DYH9_HUMAN
ID DYH9_HUMAN Reviewed; 4486 AA.
AC Q9NYC9; A2VCQ8; O15064; O95494; Q9NQ28;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Dynein axonemal heavy chain 9 {ECO:0000305};
DE AltName: Full=Axonemal beta dynein heavy chain 9;
DE AltName: Full=Ciliary dynein heavy chain 9;
GN Name=DNAH9 {ECO:0000312|HGNC:HGNC:2953}; Synonyms=DNAH17L, DNEL1, KIAA0357;
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), AND VARIANTS ARG-445 AND ILE-4374.
RA Reed W., Moats-Staats B.M., Carson J.L., Leigh M.W., Collier A.M.;
RT "A ciliary dynein heavy chain whose expression is upregulated in
RT differentiating airway epithelium.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ARG-445.
RC TISSUE=Nasal epithelium;
RX PubMed=11247663; DOI=10.1006/geno.2000.6462;
RA Bartoloni L., Blouin J.-L., Maiti A.K., Sainsbury A., Rossier C.,
RA Gehrig C., She J.X., Marron M.P., Lander E.S., Meeks M., Chung E.M.K.,
RA Armengot M., Jorissen M., Scott H.S., Delozier-Blanchet C.D.,
RA Gardiner R.M., Antonarakis S.E.;
RT "Axonemal beta heavy chain dynein DNAH9: cDNA sequence, genomic structure,
RT and investigation of its role in primary ciliary dyskinesia.";
RL Genomics 72:21-33(2001).
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).
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 [LARGE SCALE MRNA] OF 1419-4486 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [6]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R., Yamakawa H., Nomura N.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1874-1974 (ISOFORM 1).
RC TISSUE=Nasal polyp;
RA Maiti A.K., Mattei M.-G., Jorissen M., Volz A., Ziegler A., Bouvagnet P.;
RT "Chromosomal localization of human dynein heavy chain genes.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP CHARACTERIZATION.
RX PubMed=11104725; DOI=10.1165/ajrcmb.23.6.4045;
RA Reed W., Carson J.L., Moats-Staats B.M., Lucier T., Hu P.C., Brighton L.,
RA Gambling T.M., Huang C.H., Leigh M.W., Collier A.M.;
RT "Characterization of an axonemal dynein heavy chain expressed early in
RT airway epithelial ciliogenesis.";
RL Am. J. Respir. Cell Mol. Biol. 23:734-741(2000).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INVOLVEMENT IN CILD40,
RP VARIANTS CILD40 GLU-1881; HIS-2965; LEU-3398 AND ASN-4123, AND
RP CHARACTERIZATION OF VARIANTS CILD40 GLU-1881; HIS-2965 AND ASN-4123.
RX PubMed=30471717; DOI=10.1016/j.ajhg.2018.10.016;
RA Fassad M.R., Shoemark A., Legendre M., Hirst R.A., Koll F., le Borgne P.,
RA Louis B., Daudvohra F., Patel M.P., Thomas L., Dixon M., Burgoyne T.,
RA Hayes J., Nicholson A.G., Cullup T., Jenkins L., Carr S.B., Aurora P.,
RA Lemullois M., Aubusson-Fleury A., Papon J.F., O'Callaghan C., Amselem S.,
RA Hogg C., Escudier E., Tassin A.M., Mitchison H.M.;
RT "Mutations in outer dynein arm heavy chain DNAH9 cause motile cilia defects
RT and situs inversus.";
RL Am. J. Hum. Genet. 103:984-994(2018).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ODAD1, INVOLVEMENT IN
RP CILD40, VARIANTS CILD40 666-TRP--ILE-4486 DEL; ARG-1674; 2751-GLN--ILE-4486
RP DEL AND 3889-SER--ILE-4486 DEL, AND CHARACTERIZATION OF VARIANT CILD40
RP 2751-GLN--ILE-4486 DEL.
