ID   DYH11_HUMAN             Reviewed;        4516 AA.
AC   Q96DT5; Q9UJ82;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   04-FEB-2015, sequence version 4.
DT   27-MAR-2024, entry version 187.
DE   RecName: Full=Dynein axonemal heavy chain 11 {ECO:0000305};
DE   AltName: Full=Axonemal beta dynein heavy chain 11;
DE   AltName: Full=Ciliary dynein heavy chain 11;
GN   Name=DNAH11 {ECO:0000312|HGNC:HGNC:2942};
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], INVOLVEMENT IN CILD7, VARIANT CILD7 GLN-2997,
RP   AND VARIANTS LEU-34; ARG-639; CYS-654; ALA-1023; ALA-1038; GLY-1635;
RP   THR-3467; PRO-3758; VAL-4165 AND ILE-4170.
RC   TISSUE=Nasal epithelium, and Testis;
RX   PubMed=12142464; DOI=10.1073/pnas.152337699;
RA   Bartoloni L., Blouin J.-L., Pan Y., Gehrig C., Maiti A.K., Scamuffa N.,
RA   Rossier C., Jorissen M., Armengot M., Meeks M., Mitchison H.M.,
RA   Chung E.M.K., Delozier-Blanchet C.D., Craigen W.J., Antonarakis S.E.;
RT   "Mutations in the DNAH11 (axonemal heavy chain dynein type 11) gene cause
RT   one form of situs inversus totalis and most likely primary ciliary
RT   dyskinesia.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:10282-10286(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1897-1997.
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   [4]
RP   INVOLVEMENT IN CILD7, AND VARIANTS ALA-1023; ALA-1038; VAL-4165 AND
RP   ILE-4170.
RX   PubMed=18022865; DOI=10.1002/humu.20656;
RA   Schwabe G.C., Hoffmann K., Loges N.T., Birker D., Rossier C.,
RA   de Santi M.M., Olbrich H., Fliegauf M., Failly M., Liebers U., Collura M.,
RA   Gaedicke G., Mundlos S., Wahn U., Blouin J.-L., Niggemann B., Omran H.,
RA   Antonarakis S.E., Bartoloni L.;
RT   "Primary ciliary dyskinesia associated with normal axoneme ultrastructure
RT   is caused by DNAH11 mutations.";
RL   Hum. Mutat. 29:289-298(2008).
RN   [5]
RP   INVOLVEMENT IN CILD7, AND VARIANTS CILD7 VAL-117; PRO-2383 AND SER-4327.
RX   PubMed=25186273; DOI=10.1183/09031936.00052014;
RA   Raidt J., Wallmeier J., Hjeij R., Onnebrink J.G., Pennekamp P., Loges N.T.,
RA   Olbrich H., Haeffner K., Dougherty G.W., Omran H., Werner C.;
RT   "Ciliary beat pattern and frequency in genetic variants of primary ciliary
RT   dyskinesia.";
RL   Eur. Respir. J. 44:1579-1588(2014).
RN   [6]
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   [7]
RP   INTERACTION WITH CFAP45, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=33139725; DOI=10.1038/s41467-020-19113-0;
RA   Dougherty G.W., Mizuno K., Noethe-Menchen T., Ikawa Y., Boldt K.,
RA   Ta-Shma A., Aprea I., Minegishi K., Pang Y.P., Pennekamp P., Loges N.T.,
RA   Raidt J., Hjeij R., Wallmeier J., Mussaffi H., Perles Z., Elpeleg O.,
RA   Rabert F., Shiratori H., Letteboer S.J., Horn N., Young S., Struenker T.,
RA   Stumme F., Werner C., Olbrich H., Takaoka K., Ide T., Twan W.K.,
RA   Biebach L., Grosse-Onnebrink J., Klinkenbusch J.A., Praveen K.,
RA   Bracht D.C., Hoeben I.M., Junger K., Guetzlaff J., Cindric S., Aviram M.,
RA   Kaiser T., Memari Y., Dzeja P.P., Dworniczak B., Ueffing M., Roepman R.,
RA   Bartscherer K., Katsanis N., Davis E.E., Amirav I., Hamada H., Omran H.;
RT   "CFAP45 deficiency causes situs abnormalities and asthenospermia by
RT   disrupting an axonemal adenine nucleotide homeostasis module.";
RL   Nat. Commun. 11:5520-5520(2020).
