ID   DYH17_MOUSE             Reviewed;        4481 AA.
AC   Q69Z23; O08820;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Dynein axonemal heavy chain 17 {ECO:0000305};
DE   AltName: Full=Axonemal beta dynein heavy chain 17;
DE   AltName: Full=Ciliary dynein heavy chain 17;
GN   Name=Dnah17 {ECO:0000312|MGI:MGI:1917176}; Synonyms=Dnahc17, Kiaa3028;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1836-1936 (ISOFORM 1).
RC   STRAIN=NMRI; TISSUE=Testis;
RX   PubMed=9373155; DOI=10.1016/s0378-1119(97)00417-4;
RA   Neesen J., Koehler M.R., Kirschner R., Steinlein C., Kreutzberger J.,
RA   Engel W., Schmid M.;
RT   "Identification of dynein heavy chain genes expressed in human and mouse
RT   testis: chromosomal localization of an axonemal dynein gene.";
RL   Gene 200:193-202(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2192-4479 (ISOFORM 2).
RC   TISSUE=Thymus;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Force generating protein component of the outer dynein arms
CC       (ODAs) in the sperm flagellum. Produces force towards the minus ends of
CC       microtubules. Dynein has ATPase activity; the force-producing power
CC       stroke is thought to occur on release of ADP. Plays a major role in
CC       sperm motility, implicated in sperm flagellar assembly and beating.
CC       {ECO:0000250|UniProtKB:Q9UFH2}.
CC   -!- SUBUNIT: Consists of at least two heavy chains and a number of
CC       intermediate and light chains.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme
CC       {ECO:0000250|UniProtKB:Q9UFH2}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q69Z23-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q69Z23-2; Sequence=VSP_032116, VSP_032117;
CC   -!- DOMAIN: Dynein heavy chains probably consist of an N-terminal stem
CC       (which binds cargo and interacts with other dynein components), and the
CC       head or motor domain. The motor contains six tandemly-linked AAA
CC       domains in the head, which form a ring. A stalk-like structure (formed
CC       by two of the coiled coil domains) protrudes between AAA 4 and AAA 5
CC       and terminates in a microtubule-binding site. A seventh domain may also
CC       contribute to this ring; it is not clear whether the N-terminus or the
CC       C-terminus forms this extra domain. There are four well-conserved and
CC       two non-conserved ATPase sites, one per AAA domain. Probably only one
CC       of these (within AAA 1) actually hydrolyzes ATP, the others may serve a
CC       regulatory function (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the dynein heavy chain family. {ECO:0000305}.
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DR   EMBL; AL591204; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL591433; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z83807; CAB06061.1; -; mRNA.
DR   EMBL; AK173343; BAD32621.1; -; mRNA.
DR   SMR; Q69Z23; -.
DR   STRING; 10090.ENSMUSP00000101915; -.
DR   iPTMnet; Q69Z23; -.
DR   PhosphoSitePlus; Q69Z23; -.
DR   jPOST; Q69Z23; -.
DR   MaxQB; Q69Z23; -.
DR   PaxDb; Q69Z23; -.
DR   PRIDE; Q69Z23; -.
DR   ProteomicsDB; 277641; -. [Q69Z23-1]
DR   ProteomicsDB; 277642; -. [Q69Z23-2]
DR   MGI; MGI:1917176; Dnah17.
DR   eggNOG; KOG3595; Eukaryota.
DR   InParanoid; Q69Z23; -.
DR   PhylomeDB; Q69Z23; -.
DR   PRO; PR:Q69Z23; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q69Z23; protein.
DR   GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR   GO; GO:0030286; C:dynein complex; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0031514; C:motile cilium; IBA:GO_Central.
DR   GO; GO:0036157; C:outer dynein arm; ISS:UniProtKB.
DR   GO; GO:0036126; C:sperm flagellum; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0045505; F:dynein intermediate chain binding; IBA:GO_Central.
DR   GO; GO:0051959; F:dynein light intermediate chain binding; IBA:GO_Central.
DR   GO; GO:0008569; F:minus-end-directed microtubule motor activity; IBA:GO_Central.
DR   GO; GO:0003341; P:cilium movement; IBA:GO_Central.
DR   GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR   GO; GO:0036158; P:outer dynein arm assembly; ISS:UniProtKB.
DR   Gene3D; 1.10.8.710; -; 1.
DR   Gene3D; 1.10.8.720; -; 1.
DR   Gene3D; 1.20.140.100; -; 1.
DR   Gene3D; 3.10.490.20; -; 1.
DR   Gene3D; 3.20.180.20; -; 1.
DR   Gene3D; 3.40.50.300; -; 5.
