHEQLRA VIVRVLRPQV TAVAQQNQGE
VPEPQDMKVA EVLFDAADAN AIEEVNLAYE NVKEVDGLDV SKEGTEAWEA AMKRYDERID
RVETRITARL RDQLGTAKNA NEMFRIFSRF NALFVRPHIR GAIREYQTQL IQRVKDDIES
LHDKFKVQYP QSQACKMSHV RDLPPVSGSI IWAKQIDRQL TAYMKRVEDV LGKGWENHVE
GQKLKQDGDS FRMKLNTQEI FDDWARKVQQ RNLGVSGRIF TIESTRVRGR TGNVLKLKVN
FLPEIITLSK EVRNLKWLGF RVPLAIVNKA HQANQLYPFA ISLIESVRTY ERTCEKVEER
NTISLLVAGL KKEVQALIAE GIALVWESYK LDPYVQRLAE TVFNFQEKVD DLLIIEEKID
LEVRSLETCM YDHKTFSEIL NRVQKAVDDL NLHSYSNLPI WVNKLDMEIE RILGVRLQAG
LRAWTQVLLG QAEDKAEVDM DTDAPQVSHK PGGEPKIKNV VHELRITNQV IYLNPPIEEC
RYKLYQEMFA WKMVVLSLPR IQSQRYQVGV HYELTEEEKF YRNALTRMPD GPVALEESYS
AVMGIVTEVE QYVKVWLQYQ CLWDMQAENI YNRLGEDLNK WQALLVQIRK ARGTFDNAET
KKEFGPVVID YGKVQSKVNL KYDSWHKEVL SKFGQMLGSN MTEFHSQISK SRQELEQHSV
DTASTSDAVT FITYVQSLKR KIKQFEKQVE LYRNGQRLLE KQRFQFPPSW LYIDNIEGEW
GAFNDIMRRK DSAIQQQVAN LQMKIVQEDR AVESRTTDLL TDWEKTKPVT GNLRPEEALQ
ALTIYEGKFG RLKDDREKCA KAKEALELTD SGLLSGSEER VQVALEELQD LKGVWSELSK
VWEQIDQMKE QPWVSVQPRK VGLYQLQTSF RNLAKFIRCH LMSYVNMLVI ELKSEALKDR
HWKQLMKRLH VNWVVSELTL GQIWDVDLQK NEAIVKDVLL VAQGEMALEE FLKQIREVWN
TYELDLVNYQ NKCRLIRGWD DLFNKVKEHI NSVSAMKLSP YYKVFEEDAL SWEDKLNRIM
ALFDVWIDVQ RRWVYLEGIF TGSADIKHLL PVETQRFQSI STEFLALMKK VSKSPLVMDV
LNIQGVQRSL ERLADLLGKI QKALGEYLER ERSSFPRFYF VGDEDLLEII GNSKNVAKLQ
KHFKKMFAGV SSIILNEDNS VVLGISSREG EEVMFKTPVS ITEHPKINEW LTLVEKEMRV
TLAKLLAESV TEVEIFGKAT SIDPNTYITW IDKYQAQLVV LSAQIAWSEN VESALSNVGG
GGDAAPLHSV LSNVEATLNV LADSVLMEQP PLRRRKLEHL ITELVHQRDV TRSLIKSKID
NAKSFEWLSQ MRFYFDPKQT DVLQQLSIQM ANAKFNYGFE YLGVQDKLVQ TPLTDRCYLT
MTQALEARLG GSPFGPAGTG KTESVKALGH QLGRFVLVFN CDETFDFQAM GRIFVGLCQV
GAWGCFDEFN RLEERMLSAV SQQVQCIQEA LREHSNPNYD KTSAPITCEL LNKQVKVSPD
MAIFITMNPG YAGRSNLPDN LKKLFRSLAM TKPDRQLIAQ VMLYSQGFRT AEVLANKIVP
FFKLCDEQLS SQSHYDFGLR ALKSVLVSAG NVKRERIQKI KREKEERGEA VDEGEIAENL
PEQEILIQSV CETMVPKLVA EDIPLLFSLL SDVFPGVQYH RGEMTALREE LKKVCQEMYL
TYGDGEEVGG MWVEKVLQLY QITQINHGLM MVGPSGSGKS MAWRVLLKAL ERLEGVEGVA
HIIDPKAISK DHLYGTLDPN TREWTDGLFT HVLRKIIDNV RGELQKRQWI VFDGDVDPEW
VENLNSVLDD NKLLTLPNGE RLSLPPNVRI MFEVQDLKYA TLATVSRCGM VWFSEDVLST
DMIFNNFLAR LRSIPLDEGE DEAQRRRKGK EDEGEEAASP MLQIQRDAAT IMQPYFTSNG
LVTKALEHAF QLEHIMDLTR LRCLGSLFSM LHQACRNVAQ YNANHPDFPM QIEQLERYIQ
RYLVYAILWS LSGDSRLKMR AELGEYIRRI TTVPLPTAPN IPIIDYEVSI SGEWSPWQAK
