ID   DYH11_PIG               Reviewed;        4518 AA.
AC   F1SC07;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   11-DEC-2019, sequence version 4.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Dynein axonemal heavy chain 11;
DE   AltName: Full=Axonemal beta dynein heavy chain 11;
DE   AltName: Full=Ciliary dynein heavy chain 11;
GN   Name=DNAH11;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION.
RC   STRAIN=Duroc;
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   INTERACTION WITH CFAP45.
RX   PubMed=33139725; DOI=10.1038/s41467-020-19113-0;
RA   Dougherty G.W., Mizuno K., Noethe-Menchen T., Ikawa Y., Boldt K.,
RA   Ta-Shma A., Aprea I., Minegishi K., Pang Y.P., Pennekamp P., Loges N.T.,
RA   Raidt J., Hjeij R., Wallmeier J., Mussaffi H., Perles Z., Elpeleg O.,
RA   Rabert F., Shiratori H., Letteboer S.J., Horn N., Young S., Struenker T.,
RA   Stumme F., Werner C., Olbrich H., Takaoka K., Ide T., Twan W.K.,
RA   Biebach L., Grosse-Onnebrink J., Klinkenbusch J.A., Praveen K.,
RA   Bracht D.C., Hoeben I.M., Junger K., Guetzlaff J., Cindric S., Aviram M.,
RA   Kaiser T., Memari Y., Dzeja P.P., Dworniczak B., Ueffing M., Roepman R.,
RA   Bartscherer K., Katsanis N., Davis E.E., Amirav I., Hamada H., Omran H.;
RT   "CFAP45 deficiency causes situs abnormalities and asthenospermia by
RT   disrupting an axonemal adenine nucleotide homeostasis module.";
RL   Nat. Commun. 11:5520-5520(2020).
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       {ECO:0000250|UniProtKB:Q96DT5}.
CC   -!- SUBUNIT: Consists of at least two heavy chains and a number of
CC       intermediate and light chains (By similarity). Interacts with CFAP45
CC       (PubMed:33139725). {ECO:0000250|UniProtKB:Q96DT5,
CC       ECO:0000269|PubMed:33139725}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC       {ECO:0000250|UniProtKB:Q96DT5}. Note=Located in the proximal region of
CC       respiratory cilia. {ECO:0000250|UniProtKB:Q96DT5}.
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. {ECO:0000250|UniProtKB:Q96DT5}.
CC   -!- SIMILARITY: Belongs to the dynein heavy chain family. {ECO:0000305}.
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DR   EMBL; AEMK02000070; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 9823.ENSSSCP00000016307; -.
DR   PaxDb; F1SC07; -.
DR   PRIDE; F1SC07; -.
DR   Ensembl; ENSSSCT00000016754; ENSSSCP00000016307; ENSSSCG00000015379.
DR   VGNC; VGNC:87368; DNAH11.
DR   eggNOG; KOG3595; Eukaryota.
DR   GeneTree; ENSGT00940000158880; -.
DR   HOGENOM; CLU_000038_4_0_1; -.
DR   InParanoid; F1SC07; -.
DR   TreeFam; TF316836; -.
DR   Proteomes; UP000008227; Chromosome 9.
DR   Proteomes; UP000314985; Unplaced.
DR   Bgee; ENSSSCG00000015379; Expressed in oocyte and 19 other tissues.
DR   ExpressionAtlas; F1SC07; baseline and differential.
DR   GO; GO:0097729; C:9+2 motile cilium; IDA:GO_Central.
DR   GO; GO:0005930; C:axoneme; IDA:GO_Central.
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: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; 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   SMART; SM00382; AAA; 3.
DR   SUPFAM; SSF52540; SSF52540; 4.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell projection; Cilium; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Dynein; Microtubule; Motor protein; Nucleotide-binding; Reference proteome;
KW   Repeat.