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; 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; PTHR10676; PTHR10676; 1.
DR   Pfam; PF12774; AAA_6; 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; SSF52540; 4.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cell projection; Cilium; Coiled coil;
KW   Cytoplasm; Cytoskeleton; Dynein; Flagellum; Kelch repeat; Microtubule;
KW   Motor protein; Nucleotide-binding; Reference proteome; Repeat; TPR repeat.
FT   CHAIN           1..4481
FT                   /note="Dynein axonemal heavy chain 17"
FT                   /id="PRO_0000323750"
FT   REPEAT          521..569
FT                   /note="Kelch 1"
FT   REPEAT          1533..1566
FT                   /note="TPR 1"
FT   REPEAT          1688..1722
FT                   /note="TPR 2"
FT   REPEAT          2229..2275
FT                   /note="Kelch 2"
FT   REPEAT          2782..2834
FT                   /note="Kelch 3"
FT   REPEAT          4138..4173
FT                   /note="TPR 3"
FT   REPEAT          4272..4321
FT                   /note="Kelch 4"
FT   REPEAT          4339..4385
FT                   /note="Kelch 5"
FT   REGION          1..1792
FT                   /note="Stem"
FT                   /evidence="ECO:0000250"
FT   REGION          1793..2014
FT                   /note="AAA 1"
FT                   /evidence="ECO:0000250"
FT   REGION          2074..2295
FT                   /note="AAA 2"
FT                   /evidence="ECO:0000250"
FT   REGION          2401..2649
FT                   /note="AAA 3"
FT                   /evidence="ECO:0000250"
FT   REGION          2747..2996
FT                   /note="AAA 4"
FT                   /evidence="ECO:0000250"
FT   REGION          3011..3297
FT                   /note="Stalk"
FT                   /evidence="ECO:0000250"
FT   REGION          3389..3616
FT                   /note="AAA 5"
FT                   /evidence="ECO:0000250"
FT   REGION          3826..4059
FT                   /note="AAA 6"
FT                   /evidence="ECO:0000250"
FT   COILED          759..826
FT                   /evidence="ECO:0000255"
FT   COILED          3011..3071
FT                   /evidence="ECO:0000255"
FT   COILED          3241..3293
FT                   /evidence="ECO:0000255"
FT   BINDING         1831..1838
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2112..2119
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2439..2446
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2785..2792
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         3828..3852
FT                   /note="NFVEEKMGSKFVEGRSVEFSKSYKE -> EKTGIYHRQWETPQRVPGARTRG
FT                   GS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15368895"
FT                   /id="VSP_032116"
