DYH3_HUMAN
ID DYH3_HUMAN Reviewed; 4116 AA.
AC Q8TD57; O00437; O15437; O43326; Q3C0H2; Q8WUP9; Q9UEM3; Q9UEM5; Q9UG35;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Dynein axonemal heavy chain 3;
DE AltName: Full=Axonemal beta dynein heavy chain 3;
DE Short=HsADHC3;
DE AltName: Full=Ciliary dynein heavy chain 3;
DE AltName: Full=Dnahc3-b;
GN Name=DNAH3; Synonyms=DNAHC3B;
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).
RA Blouin J.-L., Gehrig C., Jeganathan D., Bartoloni L., Rossier C.,
RA Duriaux Sail G., Scamuffa N., Mitchison H.M., DeLozier Blanchet C.D.,
RA Antonarakis S.E.;
RT "DNAH3: characterization of the full length gene and mutation search in
RT patients with primary ciliary dyskinesia.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1391-1533 (ISOFORM 1), AND NUCLEOTIDE
RP SEQUENCE [GENOMIC DNA] OF 1435-1449.
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1429-1605 (ISOFORM 1).
RC 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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1429-1478, AND TISSUE SPECIFICITY.
RX PubMed=9256245; DOI=10.1016/s0014-5793(97)00800-4;
RA Chapelin C., Duriez B., Magnino F., Goossens M., Escudier E., Amselem S.;
RT "Isolation of several human axonemal dynein heavy chain genes: genomic
RT structure of the catalytic site, phylogenetic analysis and chromosomal
RT assignment.";
RL FEBS Lett. 412:325-330(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1574-4116 (ISOFORM 3).
RC TISSUE=Ovary;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3152-4116 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 3544-4116.
RX PubMed=10493829; DOI=10.1006/geno.1999.5927;
RA Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J.,
RA Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X.,
RA Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C.,
RA Adams M.D.;
RT "Genome duplications and other features in 12 Mb of DNA sequence from human
RT chromosome 16p and 16q.";
RL Genomics 60:295-308(1999).
RN [10]
RP VARIANTS [LARGE SCALE ANALYSIS] LEU-484 AND PHE-1608.
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).
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 Involved in sperm motility; implicated in sperm flagellar assembly (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Consists of at least two heavy chains and a number of
CC intermediate and light chains.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8TD57-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TD57-2; Sequence=VSP_031919, VSP_031920, VSP_031921,
CC VSP_031922, VSP_031923;
CC Name=3;
CC IsoId=Q8TD57-3; Sequence=VSP_031924, VSP_031925;
CC -!- TISSUE SPECIFICITY: Expressed primarily in trachea and testis, 2
CC tissues containing axonemal structures. Also expressed in lung.
CC {ECO:0000269|PubMed:9256245}.
CC -!- DOMAIN: Dynein heavy chains probably consist of an N-terminal stem
CC (which binds cargo and interacts with other dynein components), and the
CC head or motor domain. The motor contains six tandemly-linked AAA
CC domains in the head, which form a ring. A stalk-like structure (formed
CC by two of the coiled coil domains) protrudes between AAA 4 and AAA 5
CC and terminates in a microtubule-binding site. A seventh domain may also
CC contribute to this ring; it is not clear whether the N-terminus or the
CC C-terminus forms this extra domain. There are four well-conserved and
CC two non-conserved ATPase sites, one per AAA domain. Probably only one
CC of these (within AAA 1) actually hydrolyzes ATP, the others may serve a
CC regulatory function (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the dynein heavy chain family. {ECO:0000305}.
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DR EMBL; AF494040; AAM12861.1; -; mRNA.
DR EMBL; AK056509; BAE46616.1; -; mRNA.
DR EMBL; CH471228; EAW66851.1; -; Genomic_DNA.
DR EMBL; AJ132085; CAA10558.1; -; mRNA.
DR EMBL; AJ132092; CAA10565.1; -; Genomic_DNA.
DR EMBL; Z83805; CAB06059.1; -; mRNA.
DR EMBL; U83574; AAB82763.1; -; Genomic_DNA.
DR EMBL; BC019878; AAH19878.1; -; mRNA.
DR EMBL; AL096732; CAB46377.1; -; mRNA.
DR EMBL; AC002394; AAC05809.1; -; Genomic_DNA.
DR CCDS; CCDS10594.1; -. [Q8TD57-1]
DR PIR; T12545; T12545.
DR RefSeq; NP_001334815.1; NM_001347886.1.
DR RefSeq; NP_060009.1; NM_017539.2. [Q8TD57-1]
DR SMR; Q8TD57; -.
