ID   DYH2_HUMAN              Reviewed;        4427 AA.
AC   Q9P225; A8K992; B5MDX5; O15434; Q6PIH3; Q6ZR42;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 3.
DT   27-MAR-2024, entry version 155.
DE   RecName: Full=Dynein axonemal heavy chain 2 {ECO:0000305};
DE   AltName: Full=Axonemal beta dynein heavy chain 2;
DE   AltName: Full=Ciliary dynein heavy chain 2;
DE   AltName: Full=Dynein heavy chain domain-containing protein 3;
GN   Name=DNAH2 {ECO:0000312|HGNC:HGNC:2948};
GN   Synonyms=DNAHC2, DNHD3, KIAA1503;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA   Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XVII. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 7:143-150(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 3013-4427 (ISOFORM 2).
RC   TISSUE=Testis, and Trachea;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1820-1902 (ISOFORM 1), AND TISSUE
RP   SPECIFICITY.
RX   PubMed=9256245; DOI=10.1016/s0014-5793(97)00800-4;
RA   Chapelin C., Duriez B., Magnino F., Goossens M., Escudier E., Amselem S.;
RT   "Isolation of several human axonemal dynein heavy chain genes: genomic
RT   structure of the catalytic site, phylogenetic analysis and chromosomal
RT   assignment.";
RL   FEBS Lett. 412:325-330(1997).
RN   [6]
RP   RNA EDITING VARIANTS (ISOFORM 3).
RC   TISSUE=Brain;
RX   PubMed=20835228; DOI=10.1038/nchembio.434;
RA   Sakurai M., Yano T., Kawabata H., Ueda H., Suzuki T.;
RT   "Inosine cyanoethylation identifies A-to-I RNA editing sites in the human
RT   transcriptome.";
RL   Nat. Chem. Biol. 6:733-740(2010).
RN   [7]
RP   TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=31178125; DOI=10.1016/j.ajhg.2019.04.015;
RA   Whitfield M., Thomas L., Bequignon E., Schmitt A., Stouvenel L.,
RA   Montantin G., Tissier S., Duquesnoy P., Copin B., Chantot S., Dastot F.,
RA   Faucon C., Barbotin A.L., Loyens A., Siffroi J.P., Papon J.F., Escudier E.,
RA   Amselem S., Mitchell V., Toure A., Legendre M.;
RT   "Mutations in DNAH17, Encoding a Sperm-Specific Axonemal Outer Dynein Arm
RT   Heavy Chain, Cause Isolated Male Infertility Due to Asthenozoospermia.";
RL   Am. J. Hum. Genet. 105:198-212(2019).
RN   [8]
RP   VARIANTS SPGF45 CYS-1924; ARG-2320; TRP-3100; 3834-ARG--SER-4427 DEL AND
RP   PRO-3835, CHARACTERIZATION OF VARIANTS SPGF45 CYS-1924; ARG-2320; TRP-3100;
RP   3834-ARG--SER-4427 DEL AND PRO-3835, FUNCTION, SUBUNIT, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=30811583; DOI=10.1111/cge.13525;
RA   Li Y., Sha Y., Wang X., Ding L., Liu W., Ji Z., Mei L., Huang X., Lin S.,
RA   Kong S., Lu J., Qin W., Zhang X., Zhuang J., Tang Y., Lu Z.;
RT   "DNAH2 is a novel candidate gene associated with multiple morphological
RT   abnormalities of the sperm flagella.";
RL   Clin. Genet. 95:590-600(2019).
CC   -!- FUNCTION: As part of the axonemal inner dynein arm complex plays a
CC       central role in ciliary beat (PubMed:30811583). Expressed in sperm
CC       flagellum, it is required for sperm motility (PubMed:30811583). Dyneins
CC       are microtubule-based molecular motors possessing ATPase activities
CC       that can convert the chemical energy of ATP into relative sliding
CC       between adjacent microtubule doublets to generate ciliary bending
CC       (PubMed:30811583). {ECO:0000269|PubMed:30811583}.
CC   -!- SUBUNIT: Part of the axonemal inner dynein arm complex that consists of
CC       at least two heavy chains and a number of intermediate and light chains
CC       (PubMed:30811583). Interacts with DNAI4 (By similarity).