CC   -!- FUNCTION: Force generating protein of respiratory cilia. Produces force
CC       towards the minus ends of microtubules. Dynein has ATPase activity; the
CC       force-producing power stroke is thought to occur on release of ADP.
CC   -!- SUBUNIT: Consists of at least two heavy chains and a number of
CC       intermediate and light chains. Interacts with CFAP45 (PubMed:33139725).
CC       {ECO:0000269|PubMed:33139725}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC       {ECO:0000269|PubMed:31178125, ECO:0000269|PubMed:33139725}.
CC       Note=Located in the proximal region of respiratory cilia.
CC       {ECO:0000269|PubMed:33139725}.
CC   -!- TISSUE SPECIFICITY: Expressed in airway ciliated epithelial cells (at
CC       protein level) (PubMed:31178125, PubMed:33139725). Not detected in
CC       spermatozoa (at protein level) (PubMed:31178125).
CC       {ECO:0000269|PubMed:31178125, ECO:0000269|PubMed:33139725}.
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, 7 (CILD7) [MIM:611884]: A
CC       disorder characterized by abnormalities of motile cilia. Respiratory
CC       infections leading to chronic inflammation and bronchiectasis are
CC       recurrent, due to defects in the respiratory cilia; reduced fertility
CC       is often observed in male patients due to abnormalities of sperm tails.
CC       Half of the patients exhibit randomization of left-right body asymmetry
CC       and situs inversus, due to dysfunction of monocilia at the embryonic
CC       node. Primary ciliary dyskinesia associated with situs inversus is
CC       referred to as Kartagener syndrome. {ECO:0000269|PubMed:12142464,
CC       ECO:0000269|PubMed:18022865, ECO:0000269|PubMed:25186273}. 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; AJ320497; CAC60121.1; -; mRNA.
DR   EMBL; AC004595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC102952; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC073102; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC013481; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC005078; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC004002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC099653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJ132087; CAA10560.1; -; mRNA.
DR   CCDS; CCDS64602.1; -.
DR   RefSeq; NP_001264044.1; NM_001277115.1.
DR   SMR; Q96DT5; -.
DR   BioGRID; 114244; 9.
DR   STRING; 9606.ENSP00000475939; -.
DR   GlyConnect; 1190; 11 N-Linked glycans (1 site).
DR   GlyCosmos; Q96DT5; 2 sites, 12 glycans.
DR   GlyGen; Q96DT5; 2 sites, 11 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; Q96DT5; -.
DR   PhosphoSitePlus; Q96DT5; -.
DR   BioMuta; DNAH11; -.
DR   DMDM; 311033455; -.
DR   EPD; Q96DT5; -.
DR   jPOST; Q96DT5; -.
DR   MassIVE; Q96DT5; -.
DR   PaxDb; 9606-ENSP00000475939; -.
DR   PeptideAtlas; Q96DT5; -.
DR   ProteomicsDB; 76319; -.
DR   Antibodypedia; 44039; 82 antibodies from 19 providers.
DR   DNASU; 8701; -.
DR   Ensembl; ENST00000409508.8; ENSP00000475939.1; ENSG00000105877.19.
DR   GeneID; 8701; -.
DR   KEGG; hsa:8701; -.
DR   MANE-Select; ENST00000409508.8; ENSP00000475939.1; NM_001277115.2; NP_001264044.1.
DR   UCSC; uc064bwj.1; human.
DR   AGR; HGNC:2942; -.
DR   CTD; 8701; -.
DR   DisGeNET; 8701; -.
DR   GeneCards; DNAH11; -.
DR   GeneReviews; DNAH11; -.
DR   HGNC; HGNC:2942; DNAH11.