DR BioGRID; 120722; 7.
DR IntAct; Q8TD57; 6.
DR STRING; 9606.ENSP00000261383; -.
DR CarbonylDB; Q8TD57; -.
DR GlyGen; Q8TD57; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8TD57; -.
DR PhosphoSitePlus; Q8TD57; -.
DR BioMuta; DNAH3; -.
DR DMDM; 74762616; -.
DR EPD; Q8TD57; -.
DR jPOST; Q8TD57; -.
DR MassIVE; Q8TD57; -.
DR MaxQB; Q8TD57; -.
DR PaxDb; Q8TD57; -.
DR PeptideAtlas; Q8TD57; -.
DR PRIDE; Q8TD57; -.
DR ProteomicsDB; 74244; -. [Q8TD57-1]
DR ProteomicsDB; 74245; -. [Q8TD57-2]
DR ProteomicsDB; 74246; -. [Q8TD57-3]
DR Antibodypedia; 67049; 29 antibodies from 6 providers.
DR DNASU; 55567; -.
DR Ensembl; ENST00000261383.3; ENSP00000261383.3; ENSG00000158486.14. [Q8TD57-1]
DR GeneID; 55567; -.
DR KEGG; hsa:55567; -.
DR UCSC; uc010vbe.3; human. [Q8TD57-1]
DR CTD; 55567; -.
DR DisGeNET; 55567; -.
DR GeneCards; DNAH3; -.
DR HGNC; HGNC:2949; DNAH3.
DR HPA; ENSG00000158486; Tissue enhanced (brain, fallopian tube, testis).
DR MIM; 603334; gene.
DR neXtProt; NX_Q8TD57; -.
DR OpenTargets; ENSG00000158486; -.
DR PharmGKB; PA27402; -.
DR VEuPathDB; HostDB:ENSG00000158486; -.
DR eggNOG; KOG3595; Eukaryota.
DR GeneTree; ENSGT00940000154959; -.
DR HOGENOM; CLU_000038_0_1_1; -.
DR InParanoid; Q8TD57; -.
DR OMA; FFQSCAK; -.
DR OrthoDB; 2079at2759; -.
DR PhylomeDB; Q8TD57; -.
DR TreeFam; TF316836; -.
DR PathwayCommons; Q8TD57; -.
DR SignaLink; Q8TD57; -.
DR BioGRID-ORCS; 55567; 9 hits in 1067 CRISPR screens.
DR ChiTaRS; DNAH3; human.
DR GenomeRNAi; 55567; -.
DR Pharos; Q8TD57; Tdark.
DR PRO; PR:Q8TD57; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q8TD57; protein.
DR Bgee; ENSG00000158486; Expressed in bronchial epithelial cell and 127 other tissues.
DR Genevisible; Q8TD57; HS.
DR GO; GO:0097729; C:9+2 motile cilium; IEA:UniProt.
DR GO; GO:0005858; C:axonemal dynein complex; NAS:UniProtKB.
DR GO; GO:0030286; C:dynein complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0045505; F:dynein intermediate chain binding; IBA:GO_Central.
DR GO; GO:0051959; F:dynein light intermediate chain binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; NAS:UniProtKB.
DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0060285; P:cilium-dependent cell motility; NAS:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR Gene3D; 1.10.8.710; -; 1.
DR Gene3D; 1.10.8.720; -; 1.
DR Gene3D; 1.20.140.100; -; 1.
DR Gene3D; 3.10.490.20; -; 1.
DR Gene3D; 3.20.180.20; -; 1.
DR Gene3D; 3.40.50.300; -; 5.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR035699; AAA_6.
DR InterPro; IPR035706; AAA_9.
DR InterPro; IPR041658; AAA_lid_11.
DR InterPro; IPR042219; AAA_lid_11_sf.
DR InterPro; 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; 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; PF08393; DHC_N2; 1.
DR Pfam; PF17852; Dynein_AAA_lid; 1.
DR Pfam; PF18199; Dynein_C; 1.
DR Pfam; PF03028; Dynein_heavy; 1.