RX PubMed=30471718; DOI=10.1016/j.ajhg.2018.10.020;
RA Loges N.T., Antony D., Maver A., Deardorff M.A., Guelec E.Y., Gezdirici A.,
RA Noethe-Menchen T., Hoeben I.M., Jelten L., Frank D., Werner C., Tebbe J.,
RA Wu K., Goldmuntz E., Cuturilo G., Krock B., Ritter A., Hjeij R., Bakey Z.,
RA Pennekamp P., Dworniczak B., Brunner H., Peterlin B., Tanidir C.,
RA Olbrich H., Omran H., Schmidts M.;
RT "Recessive DNAH9 loss-of-function mutations cause laterality defects and
RT subtle respiratory ciliary-beating defects.";
RL Am. J. Hum. Genet. 103:995-1008(2018).
RN [11]
RP VARIANTS [LARGE SCALE ANALYSIS] LEU-771; HIS-2653 AND ASN-3664.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [12]
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).
CC -!- FUNCTION: Force generating protein required for cilia beating in
CC respiratory epithelia (PubMed:30471717, PubMed:30471718). Produces
CC force towards the minus ends of microtubules. Dynein has ATPase
CC activity; the force-producing power stroke is thought to occur on
CC release of ADP. {ECO:0000269|PubMed:30471717,
CC ECO:0000269|PubMed:30471718}.
CC -!- SUBUNIT: Consists of at least two heavy chains and a number of
CC intermediate and light chains. Interacts with ODAD1 (PubMed:30471718).
CC {ECO:0000269|PubMed:30471718}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000269|PubMed:30471717, ECO:0000269|PubMed:30471718,
CC ECO:0000269|PubMed:31178125}. Note=Found in the distal portion of
CC ciliary axoneme. {ECO:0000269|PubMed:30471717,
CC ECO:0000269|PubMed:30471718}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NYC9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NYC9-2; Sequence=VSP_035285;
CC Name=3;
CC IsoId=Q9NYC9-3; Sequence=VSP_043443;
CC -!- TISSUE SPECIFICITY: Expressed in upper and lower respiratory airway
CC epithelia (at protein level). Not detected in spermatozoa (at protein
CC level) (PubMed:31178125). {ECO:0000269|PubMed:30471717,
CC ECO:0000269|PubMed:31178125}.
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.
CC -!- DISEASE: Ciliary dyskinesia, primary, 40 (CILD40) [MIM:618300]: 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. Some patients exhibit randomization of left-
CC right body asymmetry and situs inversus. Primary ciliary dyskinesia
CC associated with situs inversus is referred to as Kartagener syndrome.
CC CILD40 inheritance is autosomal recessive.
CC {ECO:0000269|PubMed:30471717, ECO:0000269|PubMed:30471718}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the dynein heavy chain family. {ECO:0000305}.
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DR EMBL; AF257737; AAF69004.1; -; mRNA.
DR EMBL; AJ404468; CAB94756.1; -; mRNA.
DR EMBL; AC005209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005410; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005701; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC128421; AAI28422.1; -; mRNA.
DR EMBL; AB002355; BAA21573.2; -; mRNA.
DR EMBL; AJ132088; CAA10561.1; -; mRNA.
DR CCDS; CCDS11160.1; -. [Q9NYC9-1]
DR CCDS; CCDS11161.1; -. [Q9NYC9-3]
DR RefSeq; NP_001363.2; NM_001372.3. [Q9NYC9-1]
DR RefSeq; NP_004653.2; NM_004662.2. [Q9NYC9-3]
DR SMR; Q9NYC9; -.
DR BioGRID; 108109; 8.
DR IntAct; Q9NYC9; 1.
DR STRING; 9606.ENSP00000262442; -.
DR iPTMnet; Q9NYC9; -.
DR PhosphoSitePlus; Q9NYC9; -.
DR BioMuta; DNAH9; -.
DR DMDM; 311033454; -.
DR EPD; Q9NYC9; -.
DR jPOST; Q9NYC9; -.
DR MassIVE; Q9NYC9; -.
DR PaxDb; Q9NYC9; -.
DR PeptideAtlas; Q9NYC9; -.
DR PRIDE; Q9NYC9; -.
DR ProteomicsDB; 83213; -. [Q9NYC9-1]
DR ProteomicsDB; 83214; -. [Q9NYC9-2]
DR ProteomicsDB; 83215; -. [Q9NYC9-3]
DR Antibodypedia; 12949; 41 antibodies from 14 providers.