FT   VAR_SEQ         3853..4481
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15368895"
FT                   /id="VSP_032117"
SQ   SEQUENCE   4481 AA;  511603 MW;  A64E53D65671224E CRC64;
     MPDLRIDYLE TVSSVLLKFK ADKWGKLIGA EENMALLTEF FDKIDNPVLV LTLNAAGMII
     PCLGFPESLK SKGVYFIKMK PENITKDNYK THLIYGDISP TTVDQLIAVV EEVLYSLLNQ
     SENMDGWPRV VSEDIVKQVH RLKNEMFVMG GKIKGKTLLP IPEHLGSLDG TLDSMERIPS
     SMDNSLLHSI ETIIIDWSHQ IRDVLSKDSA QALLDGLHPL PRVEFEFWDA RLMNLQCIHE
     QLNRPKVNKI VEILEKAKSC YWPALQNVYM NVTQGLKEAN GIVLYLKPLR ILLEEMEQAD
     FTMLPSFIVK VLSTICFIWA TSEHYNTPSR VIVILREFCN QIIEMTRTYL SPDEVLKGLQ
     GEIEEVLGNI SLSVSVLKGL FQAYDFCCAN MKLFFKDRPP VPWEFPSSLA FSRMNSFFHR
     VQTIEDLYKT AIEFLKLEKI ELGGVWGNIL GNLVTQIYDE VFELVKVFAE CKYDPLDPGD
     SSFDDDYSDF ETKIQDLDRR LATIFCQAFD DCNCMESSAK LLYMCGGLLE RPLILVEVVP
     RYSVMLEMFN TELDNAKLMY DAQMAASADG QIPPIHKNMS PVSGQLKWSL ELQERLEVSM
     KYLKHIEHPV MSSMEAKLIY DKYDEMMGLL QSCRMKKYQQ WVEGVDQDCH FNLGQPLIQR
     DPFTSLIQVN FSKALVAVLR EVKYLNFQQQ KEIPESAEKL FSENETFRKF VGNLELIVGW
     YNEIKTTVKD VEFPLIKSEL EAIDVKLLSA ETTLFWNGEN VMEYIQEMRE MLYNLQNRIQ
     KAKQNVEGIT QAMQEWSANP LFERKDNKKE ALLDLDGRVA NLNKRYAAVK EAGVRIQAMV
     VENAELFRAD TTSQSWKDYV NYIDTVVLDE FDRFIRKSLN YLMDNMTMDE SIAPLFEIRM
     ELDKDGLTYN PSLEMGDEAG FLSLIEGLIN DLYNVARLIP RLAKGRLNYK SDLEDITDLI
     EMREEVSSLV IGAMKVAEEY QDSFERYSYL WVDDLQEFMK NFLIFGHAPT PEELDTKTDD
     TIPKTPPTLA QFQQQIDSYE KLYEEVSSCE NTKVFHGWLQ CDCRPFKQTL LNTIKRWSFL
     FKRYLNNHVI NSLADLESFM NITRTALKKP LKEGDYDGLV EVMGHLMKVK ERQVATDSMF
     EPLKQTIELL KSYGEEMPEE IYLKLQELPE QWTNTKKLAI QVKQNVAPLQ ANEVNILRRK
     CQQFELKQHE FREKFRRDAP FSFSDPEPYK SLNKIYLLYG VMEALCKSAS LFEVTVPDYK
     QLKACHREVR LLKELWDMIV MVNTSIDDWK TTKWKDINVE QMDIDCKKFA KDVRSLDKEM
     KPWDAFVGLD NTVKNMITSL RAVSELQNPA IRDRHWQQLM QATQVKFEMS EETTLADLLQ
     LNLHKYEDEV RNIVDKAVKE SGMEKVLKTL DITWTTMEFE HELHPRTGTM MLKSDEVLVE
     TLEDNQVQLQ NLMMSKYLSH FLKEVTSWQQ KLSTADSVIS IWFEVQRTWS HLESIFIGSE
     DIRAQLPEDS KRFDAIDQEF KALMEDAVKT PNVVEATNKP DLYNKLENLK MSLAVCEKAL
     AEYLETKRLA FPRFYFVSSA DLLDILSNGN DPVEVSRHLS KLFDSLCKLK FRLDASGKPL
     KFGLGMYSKE DEFVDFDKEC DLSGQVEVWL NRVLDRMRAT LRHEIPEAVV TYEEKPREQW
     IFDYPAQIWW TTEVGLAFAR LEEGYENAIK DYNKKQISQL NALITLLIGN LTAGDRMKIM
     TICTIDVHAR DVVAKMITVE SSQAFTWQSQ LRHRWDEEKK HCFANICDAQ IKYSYEYLGN
     TPRLVITPLT DRCYITLTQS LHLIMGGAPA GPAGTGKTET TKDLGRALGT MVYVFNCSEQ
     MDYKSCGNIY KGLAQTGAWG CFDEFNRISV EVLSVIAVQV KCVQDAIRAK KKKFNFLGEI
     ISLVPTVGIF ITMNPGYAGR TELPENLKAL FRPCAMVVPD FELICEIMLV AEGFLDARLL
     ARKFITLYTL CKELLSKQDH YDWGLRAIKS VLVVAGSLKR GDPTRAEDQV LMRALRDFNI
     PKIVTDDLPV FMGLIGDLFP ALDVPRKRDL NFEKIIKQSI VELKLQAEDS FVLKVVQLEE
     LLQVRHSVFV IGNAGSGKSQ VLKSLNKTYQ NLKRKPVAVD LDPKAVTCDE LFGIINPATR