DR Pfam; PF12777; MT; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 4.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Cell projection; Cilium; Coiled coil;
KW Cytoplasm; Cytoskeleton; Dynein; Microtubule; Motor protein;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..4116
FT /note="Dynein axonemal heavy chain 3"
FT /id="PRO_0000322544"
FT REGION 1..1390
FT /note="Stem"
FT /evidence="ECO:0000250"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1391..1612
FT /note="AAA 1"
FT /evidence="ECO:0000250"
FT REGION 1672..1903
FT /note="AAA 2"
FT /evidence="ECO:0000250"
FT REGION 2036..2284
FT /note="AAA 3"
FT /evidence="ECO:0000250"
FT REGION 2395..2646
FT /note="AAA 4"
FT /evidence="ECO:0000250"
FT REGION 2661..2960
FT /note="Stalk"
FT /evidence="ECO:0000250"
FT REGION 3045..3275
FT /note="AAA 5"
FT /evidence="ECO:0000250"
FT REGION 3488..3712
FT /note="AAA 6"
FT /evidence="ECO:0000250"
FT COILED 785..852
FT /evidence="ECO:0000255"
FT COMPBIAS 26..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1429..1436
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 1710..1717
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2074..2081
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2434..2441
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..39
FT /note="MGATGRLELTLAAPPHPGPAFQRSKARETQGEEEGSEMQ -> MGDMDCSSQ
FT K (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_031919"
FT VAR_SEQ 528..566
FT /note="KLKYIPLKFSFTAAAADRQCVKAAEPGEPSMHAAATAMA -> KVESVLFP
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_031920"
FT VAR_SEQ 762
FT /note="Y -> YEDIKLNSTLFLWPD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_031921"
FT VAR_SEQ 790..799
FT /note="CSEFELRLEG -> YRESLGLSWK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_031922"
FT VAR_SEQ 800..4116
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_031923"
FT VAR_SEQ 1883..1887
FT /note="VNDMF -> MKSGQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031924"
FT VAR_SEQ 1888..4116
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031925"
FT VARIANT 484
FT /note="I -> L (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_039412"
FT VARIANT 545
FT /note="R -> W (in dbSNP:rs16970910)"
FT /id="VAR_039413"
FT VARIANT 1565
FT /note="I -> M (in dbSNP:rs330150)"
FT /id="VAR_039414"
FT VARIANT 1583
FT /note="V -> I (in dbSNP:rs16970832)"
FT /id="VAR_039415"
FT VARIANT 1608
FT /note="S -> F (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_039416"
FT VARIANT 1752
FT /note="T -> M (in dbSNP:rs13332291)"
FT /id="VAR_039417"
FT VARIANT 2399
FT /note="I -> N (in dbSNP:rs34179606)"
FT /id="VAR_039418"
FT VARIANT 2804
FT /note="I -> V (in dbSNP:rs12929546)"