CC       {ECO:0000250|UniProtKB:P0C6F1, ECO:0000269|PubMed:30811583}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC       {ECO:0000250|UniProtKB:P0C6F1}. Cytoplasm, cytoskeleton, flagellum
CC       axoneme {ECO:0000269|PubMed:30811583}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9P225-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9P225-2; Sequence=VSP_031916, VSP_031917, VSP_031918;
CC       Name=3;
CC         IsoId=Q9P225-3; Sequence=VSP_031913, VSP_031914, VSP_031915;
CC   -!- TISSUE SPECIFICITY: Expressed primarily in trachea and testis, 2
CC       tissues containing axonemal structures. Also expressed in lung.
CC       Expressed in spermatozoa (at protein level) (PubMed:31178125).
CC       {ECO:0000269|PubMed:31178125, ECO:0000269|PubMed:9256245}.
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   -!- RNA EDITING: [Isoform 3]: Modified_positions=Not_applicable; Note=Exon
CC       13 is extensively edited in brain. {ECO:0000269|PubMed:20835228};
CC   -!- DISEASE: Spermatogenic failure 45 (SPGF45) [MIM:619094]: An autosomal
CC       recessive infertility disorder caused by spermatogenesis defects
CC       resulting in severe teratozoospermia. SPGF45 is characterized by
CC       multiple morphologic abnormalities of spermatozoa flagella. Some
CC       spermatozoa also show abnormalities of the head.
CC       {ECO:0000269|PubMed:30811583}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the dynein heavy chain family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AK128517; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAA96027.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB040936; BAA96027.2; ALT_INIT; mRNA.
DR   EMBL; AK128517; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK292607; BAF85296.1; -; mRNA.
DR   EMBL; AC025335; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC087388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC034225; AAH34225.1; -; mRNA.
DR   EMBL; U83570; AAB82760.1; -; Genomic_DNA.
DR   CCDS; CCDS32551.1; -. [Q9P225-1]
DR   CCDS; CCDS76937.1; -. [Q9P225-3]
DR   RefSeq; NP_001290199.1; NM_001303270.1. [Q9P225-3]
DR   RefSeq; NP_065928.2; NM_020877.3. [Q9P225-1]
DR   RefSeq; XP_011521969.1; XM_011523667.2. [Q9P225-1]
DR   PDB; 8J07; EM; 4.10 A; k9=1-4427.
DR   PDBsum; 8J07; -.
DR   EMDB; EMD-35888; -.
DR   SMR; Q9P225; -.
DR   BioGRID; 127007; 15.
DR   IntAct; Q9P225; 6.
DR   MINT; Q9P225; -.
DR   STRING; 9606.ENSP00000458355; -.
DR   iPTMnet; Q9P225; -.
DR   PhosphoSitePlus; Q9P225; -.
DR   BioMuta; DNAH2; -.
DR   DMDM; 172044680; -.
DR   EPD; Q9P225; -.
DR   MassIVE; Q9P225; -.
DR   PaxDb; 9606-ENSP00000458355; -.
DR   PeptideAtlas; Q9P225; -.
DR   ProteomicsDB; 83715; -. [Q9P225-1]
DR   ProteomicsDB; 83716; -. [Q9P225-2]
DR   ProteomicsDB; 83717; -. [Q9P225-3]
DR   TopDownProteomics; Q9P225-3; -. [Q9P225-3]
DR   Antibodypedia; 66685; 81 antibodies from 19 providers.
DR   DNASU; 146754; -.
DR   Ensembl; ENST00000389173.6; ENSP00000373825.2; ENSG00000183914.15. [Q9P225-1]
DR   Ensembl; ENST00000570791.5; ENSP00000460245.1; ENSG00000183914.15. [Q9P225-3]
DR   Ensembl; ENST00000572933.6; ENSP00000458355.1; ENSG00000183914.15. [Q9P225-1]
DR   GeneID; 146754; -.
DR   KEGG; hsa:146754; -.
DR   MANE-Select; ENST00000572933.6; ENSP00000458355.1; NM_020877.5; NP_065928.2.
DR   UCSC; uc002git.3; human. [Q9P225-1]
DR   AGR; HGNC:2948; -.
DR   CTD; 146754; -.
DR   DisGeNET; 146754; -.
DR   GeneCards; DNAH2; -.
DR   HGNC; HGNC:2948; DNAH2.
