DYHC2_MOUSE
ID DYHC2_MOUSE Reviewed; 4306 AA.
AC Q45VK7; B8JJF9; B8JJG0; O08822; Q5VI59; Q5VI60; Q5VI61; Q5VI62; Q69Z42;
AC Q8BJL5; Q8BL87; Q8BMC7; Q8BUI9; Q8BXK5; Q9CRR8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Cytoplasmic dynein 2 heavy chain 1;
DE AltName: Full=Cytoplasmic dynein 2 heavy chain;
DE AltName: Full=Dynein cytoplasmic heavy chain 2;
DE AltName: Full=Dynein heavy chain 11;
DE Short=mDHC11;
DE AltName: Full=Dynein heavy chain isotype 1B;
GN Name=Dync2h1; Synonyms=Dhc1b, Dnchc2, Kiaa1997;
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 [MRNA] (ISOFORM 1), FUNCTION, MUTAGENESIS OF PHE-3890,
RP AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J;
RX PubMed=16061793; DOI=10.1073/pnas.0505328102;
RA Huangfu D., Anderson K.V.;
RT "Cilia and Hedgehog responsiveness in the mouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11325-11330(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-889; 1858-2833 AND 3654-4306 (ISOFORM 1).
RC STRAIN=C57BL/6J;
RC TISSUE=Adrenal gland, Corpora quadrigemina, Heart, and Wolffian duct;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-1850; 1897-2503; 2516-2974 AND 3076-4306
RP (ISOFORM 2).
RC STRAIN=BALB/cJ; TISSUE=Thymus;
RA Barbaric I., Bauer T., Wei G.;
RT "Genomic organization of mouse cytoplasmic dynein heavy chain 2.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1662-1868 (ISOFORM 1).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3081-4306 (ISOFORM 1).
RC TISSUE=Thymus;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8666668; DOI=10.1083/jcb.133.4.831;
RA Vaisberg E.A., Grissom P.M., McIntosh J.R.;
RT "Mammalian cells express three distinct dynein heavy chains that are
RT localized to different cytoplasmic organelles.";
RL J. Cell Biol. 133:831-842(1996).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=12432068; DOI=10.1242/jcs.00168;
RA Mikami A., Tynan S.H., Hama T., Luby-Phelps K., Saito T., Crandall J.E.,
RA Besharse J.C., Vallee R.B.;
RT "Molecular structure of cytoplasmic dynein 2 and its distribution in
RT neuronal and ciliated cells.";
RL J. Cell Sci. 115:4801-4808(2002).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=11907264; DOI=10.1091/mbc.01-08-0402;
RA Grissom P.M., Vaisberg E.A., McIntosh J.R.;
RT "Identification of a novel light intermediate chain (D2LIC) for mammalian
RT cytoplasmic dynein 2.";
RL Mol. Biol. Cell 13:817-829(2002).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF TRP-2502.
RX PubMed=16229832; DOI=10.1016/j.ydbio.2005.08.050;
RA May S.R., Ashique A.M., Karlen M., Wang B., Shen Y., Zarbalis K.,
RA Reiter J., Ericson J., Peterson A.S.;
RT "Loss of the retrograde motor for IFT disrupts localization of Smo to cilia
RT and prevents the expression of both activator and repressor functions of
RT Gli.";
RL Dev. Biol. 287:378-389(2005).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Spleen, and 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).
CC -!- FUNCTION: May function as a motor for intraflagellar retrograde
CC transport. Functions in cilia biogenesis. According to PubMed:8666668,
CC it may play a role in transport between endoplasmic reticulum and Golgi
CC or organization of the Golgi in cells. {ECO:0000269|PubMed:16061793,
CC ECO:0000269|PubMed:16229832, ECO:0000269|PubMed:8666668}.
CC -!- SUBUNIT: The cytoplasmic dynein complex 2 is probably composed by a
CC heavy chain DYNC2H1 homodimer and a number of DYNC2LI1 light
CC intermediate chains. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000269|PubMed:8666668}. Cell membrane
CC {ECO:0000269|PubMed:8666668}; Peripheral membrane protein
CC {ECO:0000269|PubMed:8666668}. Cytoplasm {ECO:0000269|PubMed:8666668}.
CC Note=Localizes to the apical cytoplasm (By similarity). According to
CC PubMed:8666668, it localizes to Golgi apparatus, cytoplasmic vesicle
CC and endoplasmic reticulum (PubMed:8666668).