     EWKDGLFSTI MRDLANLTHE GPKWIVLDGD IDPMWIESLN TVMDDNKVLT LASNERIPLN
     RTMRLVFEIS HLRTATPATV SRAGILYINP ADLGWNPVVS SWIERRKVQS EKANLIILFD
     KYLPTCLDKL RIGFKRITPV PEITVIQTIL YLLECLLTEK NAPPDSPKEL YELYFVFACF
     WAFGGAMFQD QLIDYRVEFS KWWINEFKTI KLPSQGTIFD YYIDPETKKF LPWTDKVPNF
     ELDPDIPLQA SLVHTTETIR IRYFIDLLME KAWPVMLVGN AGTGKSVLMG DKLENLSTDD
     YLVQAVPFNF YTTSAMLQGV LEKPLEKKSG RNYGPPGTKK LIYFIDDMNM PEVDKYGTVA
     PHTLIRQHMD HRHWYDRQKL TLKDVHNCQY VACMNPTSGS FTIDPRLQRH FCVFAVSFPG
     QEALTSIYNT ILAQHLSFRS APLVIQRLSS HLVTAALALH QKVSATFLPT AIKFHYIFNL
     RDLSNIFQGI LFSTAEILKT PLDLVRLWLH EAERVYGDKM VDEKDQETLH RVTIASVKKF
     FDDLGEENLF AKPNIFCHFT QGIGDPKYFP VTDVAQLNKL LKDVLDSYNE VNAVMNLVLF
     EDAVAHICKI NRILESPRGN ALLVGVGGSG KQSLSRLAAY ISALDVFQIT LKKGYAIPDL
     KMDLATQYIK SAVKNVPSVF LMTDSQVAEE QFLVLINDLL ASGEIPGLFG DEDLENIISS
     MRPQVKSLGI ADTREACWKF FIEKVRRQLK VILCFSPVGS VLRVRARKFP AVVNCTAINW
     FHEWPEDALV SVSARFLEET EGIEPEVKTS ISLFMAYVHT TVNEMSKIYL TIERRYNYTT
     PKTFLEQIKL YQNLLAKKRM ELVAKIERLE NGLMKLQSTA SQVDDLKAKL AVQETELKQK
     NENADKLIQV VGVETEKVSK EKAIADEEEM KVEVINKNVT EKQKACETDL AKAEPALLAA
     QEALDTLNKN NLTELKSFGS PPDAVVNVTA AVMILTAPGG KIPKDKSWKA AKIMMGKVDT
     FLDSLKKFDK EHIPEACLKA FKPYQGNPTF DPEFIRSKST AAAGLCSWCI NIVRFYEVYC
     DVAPKRQALE EANAELAEAQ EKLSRIKNKI AELNANLSNL TSAFEKATAE KIKCQQEADA
     TNRVISLANR LVGGLASENV RWAESVENFK SQGVTLCGDV LLISAFVSYV GYFTKKYRNE
     LMEKFWIPYI NKLKVPIPIT EGLDPLTLLT DDADVATWNN QGLPSDRMST ENATILCNTE
     RWPLIVDAQL QGIKWIKNKY GSDLQAIRLG QKSYLDIIEQ AISAGDTLLI ENIGETVDPV
     LDPLLGRNTI KKGRFIKIGD KEVEYHPSFR LILHTKYFNP HYKPEMQAQC TLINFLVTRD
     GLEDQLLAAV VAKERPDLEQ LKANLTKSQN EFKIVLKELE DSLLARLSAA SGNFLGDTAL
     VENLETTKHT ANEIEEKVQE AKITEVKINE ARENYRPAAE RASLLYFILN DLNKINPIYQ
     FSLKAFNVVF EKAIQKTAPA DEVKQRVINL TDEITYSVYM YTARGLFERD KLIFLAQVTF
     QVLSMKKELN PVELDFLLRF PFKAGVVSPV DFLQHQSWGG IKALSEMDEF KNLDSDIEGS
     AKRWKKLVES EAPEKEIFPK EWKNKTALQK LCMVRCMRPD RMTYAVKNFV EEKMGSKFVE
     GRSVEFSKSY KESSPSTPIF FILSPGVDPL KDVEALGKKL GFTIDNGKLH NVSLGQGQEV
     VAENALDVAA EKGHWVILQV RGSLPQNIHL VARWLGILDK KVERYSSGSH EDYRVFISAE
     PAPTAETHII PQGILENAIK ITNEPPTGMY ANLHKALDLF TQDTLEMCTK EIEFKCILFA
     LCYFHAVVAE RRKFGAQGWN RSYPFNNGDL TISINVLYNY LEANSKVPWD DLRYLFGEIM
     YGGHITDDWD RRLCRTYLAE YIRVEMLEGE VLLAPGFQIP PNLDYKGYHE YIDENLPPES
     PYLYGLHPNA EIGFLTVTSE KLFRTVLEMQ PKETDSGAGT GVSREEKVGA VPVPEGSLGS
     EGSLGTIGLP GTGFQVKAVL DDILEKIPET FNMAEIMAKA AEKTPYVVVA FQECERMNIL
     TNEMRRSLKE LNLGLKGELT ITTDMEDLST ALFYDTVPDT WVARAYPSMM GLAAWYADLL
     QRIRELESWT TDFALPTTVW LAGFFNPQSF LTAIMQSMAR KNEWPLDKMC LSVEVTKKNR
     EDMTAPPREG SYVYGLFMEG ARWDTQTGVI AEARLKDLTP VMPVIFIKAI PVDRMETKNI
     YECPVYKTRI RGPTYVWTFN LKTKEKAAKW ILAAVALLLQ V