DR   HPA; ENSG00000105877; Tissue enriched (parathyroid).
DR   MalaCards; DNAH11; -.
DR   MIM; 603339; gene.
DR   MIM; 611884; phenotype.
DR   neXtProt; NX_Q96DT5; -.
DR   OpenTargets; ENSG00000105877; -.
DR   Orphanet; 244; Primary ciliary dyskinesia.
DR   PharmGKB; PA27396; -.
DR   VEuPathDB; HostDB:ENSG00000105877; -.
DR   eggNOG; KOG3595; Eukaryota.
DR   GeneTree; ENSGT00940000158880; -.
DR   HOGENOM; CLU_000038_4_0_1; -.
DR   InParanoid; Q96DT5; -.
DR   OMA; ICEHMAY; -.
DR   OrthoDB; 166463at2759; -.
DR   TreeFam; TF316836; -.
DR   PathwayCommons; Q96DT5; -.
DR   SIGNOR; Q96DT5; -.
DR   BioGRID-ORCS; 8701; 7 hits in 1124 CRISPR screens.
DR   ChiTaRS; DNAH11; human.
DR   GeneWiki; DNAH11; -.
DR   GenomeRNAi; 8701; -.
DR   Pharos; Q96DT5; Tbio.
DR   PRO; PR:Q96DT5; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; Q96DT5; Protein.
DR   Bgee; ENSG00000105877; Expressed in right uterine tube and 113 other cell types or tissues.
DR   ExpressionAtlas; Q96DT5; baseline and differential.
DR   GO; GO:0097728; C:9+0 motile cilium; IEA:Ensembl.
DR   GO; GO:0097729; C:9+2 motile cilium; IDA:GO_Central.
DR   GO; GO:0005930; C: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:0120134; C:proximal portion of axoneme; IDA:GO_Central.
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:0008569; F:minus-end-directed microtubule motor activity; IBA:GO_Central.
DR   GO; GO:0060411; P:cardiac septum morphogenesis; IEA:Ensembl.
DR   GO; GO:0060294; P:cilium movement involved in cell motility; IBA:GO_Central.
DR   GO; GO:0035545; P:determination of left/right asymmetry in nervous system; IEA:Ensembl.
DR   GO; GO:0007368; P:determination of left/right symmetry; IMP:SYSCILIA_CCNET.
DR   GO; GO:0060287; P:epithelial cilium movement involved in determination of left/right asymmetry; IEA:Ensembl.
DR   GO; GO:0030317; P:flagellated sperm motility; IMP:SYSCILIA_CCNET.
DR   GO; GO:0007611; P:learning or memory; IEA:Ensembl.
DR   GO; GO:0120229; P:protein localization to motile cilium; IMP:GO_Central.
DR   GO; GO:0003356; P:regulation of cilium beat frequency; 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; IPR013594; Dynein_heavy_tail.
DR   InterPro; IPR042228; Dynein_linker_3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR45703:SF12; DYNEIN AXONEMAL HEAVY CHAIN 11; 1.
DR   PANTHER; PTHR45703; DYNEIN 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; 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; P-loop containing nucleoside triphosphate hydrolases; 4.
DR   Genevisible; Q96DT5; HS.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell projection; Ciliopathy; Cilium; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Disease variant; Dynein; Kartagener syndrome; Microtubule;
KW   Motor protein; Nucleotide-binding; Primary ciliary dyskinesia;
KW   Reference proteome; Repeat.