CC {ECO:0000250|UniProtKB:Q9JJ79, ECO:0000269|PubMed:8666668}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q45VK7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q45VK7-2; Sequence=VSP_031286;
CC Name=3;
CC IsoId=Q45VK7-3; Sequence=VSP_031284, VSP_031285;
CC -!- TISSUE SPECIFICITY: Detected in brain, lung, spleen and kidney (at
CC protein level). Enriched in the ependymal layer lining the lateral
CC ventricles (at protein level). {ECO:0000269|PubMed:11907264,
CC ECO:0000269|PubMed:12432068}.
CC -!- DEVELOPMENTAL STAGE: Expressed at 9.5 and 10.5 dpc in the neural tube
CC where it is enriched in rostral part. {ECO:0000269|PubMed:16061793}.
CC -!- MISCELLANEOUS: Mice homozygous for Dync2h1 null alleles die at
CC approximately 12.5 dpc with abnormal brain morphology, frequent heart-
CC looping and occasionally with polysyndactily. Cilia have abnormal
CC morphology.
CC -!- SIMILARITY: Belongs to the dynein heavy chain family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB29399.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC38914.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; DQ104402; AAZ41367.1; -; mRNA.
DR EMBL; AK014500; BAB29399.2; ALT_INIT; mRNA.
DR EMBL; AK032860; BAC28057.1; -; mRNA.
DR EMBL; AK045978; BAC32559.1; -; mRNA.
DR EMBL; AK046538; BAC32776.1; -; mRNA.
DR EMBL; AK083433; BAC38914.1; ALT_INIT; mRNA.
DR EMBL; AK084796; BAC39280.1; -; mRNA.
DR EMBL; AC155908; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT010499; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY452064; AAS15576.1; -; mRNA.
DR EMBL; AY452065; AAS15577.1; -; mRNA.
DR EMBL; AY452066; AAS15578.1; -; mRNA.
DR EMBL; AY452067; AAS15579.1; -; mRNA.
DR EMBL; Z83809; CAB06063.1; -; mRNA.
DR EMBL; AK173324; BAD32602.1; -; mRNA.
DR CCDS; CCDS40528.1; -. [Q45VK7-1]
DR RefSeq; NP_084127.2; NM_029851.2. [Q45VK7-1]
DR RefSeq; XP_006509889.1; XM_006509826.3. [Q45VK7-2]
DR SMR; Q45VK7; -.
DR BioGRID; 225520; 2.
DR STRING; 10090.ENSMUSP00000116679; -.
DR iPTMnet; Q45VK7; -.
DR PhosphoSitePlus; Q45VK7; -.
DR EPD; Q45VK7; -.
DR MaxQB; Q45VK7; -.
DR PaxDb; Q45VK7; -.
DR PRIDE; Q45VK7; -.
DR ProteomicsDB; 277423; -. [Q45VK7-1]
DR ProteomicsDB; 277424; -. [Q45VK7-2]
DR ProteomicsDB; 277425; -. [Q45VK7-3]
DR Antibodypedia; 51715; 56 antibodies from 13 providers.
DR Ensembl; ENSMUST00000048417; ENSMUSP00000046733; ENSMUSG00000047193. [Q45VK7-1]
DR Ensembl; ENSMUST00000140466; ENSMUSP00000120007; ENSMUSG00000047193. [Q45VK7-1]
DR Ensembl; ENSMUST00000147193; ENSMUSP00000116679; ENSMUSG00000047193. [Q45VK7-2]
DR GeneID; 110350; -.
DR KEGG; mmu:110350; -.
DR UCSC; uc009occ.1; mouse. [Q45VK7-1]
DR CTD; 79659; -.
DR MGI; MGI:107736; Dync2h1.
DR VEuPathDB; HostDB:ENSMUSG00000047193; -.
DR eggNOG; KOG3595; Eukaryota.
DR GeneTree; ENSGT00940000154620; -.
DR HOGENOM; CLU_000038_7_2_1; -.
DR InParanoid; Q45VK7; -.
DR OMA; PFMLIGP; -.
DR OrthoDB; 26380at2759; -.
DR TreeFam; TF315251; -.
DR Reactome; R-MMU-5610787; Hedgehog 'off' state.
DR Reactome; R-MMU-5620924; Intraflagellar transport.
DR BioGRID-ORCS; 110350; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Dync2h1; mouse.
DR PRO; PR:Q45VK7; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q45VK7; protein.
DR Bgee; ENSMUSG00000047193; Expressed in spermatocyte and 209 other tissues.
DR ExpressionAtlas; Q45VK7; baseline and differential.
DR Genevisible; Q45VK7; MM.
DR GO; GO:0045177; C:apical part of cell; IDA:BHF-UCL.
DR GO; GO:0005930; C:axoneme; IDA:BHF-UCL.
DR GO; GO:0005868; C:cytoplasmic dynein complex; ISO:MGI.
