ID   DYH12_RAT               Reviewed;        3092 AA.
AC   Q923J6;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Dynein axonemal heavy chain 12;
DE   AltName: Full=Bm259;
GN   Name=Dnah12;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 600-736.
RC   STRAIN=SHRSP;
RX   PubMed=11489260; DOI=10.1016/s0006-8993(01)02670-1;
RA   Kirsch T., Wellner M., Luft F.C., Haller H., Lippoldt A.;
RT   "Altered gene expression in cerebral capillaries of stroke-prone
RT   spontaneously hypertensive rats.";
RL   Brain Res. 910:106-115(2001).
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   -!- 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}.
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DR   EMBL; AABR03100937; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03102926; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03102110; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03100400; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03102032; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03101661; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03100963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AY032856; AAK64519.1; -; mRNA.
DR   SMR; Q923J6; -.
DR   PhosphoSitePlus; Q923J6; -.
DR   PRIDE; Q923J6; -.
DR   UCSC; RGD:619990; rat.
DR   RGD; 619990; Dnah12.
DR   InParanoid; Q923J6; -.
DR   PhylomeDB; Q923J6; -.
DR   PRO; PR:Q923J6; -.
DR   Proteomes; UP000002494; Unplaced.
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; IBA:GO_Central.
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   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; 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; 3.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell projection; Cilium; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Dynein; Microtubule; Motor protein; Nucleotide-binding; Reference proteome;
KW   Repeat; Ubl conjugation pathway.
FT   CHAIN           1..3092
FT                   /note="Dynein axonemal heavy chain 12"
FT                   /id="PRO_0000370365"
FT   REGION          1..1212
FT                   /note="Stem"
FT                   /evidence="ECO:0000250"
FT   REGION          745..767
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          1853..2104
FT                   /note="AAA 3"
FT                   /evidence="ECO:0000250"
FT   REGION          2218..2661
FT                   /note="AAA 4"
FT                   /evidence="ECO:0000250"
FT   REGION          2662..2796
FT                   /note="Stalk"
FT                   /evidence="ECO:0000250"
FT   REGION          2875..3052
FT                   /note="AAA 5"
FT                   /evidence="ECO:0000250"
FT   COILED          592..665
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         1892..1899
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2257..2264
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   3092 AA;  357248 MW;  3A6050BB2A399DCD CRC64;
     MSDPNKTAIT AEKEALNLKL PPIVHPPKNI GVDTPKQSEL LNYRRSKEQQ KKINQLVISA
     AKKSLDKTLD KRIPPLPEPD FPPTMTSEIK KKGLNYIFMK QCVESSPIVP IQPQWLDHML
     MLIPEHLKEG KKREELLGSL INEVSMDFEK SMKRYLVQSV LVKPPVKWLE DEWGPLPESP
     EGLDYSNPWH SNFVQARSQI LANLHIVHPT MKLLLELGYT TFSDIILLDL TGIRDRGPID
     CEALRNDLSI QARKAEERIM NTWYPKVINL FTKKEALEGI KPEKVDSFYN CVSILMSNQL