DR   HPA; ENSG00000183914; Tissue enhanced (fallopian tube, parathyroid gland, retina).
DR   MalaCards; DNAH2; -.
DR   MIM; 603333; gene.
DR   MIM; 619094; phenotype.
DR   neXtProt; NX_Q9P225; -.
DR   OpenTargets; ENSG00000183914; -.
DR   PharmGKB; PA27401; -.
DR   VEuPathDB; HostDB:ENSG00000183914; -.
DR   eggNOG; KOG3595; Eukaryota.
DR   GeneTree; ENSGT00940000157623; -.
DR   HOGENOM; CLU_000038_0_3_1; -.
DR   InParanoid; Q9P225; -.
DR   OMA; ILKNDMQ; -.
DR   OrthoDB; 166463at2759; -.
DR   PhylomeDB; Q9P225; -.
DR   TreeFam; TF316836; -.
DR   PathwayCommons; Q9P225; -.
DR   SignaLink; Q9P225; -.
DR   BioGRID-ORCS; 146754; 14 hits in 1146 CRISPR screens.
DR   ChiTaRS; DNAH2; human.
DR   GenomeRNAi; 146754; -.
DR   Pharos; Q9P225; Tbio.
DR   PRO; PR:Q9P225; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q9P225; Protein.
DR   Bgee; ENSG00000183914; Expressed in bronchial epithelial cell and 102 other cell types or tissues.
DR   ExpressionAtlas; Q9P225; baseline and differential.
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:0005930; C:axoneme; IDA:UniProtKB.
DR   GO; GO:0030286; C:dynein complex; IBA:GO_Central.
DR   GO; GO:0036156; C:inner dynein arm; IMP:UniProtKB.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0031514; C:motile cilium; IDA:UniProtKB.
DR   GO; GO:0036126; C:sperm flagellum; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; 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:0060294; P:cilium movement involved in cell motility; IBA:GO_Central.
DR   GO; GO:0060285; P:cilium-dependent cell motility; IMP:UniProtKB.
DR   GO; GO:0036159; P:inner dynein arm assembly; IMP:UniProtKB.
DR   CDD; cd00009; AAA; 1.
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; IPR013594; Dynein_heavy_tail.
DR   InterPro; IPR042228; Dynein_linker_3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR45703; DYNEIN HEAVY CHAIN; 1.
DR   PANTHER; PTHR45703:SF32; DYNEINS HEAVY CHAIN; 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; PF08385; DHC_N1; 2.
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.
DR   Genevisible; Q9P225; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; Cell projection; Cilium;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Disease variant; Dynein; Flagellum;
KW   Microtubule; Motor protein; Nucleotide-binding; Reference proteome; Repeat;
KW   RNA editing; TPR repeat.
FT   CHAIN           1..4427
FT                   /note="Dynein axonemal heavy chain 2"
FT                   /id="PRO_0000322542"
FT   REPEAT          1404..1439
FT                   /note="TPR 1"
FT   REPEAT          2721..2754
FT                   /note="TPR 2"
FT   REPEAT          3072..3105
FT                   /note="TPR 3"
FT   REPEAT          4072..4104
FT                   /note="TPR 4"
FT   REPEAT          4105..4140
FT                   /note="TPR 5"
FT   REGION          1..1764
FT                   /note="Stem"
FT                   /evidence="ECO:0000250"
FT   REGION          1..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1765..1986
FT                   /note="AAA 1"
