DYH8_MOUSE
ID DYH8_MOUSE Reviewed; 4731 AA.
AC Q91XQ0; E9Q010; O08830; Q3V0D2; Q91V63; Q91XP8; Q91XP9; Q99MH8; Q9QY72;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Dynein axonemal heavy chain 8;
DE AltName: Full=Axonemal beta dynein heavy chain 8;
DE AltName: Full=Ciliary dynein heavy chain 8;
GN Name=Dnah8; Synonyms=Dnahc8;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=129/Sv, and 129S1/SvImJ; TISSUE=Testis;
RX PubMed=12297094; DOI=10.1006/dbio.2002.0769;
RA Samant S.A., Ogunkua O., Hui L., Fossella J., Pilder S.H.;
RT "The T complex distorter 2 candidate gene, Dnahc8, encodes at least two
RT testis-specific axonemal dynein heavy chains that differ extensively at
RT their amino and carboxyl termini.";
RL Dev. Biol. 250:24-43(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 490-582, FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=10602986; DOI=10.1007/s003350010003;
RA Fossella J., Samant S.A., Silver L.M., King S.M., Vaughan K.T.,
RA Olds-Clarke P., Johnson K.A., Mikami A., Vallee R.B., Pilder S.H.;
RT "An axonemal dynein at the hybrid sterility 6 locus: implications for t
RT haplotype-specific male sterility and the evolution of species barriers.";
RL Mamm. Genome 11:8-15(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2060-2264.
RC STRAIN=NMRI; TISSUE=Testis;
RX PubMed=9373155; DOI=10.1016/s0378-1119(97)00417-4;
RA Neesen J., Koehler M.R., Kirschner R., Steinlein C., Kreutzberger J.,
RA Engel W., Schmid M.;
RT "Identification of dynein heavy chain genes expressed in human and mouse
RT testis: chromosomal localization of an axonemal dynein gene.";
RL Gene 200:193-202(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3666-4731.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16054618; DOI=10.1016/j.ydbio.2005.06.002;
RA Samant S.A., Ogunkua O.O., Hui L., Lu J., Han Y., Orth J.M., Pilder S.H.;
RT "The mouse t complex distorter/sterility candidate, Dnahc8, expresses a
RT gamma-type axonemal dynein heavy chain isoform confined to the principal
RT piece of the sperm tail.";
RL Dev. Biol. 285:57-69(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=32619401; DOI=10.1016/j.ajhg.2020.06.004;
RA Liu C., Miyata H., Gao Y., Sha Y., Tang S., Xu Z., Whitfield M., Patrat C.,
RA Wu H., Dulioust E., Tian S., Shimada K., Cong J., Noda T., Li H.,
RA Morohoshi A., Cazin C., Kherraf Z.E., Arnoult C., Jin L., He X., Ray P.F.,
RA Cao Y., Toure A., Zhang F., Ikawa M.;
RT "Bi-allelic DNAH8 Variants Lead to Multiple Morphological Abnormalities of
RT the Sperm Flagella and Primary Male Infertility.";
RL Am. J. Hum. Genet. 107:330-341(2020).
CC -!- FUNCTION: Force generating protein component of the outer dynein arms
CC (ODAs) in the sperm flagellum. Produces force towards the minus ends of
CC microtubules. Dynein has ATPase activity; the force-producing power
CC stroke is thought to occur on release of ADP. Involved in sperm
CC motility; implicated in sperm flagellar assembly.
CC {ECO:0000269|PubMed:10602986, ECO:0000269|PubMed:12297094,
CC ECO:0000269|PubMed:32619401}.
CC -!- SUBUNIT: Consists of at least two heavy chains and a number of
CC intermediate and light chains.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme
CC {ECO:0000269|PubMed:16054618}. Cytoplasm {ECO:0000269|PubMed:16054618}.
CC Note=Detected in sperm tail, with almost exclusive localization to the
CC principal piece. Also detected in the cytoplasm of primary
CC spermatocytes. {ECO:0000269|PubMed:16054618}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q91XQ0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91XQ0-2; Sequence=VSP_022616, VSP_022617;
CC -!- TISSUE SPECIFICITY: Isoform 1 and/or isoform 2 are expressed in
CC spermatocytes and mature sperm (at protein level). Testis-specific.
