DYH12_MOUSE
ID DYH12_MOUSE Reviewed; 3086 AA.
AC Q3V0Q1; Q8BVT4; Q8VHS7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Dynein axonemal heavy chain 12;
DE AltName: Full=Axonemal beta dynein heavy chain 12;
DE AltName: Full=Axonemal dynein heavy chain 12-like protein;
DE AltName: Full=Axonemal dynein heavy chain 7-like protein;
DE AltName: Full=Ciliary dynein heavy chain 12;
GN Name=Dnah12; Synonyms=Dnah12l, Dnah7l, Dnahc12, Dnahc7l;
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 [LARGE SCALE MRNA] OF 1-739 AND 2541-3086.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP PROTEIN SEQUENCE OF 37-42, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
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 of respiratory cilia. Produces force
CC towards the minus ends of microtubules. Dynein has ATPase activity; the
CC force-producing power stroke is thought to occur on release of ADP.
CC Involved in sperm motility; implicated in sperm flagellar assembly (By
CC similarity). {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Consists of at least two heavy chains and a number of
CC intermediate and light chains.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000305}.
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}.
CC -!- CAUTION: Was originally derived from a readthrough transcript including
CC ASB14 and DNAH12. {ECO:0000305}.
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DR EMBL; AC121919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC133179; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK076605; BAC36411.1; -; mRNA.
DR EMBL; AK132980; BAE21453.1; -; mRNA.
DR SMR; Q3V0Q1; -.
DR iPTMnet; Q3V0Q1; -.
DR PhosphoSitePlus; Q3V0Q1; -.
DR EPD; Q3V0Q1; -.
DR MaxQB; Q3V0Q1; -.
DR PaxDb; Q3V0Q1; -.
DR PRIDE; Q3V0Q1; -.
DR ProteomicsDB; 277419; -.
DR MGI; MGI:107720; Dnah12.
DR eggNOG; KOG3595; Eukaryota.
DR InParanoid; Q3V0Q1; -.
DR PhylomeDB; Q3V0Q1; -.
DR UniPathway; UPA00143; -.
DR ChiTaRS; Dnah12; mouse.
DR PRO; PR:Q3V0Q1; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q3V0Q1; protein.
DR GO; GO:0097729; C:9+2 motile cilium; IEA:UniProt.
DR GO; GO:0030286; C:dynein complex; IBA:GO_Central.
DR GO; GO:0036156; C:inner dynein arm; ISM:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
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:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
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; -; 4.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR035699; AAA_6.
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; IPR024317; Dynein_heavy_chain_D4_dom.
DR InterPro; IPR004273; Dynein_heavy_D6_P-loop.
DR InterPro; IPR013602; Dynein_heavy_linker.
DR InterPro; IPR042228; Dynein_linker_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10676; PTHR10676; 4.
DR Pfam; PF12774; AAA_6; 1.
DR Pfam; PF12780; AAA_8; 1.
DR Pfam; PF17857; AAA_lid_1; 1.
DR Pfam; PF18198; AAA_lid_11; 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 SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 4.
PE 1: Evidence at protein level;
KW ATP-binding; Cell projection; Cilium; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Dynein; Microtubule; Motor protein;
KW Nucleotide-binding; Reference proteome; Repeat; Ubl conjugation pathway.