FT   CHAIN           1..4516
FT                   /note="Dynein axonemal heavy chain 11"
FT                   /id="PRO_0000114633"
FT   REGION          1..1854
FT                   /note="Stem"
FT                   /evidence="ECO:0000250"
FT   REGION          1855..2076
FT                   /note="AAA 1"
FT                   /evidence="ECO:0000250"
FT   REGION          2136..2366
FT                   /note="AAA 2"
FT                   /evidence="ECO:0000250"
FT   REGION          2472..2719
FT                   /note="AAA 3"
FT                   /evidence="ECO:0000250"
FT   REGION          2817..3066
FT                   /note="AAA 4"
FT                   /evidence="ECO:0000250"
FT   REGION          3072..3403
FT                   /note="Stalk"
FT                   /evidence="ECO:0000250"
FT   REGION          3459..3686
FT                   /note="AAA 5"
FT                   /evidence="ECO:0000250"
FT   REGION          3896..4122
FT                   /note="AAA 6"
FT                   /evidence="ECO:0000250"
FT   COILED          1274..1327
FT                   /evidence="ECO:0000255"
FT   COILED          3072..3136
FT                   /evidence="ECO:0000255"
FT   COILED          3312..3403
FT                   /evidence="ECO:0000255"
FT   COILED          3668..3703
FT                   /evidence="ECO:0000255"
FT   BINDING         1893..1900
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2174..2181
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2510..2517
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         2855..2862
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   VARIANT         34
FT                   /note="E -> L (requires 2 nucleotide substitutions;
FT                   dbSNP:rs398123604)"
FT                   /evidence="ECO:0000269|PubMed:12142464"
FT                   /id="VAR_013851"
FT   VARIANT         34
FT                   /note="E -> V (in dbSNP:rs2285944)"
FT                   /id="VAR_042944"
FT   VARIANT         117
FT                   /note="E -> V (in CILD7; dbSNP:rs72655968)"
FT                   /evidence="ECO:0000269|PubMed:25186273"
FT                   /id="VAR_072472"
FT   VARIANT         639
FT                   /note="Q -> R (in dbSNP:rs12670130)"
FT                   /evidence="ECO:0000269|PubMed:12142464"
FT                   /id="VAR_013852"
FT   VARIANT         654
FT                   /note="S -> C (in dbSNP:rs62441683)"
FT                   /evidence="ECO:0000269|PubMed:12142464"
FT                   /id="VAR_013853"
FT   VARIANT         1023
FT                   /note="V -> A (in dbSNP:rs10269582)"
FT                   /evidence="ECO:0000269|PubMed:12142464,