DR Ensembl; ENST00000262442.9; ENSP00000262442.3; ENSG00000007174.18. [Q9NYC9-1]
DR Ensembl; ENST00000608377.5; ENSP00000476951.1; ENSG00000007174.18. [Q9NYC9-3]
DR GeneID; 1770; -.
DR KEGG; hsa:1770; -.
DR MANE-Select; ENST00000262442.9; ENSP00000262442.3; NM_001372.4; NP_001363.2.
DR UCSC; uc002gne.3; human. [Q9NYC9-1]
DR CTD; 1770; -.
DR DisGeNET; 1770; -.
DR GeneCards; DNAH9; -.
DR HGNC; HGNC:2953; DNAH9.
DR HPA; ENSG00000007174; Group enriched (brain, choroid plexus, fallopian tube).
DR MalaCards; DNAH9; -.
DR MIM; 603330; gene.
DR MIM; 618300; phenotype.
DR neXtProt; NX_Q9NYC9; -.
DR OpenTargets; ENSG00000007174; -.
DR Orphanet; 244; Primary ciliary dyskinesia.
DR Orphanet; 157769; Situs ambiguus.
DR Orphanet; 101063; Situs inversus totalis.
DR PharmGKB; PA27406; -.
DR VEuPathDB; HostDB:ENSG00000007174; -.
DR eggNOG; KOG3595; Eukaryota.
DR GeneTree; ENSGT00940000159717; -.
DR HOGENOM; CLU_000038_9_1_1; -.
DR InParanoid; Q9NYC9; -.
DR OMA; ERRHVYT; -.
DR OrthoDB; 1492at2759; -.
DR PhylomeDB; Q9NYC9; -.
DR TreeFam; TF316836; -.
DR PathwayCommons; Q9NYC9; -.
DR SignaLink; Q9NYC9; -.
DR BioGRID-ORCS; 1770; 3 hits in 1066 CRISPR screens.
DR ChiTaRS; DNAH9; human.
DR GeneWiki; DNAH9; -.
DR GenomeRNAi; 1770; -.
DR Pharos; Q9NYC9; Tdark.
DR PRO; PR:Q9NYC9; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9NYC9; protein.
DR Bgee; ENSG00000007174; Expressed in right uterine tube and 126 other tissues.
DR ExpressionAtlas; Q9NYC9; baseline and differential.
DR Genevisible; Q9NYC9; HS.
DR GO; GO:0097729; C:9+2 motile cilium; IDA:GO_Central.
DR GO; GO:0005930; C:axoneme; IDA:UniProtKB.
DR GO; GO:0120135; C:distal portion of axoneme; IDA:UniProtKB.
DR GO; GO:0030286; C:dynein complex; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0031514; C:motile cilium; IDA:UniProtKB.
DR GO; GO:0036157; C:outer dynein arm; IEA:Ensembl.
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:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0090660; P:cerebrospinal fluid circulation; IEA:Ensembl.
DR GO; GO:0003341; P:cilium movement; IMP:UniProtKB.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0120197; P:mucociliary clearance; IEA:Ensembl.
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; IPR030443; DNAH9-like.
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 PANTHER; PTHR10676:SF257; PTHR10676:SF257; 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; 4.
DR SUPFAM; SSF52540; SSF52540; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell projection; Ciliopathy; Cilium;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Disease variant; Dynein; Kartagener syndrome; Microtubule; Motor protein;
KW Nucleotide-binding; Primary ciliary dyskinesia; Reference proteome; Repeat.
