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Database: UniProt
Entry: G1SH77_RABIT
LinkDB: G1SH77_RABIT
Original site: G1SH77_RABIT 
ID   G1SH77_RABIT            Unreviewed;      3304 AA.
AC   G1SH77;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 3.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=Dynein axonemal heavy chain 17 {ECO:0000313|Ensembl:ENSOCUP00000001972.4};
GN   Name=DNAH17 {ECO:0000313|Ensembl:ENSOCUP00000001972.4};
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000001972.4, ECO:0000313|Proteomes:UP000001811};
RN   [1] {ECO:0000313|Ensembl:ENSOCUP00000001972.4, ECO:0000313|Proteomes:UP000001811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thorbecke {ECO:0000313|Proteomes:UP000001811};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSOCUP00000001972.4}
RP   IDENTIFICATION.
RC   STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000001972.4};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the dynein heavy chain family.
CC       {ECO:0000256|ARBA:ARBA00008887}.
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DR   Ensembl; ENSOCUT00000002286.4; ENSOCUP00000001972.4; ENSOCUG00000002284.4.
DR   eggNOG; KOG3595; Eukaryota.
DR   GeneTree; ENSGT00940000154076; -.
DR   HOGENOM; CLU_000038_1_1_1; -.
DR   TreeFam; TF335573; -.
DR   Proteomes; UP000001811; Unplaced.
DR   Bgee; ENSOCUG00000002284; Expressed in testis and 5 other cell types or tissues.
DR   GO; GO:0030286; C:dynein complex; IEA:InterPro.
DR   GO; GO:0031514; C:motile cilium; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0045505; F:dynein intermediate chain binding; IEA:InterPro.
DR   GO; GO:0051959; F:dynein light intermediate chain binding; IEA:InterPro.
DR   GO; GO:0008569; F:minus-end-directed microtubule motor activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   Gene3D; 1.10.287.2610; -; 1.
DR   Gene3D; 1.10.287.2620; -; 1.
DR   Gene3D; 1.10.8.1220; -; 1.
DR   Gene3D; 1.20.1270.280; -; 1.
DR   Gene3D; 1.20.58.1120; -; 1.
DR   Gene3D; 1.20.920.20; -; 1.
DR   Gene3D; 1.20.920.30; -; 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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR   Gene3D; 1.10.8.720; Region D6 of dynein motor; 1.
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; IPR041589; DNAH3_AAA_lid_1.
DR   InterPro; IPR042222; Dynein_2_N.
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; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR45703:SF4; DYNEIN AXONEMAL HEAVY CHAIN 17; 1.
DR   PANTHER; PTHR45703; DYNEIN HEAVY CHAIN; 1.
DR   Pfam; PF12774; AAA_6; 2.
DR   Pfam; PF12775; AAA_7; 1.
DR   Pfam; PF12780; AAA_8; 1.
DR   Pfam; PF12781; AAA_9; 1.
DR   Pfam; PF17857; AAA_lid_1; 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   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
PE   3: Inferred from homology;
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Cilium {ECO:0000256|ARBA:ARBA00023069};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001811}.
FT   DOMAIN          87..178
FT                   /note="Dynein heavy chain tail"
FT                   /evidence="ECO:0000259|Pfam:PF08385"
FT   DOMAIN          553..840