FT                   ECO:0000269|PubMed:18022865"
FT                   /id="VAR_013854"
FT   VARIANT         1038
FT                   /note="T -> A (in dbSNP:rs10224537)"
FT                   /evidence="ECO:0000269|PubMed:12142464,
FT                   ECO:0000269|PubMed:18022865"
FT                   /id="VAR_013855"
FT   VARIANT         1316
FT                   /note="M -> V (in dbSNP:rs17144788)"
FT                   /id="VAR_042945"
FT   VARIANT         1635
FT                   /note="D -> G (in dbSNP:rs17144835)"
FT                   /evidence="ECO:0000269|PubMed:12142464"
FT                   /id="VAR_013856"
FT   VARIANT         2383
FT                   /note="L -> P (in CILD7; dbSNP:rs72657353)"
FT                   /evidence="ECO:0000269|PubMed:25186273"
FT                   /id="VAR_072473"
FT   VARIANT         2586
FT                   /note="Y -> H (in dbSNP:rs2003417)"
FT                   /id="VAR_060141"
FT   VARIANT         2634
FT                   /note="N -> S (in dbSNP:rs9639393)"
FT                   /id="VAR_013857"
FT   VARIANT         2675
FT                   /note="I -> V (in dbSNP:rs72657364)"
FT                   /id="VAR_013858"
FT   VARIANT         2997
FT                   /note="R -> Q (in CILD7; uncertain significance;
FT                   dbSNP:rs35865357)"
FT                   /evidence="ECO:0000269|PubMed:12142464"
FT                   /id="VAR_013859"
FT   VARIANT         3467
FT                   /note="A -> T (in dbSNP:rs2214326)"
FT                   /evidence="ECO:0000269|PubMed:12142464"
FT                   /id="VAR_013860"
FT   VARIANT         3708
FT                   /note="V -> L (in dbSNP:rs4722064)"
FT                   /id="VAR_013861"
FT   VARIANT         3758
FT                   /note="S -> P (in dbSNP:rs17145720)"
FT                   /evidence="ECO:0000269|PubMed:12142464"
FT                   /id="VAR_013862"
FT   VARIANT         4165
FT                   /note="M -> V (in dbSNP:rs6461613)"
FT                   /evidence="ECO:0000269|PubMed:12142464,
FT                   ECO:0000269|PubMed:18022865"
FT                   /id="VAR_042946"
FT   VARIANT         4170
FT                   /note="T -> I (in dbSNP:rs12537531)"
FT                   /evidence="ECO:0000269|PubMed:12142464,
FT                   ECO:0000269|PubMed:18022865"
FT                   /id="VAR_013863"
FT   VARIANT         4327
FT                   /note="L -> S (in CILD7; dbSNP:rs72658826)"
FT                   /evidence="ECO:0000269|PubMed:25186273"
FT                   /id="VAR_072474"
SQ   SEQUENCE   4516 AA;  520369 MW;  4F4F149CE7FF82D7 CRC64;
