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Database: UniProt
Entry: DYH7_HUMAN
LinkDB: DYH7_HUMAN
Original site: DYH7_HUMAN 
ID   DYH7_HUMAN              Reviewed;        4024 AA.
AC   Q8WXX0; B8ZZX8; O00433; O95492; Q4G152; Q53QX7; Q53S64; Q53T02; Q68CY5;
AC   Q8N1Z2; Q9UMS3; Q9Y2F3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 2.
DT   27-MAR-2024, entry version 161.
DE   RecName: Full=Dynein axonemal heavy chain 7;
DE   AltName: Full=Axonemal beta dynein heavy chain 7;
DE   AltName: Full=Ciliary dynein heavy chain 7;
DE   AltName: Full=Dynein heavy chain-like protein 2;
DE   AltName: Full=hDHC2;
GN   Name=DNAH7; Synonyms=KIAA0944;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS
RP   SPECTROMETRY, SUBCELLULAR LOCATION, INDUCTION, TISSUE SPECIFICITY, AND
RP   VARIANT PRO-3319.
RC   TISSUE=Tracheobronchial epithelium;
RX   PubMed=11877439; DOI=10.1074/jbc.m200348200;
RA   Zhang Y.J., O'Neal W.K., Randell S.H., Blackburn K., Moyer M.B.,
RA   Boucher R.C., Ostrowski L.E.;
RT   "Identification of dynein heavy chain 7 as an inner arm component of human
RT   cilia that is synthesized but not assembled in a case of primary ciliary
RT   dyskinesia.";
RL   J. Biol. Chem. 277:17906-17915(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS CYS-545
RP   AND PRO-3319.
RC   TISSUE=Brain;
RX   PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA   Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA   Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XIII. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 6:63-70(1999).
RN   [3]
RP   SEQUENCE REVISION.
RA   Nagase T., Kikuno R., Yamakawa H., Ohara O.;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Brain cortex;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Fetal kidney;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1290-1432 (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP   [GENOMIC DNA] OF 1356-1422 (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   TISSUE=Nasal polyp;
RX   PubMed=11175280; DOI=10.1038/sj.ejhg.5200555;
RA   Maiti A.K., Mattei M.-G., Jorissen M., Volz A., Zeigler A., Bouvagnet P.;
RT   "Identification, tissue specific expression, and chromosomal localisation
RT   of several human dynein heavy chain genes.";
RL   Eur. J. Hum. Genet. 8:923-932(2000).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1333-1503 (ISOFORM 1).
RC   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   [10]
RP   FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN CILD50, AND VARIANTS CILD50
RP   ASN-1863; ILE-2164; HIS-3204; SER-3464 AND ARG-3534.
RX   PubMed=34476482; DOI=10.1093/abbs/gmab113;
RA   Wei X., Sha Y., Wei Z., Zhu X., He F., Zhang X., Liu W., Wang Y., Lu Z.;
RT   "Bi-allelic mutations in DNAH7 cause asthenozoospermia by impairing the
RT   integrality of axoneme structure.";
RL   Acta Biochim. Biophys. Sin. 53:1300-1309(2021).
RN   [11]
RP   INVOLVEMENT IN CILD50.
RX   PubMed=35543642; DOI=10.1111/cge.14146;
RA   Gao Y., Liu L., Shen Q., Fu F., Xu C., Geng H., Lv M., Li K., Tang D.,
RA   Song B., Wu H., Xu Y., Zhang Y., Tao F., Zhou P., Wei Z., He X., Cao Y.;
RT   "Loss of function mutation in DNAH7 induces male infertility associated
RT   with abnormalities of the sperm flagella and mitochondria in human.";
RL   Clin. Genet. 102:130-135(2022).
CC   -!- FUNCTION: Force generating protein that plays an important role in
CC       respiratory cilia and sperm flagella beating (PubMed:34476482).
CC       Produces force towards the minus ends of microtubules. Dynein has
CC       ATPase activity; the force-producing power stroke is thought to occur
CC       on release of ADP (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:34476482}.