FT                   /evidence="ECO:0000250"
FT   REGION          2046..2273
FT                   /note="AAA 2"
FT                   /evidence="ECO:0000250"
FT   REGION          2378..2625
FT                   /note="AAA 3"
FT                   /evidence="ECO:0000250"
FT   REGION          2722..2974
FT                   /note="AAA 4"
FT                   /evidence="ECO:0000250"
FT   REGION          2989..3272
FT                   /note="Stalk"
FT                   /evidence="ECO:0000250"
FT   REGION          3358..3588
FT                   /note="AAA 5"
FT                   /evidence="ECO:0000250"
FT   REGION          3804..4023
FT                   /note="AAA 6"
FT                   /evidence="ECO:0000250"
FT   COILED          3012..3049
FT                   /evidence="ECO:0000255"
FT   COILED          3216..3304
FT                   /evidence="ECO:0000255"
FT   COILED          3523..3567
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        12..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..61
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1803..1810
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2084..2091
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2416..2423
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2762..2769
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         390
FT                   /note="K -> KMSNEIIRLCCHAISLDRIFEGYVSSSKEDLQGCILCCHAWKDHYVQ
FT                   AVQMHIQFSSRGWVLDQTSIFAQVDAFVQRCKDLIE (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_031913"
FT   VAR_SEQ         636..790
FT                   /note="SLLILFAEIDYWERLLFETPHYVVNVAERAEDLRILRENLLLVARDYNRIIA
FT                   MLSPDEQALFKERIRLLDKKIHPGLKKLHWALKGASAFFITECRIHASKVQMIVNEFKA
FT                   STLTIGWRAQEMSEKLLVRISGKRVYRDLEFEEDQREHRAAVQQ -> YRSHLAPFPYT
FT                   PLLQLSQEFHSHLLTPLFIILSLSHTICLLSSFYFFFSSFIFVSPHLPPCYQHFNFTTY
FT                   LKTQQNKTMIGQARWLTPVIPALWEAEVGASLEPRSLRTAWATWQNPVSAKNTKISWAW
FT                   WHKPVVSATWEGEVGGSPEPGRQRLQ (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_031914"
FT   VAR_SEQ         791..4427
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_031915"
FT   VAR_SEQ         3062..3100
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_031916"
FT   VAR_SEQ         4211..4235
FT                   /note="EKGIQGLIVMSTSLEEIFNCIFDAH -> EIPSCVSHKSERVVLELSAVKHP
FT                   RQ (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_031917"
FT   VAR_SEQ         4236..4427
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_031918"
FT   VARIANT         100
FT                   /note="A -> V (in dbSNP:rs35664870)"
FT                   /id="VAR_039407"
FT   VARIANT         312
FT                   /note="S -> T (in dbSNP:rs3744254)"
FT                   /id="VAR_039408"
FT   VARIANT         1326
FT                   /note="E -> G (in dbSNP:rs11868946)"
FT                   /id="VAR_039409"
FT   VARIANT         1924
FT                   /note="R -> C (in SPGF45; decreased protein abundance; loss