     KDLLWRTVEE FVRLFDSRYI LRLPIFKMEL TFDDDKMEFY PTFQDLEDVV LGLIERISET
     LQTVQTVPSW LSGTTAPVNL DTELPEHVMY WALSTLRIAV HQNLEGVRAH YKTYVTNYNW
     LLDGTATKMI ERFQSENHTF DEYTEFIERF FSLASEIMLL PQWAHYPMVR LDCEDLKTGL
     TNKAKAFANI LLNDIASKHR KENESICSEF ETIKEHALRV PETTEEMMEL IAFIEKARTT
     GIQNLAQRIQ ESKRQMGYFL DTFLLSQEDL NLNASVLLWP SKINPVFDEN DELIENSKRT
     KENELIAKRE KLILEIEKES RRMEEFTEFA ELDRMQQYVA DVRHLQKRIQ DSEEAVQFIN
     KEEELFKWEL TKYPELEKLK VTIEPYQKFF NFVLKWQRTE KRWMDGGFLD LNGESMEADI
     DEFSREVFKT LKFFQTKQKK ELQEKRKAAR KRSLMEEKPE EEPKESPTIT MMRARHWKQM
     SEIVGYDLTP DSGTTLRKVL KLNLTPYLES FEVISAGASK EFSLERAMNA MIATWDDISF
     HISLYRDTGV YILSSVDEIQ AILDDQIIKT QTMRGSPFIK PFENEIKAWE DRLIRIQETI
     DEWLKVQAQW LYLEPIFCSE DIMQQMPEEG RQFQTVDRHW KDIMKFCAKD PKVLAATSLT
     GLLEKLQNCN DLLDKIMKGL NAYLEKKRLF FPRFFFLSND EMLEILSETK DPLRVQPHLK
     KCFEGIAKLE FLTNLDIKAM YSSEGERVEL ISVISTSAAR GAVEKWLIQV EDLMLRSIHD
     VIAASRLAYP ESARKDWVRE WPGQVVLCVS QMFWTSETQE VISGGNEGLK KYYKELQYQL
     NDIVELVRGK LSKQTRITLG ALVTIDVHAR DVVMDMIDMG VSHDTDFQWL AQLRYYWEYE
     NARVRIVNCN VKYAYEYLGN SPRLVITPLT DRCYRTLIGA FYLNLGGAPE GPAGTGKTET
     TKDLAKALAV QCVVFNCSDG LDYLAMGKFF KGLASSGAWA CFDEFNRIEL EVLSVVAQQI
     LCIQRAIQQK LEVFVFEGTE LRLNPNCFVA ITMNPGYAGR SELPDNLKVL FRTVAMMVPN
     YALIAEISLY SYGFLNAKPL SVKIVMTYRL CSEQLSSQFH YDYGMRAVKA VLVAAGNLKL
     KYPNENEDIL LLRSIKDVNE PKFLSHDIPL FNGITSDLFP GIKLPEADYQ EFLECAYEAC
     ETQNLQPVKF FLEKIIQTYE MMIVRHGFML VGEPFAAKTE VLHILADTLT LMNERNYGDE
     EKVMYRTVNP KSITMGQLFG QFDPVSHEWT DGIVANTFRE FALAESPDRK WVVFDGPIDT
     LWIESMNTVL DDNKKLCLMS GEIIQMSPQM SLIFETMDLS QASPATVSRC GMIYLEPSQL
     GWEPIVASWL NSLKEPLNEL EHQNLLKELF NWLVQPSLEF RRKKCKVTAH RVWLFPTVYS
     SWVCLILFVL EVSAVSPKCS LKSNCYNLFH QQATFVFSLI WSVGASCDTD GRLAFDNFLR
     SLVTGKNDKA PMPVFINKWE CPFDEKGLVY DYMYELRNRG RWIHWNDLIK SSDIEDRRTK
     IQDIIVPTMD TIRYTFLMDL CISHAKPLLF VGPTGTGKSV YVKDKLMNHL EKGKYFPFYV
     NFSARTSANQ VQNIIMARLD KRRKGVFGPP MGKKCVVFID DMNMPSLEKY GAQPPIELLR
     QFFDCGHWYD LKDTTKITLV DIELIAAMGP PGGGRNAVTP RFIRHFNICT INSFSDETMV
     RIFSSIMMFY LRTHDFSPEY FVLGHQIVSA TMEIYKQSMG NLLPTPAKSH YTFNLRDFSR
     VIRGCLLIDK EAIESKHTMI RLFVHEVLRV FYDRLINDED RNWLFLLIKN VIKDHFKESL
     ENVFSHLRRG NSSINEEDLR NLMFGDYMNP DLEGDDRVYI EILNIHQFNE VVDQCLDEYN
     QTHKRRMNLV VFRYVLEHLS RICRILKQSG GNALLIGLGG SGRQSLTSLA TSMAKMQIFQ
     PEISKSYGMN EWREDIKPNL MSVFYATSIR DNLSKILEKR LRYLNDHFTY NLYCNICRSL
     FEKDKLLFSF LLCANLLLAK KEIEYQELMF LLTGGVSLKS AEKNPDPNWL QDKSWEEICR
     ASELPVFHGL REHFCNHIRE WEDIYNSKEP HNMKLPESMD KTLNELQKII ILRCLRPDKI
     TPAITNYVTD KLGKKFVEPP PFDLTKSYLD SNCTIPLIFV LSPGADPMAS LLKFANDKSM
     SGNKFQAISL GQGQGPVATK MITAAIEEGT WVCLQNCHLA VSWMPTLEKI CEDFSPEICN
     PTFRLWLTSY PSPKFPVTIL QNGVKMTNEP PTGLRLNLLQ SYLSDPISDP EFFNGCPGKE
     LAWEKLLFGV CFFHALVQER KKFGPLGWNI PYGFNESDLR ISIRQLQLFI NEYDTIPFEA
     ISYLTGECNY GGRVTDDWDR RLLLTMLADF YNSLIIENPH YKFSPSGNYF APPKGTYDEY
     IEFIKKLPFT QEPEIFGLHE NVDISKDLQQ TKLLFESLLL TQGGVKQTGS SGSTDQILLE
     ITEDILTQLP NDFDIEAALR SYPVRYEESM NTVLVQEMER FNNLIITIRN TLRDLKKAIK
     GVVVMDSALE ALSGSLLIGK VPEMWAQRSY PSLKPLGSYI TDFLTRLKFL EDWFTMGKPN
     VFWISGFFFT QAFLTGAMQN YARKYTIPID LLGYEFEVIP SDNATNPPED GVYIHGLYLD
     GARWNRTSGL LAEQHPKLLF DLMPIIWIKP NVKTEIVKTD AYVCPLYKTS ERKGTLSTTG
     HSTNFVIAML LRTELPAQHW IKRGVALLCQ LD