FT CHAIN 1..4486
FT /note="Dynein axonemal heavy chain 9"
FT /id="PRO_0000114632"
FT REGION 1..1831
FT /note="Stem"
FT /evidence="ECO:0000250"
FT REGION 1832..2053
FT /note="AAA 1"
FT /evidence="ECO:0000250"
FT REGION 2113..2334
FT /note="AAA 2"
FT /evidence="ECO:0000250"
FT REGION 2440..2688
FT /note="AAA 3"
FT /evidence="ECO:0000250"
FT REGION 2787..3036
FT /note="AAA 4"
FT /evidence="ECO:0000250"
FT REGION 3051..3341
FT /note="Stalk"
FT /evidence="ECO:0000250"
FT REGION 3429..3656
FT /note="AAA 5"
FT /evidence="ECO:0000250"
FT REGION 3866..4092
FT /note="AAA 6"
FT /evidence="ECO:0000250"
FT COILED 381..410
FT /evidence="ECO:0000255"
FT COILED 504..529
FT /evidence="ECO:0000255"
FT COILED 639..662
FT /evidence="ECO:0000255"
FT COILED 752..823
FT /evidence="ECO:0000255"
FT COILED 1326..1355
FT /evidence="ECO:0000255"
FT COILED 3051..3154
FT /evidence="ECO:0000255"
FT COILED 3285..3341
FT /evidence="ECO:0000255"
FT COILED 3640..3675
FT /evidence="ECO:0000255"
FT BINDING 1870..1877
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2151..2158
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2478..2485
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2825..2832
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..3688
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043443"
FT VAR_SEQ 3961..4036
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9205841"
FT /id="VSP_035285"
FT VARIANT 151
FT /note="R -> H (in dbSNP:rs17599639)"
FT /id="VAR_046312"
FT VARIANT 445
FT /note="Q -> R (in dbSNP:rs9892256)"
FT /evidence="ECO:0000269|PubMed:11247663, ECO:0000269|Ref.1"
FT /id="VAR_046313"
FT VARIANT 666..4486
FT /note="Missing (in CILD40)"
FT /evidence="ECO:0000269|PubMed:30471718"
FT /id="VAR_081802"
FT VARIANT 771
FT /note="R -> L (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036214"
FT VARIANT 842
FT /note="R -> W (in dbSNP:rs16945138)"
FT /id="VAR_046314"
FT VARIANT 1158
FT /note="R -> W (in dbSNP:rs8070501)"
FT /id="VAR_046315"
FT VARIANT 1221
FT /note="T -> A (in dbSNP:rs9916482)"
FT /id="VAR_046316"
FT VARIANT 1674
FT /note="G -> R (in CILD40; unknown pathological
FT significance; dbSNP:rs140721719)"
FT /evidence="ECO:0000269|PubMed:30471718"
FT /id="VAR_081803"
FT VARIANT 1881
FT /note="K -> E (in CILD40; associated in cis with H-2965; no
FT protein detected by Western blot when associated with H-
FT 2965; loss of localization to cilium axonema associated
FT with H-2965; dbSNP:rs1567747142)"