FT                   /note="Dynein heavy chain linker"
FT                   /evidence="ECO:0000259|Pfam:PF08393"
FT   DOMAIN          1057..1144
FT                   /note="Dynein heavy chain hydrolytic ATP-binding dynein
FT                   motor region"
FT                   /evidence="ECO:0000259|Pfam:PF12774"
FT   DOMAIN          1173..1254
FT                   /note="Dynein heavy chain hydrolytic ATP-binding dynein
FT                   motor region"
FT                   /evidence="ECO:0000259|Pfam:PF12774"
FT   DOMAIN          1382..1478
FT                   /note="Dynein heavy chain AAA 5 extension"
FT                   /evidence="ECO:0000259|Pfam:PF17852"
FT   DOMAIN          1679..1771
FT                   /note="Dynein heavy chain 3 AAA+ lid"
FT                   /evidence="ECO:0000259|Pfam:PF17857"
FT   DOMAIN          1815..2074
FT                   /note="Dynein heavy chain AAA module D4"
FT                   /evidence="ECO:0000259|Pfam:PF12780"
FT   DOMAIN          2087..2422
FT                   /note="Dynein heavy chain coiled coil stalk"
FT                   /evidence="ECO:0000259|Pfam:PF12777"
FT   DOMAIN          2449..2666
FT                   /note="Dynein heavy chain ATP-binding dynein motor region"
FT                   /evidence="ECO:0000259|Pfam:PF12781"
FT   DOMAIN          2780..2900
FT                   /note="Dynein heavy chain region D6 P-loop"
FT                   /evidence="ECO:0000259|Pfam:PF03028"
FT   DOMAIN          2932..2983
FT                   /note="Dynein heavy chain AAA lid"
FT                   /evidence="ECO:0000259|Pfam:PF18198"
FT   DOMAIN          3029..3302
FT                   /note="Dynein heavy chain C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18199"
FT   REGION          1..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          208..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2722..2751
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3000..3031
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          2096..2130
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2293..2349
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2656..2686
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        25..39
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..65
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3304 AA;  371728 MW;  3ED14697A21CFBC5 CRC64;
     VTRAVQGPRR GRRQEWGCPG RVEAAGRQRT ERWNAPSERD GDGTVRMGSS RRQSRPGSAS
     QARRQPQGAV APLLPSAAPP GRPLTRSLFA VQLVAVLREV KYLNFQQQKE IPQSAENLFA
     ENETFRKFVG SLELIVGWYN EIKTTVMEVE FPLIKSELEA IDVKLLSAET TLFWNSEGAG
     RGHAPWVTRG VRHVTRVQPL SWQPLQRQGG VSVERMDQPP SSAPPGVCPT GVSLGRHCPP
     RELLPEAGAR SAPWGQTRCL SRVPPPCPQT DLEDIPDLIE MREELSTLVV NAIKEAEEYQ
     DSIERFSYLW TDDPQEFMRN FLIFGHVPTP EELDTRTDDM VPKAQPTLAQ FQQQIDSYEK
     LYEEVSRCEN TRVFHGWLQC DCRPFKQALL NTIKRWSLMF KRHLSSHVVS SLADLEAFMK
     VARAGLTKPL KEGDYNGLVE VMGHLMKVKE RQVELPEQWT NTKKLAIQVK QNVAPLQANE
     VSILRRRCQQ FELKQHEFRE KFRHEAPFSF KDPEPYKSLN KQQKSIAAME DIMESLCKSG
     SLFEVTVPDY KQLKACHREA LLLKELWDMI FTVNTSIDDW KTTKWKDINV EQMDLDCKKF
     AKDVRSLDKE MKAWDAFVGL DNTVKNMITS LRAVSELQNP AIRDRHWQQL TQATQVKFEM