FT                   of inner dynein arm assembly; in spermatozoa from
FT                   patients)"
FT                   /evidence="ECO:0000269|PubMed:30811583"
FT                   /id="VAR_085171"
FT   VARIANT         2320
FT                   /note="S -> R (in SPGF45; uncertain significance; decreased
FT                   protein abundance)"
FT                   /evidence="ECO:0000269|PubMed:30811583"
FT                   /id="VAR_085172"
FT   VARIANT         2548
FT                   /note="R -> H (in dbSNP:rs11656500)"
FT                   /id="VAR_039410"
FT   VARIANT         2904
FT                   /note="R -> H (in dbSNP:rs2309808)"
FT                   /id="VAR_060134"
FT   VARIANT         3100
FT                   /note="R -> W (in SPGF45; uncertain significance; decreased
FT                   protein abundance)"
FT                   /evidence="ECO:0000269|PubMed:30811583"
FT                   /id="VAR_085173"
FT   VARIANT         3600
FT                   /note="T -> I (in dbSNP:rs7213894)"
FT                   /id="VAR_039411"
FT   VARIANT         3834..4427
FT                   /note="Missing (in SPGF45; decreased protein abundance;
FT                   loss of inner dynein arm assembly; in spermatozoa from
FT                   patients)"
FT                   /evidence="ECO:0000269|PubMed:30811583"
FT                   /id="VAR_085174"
FT   VARIANT         3835
FT                   /note="S -> P (in SPGF45; uncertain significance; decreased
FT                   protein abundance)"
FT                   /evidence="ECO:0000269|PubMed:30811583"
FT                   /id="VAR_085175"
FT   CONFLICT        593
FT                   /note="E -> G (in Ref. 4; AAH34225)"
FT                   /evidence="ECO:0000305"
FT   VARIANT         Q9P225-3:812
FT                   /note="E -> G (in RNA edited version)"
FT                   /evidence="ECO:0000305"
FT                   /id="VAR_082806"
FT   VARIANT         Q9P225-3:814
FT                   /note="E -> G (in RNA edited version)"
FT                   /evidence="ECO:0000305"
FT                   /id="VAR_082807"
FT   VARIANT         Q9P225-3:826
FT                   /note="T -> A (in RNA edited version)"
FT                   /evidence="ECO:0000305"
FT                   /id="VAR_082808"
FT   VARIANT         Q9P225-3:833
FT                   /note="N -> D (in RNA edited version)"
FT                   /evidence="ECO:0000305"
FT                   /id="VAR_082809"
FT   VARIANT         Q9P225-3:838
FT                   /note="K -> E (in RNA edited version)"
FT                   /evidence="ECO:0000305"
FT                   /id="VAR_082810"
FT   VARIANT         Q9P225-3:839
FT                   /note="N -> D (in RNA edited version)"
FT                   /evidence="ECO:0000305"
FT                   /id="VAR_082811"
FT   VARIANT         Q9P225-3:841
FT                   /note="K -> E (in RNA edited version)"
FT                   /evidence="ECO:0000305"
FT                   /id="VAR_082812"
FT   VARIANT         Q9P225-3:843
FT                   /note="S -> G (in RNA edited version)"