CC Accumulates exclusively in mid to late spermatocytes.
CC {ECO:0000269|PubMed:10602986, ECO:0000269|PubMed:12297094,
CC ECO:0000269|PubMed:16054618}.
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 -!- DISRUPTION PHENOTYPE: Homozygous knockout male mice are sterile due to
CC diminished sperm movement (PubMed:32619401). Sperm flagella show
CC disorganized microtubules and outer dense fibers resulting in
CC significantly higher rates of abnormal flagella (PubMed:32619401).
CC {ECO:0000269|PubMed:32619401}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the dynein heavy chain family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE21572.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF356520; AAK60621.1; -; mRNA.
DR EMBL; AF356521; AAK60622.1; -; mRNA.
DR EMBL; AF356522; AAK60623.1; -; mRNA.
DR EMBL; AF356523; AAK60624.1; -; mRNA.
DR EMBL; AF363577; AAK60632.1; -; mRNA.
DR EMBL; AF342999; AAK18309.1; -; Genomic_DNA.
DR EMBL; AC165951; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC165962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC166166; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC174471; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF117305; AAF20213.1; -; mRNA.
DR EMBL; Z83817; CAB06071.1; -; mRNA.
DR EMBL; AK133238; BAE21572.1; ALT_INIT; mRNA.
DR CCDS; CCDS37541.1; -. [Q91XQ0-1]
DR RefSeq; NP_038839.2; NM_013811.3. [Q91XQ0-1]
DR RefSeq; XP_006523651.1; XM_006523588.2. [Q91XQ0-1]
DR SMR; Q91XQ0; -.
DR IntAct; Q91XQ0; 1.
DR MINT; Q91XQ0; -.
DR STRING; 10090.ENSMUSP00000127878; -.
DR iPTMnet; Q91XQ0; -.
DR PhosphoSitePlus; Q91XQ0; -.
DR EPD; Q91XQ0; -.
DR MaxQB; Q91XQ0; -.
DR PaxDb; Q91XQ0; -.
DR PRIDE; Q91XQ0; -.
DR ProteomicsDB; 277696; -. [Q91XQ0-1]
DR ProteomicsDB; 277697; -. [Q91XQ0-2]
DR Antibodypedia; 29878; 49 antibodies from 16 providers.
DR DNASU; 13417; -.
DR Ensembl; ENSMUST00000170651; ENSMUSP00000127878; ENSMUSG00000033826. [Q91XQ0-1]
DR Ensembl; ENSMUST00000235390; ENSMUSP00000158051; ENSMUSG00000033826. [Q91XQ0-1]
DR Ensembl; ENSMUST00000236140; ENSMUSP00000157469; ENSMUSG00000033826. [Q91XQ0-1]
DR GeneID; 13417; -.
DR KEGG; mmu:13417; -.
DR UCSC; uc008bua.1; mouse. [Q91XQ0-2]
DR UCSC; uc008bub.1; mouse. [Q91XQ0-1]
DR CTD; 1769; -.
DR MGI; MGI:107714; Dnah8.
DR VEuPathDB; HostDB:ENSMUSG00000033826; -.
DR eggNOG; KOG3595; Eukaryota.
DR GeneTree; ENSGT00940000158992; -.
DR HOGENOM; CLU_000038_9_1_1; -.
DR InParanoid; Q91XQ0; -.
DR OMA; VECCVGD; -.
DR OrthoDB; 6295at2759; -.
DR PhylomeDB; Q91XQ0; -.
DR TreeFam; TF316836; -.
DR BioGRID-ORCS; 13417; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Dnah8; mouse.
DR PRO; PR:Q91XQ0; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q91XQ0; protein.
DR Bgee; ENSMUSG00000033826; Expressed in spermatocyte and 86 other tissues.
DR ExpressionAtlas; Q91XQ0; baseline and differential.
DR Genevisible; Q91XQ0; MM.
DR GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR GO; GO:0030286; C:dynein complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0036157; C:outer dynein arm; ISM:MGI.
DR GO; GO:0036126; C:sperm flagellum; ISS: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; ISS:UniProtKB.
DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0036158; P:outer dynein arm assembly; 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; 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; PTHR10676; PTHR10676; 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; 3.