VPQIEVETHK VAAPDVVVPT LDTVRHEALL YTWLAEHKPL VLCGPPGSGK TMTLFSALRA
LPDMEVVGLN FSSATTPELL LKTFDHYCEY RRTPNGVVLA PVQLGKWLVL FCDEINLPDM
DKYGTQRVIS FIRQMVEHGG FYRTSDQTWV KLERIQFVGA CNPPTDPGRK PLSHRFLRHV
PVVYVDYPGP ASLTQIYGTF NRAMLRLIPS LRTYAEPLTA AMVEFYTMSQ ERFTQDTQPH
YIYSPREMTR WVRGIFEALR PLETLPVEGL IRIWAHEALR LFQDRLVEDE ERRWTDENID
MVALKHFPNI DKEKAMSRPI LYSNWLSKDY IPVDQEELRD YVKARLKVFY EEELDVPLVL
FNEVLDHVLR IDRIFRQPQG HLLLIGVSGA GKTTLSRFVA WMNGLSVYQI KVHRKYTGED
FDEDLRTVLR RSGCKNEKIA FIMDESNVLD SGFLERMNTL LANGEVPGLF EGDEYATLMT
QCKEGAQKEG LMLDSHEELY KWFTSQVIRN LHVVFTMNPS SEGLKDRAAT SPALFNRCVL
NWFGDWSTEA LYQVGKEFTS KMDLEKPNYI VPDYMPVVYD KLPQPPSHRE AIVNSCVFVH
QTLHQANARL AKRGGRTMAI TPRHYLDFIN HYANLFHEKR SELEEQQMHL NVGLRKIKET
VDQVEELRRD LRIKSQELEV KNAAANDKLK KMVKDQQEAE KKKVMSQEIQ EQLHKQQEVI
ADKQMSVKED LDKVEPAVIE AQNAVKSIKK QHLVEVRSMA NPPAAVKLAL ESICLLLGES
TTDWKQIRSI IMRENFIPTI VNFSAEEISD AIREKMKKNY MSNPSYNYEI VNRASLACGP
MVKWAIAQLN YADMLKRVEP LRNELQKLED DAKDNQQKAN EVEQMIRDLE ASIARYKEEY
AVLISEAQAI KADLAAVEAK VNRSTALLKS LSAERERWEK TSETFKNQMS TIAGDCLLSA
AFIAYAGYFD QQMRQNLFTT WSHHLQQANI QFRTDIARTE YLSNADERLR WQASSLPADD
LCTENAIMLK RFNRYPLIID PSGQATEFIM NEYKDRKITR TSFLDDAFRK NLESALRFGN
PLLVQDVESY DPVLNPVLNR EVRRTGGRVL ITLGDQDIDL SPSFVIFLST RDPTVEFPPD
LCSRVTFVNF TVTRSSLQSQ CLNEVLKAER PDVDEKRSDL LKLQGEFQLR LRQLEKSLLQ
ALNEVKGRIL DDDTIITTLE NLKREAAEVT RKVEETDIVM QEVETVSQQY LPLSTACSSI
YFTMESLKQI HFLYQYSLQF FLDIYHNVLY ENPNLKGITD HTQRLSIITK DLFQVAFNRV
ARGMLHQDHI TFAMLLARIK LKGTMGEPTY DAEFQHFLRG KEMVLSAGST PKIQGLTVEQ
AEAVVRLSCL PAFRDLISKI QADEQFGIWL DSSSPEQTVP YLWSEETPAT PIGQAVHRLL
LIQAFRPDRL LAMAHVFVST NLGESFMSIM EQPLDLTHIV GTEVKPNTPV LMCSVPGYDA
SGHVEDLAAE QNTQITSIAI GSAEGFNQAD KAINTAVKSG RWVMLKNVHL APGWLMQLEK
KLHSLQPHAC FRLFLTMEIN PKVPVNLLRA GRIFVFEPPP GVKANMLRTF SSIPVSRICK
SPNERARLYF LLAWFHAVIQ ERLRYAPLGW SKKYEFGESD LRSACDTVDT WLDDTAKGRQ
NISPDKIPWS ALKTLMAQSI YGGRVDNEFD QRLLNTFLER LFTTRSFDSE FKLACKVDGH
KDIQMPDGIR REEFVQWVEL LPDTQTPSWL GLPNNAERVL LTTQGVDMIS KMLKMQMLED
EDDLAYAETE KKTRTDSTSD GRPAWMRTLH TTASNWLHLI PQTLSHLKRT VENIKDPLFR
FFEREVKMGA KLLQDVRQDL ADVVQVCEGK KKQTNYLRTL INELVKGILP RSWSHYTVPA
GMTVIQWVSD FSERIKQLQN ISLAAASGGA KELKNIHVCL GGLFVPEAYI TATRQYVAQA
NSWSLEELCL EVNVTTSQSA TLDACSFGVT GLKLQGATCS NNKLSLSNAI STVLPLTQLR
WVKQTSPEKK ANVVTLPVYL NFTRADLIFT VDFEIATKED PRSFYERGVA VLCTE
//