FT   CHAIN           1..4518
FT                   /note="Dynein axonemal heavy chain 11"
FT                   /id="PRO_0000454207"
FT   REGION          1..1857
FT                   /note="Stem"
FT                   /evidence="ECO:0000250"
FT   REGION          1858..2079
FT                   /note="AAA 1"
FT                   /evidence="ECO:0000250"
FT   REGION          2139..2368
FT                   /note="AAA 2"
FT                   /evidence="ECO:0000250"
FT   REGION          2474..2721
FT                   /note="AAA 3"
FT                   /evidence="ECO:0000250"
FT   REGION          2819..3068
FT                   /note="AAA 4"
FT                   /evidence="ECO:0000250"
FT   REGION          3074..3405
FT                   /note="Stalk"
FT                   /evidence="ECO:0000250"
FT   REGION          3461..3688
FT                   /note="AAA 5"
FT                   /evidence="ECO:0000250"
FT   REGION          3898..4124
FT                   /note="AAA 6"
FT                   /evidence="ECO:0000250"
FT   COILED          3322..3391
FT                   /evidence="ECO:0000255"
FT   BINDING         1896..1903
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2177..2184
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2512..2519
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2857..2864
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   4518 AA;  519618 MW;  AB314AC47555A7AE CRC64;
     MAASVAAQEA HGFRKVPTLS LTPGVGMEAA GLVELEEEEE EEEEEEAAAR RARSFVQDAR
     VRFVGGRLEQ MLGFPEEKWS QHLESEDNRQ ILGEFLESPG PACLVFSIAA AGQLATSHQI
     PRDAKHKLVY IAKKITENTG VNDFSQTVVF GELPASSVGY VTAFLDEILV PIISNKNNHK
     SWSCFISQDM ERHVEVMRNK MHIFRGKMLR RTLLPIPTIA GNIDLDQKYS ETRLEPNERT
     ILHVLESVVI KWSHQIQEVV EKDSVQPLLS GLHSNPETEL DFWTMRRENL SCIYDQLQAP
     IVLKMVKILK NKQSSYFPTL RDIFLSVKNA LREAQDVELY LRPLRRHIQC LQETEFPQTR
     VLIAPLFHTI CLIWSHSKFY NTPARVIVLL QEFCNLFIDQ ARAYLSPEHL LKGELEDSLE
     KVQVVINVFK TFKNSFFNYR KGLASYFMGK KEMKPWDFRS HLVFWRFDKF LDRFMKIEDI
     FVTTLEFEKL ERLEFGGTKG AIFNGQIHEM SEELMELCKV FKQSTYDPSD YNNMEFESEY
     AMFKSKTVDF DRRLGTILCV ALFNCNGLEA AFKLLTIFGN FLEKPVVMEI FSPHYSTLVH
     MFNAELDMCK QLYNEHVKQI EQGTVVLNKN MPFTSGNIKW AKEVLDRLQM FWSNFASLRY
     LSLESPDDAV VYQKYTEMTT LLDQFENHVY NEWKSNVEEI CDFSLNQPLI RFSAVNGLLS