DR SUPFAM; SSF52540; SSF52540; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell projection; Cilium; Coiled coil;
KW Cytoplasm; Cytoskeleton; Dynein; Flagellum; Microtubule; Motor protein;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..4731
FT /note="Dynein axonemal heavy chain 8"
FT /id="PRO_0000274045"
FT REGION 1..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1177..1201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2049..2271
FT /note="AAA 1"
FT /evidence="ECO:0000250"
FT REGION 2331..2550
FT /note="AAA 2"
FT /evidence="ECO:0000250"
FT REGION 2657..2910
FT /note="AAA 3"
FT /evidence="ECO:0000250"
FT REGION 3021..3275
FT /note="AAA 4"
FT /evidence="ECO:0000250"
FT REGION 3290..3587
FT /note="Stalk"
FT /evidence="ECO:0000250"
FT REGION 3673..3903
FT /note="AAA 5"
FT /evidence="ECO:0000250"
FT REGION 4118..4332
FT /note="AAA 6"
FT /evidence="ECO:0000250"
FT COILED 145..169
FT /evidence="ECO:0000255"
FT COILED 1543..1567
FT /evidence="ECO:0000255"
FT COILED 3313..3405
FT /evidence="ECO:0000255"
FT COILED 3531..3583
FT /evidence="ECO:0000255"
FT COILED 3836..3871
FT /evidence="ECO:0000255"
FT COMPBIAS 11..52
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2087..2094
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2369..2376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 917
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96JB1"
FT VAR_SEQ 4200..4202
FT /note="GGW -> VCN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12297094"
FT /id="VSP_022616"
FT VAR_SEQ 4203..4731
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12297094"
FT /id="VSP_022617"
FT CONFLICT 127..128
FT /note="GI -> RL (in Ref. 1; AAK60623/AAK60624/AAK60632)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="R -> C (in Ref. 1; AAK60623/AAK60624/AAK60632)"
FT /evidence="ECO:0000305"
FT CONFLICT 567
FT /note="C -> R (in Ref. 1; AAK60621/AAK60622)"
FT /evidence="ECO:0000305"
FT CONFLICT 813
FT /note="T -> R (in Ref. 1; AAK60623/AAK60624/AAK60632)"
FT /evidence="ECO:0000305"
FT CONFLICT 963
FT /note="D -> N (in Ref. 1; AAK60623/AAK60624/AAK60632)"
FT /evidence="ECO:0000305"
FT CONFLICT 982
FT /note="T -> A (in Ref. 1; AAK60623/AAK60624/AAK60632)"
FT /evidence="ECO:0000305"
FT CONFLICT 1051
FT /note="E -> K (in Ref. 1; AAK60623/AAK60624/AAK60632)"
