DYH2_HUMAN
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 03-AUG-2022, entry version 147.
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}; 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 SMR; Q9P225; -.
DR BioGRID; 127007; 13.
DR IntAct; Q9P225; 7.
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; Q9P225; -.
DR PeptideAtlas; Q9P225; -.
DR PRIDE; 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; 69 antibodies from 18 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 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; DPKMRSW; -.
DR OrthoDB; 1492at2759; -.
DR PhylomeDB; Q9P225; -.
DR TreeFam; TF316836; -.
DR PathwayCommons; Q9P225; -.
DR SignaLink; Q9P225; -.
DR BioGRID-ORCS; 146754; 12 hits in 1068 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 100 other tissues.
DR ExpressionAtlas; Q9P225; baseline and differential.
DR Genevisible; Q9P225; HS.
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: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:0003777; F:microtubule motor activity; NAS:UniProtKB.
DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; 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 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; 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 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; 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; SSF52540; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell projection; Cilium; Coiled coil;
KW Cytoplasm; Cytoskeleton; Disease variant; Dynein; Flagellum; Microtubule;
KW Motor protein; Nucleotide-binding; Reference proteome; Repeat; RNA editing;
KW 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; unknown pathological
FT significance; decreased 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; unknown pathological
FT significance; decreased 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; unknown pathological
FT significance; decreased 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