FT /evidence="ECO:0000269|PubMed:30471717"
FT /id="VAR_081804"
FT VARIANT 2087
FT /note="M -> V (in dbSNP:rs9892290)"
FT /id="VAR_046317"
FT VARIANT 2195
FT /note="N -> S (in dbSNP:rs3744581)"
FT /id="VAR_046318"
FT VARIANT 2438
FT /note="Q -> H (in dbSNP:rs2277658)"
FT /id="VAR_046319"
FT VARIANT 2653
FT /note="D -> H (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036215"
FT VARIANT 2751..4486
FT /note="Missing (in CILD40; loss of localization to cilium
FT axonema)"
FT /evidence="ECO:0000269|PubMed:30471718"
FT /id="VAR_081805"
FT VARIANT 2961
FT /note="K -> R (in dbSNP:rs11870983)"
FT /id="VAR_046320"
FT VARIANT 2965
FT /note="R -> H (in CILD40; associated in cis with E-1881; no
FT protein detected by Western blot when associated with E-
FT 1881; loss of localization to cilium axonema when
FT associated with E-1881; dbSNP:rs375908701)"
FT /evidence="ECO:0000269|PubMed:30471717"
FT /id="VAR_081806"
FT VARIANT 2968
FT /note="K -> N (in dbSNP:rs11871037)"
FT /id="VAR_046321"
FT VARIANT 3398
FT /note="R -> L (in CILD40; dbSNP:rs763238622)"
FT /evidence="ECO:0000269|PubMed:30471717"
FT /id="VAR_081807"
FT VARIANT 3664
FT /note="T -> N (in a breast cancer sample; somatic mutation;
FT dbSNP:rs138874996)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036216"
FT VARIANT 3726
FT /note="R -> Q (in dbSNP:rs16945431)"
FT /id="VAR_046322"
FT VARIANT 3726
FT /note="R -> W (in dbSNP:rs3760436)"
FT /id="VAR_046323"
FT VARIANT 3889..4486
FT /note="Missing (in CILD40)"
FT /evidence="ECO:0000269|PubMed:30471718"
FT /id="VAR_081808"
FT VARIANT 4036
FT /note="D -> N (in dbSNP:rs17612861)"
FT /id="VAR_046324"
FT VARIANT 4123
FT /note="D -> N (in CILD40; loss of localization to cilium
FT axonema; dbSNP:rs1267599270)"
FT /evidence="ECO:0000269|PubMed:30471717"
FT /id="VAR_081809"
FT VARIANT 4374
FT /note="M -> I (in dbSNP:rs1990236)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_046325"
FT VARIANT 4443
FT /note="R -> C (in dbSNP:rs9913494)"
FT /id="VAR_046326"
FT VARIANT 4462
FT /note="W -> R (in dbSNP:rs8074656)"
FT /id="VAR_046327"
FT CONFLICT 2216
FT /note="I -> T (in Ref. 5; BAA21573)"
FT /evidence="ECO:0000305"
FT CONFLICT 2505
FT /note="V -> L (in Ref. 1; AAF69004)"
FT /evidence="ECO:0000305"
FT CONFLICT 3678
FT /note="A -> T (in Ref. 1; AAF69004)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 4486 AA; 511877 MW; 27EB53C39FA3A293 CRC64;
MRLAEERAAL AAENADGEPG ADRRLRLLGT YVAMSLRPAA GAWERCAGSA EAEQLLQAFL