FT /evidence="ECO:0000305"
FT CONFLICT 1291
FT /note="K -> E (in Ref. 1; AAK60623/AAK60624/AAK60632)"
FT /evidence="ECO:0000305"
FT CONFLICT 1421
FT /note="V -> I (in Ref. 1; AAK60623/AAK60624/AAK60632)"
FT /evidence="ECO:0000305"
FT CONFLICT 1429
FT /note="K -> Q (in Ref. 1; AAK60621/AAK60622/AAK60623/
FT AAK60624/AAK60632/AAK18309)"
FT /evidence="ECO:0000305"
FT CONFLICT 1437
FT /note="N -> S (in Ref. 1; AAK60623/AAK60624/AAK60632)"
FT /evidence="ECO:0000305"
FT CONFLICT 1463
FT /note="V -> E (in Ref. 1; AAK60623/AAK60624/AAK60632)"
FT /evidence="ECO:0000305"
FT CONFLICT 1566
FT /note="A -> G (in Ref. 1; AAK60623/AAK60624/AAK60632)"
FT /evidence="ECO:0000305"
FT CONFLICT 1569
FT /note="D -> N (in Ref. 1; AAK60623/AAK60624/AAK60632)"
FT /evidence="ECO:0000305"
FT CONFLICT 2060
FT /note="L -> F (in Ref. 4; CAB06071)"
FT /evidence="ECO:0000305"
FT CONFLICT 2157
FT /note="Y -> N (in Ref. 4; CAB06071)"
FT /evidence="ECO:0000305"
FT CONFLICT 2164
FT /note="K -> R (in Ref. 4; CAB06071)"
FT /evidence="ECO:0000305"
FT CONFLICT 2167
FT /note="K -> T (in Ref. 4; CAB06071)"
FT /evidence="ECO:0000305"
FT CONFLICT 2224
FT /note="V -> A (in Ref. 1; AAK60623/AAK60624/AAK60632)"
FT /evidence="ECO:0000305"
FT CONFLICT 2264
FT /note="N -> A (in Ref. 4; CAB06071)"
FT /evidence="ECO:0000305"
FT CONFLICT 3408
FT /note="P -> T (in Ref. 1; AAK60623/AAK60624/AAK60632)"
FT /evidence="ECO:0000305"
FT CONFLICT 3893
FT /note="I -> V (in Ref. 1; AAK60623/AAK60624/AAK60632)"
FT /evidence="ECO:0000305"
FT CONFLICT 4229
FT /note="E -> K (in Ref. 1; AAK60623)"
FT /evidence="ECO:0000305"
FT CONFLICT 4310
FT /note="L -> W (in Ref. 5; BAE21572)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 4731 AA; 541238 MW; 37711771223CEC0A CRC64;
MESEEGNAEP PPPSEEAPPP VVEEAPPPLP PEDTAPPPPE EQAPPPEGDA APPPTGDAFQ
LTVEGEAPHP EDPKLLSEQG PATSVTDYRS LIPSDEEVTL PEDEESGQAR VRARHTPRPA
QSVLSDGISQ SSRRPSKFRR SMTGIPNLQE TLKEKQARFR EARENRKMKI GPSHKYIFEV
LGEKLGLDLV TVEELILDCP SLDPFTSFFE KGGCKTLKFL YQEGEVPGFE CGRTITGVPK
GGKMMRIYVD NAAPDKLKGL CLFFVRCRND VAINSKTIHE DVLFSFLDAS KGLLEGIKHM
LKSIFLPAIL ATSNWGALNQ SKQGESEKHI FIETIHRYLA SLDDATISIE GTVMLKKVDN
IDFSKLHTFE EVTAAASSSE MVHQLEEVLM VWYKQIEQVL IESEQMRKEA DDSGPLTELE
HWKRMSAKFN FIIEQIKGSN CKAVINVLNV AHSKLLKNWR DLDARITDSA NESKDNVRYL
YTLEKVCQPL YNYDLVSMAH GIQNLINAIR MIHSVSRYYN TSERMTSLFI KVTNQMVTAC