CC   -!- SUBUNIT: The dynein complex consists of at least two heavy chains and a
CC       number of intermediate and light chains. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC       {ECO:0000269|PubMed:11877439}. Cell projection, cilium, flagellum
CC       {ECO:0000269|PubMed:34476482}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q8WXX0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8WXX0-2; Sequence=VSP_031131;
CC       Name=3;
CC         IsoId=Q8WXX0-3; Sequence=VSP_031132, VSP_031135, VSP_031136;
CC       Name=4;
CC         IsoId=Q8WXX0-4; Sequence=VSP_031133, VSP_031134;
CC   -!- TISSUE SPECIFICITY: Detected in brain, testis and trachea. Detected in
CC       bronchial cells (at protein level). {ECO:0000269|PubMed:11175280,
CC       ECO:0000269|PubMed:11877439}.
CC   -!- INDUCTION: Up-regulated during ciliogenesis (at protein level).
CC       {ECO:0000269|PubMed:11877439}.
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   -!- DISEASE: Ciliary dyskinesia, primary, 50 (CILD50) [MIM:620356]: A form
CC       of primary ciliary dyskinesia, a disorder characterized by
CC       abnormalities of motile cilia. Respiratory infections leading to
CC       chronic inflammation and bronchiectasis are recurrent, due to defects
CC       in the respiratory cilia. CILD50 is an autosomal recessive form
CC       characterized by chronic sinusitis and bronchitis as well as male
CC       infertility. Patient sperm have markedly reduced progressive motility,
CC       and multiple morphologic abnormalities of the flagella.
CC       {ECO:0000269|PubMed:34476482, ECO:0000269|PubMed:35543642}. Note=The
CC       disease may be caused by variants affecting the gene represented in
CC       this entry.
CC   -!- SIMILARITY: Belongs to the dynein heavy chain family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA76788.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAB06055.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAH18445.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAH18445.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
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DR   EMBL; AF327442; AAL37427.1; -; mRNA.
DR   EMBL; AB023161; BAA76788.2; ALT_INIT; mRNA.
DR   EMBL; AK094515; BAC04372.1; -; mRNA.
DR   EMBL; CR749651; CAH18445.1; ALT_SEQ; mRNA.
DR   EMBL; AC013274; AAY14776.1; -; Genomic_DNA.
DR   EMBL; AC068919; AAY14995.1; -; Genomic_DNA.
DR   EMBL; AC104600; AAY24051.1; -; Genomic_DNA.
DR   EMBL; AC114760; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC029567; AAH29567.1; -; mRNA.
DR   EMBL; AJ132084; CAA10557.1; -; mRNA.
DR   EMBL; AJ132093; CAB46444.1; -; Genomic_DNA.
DR   EMBL; Z83801; CAB06055.1; ALT_FRAME; mRNA.
DR   CCDS; CCDS42794.1; -. [Q8WXX0-1]
DR   RefSeq; NP_061720.2; NM_018897.2. [Q8WXX0-1]
DR   RefSeq; XP_011509789.1; XM_011511487.2.
DR   PDB; 6RZA; EM; 5.40 A; X=2675-2812.
DR   PDB; 8J07; EM; 4.10 A; g2/g4=1-4024.
DR   PDBsum; 6RZA; -.
DR   PDBsum; 8J07; -.
DR   EMDB; EMD-35888; -.
DR   SMR; Q8WXX0; -.
DR   BioGRID; 121102; 15.
DR   IntAct; Q8WXX0; 5.
DR   MINT; Q8WXX0; -.
DR   STRING; 9606.ENSP00000311273; -.
DR   GlyGen; Q8WXX0; 2 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8WXX0; -.
DR   PhosphoSitePlus; Q8WXX0; -.
DR   BioMuta; DNAH7; -.
DR   DMDM; 311033375; -.
DR   EPD; Q8WXX0; -.
DR   jPOST; Q8WXX0; -.
DR   MassIVE; Q8WXX0; -.
DR   MaxQB; Q8WXX0; -.
DR   PaxDb; 9606-ENSP00000311273; -.
DR   PeptideAtlas; Q8WXX0; -.
