DYH11_HUMAN
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 03-AUG-2022, entry version 178.
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; 5.
DR STRING; 9606.ENSP00000475939; -.
DR GlyConnect; 1190; 11 N-Linked glycans (1 site).
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; Q96DT5; -.
DR PeptideAtlas; Q96DT5; -.
DR PRIDE; Q96DT5; -.
DR ProteomicsDB; 76319; -.
DR Antibodypedia; 44039; 67 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 CTD; 8701; -.
DR DisGeNET; 8701; -.
DR GeneCards; DNAH11; -.
DR GeneReviews; DNAH11; -.
DR HGNC; HGNC:2942; DNAH11.
DR HPA; ENSG00000105877; Group enriched (choroid plexus, parathyroid gland).
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; DYYLDHQ; -.
DR OrthoDB; 1492at2759; -.
DR TreeFam; TF316836; -.
DR PathwayCommons; Q96DT5; -.
DR SIGNOR; Q96DT5; -.
DR BioGRID-ORCS; 8701; 6 hits in 1046 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 112 other tissues.
DR ExpressionAtlas; Q96DT5; baseline and differential.
DR Genevisible; Q96DT5; HS.
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: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:0060411; P:cardiac septum morphogenesis; IEA:Ensembl.
DR GO; GO:0003341; P:cilium movement; 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:0007018; P:microtubule-based movement; IBA:GO_Central.
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; 1.10.8.710; -; 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; 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 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; unknown pathological 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