     VNFDPKLVAV LREVKYLLML KKSDIPDSAL AIFKKRDTLL KYIGNLELLV QGYNKLRQTL
     LDVEYPLIKD ELRAVDEELQ AAATSLTWQD DCLRDIERVK TATSELERRV EHTHDNVRAI
     QQMMRAWAEG TLLPRREHRR ETALTWEDKG DLFMKKYKQI QEDGCKIHSL VEENRRLFKA
     NPSLDTWKIY VEFIDDIVVE GFFQTIMHDL DFFLMNTEKQ LKPAPFFQAQ MILMPPEILF
     KPSLEREAGD GFYDLVEEML CSSFRMSAQM KRVAAHLGVA NYQNDMDNML GLAEVRQEIM
     KRVADVISKV LDFRSTLDMY AYLWVDDRAE FMKHFLLYGH IVSSEETDPL ADEDIPEQSP
     TLEQFKEQID IYEALYVQMS KFDDFRVFDS WFKVDMKPFK VSLLNIIRKW SWMFQEHLLR
     FVIDSLNELQ EFIKETDAGL QRELSEGDHD GLVDIMGHLL AVRSRQRATD ELFEPLKETI
     TLLETYGQKM PEQIYVQLEE LPERWETTKK IAATVRHEVS PLQNAEVTLI RKKCISFDEK
     QAEFRERFRL CAPLGFNAEN PYTVLDKAHQ ELEALEEEVL QMQESTHVFE VALPEYKQMK
     QCRKEIKLLK GLWDVIIYVR RSIDNWTKTQ WRQINVEQMD VELRRFAKEI WSLDKEVRVW
     DAYSGLEGTV KDMTTSLRAV AELQSPALRD RHWHQLMKAI GVKFSINEAM TLADLLALQL
     HQVEEDVRSI VDKAVKELGT EKVINEIIQT WATMEFSYEV HYRTGIPLLK SDEQLFETLE
     HNQVQLQTLL QSKYVEYFIE QVTSWQHKLN TADSAIFTWM EVQRTWSHLE SIFVCSEDVR
     IQLKEDARRF DEVDVEFKEL MFRTAKIKNV LQATCRPNLC EKLKDLQYRL SLCEKALAEY
     LETKRVAFPR FYFISSADLL DILSKGAQPA QVTRHLSKLF DSIADLRFED DQDVSASRAV
     GMYSKEKEYV PFSATCECTG HVETWLLQLE QIMKETVRHS ITEAIAAYED KPREVWIFDF
     PAQVALTSSQ IWWTTDVGIA FSRLEEGYET ALKDFHKKQI SQLNTLIALL LGELLPGDRQ
     KIMTICTIDV HARDVVAKLI SQKVRSPQAF AWLSQLRHQW EDTRKHCLVH ICDAQFQYFY
     EYLGNSPRLV ITPLTDRCYI TLTQSLHLTM SGAPAGPAGT GKTETTKDLG RALGMMVYVF
     NCSEQMDYKS IGNIYKGLVQ TGAWGCFDEF NRISVEVLSV VAVQVKMIHD AIRNRKKRFV
     FLGEAITLKP SVGIFITMNP GYAGRTELPE NLKALFRPCA MVAPDIELIC EIMLVAEGFV
     DARSLAHKFI TLYTLCRELL SKQDHYDWGL RAVKSVLVVA GSLKRGDKSR PEEQVLMRAL
     RDFNMPKIVT DDIPVFLGLV SDLFPALDVP RRRAPHFEQM VRQSTVELRL QPEENFILKV
     VQLEELLAVR HSVFVIGNAG TGKSKILRTL NRTYVNMKQK PVWNDLNPKA VTTDELFGFI
     HHATREWKDG NVVYSLIGLF SSLLREQANL RQDGPKWIVL DGDIDPMWIE SLNTVMDDNK
     VLTLASNERI ALTPSMRLLF EIHHLRTATP ATVSRAGILY VNPQDLGWNP YVASWIDRRR
     HQSEKANLTI LFDKYVPACL DKLRTSFKTI TSIPESSLVQ TVCTLLECLL TPENVPSDSP
     KDVYEVYFVF ACVWAFGGTL SQDQLSGCQA EFSRWWHKEM KAVKFPSQGT IFDYYLDHKT
     KKFLPWADKI PKFTMDPEVP LQRVLVHTSE TTRLRYFIEL LLEKGQPLML VGNAGVGKTV
     FVGDMLTSLS EAYIVSRVPF NYYTTSAALQ RILEKPLEKK AGRNYGPGGN KKMVYFIDDM
     NMPEVDLYGT VQPHTLIRQH IDYGHWYDRQ KVRLKEIHGC QYVACMNPMV GSFTINPRLQ