FT CHAIN 1..3086
FT /note="Dynein axonemal heavy chain 12"
FT /id="PRO_0000066952"
FT REGION 1..1212
FT /note="Stem"
FT /evidence="ECO:0000250"
FT REGION 745..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1213..1434
FT /note="AAA 1"
FT /evidence="ECO:0000250"
FT REGION 1494..1634
FT /note="AAA 2"
FT /evidence="ECO:0000250"
FT REGION 1847..2098
FT /note="AAA 3"
FT /evidence="ECO:0000250"
FT REGION 2212..2654
FT /note="AAA 4"
FT /evidence="ECO:0000250"
FT REGION 2655..2789
FT /note="Stalk"
FT /evidence="ECO:0000250"
FT REGION 2868..3045
FT /note="AAA 5"
FT /evidence="ECO:0000250"
FT COILED 592..665
FT /evidence="ECO:0000255"
FT COILED 2847..2875
FT /evidence="ECO:0000255"
FT MOTIF 1251..1258
FT /note="GPAGTGKT motif"
FT MOTIF 1301..1307
FT /note="CFDEFNR motif"
FT BINDING 1251..1258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 1532..1539
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 1886..1893
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2251..2258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 3086 AA; 356231 MW; E3EBA9274AB70310 CRC64;
MSDPNKTAIA AEKEALNLKL PPIVQPPKNI GVDTPKQSEL LKYRRSKEQQ KKINQLVISG
AKKSLDKTLD KRIPPLPEPD FPPTMTSEIK KRGLNYIFMK QCVENSPIVP IQSQWLDNML
MLVPEHLKEG EKSEELLGSL IDEVSMDYEK SMKRYLVQSV LVKPPVKWLE DEGGPLPESP
EGLDYSNPWH SNFVQARSQI LANLHIVHPT MKMLLELGYT AFAKIILLDL TGIRARGPID
CEALRNDLSI QARKSEEKIM NTWYPKVINL FTKKEALEGI KTEKLDSFYN CVSILMSNQL
KDLLWRTVEE FIKLFDPRYL NRLPIFKMEL TFDDDKMEFY PTFQDLEDVV LGLIERISET
LQTVQTVPSW LSGTSSPVNL DTEIPEHVLQ WALCTLRTAI QHNLEGAKAH HKTYVTKYNW
LLDGTATKMI QRFQAENHTF DEYTEFIEKF FNLASEIMLL PQWAHYPMVR LDCEDLKIGL
TNKARAFANI LLNDIASKHR KENESICSEF EAIRDHALRV PETTEEMMEL IAFVERARTV
GILDLALRIQ ESKRQMSYFL DALLMSQEDL NLNATVLLWP TKITPVFDEN DELIENAKHA
KENELIAKRE KLILEIEKES RRMEEFTEFA ELDRMHQYVA DVRQLQKRIQ ESEEAVQFIN
KEEELFKWEL TKYPELEKLK VTIEPYQKFF NFVLKWQRTE KRWMDGGFLD LNGESMEADI
DDFSREVFRT LKFFHAKQKK ELQERRKAAR KRSLMEEKPE EEPKENPTIT MMRARHWKQM
SEIVGYDLTP DSGTTLRKVL KLNLSPYLES FEVISAGASK EFSLERSMNA MIATWDDISF
HISLYRDTGI GILSSVDEIQ AILDDQIIKT QTMRGSPFIK PFENEIKAWE DRLIRIQETI
DEWLKVQAQW LYLEPIFCSE DIMQQMPEEG RQFQTVDRHW KDIMKFCAKD PKVLAATSLT
GLLEKLQNCN DLLEKIMKGL NAYLEKKRLF FPRFFFLSND EMLEILSETK DPLRVQPHLK