     MAAQVAAREA RDFREAPTLR LTSGAGLEAV GAVELEEEEE NEEEAAARRA RSFAQDARVR
     FLGGRLAMML GFTEEKWSQY LESEDNRQVL GEFLESTSPA CLVFSFAASG RLAASQEIPR
     DANHKLVFIS KKITESIGVN DFSQVVLFGE LPALSLGHVS AFLDEILVPV LSNKNNHKSW
     SCFTSQDMEY HIEVMKKKMY IFRGKMSRRT LLPIPTVAGK MDLDQNCSEN KPPSNERIIL
     HAIESVVIEW SHQIQEIIER DSVQRLLNGL HLSPQAELDF WMMRRENLSC IYDQLQAPVV
     LKMVKILTTK QSSYFPTLKD IFLAVENALL EAQDVELYLR PLRRHIQCLQ ETEFPQTRIL
     IAPLFHTICL IWSHSKFYNT PARVIVLLQE FCNLFINQAT AYLSPEDLLR GEIEESLEKV
     QVAVNILKTF KNSFFNYRKK LASYFMGRKL RPWDFQSHLV FCRFDKFLDR LIKIEDIFAT
     TLEFEKLERL EFGGTKGAIL NGQVHEMSEE LMELCKLFKQ STYDPSDCTN MEFESDYVAF
     KSKTLEFDRR LGTIICEAFF NCNGLEAAFK LLTIFGNFLE KPVVMEIFSL HYSTLVHMFN
     TELDVCKQLY NEHMKQIECG HVVLNKNMPF TSGNMKWAQQ VLQRLQMFWS NFASLRYLFL
     GNPDHALVYQ KYVEMTTLLD QFESRIYNEW KSNVDEICEF NLNQPLVKFS AINGLLCVNF
     DPKLVAVLRE VKYLLMLKKQ DIPDSALAIF KKRNTILKYI GNLDLLVQGY NKLKQTLLEV
     EYPLIEDELR AIDEQLTAAT TWLTWQDDCW GYIERVRAAT SELEHRVERT QKNVKVIQQT
     MRGWARCVLP PRREHRREAA FTLEDKGDLF TKKYKLIQGD GCKIHNLVEE NRKLFKANPS
     LDTWKIYVEF IDDIVVEGFF QAIMHDLDFF LKNTEKQLKP APFFQAQMIL LPPEIVFKPS
     LDREAGDGFY DLVEEMLCNS FRMSAQMNRI ATHLEIKNYQ NDMDNMLGLA EVRQEIMNRV
     VNVINKVLDF RNTLETHTYL WVDDRAEFMK HFLLYGHAVS SDEMDAHANE EIPEQPPTLE
     QFKEQIDIYE ALYVQMSKFE DFRVFDSWFK VDMKPFKVSL LTIIKKWSWM FQEHLLRFVI
     DSLNELQEFI KETDSGLQRE LNEGDHDGLV DIMVHLLAVR SRQRATDELF EPLKETITLL
     ESYGQKMPEQ VYIQLEELPE RWETTKKIAA TVRHEVSPLH NAEVTLIRKK CILFDAKQAE
     FRERFRHYAP LGFNAENPYT ALDKANEELE ALEEEMLQMQ ESTRLFEVAL PEYKQMKQCR
     KEIKLLKGLW DVIIYVRRSI DNWTKTQWRQ IHVEQMDVEL RRFAKEIWSL NKEVRVWDAY
     TGLEGTVKDM TASLRAITEL QSPALRDRHW HQLMKAIGVK FLINEATTLA DLLALRLHRV
     EDDVRRIVDK AVKELGTEKV ITEISQTWAT MKFSYEVHYR TGIPLLKSDE QLFETLEHNQ
     VQLQTLLQSK YVEYFIEQVL SWQNKLNIAD LVIFTWMEVQ RTWSHLESIF VCSEDIRIQL
     VKDARRFDGV DAEFKELMFK TAKVENVLEA TCRPNLYEKL KDLQSRLSLC EKALAEYLET
     KRIAFPRFYF VSSADLLDIL SKGAQPKQVT CHLAKLFDSI ADLQFEDNQD VSAHRAVGMY
     SKEKEYVPFQ AECECVGHVE TWLLQLEQTM QETVRHSITE AIVAYEEKPR ELWIFDFPAQ
     VALTSSQIWW TTDVGIAFSR LEEGYETALK DFHKKQISQL NTLITLLLGE LPPGDRQKIM
     TICTIDVHAR DVVAKLISQK VVSPQAFTWL SQLRHRWEDT QKHCFVNICD AQFQYFYEYL
     GNSPRLVITP LTDRCYITLT QSLHLTMSGA PAGPAGTGKT ETTKDLGRAL GMMVYVFNCS
     EQMDYKSIGN IYKGLVQTGA WGCFDEFNRI SVEVLSVVAV QVKMIHDAIR NRKKRFVFLG
     EAITLKPSVG IFITMNPGYA GRTELPENLK ALFRPCAMVA PDIELICEIL LVAEGFVDAR
     ALARKFITLY TLCKELLSKQ DHYDWGLRAI KSVLVVAGSL KRGDKNRPED QVLMRALRDF
     NMPKIVTDDI PVFLGLVGDL FPALDVPRRR KLHFEQMVRQ STLELRLQPE ESFILKVVQL
     EELLAVRHSV FVVGNAGTGK SKILRTLNRT YVNMKQKPVW NDLNPKAVTT DELFGFIHHA
     TREWKDGKIV YSYFIGLFSS ILREQANLKH DGPKWIVLDG DIDPMWIESL NTVMDDNKVL