GRDAAEGPRP LLVVRPGPRG LAIRPGLEVG PESGLAGAKA LFFLRTGPEP PGPDSFRGAV
VCGDLPAAPL EHLAALFSEV VLPVLANEKN RLNWPHMICE DVRRHAHSLQ CDLSVILEQV
KGKTLLPLPA GSEKMEFADS KSETVLDSID KSVIYAIESA VIKWSYQVQV VLKRESSQPL
LQGENPTPKV ELEFWKSRYE DLKYIYNQLR TITVRGMAKL LDKLQSSYFP AFKAMYRDVV
AALAEAQDIH VHLIPLQRHL EALENAEFPE VKPQLRPLLH VVCLIWATCK SYRSPGRLTV
LLQEICNLLI QQASNYLSPE DLLRSEVEES QRKLQVVSDT LSFFKQEFQD RRENLHTYFK
ENQEVKEWDF QSSLVFVRLD GFLGQLHVVE GLLKTALDFH KLGKVEFSGV RGNALSQQVQ
QMHEEFQEMY RLLSGSSSDC LYLQSTDFEN DVSEFNQKVE DLDRRLGTIF IQAFDDAPGL
EHAFKLLDIA GNLLERPLVA RDTSDKYLVL IQMFNKDLDA VRMIYSQHVQ EEAELGFSPV
HKNMPTVAGG LRWAQELRQR IQGPFSNFGR ITHPCMESAE GKRMQQKYED MLSLLEKYET
RLYEDWCRTV SEKSQYNLSQ PLLKRDPETK EITINFNPQL ISVLKEMSYL EPREMKHMPE
TAAAMFSSRD FYRQLVANLE LMANWYNKVM KTLLEVEFPL VEEELQNIDL RLRAAEETLN
WKTEGICDYV TEITSSIHDL EQRIQKTKDN VEEIQNIMKT WVTPIFKTKD GKRESLLSLD
DRHDRMEKYY NLIKESGLKI HALVQENLGL FSADPTSNIW KTYVNSIDNL LLNGFFLAIE
CSLKYLLENT ECKAGLTPIF EAQLSLAIPE LVFYPSLESG VKGGFCDIVE GLITSIFRIP
SLVPRLSPQN GSPHYQVDLD GIPDLANMRR TLMERVQRMM GLCCGYQSTF SQYSYLYVED
RKEVLGQFLL YGHILTPEEI EDHVEDGIPE NPPLLSQFKV QIDSYETLYE EVCRLEPIKV
FDGWMKIDIR PFKASLLNII KRWSLLFKQH LVDHVTHSLA NLDAFIKKSE SGLLKKVEKG
DFQGLVEIMG HLMAVKERQS NTDEMFEPLK QTIELLKTYE QELPETVFKQ LEELPEKWNN
IKKVAITVKQ QVAPLQANEV TLLRQRCTAF DAEQQQFWEQ FHKEAPFRFD SIHPHQMLDA
RHIEIQQMES TMASISESAS LFEVNVPDYK QLRQCRKEVC QLKELWDTIG MVTSSIHAWE
TTPWRNINVE AMELECKQFA RHIRNLDKEV RAWDAFTGLE STVWNTLSSL RAVAELQNPA
IRERHWRQLM QATGVSFTMD QDTTLAHLLQ LQLHHYEDEV RGIVDKAAKE MGMEKTLKEL
QTTWAGMEFQ YEPHPRTNVP LLCSDEDLIE VLEDNQVQLQ NLVMSKYVAF FLEEVSGWQK
KLSTVDAVIS IWFEVQRTWT HLESIFTGSE DIRAQLPQDS KRFEGIDIDF KELAYDAQKI
PNVVQTTNKP GLYEKLEDIQ GRLCLCEKAL AEYLDTKRLA FPRFYFLSSS DLLDILSNGT
APQQVQRHLS KLFDNMAKMR FQLDASGEPT KTSLGMYSKE EEYVAFSEPC DCSGQVEIWL
NHVLGHMKAT VRHEMTEGVT AYEEKPREQW LFDHPAQVAL TCTQIWWTTE VGMAFARLEE
GYESAMKDYY KKQVAQLKTL ITMLIGQLSK GDRQKIMTIC TIDVHARDVV AKMIAQKVDN
AQAFLWLSQL RHRWDDEVKH CFANICDAQF LYSYEYLGNT PRLVITPLTD RCYITLTQSL
HLTMSGAPAG PAGTGKTETT KDLGRALGIL VYVFNCSEQM DYKSCGNIYK GLAQTGAWGC
FDEFNRISVE VLSVVAVQVK SIQDAIRDKK QWFSFLGEEI SLNPSVGIFI TMNPGYAGRT
ELPENLKSLF RPCAMVVPDF ELICEIMLVA EGFIEAQSLA RKFITLYQLC KELLSKQDHY
DWGLRAIKSV LVVAGSLKRG DPDRPEDQVL MRSLRDFNIP KIVTDDMPIF MGLIGDLFPA
LDVPRRRDPN FEALVRKAIV DLKLQAEDNF VLKVVQLEEL LAVRHSVFVV GGAGTGKSQV
LRSLHKTYQI MKRRPVWTDL NPKAVTNDEL FGIINPATGE WKDGLFSSIM RELANITHDG
PKWILLDGDI DPMWIESLNT VMDDNKVLTL ASNERIPLNP TMKLLFEISH LRTATPATVS