DR   ProteomicsDB; 75108; -. [Q8WXX0-1]
DR   ProteomicsDB; 75109; -. [Q8WXX0-2]
DR   ProteomicsDB; 75110; -. [Q8WXX0-3]
DR   ProteomicsDB; 75111; -. [Q8WXX0-4]
DR   ABCD; Q8WXX0; 1 sequenced antibody.
DR   Antibodypedia; 49680; 57 antibodies from 13 providers.
DR   Ensembl; ENST00000312428.11; ENSP00000311273.6; ENSG00000118997.14. [Q8WXX0-1]
DR   Ensembl; ENST00000409063.5; ENSP00000386912.1; ENSG00000118997.14. [Q8WXX0-2]
DR   Ensembl; ENST00000410072.5; ENSP00000386260.1; ENSG00000118997.14. [Q8WXX0-4]
DR   GeneID; 56171; -.
DR   KEGG; hsa:56171; -.
DR   MANE-Select; ENST00000312428.11; ENSP00000311273.6; NM_018897.3; NP_061720.2.
DR   UCSC; uc002uti.5; human. [Q8WXX0-1]
DR   AGR; HGNC:18661; -.
DR   CTD; 56171; -.
DR   DisGeNET; 56171; -.
DR   GeneCards; DNAH7; -.
DR   HGNC; HGNC:18661; DNAH7.
DR   HPA; ENSG00000118997; Tissue enhanced (choroid plexus, testis).
DR   MalaCards; DNAH7; -.
DR   MIM; 610061; gene.
DR   MIM; 620356; phenotype.
DR   neXtProt; NX_Q8WXX0; -.
DR   OpenTargets; ENSG00000118997; -.
DR   PharmGKB; PA38625; -.
DR   VEuPathDB; HostDB:ENSG00000118997; -.
DR   eggNOG; KOG3595; Eukaryota.
DR   GeneTree; ENSGT00940000155282; -.
DR   HOGENOM; CLU_000038_1_3_1; -.
DR   InParanoid; Q8WXX0; -.
DR   OMA; GRDIPCS; -.
DR   OrthoDB; 166463at2759; -.
DR   PhylomeDB; Q8WXX0; -.
DR   TreeFam; TF316836; -.
DR   PathwayCommons; Q8WXX0; -.
DR   SignaLink; Q8WXX0; -.
DR   BioGRID-ORCS; 56171; 8 hits in 1145 CRISPR screens.
DR   ChiTaRS; DNAH7; human.
DR   GenomeRNAi; 56171; -.
DR   Pharos; Q8WXX0; Tbio.
DR   PRO; PR:Q8WXX0; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q8WXX0; Protein.
DR   Bgee; ENSG00000118997; Expressed in right uterine tube and 146 other cell types or tissues.
DR   ExpressionAtlas; Q8WXX0; baseline and differential.
DR   Genevisible; Q8WXX0; HS.
DR   GO; GO:0097729; C:9+2 motile cilium; IBA:GO_Central.
DR   GO; GO:0005858; C:axonemal dynein complex; NAS:UniProtKB.
DR   GO; GO:0005929; C:cilium; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0036156; C:inner dynein arm; IMP:SYSCILIA_CCNET.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion 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:0003777; F:microtubule motor activity; NAS:UniProtKB.
DR   GO; GO:0008569; F:minus-end-directed microtubule motor activity; IBA:GO_Central.
DR   GO; GO:0003341; P:cilium movement; IMP:SYSCILIA_CCNET.
DR   GO; GO:0060294; P:cilium movement involved in cell motility; IBA:GO_Central.
DR   GO; GO:0060285; P:cilium-dependent cell motility; NAS:UniProtKB.
DR   GO; GO:0036159; P:inner dynein arm assembly; IMP:SYSCILIA_CCNET.
DR   Gene3D; 1.10.287.2620; -; 1.
DR   Gene3D; 1.10.472.130; -; 1.
DR   Gene3D; 1.10.8.1220; -; 1.
DR   Gene3D; 1.10.8.710; -; 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; 3.20.180.20; Dynein heavy chain, N-terminal domain 2; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 5.
DR   Gene3D; 1.10.8.720; Region D6 of dynein motor; 1.
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; IPR042228; Dynein_linker_3.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR46961:SF18; DYNEIN AXONEMAL HEAVY CHAIN 1; 1.