KCFEGIAKLE FLANLDIKAM YSSEGERVEL IALISTTAAR GAVEKWLIQV EDLMLRSIRD
VIAASRLAYP ESARKDWVRE WPGQVVLCVS QMFWTSETQE IISGGTEGLK KYYKELQYQL
NDIVELVRGK LSKQTRITLG ALVTIDVHAR DVVMDMIEMG VSHDTDFQWL AQLRYYWEYE
NARVRIINCN VKYAYEYLGN SPRLVITPLT DRCYRTLIGA FYLNLGGAPE GPAGTGKTET
TKDLAKALAV QCVVFNCSDG LDYLAMGKFF KGLASSGAWA CFDEFNRIEL EVLSVVAQQI
LCIQRAIQQK LEAFVFEGTE LRLNPNCFVA ITMNPGYAGR SELPDNLKVL FRTVAMMVPN
YALIAEISLY SYGFLNAKPL SVKIVMTYRL CSEQLSSQFH YDYGMRAVKA VLVAAGNLKL
KYPNENEDIL LLRSIKDVNE PKFLSHDIPL FNGITSDLFP GIKLPEADYK EFLECAHETC
QTHNLQPVKF FLEKIIQTYE MMIVRHGFML VGEPFAAKTE VLHVLADTLT LMNERNYGDE
EKVMYRTVNP KSITMGQLFG QFDPVSHEWT DGIVANTFRE FALAESPDRK WVVFDGPIDT
LWIESMNTVL DDNKKLCLMS GEIIQMSPQM SLIFETMDLS QASPATVSRC GMIYLEPSQL
GWEPLVASWL NSLKEPLSEL EHQNLLKELF DWLVPPSLVF RRKKCKFLSL HDLSKYFKQV
LIYYILVVSP KFSLKSNHYK IFFHQQASFI FSLIWSIGAS CDTDGRLAFD AFLRTAVSGR
NEEAPMPVSI SKWECPFDEK GLVYDYMYEL RNRGRWIHWN ELIKSSDLED KRAKIQDIIV
PTMDTIRYTF LMDLSITSAK PLLFVGPTGT GKSVYVKDKL MNHLEKEKYF PFYVNFSART
SANQVQNIIM ARLDKRRKGV FGPPMGKKCV IFIDDMNMPS LEKYGAQPPI ELLRQFFDCG
HWYDLKDTSK ITLIDIELIA AMGPPGGGRN AVTPRFIRHF NICTINTFSD ETMVRIFSSI
MAFYLRTHAF SPEYFVLGNQ IVSGTMEVYK QSMGNLLPTP AKSHYTFNLR DFSRVIRGCL
LIEKDAIESK HTMIRLFVHE VLRVFYDRLI NDEDRNWLFL LIKNVIKDHF KESFDTVFHH
LRNGNAPVTE EDLRNLMFGD YMNPDLEGDD RVYIEIPDIH HFNEVVDQCL DEYNQTHKRR
MNLVVFRYVL EHLSRICRIL KQSGGNALLI GLGGSGRQSL TKLATSMAKM QIFQPEISKS
YGMNEWREDI KGFLLLIIIW AVVESLSKIL EKRLRYLNDH FTYNLYCNIC RSLFEKDKLL
FSFLLCANLL LAKKEIEYQE LMFLLTGGVS LKSAEKNPDP DWLQDKSWEE ICRASELPVF
HGLREHFCNY IYLWEEIYDS KEPHNMKFPE PMDKTLNELQ KIIILRCLRP DKITPAITNY
VTDKLGKKFV EPPPFDLTKS YLDSNCTIPL VFVLSPGADP MASLLKFAND KSMSGNKFQA
ISLGQGQGPV ASKMITAAIE EGTWVCLQNC HLAVSWMPTL EKICEDFSPE TCNPTFRLWL
TSYPSPKFPV TILQNGVKMT NEPPTGLRLN LLQSYLSDPI SDTQFFKGCP GKELAWEKLL
FGVCFFHALV QERKKFGPLG WNIPYGFNES DLRISVRQLQ LFINEYDTIP FEAISYLTGE
CNYGGRVTDD WDRRLLLTML ADFYNSFIIE NPHYKFSPSG NYYAPPKGTY DDYIEFIKKL
PFTQEPEIFG LHENVDISKD LQQTKVLFES LLLTQGGAKQ TGSSGSTDQV LLEITEDILT
QLPNDFDIEA ALKNYPVRYE ESMNTVLVQE MERFNNLIRT IRNTLRDLKK AIKGLVVMDS
ALEALSGSLL IGKVPEMWAK RSYPSLKPLG SYITDFLARL KFLEDWFSSG KPSVFWISGF
FFTQAFLTGA MQNFARKYTI PIDLLGYEFE VIPFDYSDTP PEDGVYIHGL YLDGARWDRF
SGLLAEQYPK LLFDLMPIIW IKPNLKIEIV KIEAYICPLY KTSERKGTLS TTGHSTNFVI
AMLLKTDQPT QHWIKRGVAL LCQLDN
