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   27-MAR-2024, entry version 156.
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   PDB; 8J07; EM; 4.10 A; g3=1-4116.
DR   PDBsum; 8J07; -.
DR   EMDB; EMD-35888; -.
DR   SMR; Q8TD57; -.
DR   BioGRID; 120722; 9.
DR   IntAct; Q8TD57; 6.
DR   STRING; 9606.ENSP00000261383; -.
DR   CarbonylDB; Q8TD57; -.
DR   GlyCosmos; Q8TD57; 1 site, 1 glycan.
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; 9606-ENSP00000261383; -.
DR   PeptideAtlas; Q8TD57; -.
DR   ProteomicsDB; 74244; -. [Q8TD57-1]
DR   ProteomicsDB; 74245; -. [Q8TD57-2]
DR   ProteomicsDB; 74246; -. [Q8TD57-3]
DR   Pumba; Q8TD57; -.
DR   Antibodypedia; 67049; 29 antibodies from 6 providers.
DR   DNASU; 55567; -.
DR   Ensembl; ENST00000261383.3; ENSP00000261383.3; ENSG00000158486.15. [Q8TD57-1]
DR   GeneID; 55567; -.
DR   KEGG; hsa:55567; -.
DR   UCSC; uc010vbe.3; human. [Q8TD57-1]
DR   AGR; HGNC:2949; -.
DR   CTD; 55567; -.
DR   DisGeNET; 55567; -.
DR   GeneCards; DNAH3; -.
DR   HGNC; HGNC:2949; DNAH3.
DR   HPA; ENSG00000158486; Tissue enhanced (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; 166463at2759; -.
DR   PhylomeDB; Q8TD57; -.
DR   TreeFam; TF316836; -.
DR   PathwayCommons; Q8TD57; -.
DR   SignaLink; Q8TD57; -.
DR   BioGRID-ORCS; 55567; 9 hits in 1145 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 129 other cell types or tissues.
DR   GO; GO:0097729; C:9+2 motile cilium; IBA:GO_Central.
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: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:0003777; F:microtubule motor activity; NAS:UniProtKB.
DR   GO; GO:0008569; F:minus-end-directed microtubule motor activity; IBA:GO_Central.
DR   GO; GO:0060294; P:cilium movement involved in cell motility; IBA:GO_Central.
DR   GO; GO:0060285; P:cilium-dependent cell motility; NAS:UniProtKB.
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; IPR042228; Dynein_linker_3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR46961:SF8; DYNEIN AXONEMAL HEAVY CHAIN 3; 1.
DR   PANTHER; PTHR46961; DYNEIN HEAVY CHAIN 1, AXONEMAL-LIKE PROTEIN; 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; 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; P-loop containing nucleoside triphosphate hydrolases; 4.
DR   Genevisible; Q8TD57; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; Cell projection; Cilium;
KW   Coiled coil; 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
//