RAGILYINPA DLGWNPPVSS WIEKREIQTE RANLTILFDK YLPTCLDTLR TRFKKIIPIP
EQSMVQMVCH LLECLLTTED IPADCPKEIY EHYFVFAAIW AFGGAMVQDQ LVDYRAEFSK
WWLTEFKTVK FPSQGTIFDY YIDPETKKFE PWSKLVPQFE FDPEMPLQAC LVHTSETIRV
CYFMERLMAR QRPVMLVGTA GTGKSVLVGA KLASLDPEAY LVKNVPFNYY TTSAMLQAVL
EKPLEKKAGR NYGPPGNKKL IYFIDDMNMP EVDAYGTVQP HTIIRQHLDY GHWYDRSKLS
LKEITNVQYV SCMNPTAGSF TINPRLQRHF SVFVLSFPGA DALSSIYSII LTQHLKLGNF
PASLQKSIPP LIDLALAFHQ KIATTFLPTG IKFHYIFNLR DFANIFQGIL FSSVECVKST
WDLIRLYLHE SNRVYRDKMV EEKDFDLFDK IQTEVLKKTF DDIEDPVEQT QSPNLYCHFA
NGIGEPKYMP VQSWELLTQT LVEALENHNE VNTVMDLVLF EDAMRHVCHI NRILESPRGN
ALLVGVGGSG KQSLTRLAAF ISSMDVFQIT LRKGYQIQDF KMDLASLCLK AGVKNLNTVF
LMTDAQVADE RFLVLINDLL ASGEIPDLYS DDEVENIISN VRNEVKSQGL VDNRENCWKF
FIDRIRRQLK VTLCFSPVGN KLRVRSRKFP AIVNCTAIHW FHEWPQQALE SVSLRFLQNT
EGIEPTVKQS ISKFMAFVHT SVNQTSQSYL SNEQRYNYTT PKSFLEFIRL YQSLLHRHRK
ELKCKTERLE NGLLKLHSTS AQVDDLKAKL AAQEVELKQK NEDADKLIQV VGVETDKVSR
EKAMADEEEQ KVAVIMLEVK QKQKDCEEDL AKAEPALTAA QAALNTLNKT NLTELKSFGS
PPLAVSNVSA AVMVLMAPRG RVPKDRSWKA AKVTMAKVDG FLDSLINFNK ENIHENCLKA
IRPYLQDPEF NPEFVATKSY AAAGLCSWVI NIVRFYEVFC DVEPKRQALN KATADLTAAQ
EKLAAIKAKI AHLNENLAKL TARFEKATAD KLKCQQEAEV TAVTISLANR LVGGLASENV
RWADAVQNFK QQERTLCGDI LLITAFISYL GFFTKKYRQS LLDRTWRPYL SQLKTPIPVT
PALDPLRMLM DDADVAAWQN EGLPADRMSV ENATILINCE RWPLMVDPQL QGIKWIKNKY
GEDLRVTQIG QKGYLQIIEQ ALEAGAVVLI ENLEESIDPV LGPLLGREVI KKGRFIKIGD
KECEYNPKFR LILHTKLANP HYQPELQAQA TLINFTVTRD GLEDQLLAAV VSMERPDLEQ
LKSDLTKQQN GFKITLKTLE DSLLSRLSSA SGNFLGETVL VENLEITKQT AAEVEKKVQE
AKVTEVKINE AREHYRPAAA RASLLYFIMN DLSKIHPMYQ FSLKAFSIVF QKAVERAAPD
ESLRERVANL IDSITFSVYQ YTIRGLFECD KLTYLAQLTF QILLMNREVN AVELDFLLRS
PVQTGTASPV EFLSHQAWGA VKVLSSMEEF SNLDRDIEGS AKSWKKFVES ECPEKEKLPQ
EWKNKTALQR LCMLRAMRPD RMTYALRDFV EEKLGSKYVV GRALDFATSF EESGPATPMF
FILSPGVDPL KDVESQGRKL GYTFNNQNFH NVSLGQGQEV VAEAALDLAA KKGHWVILQN
IHLVAKWLST LEKKLEEHSE NSHPEFRVFM SAEPAPSPEG HIIPQGILEN SIKITNEPPT
GMHANLHKAL DNFTQDTLEM CSRETEFKSI LFALCYFHAV VAERRKFGPQ GWNRSYPFNT
GDLTISVNVL YNFLEANAKV PYDDLRYLFG EIMYGGHITD DWDRRLCRTY LGEFIRPEML
EGELSLAPGF PLPGNMDYNG YHQYIDAELP PESPYLYGLH PNAEIGFLTQ TSEKLFRTVL
ELQPRDSQAR DGAGATREEK VKALLEEILE RVTDEFNIPE LMAKVEERTP YIVVAFQECG
RMNILTREIQ RSLRELELGL KGELTMTSHM ENLQNALYFD MVPESWARRA YPSTAGLAAW
FPDLLNRIKE LEAWTGDFTM PSTVWLTGFF NPQSFLTAIM QSTARKNEWP LDQMALQCDM
TKKNREEFRS PPREGAYIHG LFMEGACWDT QAGIITEAKL KDLTPPMPVM FIKAIPADKQ
DCRSVYSCPV YKTSQRGPTY VWTFNLKTKE NPSKWVLAGV ALLLQI