DR   PANTHER; PTHR46961; DYNEIN HEAVY CHAIN 1, AXONEMAL-LIKE PROTEIN; 1.
DR   Pfam; PF12774; AAA_6; 1.
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; 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; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; Cell projection;
KW   Ciliopathy; Cilium; Coiled coil; Cytoplasm; Cytoskeleton; Dynein;
KW   Flagellum; Microtubule; Motor protein; Nucleotide-binding;
KW   Primary ciliary dyskinesia; Reference proteome; Repeat.
FT   CHAIN           1..4024
FT                   /note="Dynein axonemal heavy chain 7"
FT                   /id="PRO_0000317666"
FT   REGION          1..1289
FT                   /note="Stem"
FT                   /evidence="ECO:0000250"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          49..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1290..1511
FT                   /note="AAA 1"
FT                   /evidence="ECO:0000250"
FT   REGION          1571..1802
FT                   /note="AAA 2"
FT                   /evidence="ECO:0000250"
FT   REGION          1938..2189
FT                   /note="AAA 3"
FT                   /evidence="ECO:0000250"
FT   REGION          2302..2555
FT                   /note="AAA 4"
FT                   /evidence="ECO:0000250"
FT   REGION          2572..2873
FT                   /note="Stalk"
FT                   /evidence="ECO:0000250"
FT   REGION          2954..3184
FT                   /note="AAA 5"
FT                   /evidence="ECO:0000250"
FT   REGION          3397..3620
FT                   /note="AAA 6"
FT                   /evidence="ECO:0000250"
FT   COILED          685..745
FT                   /evidence="ECO:0000255"
FT   COILED          2827..2883
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..18
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..99
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         132..139
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         1328..1335
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         1609..1616
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         1976..1983
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2341..2348
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..3517
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_031131"
FT   VAR_SEQ         1..1452
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_031132"
FT   VAR_SEQ         452..501
FT                   /note="ESKSKPTTLKPIILNEIVDAHKEKIKEVIMKESVAPTEHLRLYDKYDFLI
FT                   -> RNKAKPGHFYFSHIQRSVTFQHSEVSSPQNSHFKIVSPFSVLGFTWRCQL (in
FT                   isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_031133"
FT   VAR_SEQ         502..4024
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_031134"
FT   VAR_SEQ         1633..1639
FT                   /note="GLMEENK -> ASILLMH (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_031135"
FT   VAR_SEQ         1640..4024
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_031136"
FT   VARIANT         169