FT /id="VAR_039419"
FT VARIANT 2949
FT /note="K -> T (in dbSNP:rs33928718)"
FT /id="VAR_039420"
FT VARIANT 3457
FT /note="E -> K (in dbSNP:rs3743695)"
FT /id="VAR_039421"
FT VARIANT 3639
FT /note="L -> I (in dbSNP:rs34771199)"
FT /id="VAR_039422"
FT VARIANT 3645
FT /note="R -> C (in dbSNP:rs12924551)"
FT /id="VAR_039423"
FT VARIANT 3744
FT /note="R -> W (in dbSNP:rs2301620)"
FT /id="VAR_039424"
FT CONFLICT 1393
FT /note="Y -> F (in Ref. 4; CAA10558)"
FT /evidence="ECO:0000305"
FT CONFLICT 1441
FT /note="D -> V (in Ref. 5; CAB06059)"
FT /evidence="ECO:0000305"
FT CONFLICT 1601..1604
FT /note="YGMR -> FGLH (in Ref. 5; CAB06059)"
FT /evidence="ECO:0000305"
FT CONFLICT 3828
FT /note="Q -> M (in Ref. 8; CAB46377)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 4116 AA; 470771 MW; AF387246540D9DF2 CRC64;
MGATGRLELT LAAPPHPGPA FQRSKARETQ GEEEGSEMQI AKSDSIHHMS HSQGQPELPP
LPASANEEPS GLYQTVMSHS FYPPLMQRTS WTLAAPFKEQ HHHRGPSDSI ANNYSLMAQD
LKLKDLLKVY QPATISVPRD RTGQGLPSSG NRSSSEPMRK KTKFSSRNKE DSTRIKLAFK
TSIFSPMKKE VKTSLTFPGS RPMSPEQQLD VMLQQEMEME SKEKKPSESD LERYYYYLTN
GIRKDMIAPE EGEVMVRISK LISNTLLTSP FLEPLMVVLV QEKENDYYCS LMKSIVDYIL
MDPMERKRLF IESIPRLFPQ RVIRAPVPWH SVYRSAKKWN EEHLHTVNPM MLRLKELWFA
EFRDLRFVRT AEILAGKLPL QPQEFWDVIQ KHCLEAHQTL LNKWIPTCAQ LFTSRKEHWI
HFAPKSNYDS SRNIEEYFAS VASFMSLQLR ELVIKSLEDL VSLFMIHKDG NDFKEPYQEM
KFFIPQLIMI KLEVSEPIIV FNPSFDGCWE LIRDSFLEII KNSNGIPKLK YIPLKFSFTA
AAADRQCVKA AEPGEPSMHA AATAMAELKG YNLLLGTVNA EEKLVSDFLI QTFKVFQKNQ
VGPCKYLNVY KKYVDLLDNT AEQNIAAFLK ENHDIDDFVT KINAIKKRRN EIASMNITVP
LAMFCLDATA LNHDLCERAQ NLKDHLIQFQ VDVNRDTNTS ICNQYSHIAD KVSEVPANTK
ELVSLIEFLK KSSAVTVFKL RRQLRDASER LEFLMDYADL PYQIEDIFDN SRNLLLHKRD
QAEMDLIKRC SEFELRLEGY HRELESFRKR EVMTTEEMKH NVEKLNELSK NLNRAFAEFE
LINKEEELLE KEKSTYPLLQ AMLKNKVPYE QLWSTAYEFS IKSEEWMNGP LFLLNAEQIA
EEIGNMWRTT YKLIKTLSDV PAPRRLAENV KIKIDKFKQY IPILSISCNP GMKDRHWQQI
SEIVGYEIKP TETTCLSNML EFGFGKFVEK LEPIGAAASK EYSLEKNLDR MKLDWVNVTF
SFVKYRDTDT NILCAIDDIQ MLLDDHVIKT QTMCGSPFIK PIEAECRKWE EKLIRIQDNL
DAWLKCQATW LYLEPIFSSE DIIAQMPEEG RKFGIVDSYW KSLMSQAVKD NRILVAADQP
RMAEKLQEAN FLLEDIQKGL NDYLEKKRLF FPRFFFLSND ELLEILSETK DPLRVQPHLK
KCFEGIAKLE FTDNLEIVGM ISSEKETVPF IQKIYPANAK GMVEKWLQQV EQMMLASMRE
VIGLGIEAYV KVPRNHWVLQ WPGQVVICVS SIFWTQEVSQ ALAENTLLDF LKKSNDQIAQ
IVQLVRGKLS SGARLTLGAL TVIDVHARDV VAKLSEDRVS DLNDFQWISQ LRYYWVAKDV
QVQIITTEAL YGYEYLGNSP RLVITPLTDR CYRTLMGALK LNLGGAPEGP AGTGKTETTK
DLAKALAKQC VVFNCSDGLD YKAMGKFFKG LAQAGAWACF DEFNRIEVEV LSVVAQQILS
IQQAIIRKLK TFIFEGTELS LNPTCAVFIT MNPGYAGRAE LPDNLKALFR TVAMMVPDYA
LIGEISLYSM GFLDSRSLAQ KIVATYRLCS EQLSSQHHYD YGMRAVKSVL TAAGNLKLKY
PEENESVLLL RALLDVNLAK FLAQDVPLFQ GIISDLFPGV VLPKPDYEVF LKVLNDNIKK