KAYITDGGTN HVWDQETPAV LKKIQDCIFL FKEYQASFHK TRKQILESSG EKSFEVSEMY
IFGKFEAFCK RLEKITEMIT IVQTYSALSN STIEGIDILG IKFKNIYQGI KKNQYDILDP
RRTEFDTDFT EFMGKINILE IQIQAFMNST FGKILSSQQA LQLLQRFQKL NIPCLHLEIN
HTIERILQCY VAELEFTKKL YLSQKDDPPL ARNMPPIAGK ILWVRQLFRR INEPINYFFK
NSDILSSTEG KAVIRQYNRI AYVLVEFEVA YHTAWFKEVS QLQYALQATL FVRHPETGKL
LVNFDPKILE VVRETKCMIK MKLDVPEQAK NLLKLESKLK ADKLYLQGLL QYYDDLCQEV
PSVFVNLMTP KMKKVESVLR QGLTVLTWSS LMLESFFKEV ESVLDMFNQL LKKVNDLCEM
HIDTVLKEIA KTLLISLSDS GTTKVEDMLT LNETYTKECA DILNHKSRHV EEAVKELILI
FEQIYEVKYT GKAAKSVKEQ RKRVVFGSEA EETEGLDFES TTMEVDTNDK EDEFKKECKE
VYAFFSHQLL DSLQKATRLS LDTMKRRIFV GSQGRRRSED IVSFIKTEVH LAIPNVVMVP
SLDDIQQAIN RMIQLTLEVS RGVAHWGQQQ VRQIKSFQNN SRGSDQPPAS GKPLKKEERS
FEETIPARKL KNFYPGVAEH KDISKLVLLL SSSVNSLRKA ATEALQDFQK YKTLWIEDRH
VKVKEFLANN PSLTEIRSEI LHYATLEQEI KELKPIIVVG SLELHTEPMK LALSIEAKAW
KMLLCRYLNE EYKKKMSDMI TFINEYLKKL SRPIRDLDDV RFAMEALSCI RDNEIQMDMT
LGPIEEAYGI LNRFEVKVTK EESEGVDTLR YSFNKLQSKA VSVQGELVKV QPKFKSNLLE
SVKVFCEDVI NFTEAYETEG PMVPNIPPQE ASNRLQIFQA NFDDLWRKFV TYSSGEQLFG
LPVTDYEVLH KTRKELNLLQ KLYGLYDTVM GSISGYYEIL WGDVDIEKIN AELQEFQNRC
RKLPRALKDW QAFLDLKKRI DDFSESCPLL EMMTNKAMKQ RHWDRISELT GTPFDVESDT
FCLRNIMEAP LLKNKDDIED ICISAIKEKD IEAKLTQVIE NWTYQNLSFA AFKGKGELLL
KGTESGEIIT LMEDSLMVLG SLLSNRYNTP FKKNIQNWVF KLSTSSDIIE EWLIVQNLWV
YLEAVFVGGD IAKQLPQEAK RFQNIDKSWI KIMQRAHENP NVISCCVGDE TMGQLLPHLH
EQLEVCQKSL TGYLEKKRLL FPRFFFVSDP VLLEILGQAS DSHTIQPHLP AVSDNINEVT
FHAKDYDRMT AVISREGEKI MLDTPVMAKG PVEIWLLDLL KVQMSSLHNI IRSAFYQISD
SGFLLLPFLN HFPAQVGLLG IQMLWTHDSE EALNNAKDDR KIMQITNQKF LDILNTLISQ
TTHDLTKFDR VKFETLITIH VHQRDIFDDL VKMHIKSVTD FEWLKQSRFY FKEDLDQTVV
SITDVDFIYQ NEFLGCTDRL VITPLTDRCY ITLAQALGMN MGGAPAGPAG TGKTETTKDM
GRCLGKYVVV FNCSDQMDFR GLGRIFKGLA QSGSWGCFDE FNRIELPVLS VAAQQIYIVL
TARKERKKQF IFSDGDCVDL NPEFGIFLTM NPGYAGRQEL PENLKIQFRT VAMMVPDRQI
IMRVKLASCG FLENVILAQK FYVLYKLCEE QLTKQVHYDF GLRNILSVLR TLGSQKRARP
EDSELSTVMR GLRDMNLSKL VDEDEPLFLS LINDLFPGLQ LDSSTYAELQ SAVDNQVNLE
GLINHPPWNL KLVQLYETSL VRHGLMTLGP SGSGKTTVIT ILMKSLTECG RPHREMRMNP
KAITAPQMFG RLDTATNDWT DGIFSTLWRK TLKAKKGENI FLILDGPVDA IWIENLNSVL
DDNKTLTLAN GDRIPMAPTC KLLFEVHNIE NASPATVSRM GMVYISSSAL SWRPILQAWL
KKRSQQEASV FLSLYDKVFE DAYTYMKLSL NPKMQLLECN YIMQSLNLLE GLIPSKEEGG
VSSGDHLHKL FVFGLMWSLG ALLELDSREK LEVFLRGHGS KLNLPEIPKG SQQTMYEFYV