FT                   /evidence="ECO:0000305"
FT                   /id="VAR_082813"
FT   VARIANT         Q9P225-3:855
FT                   /note="T -> A (in RNA edited version; dbSNP:rs1019704300)"
FT                   /evidence="ECO:0000305"
FT                   /id="VAR_082814"
FT   VARIANT         Q9P225-3:865
FT                   /note="E -> G (in RNA edited version)"
FT                   /evidence="ECO:0000305"
FT                   /id="VAR_082815"
FT   VARIANT         Q9P225-3:869
FT                   /note="Q -> R (in RNA edited version)"
FT                   /evidence="ECO:0000305"
FT                   /id="VAR_082816"
FT   VARIANT         Q9P225-3:872
FT                   /note="Q -> R (in RNA edited version)"
FT                   /evidence="ECO:0000305"
FT                   /id="VAR_082817"
SQ   SEQUENCE   4427 AA;  507698 MW;  A270F73DBDE2C3C4 CRC64;
     MSSKAEKKQR LSGRGSSQAS WSGRATRAAV ATQEQGNAPA VSEPELQAEL PKEEPEPRLE
     GPQAQSEESV EPEADVKPLF LSRAALTGLA DAVWTQEHDA ILEHFAQDPT ESILTIFIDP
     CFGLKLELGM PVQTQNQLVY FIRQAPVPIT WENFEATVQF GTVRGPYIPA LLRLLGGVFA
     PQIFANTGWP ESIRNHFASH LHKFLACLTD TRYKLEGHTV LYIPAEAMNM KPEMVIKDKE
     LVQRLETSMI HWTRQIKEML SAQETVETGE NLGPLEEIEF WRNRCMDLSG ISKQLVKKGV
     KHVESILHLA KSSYLAPFMK LAQQIQDGSR QAQSNLTFLS ILKEPYQELA FMKPKDISSK
     LPKLISLIRI IWVNSPHYNT RERLTSLFRK VCDCQYHFAR WEDGKQGPLP CFFGAQGPQI
     TRNLLEIEDI FHKNLHTLRA VRGGILDVKN TCWHEDYNKF RAGIKDLEVM TQNLITSAFE
     LVRDVPHGVL LLDTFHRLAS REAIKRTYDK KAVDLYMLFN SELALVNRER NKKWPDLEPY
     VAQYSGKARW VHILRRRIDR VMTCLAGAHF LPRIGTGKES VHTYQQMVQA IDELVRKTFQ
     EWTSSLDKDC IRRLDTPLLR ISQEKAGMLD VNFDKSLLIL FAEIDYWERL LFETPHYVVN
     VAERAEDLRI LRENLLLVAR DYNRIIAMLS PDEQALFKER IRLLDKKIHP GLKKLHWALK
     GASAFFITEC RIHASKVQMI VNEFKASTLT IGWRAQEMSE KLLVRISGKR VYRDLEFEED
     QREHRAAVQQ KLMNLHQDVV TIMTNSYEVF KNDGPEIQQQ WMLYMIRLDR MMEDALRLNV
     KWSLLELSKA INGDGKTSPN PLFQVLVILK NDLQGSVAQV EFSPTLQTLA GVVNDIGNHL
     FSTISVFCHL PDILTKRKLH REPIQTVVEQ DEDIKKIQTQ ISSGMTNNAS LLQNYLKTWD
     MYREIWEINK DSFIHRYQRL NPPVSSFVAD IARYTEVANN VQKEETVTNI QFVLLDCSHL
     KFSLVQHCNE WQNKFATLLR EMAAGRLLEL HTYLKENAEK ISRPPQTLEE LGVSLQLVDA
     LKHDLANVET QIPPIHEQFA ILEKYEVPVE DSVLEMLDSL NGEWVVFQQT LLDSKQMLKK
     HKEKFKTGLI HSADDFKKKA HTLLEDFEFK GHFTSNVGYM SALDQITQVR AMLMAMREEE
     NSLRANLGIF KIEQPPSKDL QNLEKELDAL QQIWEIARDW EENWNEWKTG RFLILQTETM
     ETTAHGLFRR LTKLAKEYKD RNWEIIETTR SKIEQFKRTM PLISDLRNPA LRERHWDQVR
     DEIQREFDQE SESFTLEQIV ELGMDQHVEK IGEISASATK ELAIEVALQN IAKTWDVTQL
     DIVPYKDKGH HRLRGTEEVF QALEDNQVAL STMKASRFVK AFEKDVDHWE RCLSLILEVI
     EMILTVQRQW MYLENIFLGE DIRKQLPNES TLFDQVNSNW KAIMDRMNKD NNALRSTHHP
     GLLDTLIEMN TILEDIQKSL DMYLETKRHI FPRFYFLSND DLLEILGQSR NPEAVQPHLK
     KCFDNIKLLR IQKVGGPSSK WEAVGMFSGD GEYIDFLHSV FLEGPVESWL GDVEQTMRVT
     LRDLLRNCHL ALRKFLNKRD KWVKEWAGQV VITASQIQWT ADVTKCLLTA KERADKKILK
     VMKKNQVSIL NKYSEAIRGN LTKIMRLKIV ALVTIEIHAR DVLEKLYKSG LMDVNSFDWL
     SQLRFYWEKD LDDCVIRQTN TQFQYNYEYL GNSGRLVITP LTDRCYMTLT TALHLHRGGS
     PKGPAGTGKT ETVKDLGKAL GIYVIVVNCS EGLDYKSMGR MYSGLAQTGA WGCFDEFNRI