MKLQPVPWFI GKIIQIYEMM LVRHGYMIVG DPMGGKTSAY KVLAAALGDL HAANQMEEFA
VEYKIINPKA ITMGQLYGCF DQVSHEWMDG VLANAFREQA SSLSDDRKWI IFDGPVDAIW
IENMNTVLDD NKKLCLMSGE IIQMNSKMSL IFEPADLEQA SPATVSRCGM IYMEPHQLGW
KPLKDSYMDT LPSSLTKEHK ELVNDMFMWL VQPCLEFGRL HCKFVVQTSP IHLAFSMMRL
YSSLLDEIRA VEEEEMELGE GLSSQQIFLW LQGLFLFSLV WTVAGTINAD SRKKFDVFFR
NLIMGMDDNH PRPKSVKLTK NNIFPERGSI YDFYFIKQAS GHWETWTQYI TKEEEKVPAG
AKVSELIIPT METARQSFFL KTYLDHEIPM LFVGPTGTGK SAITNNFLLH LPKNTYLPNC
INFSARTSAN QTQDIIMSKL DRRRKGLFGP PIGKKAVVFV DDLNMPAKEV YGAQPPIELL
RQWIDHGYWF DKKDTTRLDI VDMLLVTAMG PPGGGRNDIT GRFTRHLNII SINAFEDDIL
TKIFSSIVDW HFGKGFDVMF LRYGKMLVQA TKTIYRDAVE NFLPTPSKSH YVFNLRDFSR
VIQGVLLCPH THLQDVEKCI RLWIHEVYRV FYDRLIDKED RQVFFNMVKE TTSNCFKQTI
EKVLIHLSPT GKIVDDNIRS LFFGDYFKPE SDQKIYDEIT DLKQLTVVME HYLEEFNNIS
KAPMSLVMFR FAIEHISRIC RVLKQDKGHL LLVGIGGSGR QSAAKLSTFM NAYELYQIEI
TKNYAGNDWR EDLKKIILQV GVATKSTVFL FADNQIKDES FVEDINMLLN TGDVPNIFPA
DEKADIVEKM QTAARTQGEK VEVTPLSMYN FFIERVINKI SFSLAMSPIG DAFRNRLRMF
PSLINCCTID WFQSWPTDAL ELVANKFLED VELDDNIRVE VVSMCKYFQE SVKKLSLDYY
NKLRRHNYVT PTSYLELILT FKTLLNSKRQ EVAMMRNRYL TGLQKLDFAA SQVAVMQREL
TALQPQLILT SEETAKMMVK IEAETREADG KKLLVQADEK EANVAAAIAQ GIKNECEGDL
AEAMPALEAA LAALDTLNPA DISLVKSMQN PPGPVKLVME SICIMKGMKP ERKPDPSGSG
KMIEDYWGVS KKILGDLKFL ESLKTYDKDN IPPLTMKRIR ERFINHPEFQ PAVIKNVSSA
CEGLCKWVRA MEVYDRVAKV VAPKRERLRE AEGKLAAQMQ KLNQKRAELK LVVDRLQALN
DDFEEMNTKK KDLEENIEIC SQKLVRAEKL ISGLGGEKDR WTEAARQLGI RYTNLTGDVL
LSSGTVAYLG AFTVDYRVQC QNQWLAECKD KVIPGFSDFS LSHTLGDPIK IRAWQIAGLP
VDSFSIDNGI IVSNSRRWAL MIDPHGQANK WIKNMEKANK LAVIKFSDSN YMRMLENALQ
LGTPVLIENI GEELDASIEP ILLKATFKQQ GVEYMRLGEN IIEYSRDFKL YITTRLRNPH
YLPEVAVKVC LLNFMITPLG LQDQLLGIVA AKEKPELEEK KNQLIVESAK NKKHLKEIED
KILEVLSMSK GNILEDETAI KVLSSSKVLS EEISEKQKVA SMTETQIDET RMGYKPVAVH
SATIFFCISD LANIEPMYQY SLTWFINLYM HSLTHSTKSE ELNLRIKYII DHFTLSIYNN
VCRSLFEKDK LLFSLLLTIG IMKQKKEITE EVWYFLLTGG IALDNPYPNP APQWLSEKAW
AEIVRASALP KLHGLMEHLE QNLGEWKLIY DSAWPHEEQL PGSWKFSQGL EKMVILRCLR
PDKMVPAVRE FIAEHMGKLY IEAPTFDLQG SYNDSSCCAP LIFVLSPSAD PMAGLLKFAD
DLGMGGTRTQ TISLGQGQGP IAAKMINNAI KDGTWVVLQN CHLAASWMPT LEKICEEVIV
PESTNARFRL WLTSYPSEKF PVSILQNGIK MTNEPPKGLR ANLLRSYLND PISDPVFFQS
CAKAVMWQKM LFGLCFFHAV VQERRNFGPL GWNIPYEFNE SDLRISMWQI QMFLNDYKEV
PFDALTYLTG ECNYGGRVTD DKDRRLLLSL LSMFYCKEIE EDYYSLAPGD TYYIPPHGSY
QSYIDYLRNL PITAHPEVFG LHENADITKD NQETNQLFEG VLLTLPRQSG GSGKSPQEVV
EELAQDILSK LPRDFDLEEV MKLYPVVYEE SMNTVLRQEL IRFNRLTKVV RRSLINLGRA
IKGQVLMSSE LEEVFNSMLV GKVPAMWAAK SYPSLKPLGG YVADLLARLT FFQEWIDKGP
PVVFWISGFY FTQSFLTGVS QNYARKYTIP IDHIGFEFEV TPQETVMENN PEDGAYIKGL
FLEGARWDRK TMQIGESLPK ILYDPLPIIW LKPGESAMFL HQDIYVCPVY KTSARRGTLS
TTGHSTNYVL SIELPTDMPQ KHWINRGVAS LCQLDN