FT                   /note="H -> P (in dbSNP:rs1072599)"
FT                   /id="VAR_038580"
FT   VARIANT         280
FT                   /note="A -> T (in dbSNP:rs2375643)"
FT                   /id="VAR_038581"
FT   VARIANT         315
FT                   /note="I -> V (in dbSNP:rs17838596)"
FT                   /id="VAR_038582"
FT   VARIANT         438
FT                   /note="S -> N (in dbSNP:rs16843720)"
FT                   /id="VAR_038583"
FT   VARIANT         545
FT                   /note="R -> C (in dbSNP:rs10931715)"
FT                   /evidence="ECO:0000269|PubMed:10231032"
FT                   /id="VAR_038584"
FT   VARIANT         565
FT                   /note="D -> H (in dbSNP:rs2635718)"
FT                   /id="VAR_038585"
FT   VARIANT         675
FT                   /note="K -> E (in dbSNP:rs10198893)"
FT                   /id="VAR_038586"
FT   VARIANT         825
FT                   /note="K -> E (in dbSNP:rs6719500)"
FT                   /id="VAR_038587"
FT   VARIANT         1422
FT                   /note="P -> T (in dbSNP:rs168192)"
FT                   /id="VAR_038588"
FT   VARIANT         1525
FT                   /note="E -> K (in dbSNP:rs13415574)"
FT                   /id="VAR_038589"
FT   VARIANT         1863
FT                   /note="D -> N (in CILD50; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:34476482"
FT                   /id="VAR_088453"
FT   VARIANT         1886
FT                   /note="R -> Q (in dbSNP:rs13034775)"
FT                   /id="VAR_038590"
FT   VARIANT         1940
FT                   /note="P -> L (in dbSNP:rs2375544)"
FT                   /id="VAR_038591"
FT   VARIANT         1971
FT                   /note="P -> L (in dbSNP:rs2889109)"
FT                   /id="VAR_038592"
FT   VARIANT         2020
FT                   /note="M -> T (in dbSNP:rs10184131)"
FT                   /id="VAR_038593"
FT   VARIANT         2164
FT                   /note="M -> I (in CILD50; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:34476482"
FT                   /id="VAR_088454"
FT   VARIANT         2459
FT                   /note="N -> K (in dbSNP:rs16841199)"
FT                   /id="VAR_038594"
FT   VARIANT         2569
FT                   /note="T -> I (in dbSNP:rs2293066)"
FT                   /id="VAR_038595"
FT   VARIANT         2809
FT                   /note="I -> V (in dbSNP:rs16841018)"
FT                   /id="VAR_038596"
FT   VARIANT         3204
FT                   /note="R -> H (in CILD50; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:34476482"
FT                   /id="VAR_088455"
FT   VARIANT         3319
FT                   /note="L -> P (in dbSNP:rs13411834)"
FT                   /evidence="ECO:0000269|PubMed:10231032,
FT                   ECO:0000269|PubMed:11877439"
FT                   /id="VAR_038597"
FT   VARIANT         3386
FT                   /note="R -> H (in dbSNP:rs6708527)"
FT                   /id="VAR_038598"
FT   VARIANT         3464
FT                   /note="G -> S (in CILD50; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:34476482"