     RHFTVFAFNF PSMDALNTIY SQILSSHFQH QAFGPSVLRS GPALIQATIA FHQTMTHNFL
     PTAIKFHYLF NLRDLSNVFQ GILFASSECL KGPNDLIQLW LHESYRVYGD RLIDTKDCNL
     FQKKMLETAN KYFEGVDSQL LLQQPLIYCH FANGKEDLCY MPVKDWEVLK TFLTEALDNY
     NDLNAAMPLV LFEDAMQHVC RISRILQTPQ GSALLIGVGG SGKQSLSRLA AYICGLEVFQ
     VTLTQGFGIQ ELRVDLANLY IRTGAKNLPT AFLLTDAQVL DESFLVLIND LLASGEIPDL
     FSDEDVDKII SGIRNEVRSL GMVDSKENCW KFFLARARLH LKIILCFSPV GHTLRDRARK
     FPALVNCTAV DWFHAWPREA LVTVSRRFIE ETRGIEPLDK DSISLFMAHV HTSVNEMSTR
     FYQNEGRHNY TTPKSFLEQI SLFKNLLKKK QKEVSQKKEH LVNGIQKLKT TASQVGALKA
     RLASQEAELQ LRNQDAEALI AKIGLQTEKV SREKAIADAE ERKVTAIQTE VSQKQRECEA
     DLLKAEPALV AATAALNTLN RVNLTELKVF PNPPNAVTNV TAAVMVLLAP QGRVPKDRSW
     KAAKVFMGKV DDFLQALINY DKEHIPENCL KVVNEQYLKD PEFNPNLIRT KSFAAAGLCA
     WVINIIKFYE VYCDVEPKRH ALAQANLELA TATEKLEAIR KKLADLDRNL SRLTASFEKA
     IAEKVRCQEE VNQTNKTIKL ANRLVKELEV KKIRWGQSIK SFEAQEKTLC GDILLTAAYV
     SYVGPFTQQY RQELVDCMWV PFLHWKVSIP MTEGLDVIAM LTDDATIATW NNEGLPNDRM
     STENAAILTH CQRWPLMIDP QQQGIKWIKK KYGTDLKVTH LGQKGFLNDI ETALAFGDVI
     LIENLEETID PVLDPLLGRN TIKKGKYIKI GDKECEFNHN FRLILHTKLA NPHYKPELQA
     QTTLLNFTVT QDGLEAQLLA EVVSIERPDL EKLKLVLTKH QNDCKIELKY LEDDLLLRLS
     AAEGSFLDDT KLVERLETAK ATAAEIERKV IEARENERKI NEARERYRPV AARASLLYFV
     INDLRKINPI YQFSLKAFNL LFQRAIEQAD KVEDAQGRIS ALTESITHAV FLSTSQALFE
     KDKLTFLSQM AFQILLRKKE IDPLELDFLL RFTVEHTYPS PVDFLTPQAW SALKAVALRE
     EFRGLDRDVE GSAKQWRRWA ESECPEKEKL PQEWKKKSLI QKLIILRALR PDRMTYALRN
     FVEEKLGAKY VERTRLDLIK ALEESSPACP VFFILSPGVD ALKDLEILGK RLGFTSDLGT
     FHNVSLGQGQ EMVAEVALEK ASKGGHWVML QNVHLVAKWL GTLEKLLERF SQGSHRDYRV
     FMSAESAPTP HEHVIPPGLL ENSIKITNEP PTGMLANLHA ALYNFDQDTL EACSKEQEFK
     SILFSLCYFH ACVAGRLRFG PQGWSRSYPF SPRDLTICAH VLYNYLEANP HVPWEDLRYL
     FGEIMYGGHV TDEWDRKLCR VYLEEFMNPS LIDDELMLAP GFAAPPNLDY SGYHQYIEEM
     LPPESPALYG LHPNAEIEFL TVTSNTLFRT LLEIQPKNAL SNEELGQSTE DKVKNVLEDI
     LEKLPEEFNM AEIMQKNPNR SPYVLVCFQE CERMNILLQE IRVSLQRLDL GLKGELTLSP
     DMEAQQSALS YDAVPDTWSK VAYPSTYGLA QWFNDLLLRC RELDTWTQDL ALPAVVWLSG
     FFNPQSFLTA IMQTMARKNE WPLDKMCLTI DVTKKMKEDY GHAPREGAYL HGLLLEGARW
     DSQSGTIVDA HLKELRSAMP VIFAKAIPMD RQETKHTYEC PVYRTKMRGP NYVWTFRLKS
     KEKTAKWVLA GVALLLEA