     SDQTTLADLL QLNLHKYEDE VRNIVDKAVK ESGMEKTLDS TWTTMEFEHE PHPRTGTMML
     KSDEVLVETL EDNQVQLQNL MMSKYLSHFL EEVTSWQQKL STADSVISIW FEVQRTWSHL
     ESIFIGSEDI RAQLPEDSKR FDDIDLEFKA LMEDAVKTPN VVEATNKPGL YDKLEALKKR
     WVPRPAAGGG VARRCWVLGS RCLRPQRRAS LEPAVPVAPC GQSHCRPQVE VWLNRVLDRM
     CATLRHEIPE AVVTYEEKPR EQWIFDYPAQ VALTCTQIWW TTEVGMAFAR LEEGYENAIK
     DYNKKQISQL NALITLLIGN LNAGDRMKIM TVCTIDVHAR DVVAKMITAK VESSQAFTWQ
     SQLRHRWDEE KRHCFANICD AQIQYSYEYL GNTPRLSCGN IYKGLAQTGA WGCFDEFNRI
     SVEVLSVIAV QVKCVQDAIR AKKKTFNFLG EMISLIPTVG IFITMNPGYA GRTELPENLK
     ALFRCGAQGP GASAGREAGG RPARARGPCV RIHLLPGIVT DDLPVFMGLI GDLFPALDVP
     RKRDLNFEKV IKQSVVELRL QAEDSFVLKV VQLEELLQVR HSVFVIGNAG SGKSQVLRSL
     NKTYQNLKRK PVAIDLDPKA VTCDELFGII NPATREWKDG LFSTIMRDLA NITHDGPKWI
     VLDGDIDPMW IESLNTVMDD NKVLTLASNE RIPLNRTMRL VFEISHLRTA TPATVSRAGI
     LYINPITVIQ TILYLLECVI TEKTAPPDSS KELYELYFVF ACLWAFGGAM FQDQLVDYRV
     EFSRWWINEF KTIKFPSQGT VFDYYIDPDT KKFLPWTDKV PTFELDPDVP LQASLVHTTE
     TTRIRYFMDL LMEKSWPVML VGNAGTGKSV LMGDKLDGLS TDDYLVQAVP FNFYTTSAML
     QGVLEKPLEK KSGRNYGPPG TKKLIYFIDD MNMPEVDKYG TAAPHTLIRQ HMDHGHWVRV
     WGGGGRPEAG PGTCLTGARA RSGQRHFCVF AVSFPGQEAL TTIYSTILTQ TRASVPPPAL
     HQKVTTTFLP TAIKFHYVFN LRDLSNIFQG LLFSTAELLK SPLDLVRLWL HEAERVYGDK
     MVDEKDQDTL RRVTMASTKK FFDLGDELLF ARPNIFCHFA QGIGESKYLS VTDVAYLNKL
     LVDVLDSYNE VNAVMNLVLF EDAVAHICRI NRILESPRGN ALLVGVGGSG KQSLSRLAAF
     ISALDVFQIT LKKGYGIPDL KVDLAAQYIK SAVKNVPSVF LMTDSQVSEE QFLVLMNDLL
     ASGEIPGLFA DDEVENIIAS MRPQVKSLGV ADTREACWKF FIDKVRKQLK VILCFSPVGS
     VLRVRARKFP AVVNCTAINW FHEWPEDALV SVSARFLQET PGIQPEVKAS ISLFMSYVHT
     TVNEMSKVYL ATERRYNYTT PKTFLEQIKL YQNLLAKKRM ELAAKIERLD NGLMKLQSTA
     SQVDDLKAKL AVQETELKQK NENADKLIQV VGVETEKVSK EKAIADEEEV KVPLGTAPSP
     APSPCSVSPL VSSPCLCAPA NTLRKLESLG SAPDAVVNVT AAVMILTAPG GKIPKDKSWK
     AAKIMMGKVD SFLDSLKRFD KEHIPEACLK AFKPYQGNPT FDPEFIRSKS TAAAGLCSWC
     INIVRFYEVY CDVAPKRQAL EEANAELAEA QEKLSRIKNK IAVSLNANLN NLTSAFEKAT
     AEKIKCQQEA DATNRVISLA NRLVGGLASE NVRWAESVES YKCQGATLCG DVLLVSAFVS
     YVGYFTKKYR NELMEKFWIP YINNLKVPIP ITKGLDPLSL LTDDADVATW NNQGLPSDRM
     STENATILCN TERWPLIVDA QLQGIKWIKN KYGGDLRAIR LGQKSYLDMI EQAVSEGDTL
     LIENIGETVD PVLDPLLGRN TIKKGRFIKI GDKEVEYHPK FRLILHTKYF NPHYKPEMQA
     QCTLINFLVT RDGLEDQLLA AVVAKERPDL EQLKANLTKS QNEFKIVLKE LEDSLLARLS
     AASGHFLGDT ALVENLETTK HTASEIEEKV QEAKITETKI NEARENYRPA AERASLLYFI
     LNDLSKINPI YQFSLKVGAP AAGAGRGGAG PRSPSPEPRL PRSPSPEPRL SWNFVEEKMG
     SKFVEGRSVE FSKSYEESSP STPIFFILSP GVDPLKDVEA LGKKLGFTID NGKLHNVSLG
     QGQEVVAENA LDVAAENGHW VILQNIHLVA RWLSTLDKKV ERYSTGSHED YRVFISAEPA
     PSPEAHIIPQ GILENAIKIT NEPPTGMHAN LHKALDLFTQ DTLEMCTKEV EFKCILFALC
     YFHAVVAERR KFGAQGWNRS YPFNNGDLTI SINVLYNYLE ANAKVRRLTS QGDWERRVRS
     VHSAGADTDT GADTGTGADT GADTGVGTGA DTGTGASQVK AVLDDILEKI PEAFSMAEIM
     AKAAEKTPYV VVAFQECERM NILTNEMRRS LKELSLGLKG ELTITTDMED LSTALFYDTV
     PDTWVARAYP SMMGLAAWYA DLLLRIRELE AWTTDFALPT TVWLAGFFNP QSFLTAIMQS
     MARKNEWPLD KMCLSVEVTK KNREDMTAPP REGAYVYGLF MEGARWDIQT GVIAEARLKE
     LTPAMPVIFI KAIPVDRMET KNIYECPVYK TRLRGPTYVW TFNLKTKERA AKWILAAVAL
     LLQV
//
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