FT                   /id="VAR_088456"
FT   VARIANT         3534
FT                   /note="Q -> R (in CILD50; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:34476482"
FT                   /id="VAR_088457"
FT   CONFLICT        433
FT                   /note="M -> V (in Ref. 4; BAC04372)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1020
FT                   /note="I -> T (in Ref. 2; BAA76788)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1292
FT                   /note="Y -> F (in Ref. 8; CAA10557)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1353
FT                   /note="N -> D (in Ref. 9; CAB06055)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1355
FT                   /note="S -> P (in Ref. 9; CAB06055)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1467
FT                   /note="Y -> H (in Ref. 5; CAH18445)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1502
FT                   /note="M -> L (in Ref. 9; CAB06055)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3563
FT                   /note="P -> L (in Ref. 7; AAH29567)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   4024 AA;  461159 MW;  3C2E3B2D7B886540 CRC64;
     MSSEQDKSAS KEKSKKPVRF LPQLSMEKLA SKEKFKAPAR ALPQLSMVST KPHWQQAAPS
     FHLSVKQDDE SPEPFSVKNE QSHAEYMERF GKKGKLPHQV DDSYVGPSTS KSKGKSPHKE
     RENFRSTLVN VIMQQDADLD SAVPDGSTIP KPTASAIEKD ILRYYYYIHH GIDTDHVAPM
     EDSWLEHVLD LVPQHLKVFT DSIVTLSDEM REDYLLSVRK SIVDFVLKDP REKGDDKKTD
     ELPAHRAEME ILPKPWRKSF LAASSYIRDH LNAMNPTMLA VLDLWHTNFK KLRLVDIKEF
     HNCQDALELS SFQNIIMRHM DSAKETLLKM WFPEVQNIYY QGNKKKQLPT GDSSAKLESF
     FNCAAALMTL QLQDLTLVSM QDFTDLIAQP PDSVRAFEHP GFIMRLILDN DTIKFEPELS
     DYIDIFLNVY DVMIKAVSFV PRVETKLYSK WESKSKPTTL KPIILNEIVD AHKEKIKEVI
     MKESVAPTEH LRLYDKYDFL ITRKAERDVD NFLAENHSYE KIIDEICKYQ KLIEEIQYTS
     IKTIRLGMFE MHCEELIRAL VKRADIICGK LLAKMFRDHQ EVNTRLCDEF ERIAEKALST
     PPNTAELMEM KAYIQKVEVT DMIELEQRLV DSKNCLAFLI EYVNFSPADM RLNNSVFQWY
     GRMGEIFEEH RKIIKEKIEQ YQEGLKLRCE RFVEELESYA KQSEEFYSFG DLQDVQRYLK
     KAQILNGKLD LAADKIEQFN AEEEAFGWLP SVYPQRKKIQ DGLNPYLRLY ETAVEFSSNY
     RAWTEGPYHK VNPDQVEADI GNYWRGLYKL EKTFHDSPYA LAMTKKVRSK VEDFKQHIPL
     IQVICNPGLR PRHWEAMSAI VGYPLQPSDD STVSSFLDMN LEPYIDRFEG ISEAASKEYS
     LEKAMEKMIT EWDAVEFVIH SYRETGTFIL ASVDEIQMLL DDHIIKTQTM RGSPFIKPYE
     KQMREWEGKL LLLQEILDEW LKVQATWLYL EPIFSSPDIM SQMPEEGRRF TAVDKTWRDI
     MRSVMQDKHV LTVVTIDRML ERLKKSNELL ELILKGLNEY LEKKRLFFPR FFFLSNDELL
     EILSETKDPT RVQPHLKKCF EGIAKVEFTE TLDITHMKSS EGEVVELIEI ISTAKARGQV
     EKWLVELERV MINSIHKVTG DATFAYTKYE RINWVRDWPG QTVLCVSQIF WTKEVQTAIP
     MGIKALEQYL KTCNRQIDDI VTLVRGKLSM QNRVTLGALV VLDVHARDVL SSLVKKNISD
     DSDFEWLSQL RYYWQENHLE TKMINAGLRY GYEYLGNSPR LVITPLTDRC YRTLFGALHL
     HLGGAPEGPA GTGKTETTKD LAKAVAKQCV VFNCSDGLDY LALGKFFKGL LSCGAWACFD
     EFNRIDLEVL SVVAQQILTI QRGINAGADI LMFEGTELKL DPTCAVFITM NPGYAGRSEL
     PDNLKALFRT VAMMVPDYAM IAEIVLYSCG FVTARPLSVK IVATYRLCSE QLSSQHHYDY