     NIEVLSVVAH QILCILSALA AGLTHFHFDG FEINLVWSCG IFITMNPGYA GRTELPENLK
     SMFRPIAMVV PDSTLIAEII LFGEGFGNCK ILAKKVYTLY SLAVQQLSRQ DHYDFGLRAL
     TSLLRYAGKK RRLQPDLTDE EVLLLSMRDM NIAKLTSVDA PLFNAIVQDL FPNIELPVID
     YGKLRETVEQ EIRDMGLQST PFTLTKVFQL YETKNSRHST MIVGCTGSGK TASWRILQAS
     LSSLCRAGDP NFNIVREFPL NPKALSLGEL YGEYDLSTNE WTDGILSSVM RTACADEKPD
     EKWILFDGPV DTLWIENMNS VMDDNKVLTL INGERIAMPE QVSLLFEVED LAMASPATVS
     RCGMVYTDYA DLGWKPYVQS WLEKRPKAEV EPLQRMFEKL INKMLAFKKD NCKELVPLPE
     YSGITSLCKL YSALATPENG VNPADGENYV TMVEMTFVFS MIWSVCASVD EEGRKRIDSY
     LREIEGSFPN KDTVYEYFVD PKIRSWTSFE DKLPKSWRYP PNAPFYKIMV PTVDTVRYNY
     LVSSLVANQN PILLVGPVGT GKTSIAQSVL QSLPSSQWSV LVVNMSAQTT SNNVQSIIES
     RVEKRTKGVY VPFGGKSMIT FMDDLNMPAK DMFGSQPPLE LIRLWIDYGF WYDRTKQTIK
     YIREMFLMAA MGPPGGGRTV ISPRLRSRFN IINMTFPTKS QIIRIFGTMI NQKLQDFEEE
     VKPIGNVVTE ATLDMYNTVV QRFLPTPTKM HYLFNLRDIS KVFQGMLRAN KDFHDTKSSI
     TRLWIHECFR VFSDRLVDAA DTEAFMGIIS DKLGSFFDLT FHHLCPSKRP PIFGDFLKEP
     KVYEDLTDLT VLKTVMETAL NEYNLSPSVV PMQLVLFREA IEHITRIVRV IGQPRGNMLL
     VGIGGSGRQS LARLASSICD YTTFQIEVTK HYRKQEFRDD IKRLYRQAGV ELKTTSFIFV
     DTQIADESFL EDINNILSSG EVPNLYKPDE FEEIQSHIID QARVEQVPES SDSLFAYLIE
     RVQNNLHIVL CLSPMGDPFR NWIRQYPALV NCTTINWFSE WPQEALLEVA EKCLIGVDLG
     TQENIHRKVA QIFVTMHWSV AQYSQKMLLE LRRHNYVTPT KYLELLSGYK KLLGEKRQEL
     LAQANKLRTG LFKIDETREK VQVMSLELED AKKKVAEFQK QCEEYLVIIV QQKREADEQQ
     KAVTANSEKI AVEEIKCQAL ADNAQKDLEE ALPALEEAMR ALESLNKKDI GEIKSYGRPP
     AQVEIVMQAV MILRGNEPTW AEAKRQLGEQ NFIKSLINFD KDNISDKVLK KIGAYCAQPD
     FQPDIIGRVS LAAKSLCMWV RAMELYGRLY RVVEPKRIRM NAALAQLREK QAALAEAQEK
     LREVAEKLEM LKKQYDEKLA QKEELRKKSE EMELKLERAG MLVSGLAGEK ARWEETVQGL
     EEDLGYLVGD CLLAAAFLSY MGPFLTNYRD EIVNQIWIGK IWELQVPCSP SFAIDNFLCN
     PTKVRDWNIQ GLPSDAFSTE NGIIVTRGNR WALMIDPQAQ ALKWIKNMEG GQGLKIIDLQ
     MSDYLRILEH AIHFGYPVLL QNVQEYLDPT LNPMLNKSVA RIGGRLLMRI GDKEVEYNTN
     FRFYITTKLS NPHYSPETSA KTTIVNFAVK EQGLEAQLLG IVVRKERPEL EEQKDSLVIN
     IAAGKRKLKE LEDEILRLLN EATGSLLDDV QLVNTLHTSK ITATEVTEQL ETSETTEINT
     DLAREAYRPC AQRASILFFV LNDMGCIDPM YQFSLDAYIS LFILSIDKSH RSNKLEDRID
     YLNDYHTYAV YRYTCRTLFE RHKLLFSFHM CAKILETSGK LNMDEYNFFL RGGVVLDREG
     QMDNPCSSWL ADAYWDNITE LDKLTNFHGL MNSFEQYPRD WHLWYTNAAP EKAMLPGEWE
     NACNEMQRML IVRSLRQDRV AFCVTSFIIT NLGSRFIEPP VLNMKSVLED STPRSPLVFI
     LSPGVDPTSA LLQLAEHMGM AQRFHALSLG QGQAPIAARL LREGVTQGHW VFLANCHLSL
     SWMPNLDKLV EQLQVEDPHP SFRLWLSSIP HPDFPISILQ VSIKMTTEPP KGLKANMTRL
     YQLMSEPQFS RCSKPAKYKK LLFSLCFFHS VLLERKKFLQ LGWNIIYGFN DSDFEVSENL
     LSLYLDEYEE TPWDALKYLI AGINYGGHVT DDWDRRLLTT YINDYFCDQS LSTPFHRLSA
     LETYFIPKDG SLASYKEYIS LLPGMDPPEA FGQHPNADVA SQITEAQTLF DTLLSLQPQI
     TPTRAGGQTR EEKVLELAAD VKQKIPEMID YEGTQKLLAL DPSPLNVVLL QEIQRYNTLM
     QTILFSLTDL EKGIQGLIVM STSLEEIFNC IFDAHVPPLW GKAYPSQKPL AAWTRDLAMR
     VEQFELWASR ARPPVIFWLS GFTFPTGFLT AVLQSSARQN NVSVDSLSWE FIVSTVDDSN
     LVYPPKDGVW VRGLYLEGAG WDRKNSCLVE AEPMQLVCLM PTIHFRPAES RKKSAKGMYS
     CPCYYYPNRA GSSDRASFVI GIDLRSGAMT PDHWIKRGTA LLMSLDS
//