     TLASNERIAL TPFMRLLFEI HHLRSATPAT VSRAGILYVN PQDLGWNPYV ASWIDRRRHQ
     SEKANLTILF DKYVPACLDK LRTSFKTITS IPESSLVQTL CVLLECLLTP ENVPSDSPKE
     VYEVYFVFAC IWAFGGTLLQ DQISDYQADF SRWWQKEMKA VKFPSQGTIF DYYVDHKTKK
     LLPWADKIAQ FTMDPDVPLQ TVLVHTTETA RLRYFMELLL EKGKPLMLVG NAGVGKTVFV
     GDTLASLSED YIVSRVPFNY YTTSTALQKI LEKPLEKKAG HNYGPGGNKK LIYFIDDMNM
     PEVDLYGTVQ PHTLIRQHID YGHWYDRQKV MLKEIHNCQY VACMNPMVGS FTINPRLQRH
     FTVFAFNFPS LDALNTIYGQ IFSFHFQQQA FAPSILRSGP TLIQATIAFH QTMMCNFLPT
     AIKFHYIFNL RDLSNVFQGI LFASPECLKG PLDLIHLWLH ESARVYGDKL IDKKDCDLFQ
     RRMLETAYKY FEGIDSHMLL QQPLIYCHFA DRGKDPHYMP VKDWEVLKTI LTETLDNYNE
     LNAAMHLVLF EDAMQHVCRI SRILRTPQGC ALLVGVGGSG KQSLSRLAAY LRGLEVFQIT
     LTEGYGIQEL RVDLANLYIR TGAKNMPTVF LLTDAQVLDE SFLVLINDLL ASGEIPDLFS
     DEDVDKIISG IHNEVHALGM VDSRENCWKF FMARVRLQLK IILCFSPVGR TLRVRARKFP
     AIVNCTAIDW FHAWPQEALV SVSRRFIEET KGIEPVHKDS ISLFMAHVHT TVNEMSTRYY
     QNERRHNYTT PKSFLEQISL FKNLLKKKQN EVSEKKERLV NGIQKLKTTA SQVGDLKARL
     ASQEAELQLR NHDAEALITK IGLQTEKVSR EKTIADAEER KVTAIQTEVF QKQRECEADL
     LKAEPALVAA TAALNTLNRV NLSELKAFPN PPIAVTNVTA AVMVLLAPRG RVPKDRSWKA
     AKVFMGKVDD FLQALINYDK EHIPENCLKV VNEHYLKDPE FNPNLIRTKS FAAAGLCAWV
     INIIKFYEVY CDVEPKRQAL AQANLELAAA TEKLEAIRKK LVDLDRNLSR LTASFEKATA
     EKVRCQEEVN QTNKTIKLAN RLVKELEAKK IRWGQSIKSF EAQEKTLCGD VLLTAAFVSY
     VGPFTRQYRQ ELVHCKWVPF LQQKVSIPLT EGLDLISMLT DDATIAAWNN EGLPSDRMST
     ENAAILTHCE RWPLVIDPQQ QGIKWIKNKY GMDLKVTHLG QKGFLNAIET ALAFGDVILI
     ENLEETIDPV LDPLLGRNTI KKGKYIRIGD KECEFNKNFR LILHTKLANP HYKPELQAQT
     TLLNFTVTED GLEAQLLAEV VSIERPDLEK LKLVLTKHQN DFKIELKYLE DDLLLRLSAA
     EGSFLDDTKL VERLEATKTT VAEIEHKVIE AKENERKINE ARECYRPVAA RASLLYFVIN
     DLQKINPLYQ FSLKAFNVLF HRAIEQADKV EDMQGRISIL MESITHAVFL YTSQALFEKD
     KLTFLSQMAF QILLRKKEID PLELDFLLRF TVEHTHLSPV DFLTSQSWSA IKAIAVMEEF
     RGIDRDVEGS AKQWRKWVES ECPEKEKLPQ EWKKKSLIQK LILLRAMRPD RMTYALRNFV
     EEKLGAKYVE RTRLDLVKAF EESSPATPIF FILSPGVDAL KDLEILGKRL GFTIDSGKFH
     NVSLGQGQET VAEVALEKAS KGGHWVILQN VHLVAKWLGT LEKLLERFSQ GSHRDYRVFM
     SAESAPTPDE HIIPQGLLEN SIKITNEPPT GMLANLHAAL YNFDQDTLEI CSKEQEFKSI
     LFSLCYFHAC VAGRLRFGPQ GWSRSYPFNP GDLTICASVL YNYLEANSKV PWEDLRYLFG
     EIMYGGHITD DWDRKLCRVY LEEFMNPSLT EDELMLAPGF AAPPYLDYAG YHQYIEEMLP
     PESPALYGLH PNAEIEFLTV TSNTLFRTLL EMQPRNALSG DELGQSTEEK VKNVLDDILE
     KLPEEFNMAE IMQKNSNRSP YVLVCFQECE RMNILIREIR ISLEQLDLSL KGELALSPAV
     EAQQFALSYD TVPDTWSKLA YPSTYGLAQW FNDLLLRCRE LDTWTQDLTL PAVVWLSGFF
     NPQSFLTAIM QTMARKNEWP LDKTRLTADV TKKTKEDYGH PPREGAYLHG LFMEGARWDT
     QAGTIVEARL KELACPMPVI FAKATPVDRQ ETKQTYECPV YRTKLRGPSY IWTFRLKSEE
     KTAKWVLAGV ALLLEA
//