     GMRAVKSVLT AAGNLKLKYP NENEEILLLR SIIDVNLPKF LSHDLPLFEG ITSDLFPGVK
     LPKPDYNDLL AAIKDNCASM NLQMTAFFSE KILQVYEMMI VRHGFMIVGE PFGGKTSAYR
     VLAGALNDIC EKGLMEENKV QITVLNPKSV TMGQLYGQFD SVSHEWSDGV LAVSFRAFAS
     SVTPDRKWLI FDGPVDAVWI ENMNTVLDDN KKLCLMSGEI IQMSPQMNLI FEPMDLEVAS
     PATVSRCGMI YMEPHMLGWR PLMLSWVNLL PASVSVIQKE FIMGLFDRMV PVSVEFIRKH
     TKELSPTSDT NLVRSLMNLI DCFMDDFADE VKLKERNDRE TYSLLEGIFL FSLIWSVGAS
     CTDDDRLKFN KILRELMESP ISDRTRNTFK LQSGTEQTSS KALTVPFPEK GTIYDYQFVT
     EGIGKWEPWI KKLKEAPPIP KDVMFNEIIV PTLDTIRYSA LMELLTTHQK PSIFVGPTGT
     GKSVYITNFL LNQLNKEIYK PLLINFSAQT TAAQTQNIVM SKLDKRRKGV FGPPLGKRMV
     VFVDDVNMPA REVYGAQPPI ELLRQWLDHW NWYDLKDCSM IKLVDIQIMC AMGPPGGGRN
     PVTPRYMRHF NIITINEFSD KSMYTIFSRI LTWHLEICYK FPDEFLDLTT QIVNGTMTLY
     KEAMKNLLPT PAKSHYLFNL RDFSRVIQGV CLSRPETTET TEVIKRLWVH EVLRVYYDRL
     LDNTDRSWLI NYIQEILRNY MYEDFHELFQ RLDFDNDGMV EADDLRSLMF CDFHDPKRED
     TNYREIADVD NLRMIVEIHL EEYNNISKKP MNLVLFRFAI EHISRISRIL KQPRSHALLV
     GVGGSGRQSV TRLAAHMADY SVFQVEISKG YDTTEWHEDL KVILRKCAEG EMQGVFLFTD
     TQIKEESFLE DVSNLLNAGE IPNLFALDEK QEICDKMRQL DRQRDKTKQT DGSPIALFNM
     FIDHCRSQLH VVLAMSPIGD AFRNRLRKFP ALVNCCTIDW FQSWPEDALQ AVASRFLEEI
     EMSEEIRDGC IDMCKSFHTS TIDLSKSFFV ELQRYNYVTP TSYLELISTF KLLLEKKRSE
     VMKMKKRYEV GLEKLDSASS QVATMQMELE ALHPQLKVAS KEVDEMMIMI EKESVEVAKT
     EKIVKADETI ANEQAMASKA IKDECDADLA GALPILESAL AALDTLTAQD ITVVKSMKSP
     PAGVKLVMEA ICILKGIKAD KIPDPTGSGK KIEDFWGPAK RLLGDMRFLQ SLHEYDKDNI
     PPAYMNIIRK NYIPNPDFVP EKIRNASTAA EGLCKWVIAM DSYDKVAKIV APKKIKLAAA
     EGELKIAMDG LRKKQAALKE VQDKLARLQD TLELNKQKKA DLENQVDLCS KKLERAEQLI
     GGLGGEKTRW SHTALELGQL YINLTGDILI SSGVVAYLGA FTSTYRQNQT KEWTTLCKGR
     DIPCSDDCSL MGTLGEAVTI RTWNIAGLPS DSFSIDNGII IMNARRWPLM IDPQSQANKW
     IKNMEKANSL YVIKLSEPDY VRTLENCIQF GTPVLLENVG EELDPILEPL LLKQTFKQGG
     STCIRLGDST IEYAPDFRFY ITTKLRNPHY LPETSVKVTL LNFMITPEGM QDQLLGIVVA
     QERPDLEEEK QALILQGAEN KRQLKEIEDK ILEVLSSSEG NILEDETAIK ILSSSKALAN
     EISQKQEVAE ETEKKIDTTR MGYRPIAIHS SILFFSLADL ANIEPMYQYS LTWFINLFIL
     SIENSEKSEI LAKRLQILKD HFTYSLYVNV CRSLFEKDKL LFSFCLTINL LLHERAINKA
     EWRFLLTGGI GLDNPYANLC TWLPQKSWDE ICRLDDLPAF KTIRREFMRL KDGWKKVYDS
     LEPHHEVFPE EWEDKANEFQ RMLIIRCLRP DKVIPMLQEF IINRLGRAFI EPPPFDLAKA
     FGDSNCCAPL IFVLSPGADP MAALLKFADD QGYGGSKLSS LSLGQGQGPI AMKMLEKAVK
     EGTWVVLQNC HLATSWMPTL EKVCEELSPE STHPDFRMWL TSYPSPNFPV SVLQNGVKMT
     NEAPKGLRAN IIRSYLMDPI SDPEFFGSCK KPEEFKKLLY GLCFFHALVQ ERRKFGPLGW
     NIPYEFNETD LRISVQQLHM FLNQYEELPY EALRYMTGEC NYGGRVTDDW DRRTLRSILN
     KFFNPELVEN SDYKFDSSGI YFVPPSGDHK SYIEYTKTLP LTPAPEIFGM NANADITKDQ
     SETQLLFDNI LLTQSRSAGA GAKSSDEVVN EVASDILGKL PNNFDIEAAM RRYPTTYTQS
     MNTVLVQEMG RFNKLLKTIR DSCVNIQKAI KGLAVMSTDL EEVVSSILNV KIPEMWMGKS
     YPSLKPLGSY VNDFLARLKF LQQWYEVGPP PVFWLSGFFF TQAFLTGAQQ NYARKYTIPI
     DLLGFDYEVM EDKEYKHPPE DGVFIHGLFL DGASWNRKIK KLAESHPKIL YDTVPVMWLK
     PCKRADIPKR PSYVAPLYKT SERRGVLSTT GHSTNFVIAM TLPSDQPKEH WIGRGVALLC
     QLNS
//
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