TDYGDWEHWN KRIQPYFYPT DSIPEYSSIL VPNVDNIRTN FLIDTIAKQH KAVLLTGEQG
TAKTVMVKAY LKKYDPEVQL SKSLNFSSAT EPMMFQRTIE SYVDKRMGST YGPPGGRKMT
VFIDDINMPV INEWGDQITN EIVRQMMEME GMYSLDKPGD FTTIVDVQLI AAMIHPGGGR
NDIPQRLKRQ FTVFNCTLPS NTSIDKIFGI IGCGYFDPCR KFRPEICDMV GNLVSVSRVL
WQWTKVKMLP TPSKFHYIFN LRDLSRIWQG MLTVKAEECS SIPILLSLFK HECNRVIADR
FITPDDEQWF NSQLIRAVEE NISPEVAANI LPEPYFVDFL RDMPEPTGDE PEDTMFEVPK
IYELVPSFEF LSEKLQFYQR QFNEIIRGTS LDLVFFKDAM THLVKISRII RTSCGNALLV
GVGGSGKQSL SKLASFIAGY QIFQITLTRS YNVSNLIEDL KNLYKVAGAE GKGITFIFTD
NEIKDEAFLE YLNNLLSSGE ISNLFARDEM DEITQGLISV MKRELPRHPP TFDNLYEYFI
TRSRKNLHVV LCFSPVGEKF RARSLKFPGL ISGCTMDWFS RWPKEALIAV ASYFLLDYNI
VCSIETKRHV VETMGLFHDM VSESCENYFQ RYRRRAHVTP KSYLSFINGY KSIYTDKVKY
INEQAERMNI GLDKLMEASE SVAKLSQDLA VKEKELAVAS IKADEVLAEV TVSAQASAKV
KNEVQEVKDK AQKIVDEIDS EKVKAETKLE AAKPALEEAE AALNTIKPND IATVRKLAKP
PHLIMRIMDC VLLLFQKKID PVTMDPEKPC CKPSWGESLK LMSATGFLFS LQQFPKDTIN
EETVELLQPY FNMDDYTFES AKKVCGNVAG LLSWTLAMVI FYGINREVLP LKANLAKQEG
RLAVANVELG KAQALLDEKQ AELDKVQAKF DAAMKEKMDL LNDADMCRKK MQAASTLIDG
LSGEKVRWTQ QSKEFKTQIN RLVGDVLLCT GFLSYLGPFN QIFRNYLLKD QWELELKARK
IPFTENLNLI AMLVDPPTIG EWGLQGLPGD DLSIQNGIIV TKATRYPLLI DPQTQGKTWI
KSKEKENDLQ VTSLNHKYFR THLEDSLSLG RPLLIEDIRE ELDPALDNVL EKNFIKSGTA
FKVKVGDKEC DIMDTFKLYI TTKLPNPAFT PEINAKTSVI DFTVTMKGLE NQLLRRVILT
EKQELESERV KLLEDVTFNK RKMKELEDNL LYKLSATKGS LVDDESLIGV LRITKQTAAE
VSEKLHVAAE TEIKINTAQE EFRPAATRGS ILYFLITEMS MVNIMYQTSL AQFLKLFDQS
MARSEKSPLP QKRITNIIEY LTYEVFTYSV RGLYENHKFL FVLLMTLKID LQRGTVKHKE
FQALIKGGAA LDLKACPPKP FRWILDMTWL NLVELSKLPQ FAEIMNQISR NEKGWKNWFD
KDAPEEEIIP DGYNDSLDTC RKLLLIRSWC PDRTVFQARK YIADSLEEKY TEPVILNLEK
TWEESDTHTP LICFLSMGSD PTIQIDALAK KLKLECRTIS MGQGQEVHAR KLIQLSMQQG
GWVLLQNCHL GLEFMEELLE MLMVTETTED SFRVWITTEP HDRFPITLLQ TSIKFTNEPP
QGVRAGLKRT FAGINQDLLD ISNLPMWKPM LYTVAFLHST VQERRKFGPL GWNIPYEFNS
ADFSASVQFI QNHLDECDIK KGVSWSTVRY MIGEVQYGGR VTDDFDKRLL NCFARVWFSE
KMFEPSFCFY TGYKIPICKT LDQYFEFIQS LPSLDNPEVF GLHPNADITY QSNTASDVLE
TITNIQPKES GGGVGETREA IVYRLSEDML SKLPPNYVPH EVKARLMKMG HLNSMNIFLR
QEIDRMQKVI SILRSSLSDL KLAIEGTIIM SENLRDALDN MYDARIPQLW KRVSWDSSTL
GFWFTELLER NAQFSTWIFE GRPNVFWMTG FFNPQGFLTA MRQEVTRAHK GWALDTVTIH
NEVLRQTKEE IITPPAEGVY IYGLYMDGAS WDRRNGKLTE STPKVLFTQL PVLHIFAINS
TAPKDPKLYV CPIYKKPRRT DLTFITVVYL RTVLSPDHWI LRGVALLCDI K