DR GO; GO:0030286; C:dynein complex; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0031514; C:motile cilium; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; ISO:MGI.
DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; ISO:MGI.
DR GO; GO:0060271; P:cilium assembly; IMP:MGI.
DR GO; GO:0060976; P:coronary vasculature development; IMP:MGI.
DR GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:MGI.
DR GO; GO:0030326; P:embryonic limb morphogenesis; IMP:MGI.
DR GO; GO:0030900; P:forebrain development; IMP:MGI.
DR GO; GO:0007030; P:Golgi organization; ISO:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0035721; P:intraciliary retrograde transport; IMP:MGI.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0030182; P:neuron differentiation; IMP:MGI.
DR GO; GO:1905515; P:non-motile cilium assembly; IMP:MGI.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IMP:MGI.
DR GO; GO:0061512; P:protein localization to cilium; IMP:MGI.
DR GO; GO:0016485; P:protein processing; IMP:MGI.
DR GO; GO:0021522; P:spinal cord motor neuron differentiation; IGI:MGI.
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; IPR026815; DYNC2H1.
DR InterPro; IPR042222; Dynein_2_N.
DR InterPro; IPR043157; Dynein_AAA1S.
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 PANTHER; PTHR10676:SF352; PTHR10676:SF352; 1.
DR Pfam; PF12774; AAA_6; 1.
DR Pfam; PF12780; AAA_8; 1.
DR Pfam; PF12781; AAA_9; 1.
DR Pfam; PF18198; AAA_lid_11; 1.
DR Pfam; PF08385; DHC_N1; 1.
DR Pfam; PF08393; DHC_N2; 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 membrane; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Developmental protein; Dynein; Membrane; Microtubule; Motor protein;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..4306
FT /note="Cytoplasmic dynein 2 heavy chain 1"
FT /id="PRO_0000318744"
FT REGION 1..1650
FT /note="Stem"
FT /evidence="ECO:0000250"
FT REGION 1651..1875
FT /note="AAA 1"
FT /evidence="ECO:0000250"
FT REGION 1941..2161
FT /note="AAA 2"
FT /evidence="ECO:0000250"
FT REGION 2249..2505
FT /note="AAA 3"
FT /evidence="ECO:0000250"
FT REGION 2617..2862
FT /note="AAA 4"
FT /evidence="ECO:0000250"
FT REGION 2880..3168
FT /note="Stalk"
FT /evidence="ECO:0000250"
FT REGION 3243..3472
FT /note="AAA 5"
FT /evidence="ECO:0000250"
FT REGION 3689..3904
FT /note="AAA 6"
FT /evidence="ECO:0000250"
FT COILED 669..696
FT /evidence="ECO:0000255"
FT COILED 2896..2981
FT /evidence="ECO:0000255"
FT COILED 3108..3199
FT /evidence="ECO:0000255"
FT COILED 3407..3441
FT /evidence="ECO:0000255"
FT BINDING 145..152
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 1689..1696
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 1979..1986
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2291..2298
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2655..2662
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VAR_SEQ 335
FT /note="L -> P (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031284"
FT VAR_SEQ 337..4306
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031285"
FT VAR_SEQ 3272
FT /note="Q -> QIIGLKSW (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_031286"
FT MUTAGEN 2502
FT /note="W->R: Loss of function."
FT /evidence="ECO:0000269|PubMed:16229832"
FT MUTAGEN 3890
FT /note="F->S: In lln mutant; loss of function."
FT /evidence="ECO:0000269|PubMed:16061793"
FT CONFLICT 33
FT /note="L -> F (in Ref. 2; BAC28057)"
FT /evidence="ECO:0000305"
FT CONFLICT 1254
FT /note="A -> P (in Ref. 4; AAS15576)"
FT /evidence="ECO:0000305"
FT CONFLICT 1664
FT /note="Y -> I (in Ref. 5; CAB06063)"
FT /evidence="ECO:0000305"
FT CONFLICT 1687
FT /note="P -> G (in Ref. 5; CAB06063)"
FT /evidence="ECO:0000305"
FT CONFLICT 1773
FT /note="E -> D (in Ref. 5; CAB06063)"
FT /evidence="ECO:0000305"
FT CONFLICT 1864
FT /note="W -> Y (in Ref. 5; CAB06063)"
FT /evidence="ECO:0000305"
FT CONFLICT 1866..1867
FT /note="LR -> IS (in Ref. 5; CAB06063)"
FT /evidence="ECO:0000305"
FT CONFLICT 2687
FT /note="P -> R (in Ref. 4; AAS15578)"
FT /evidence="ECO:0000305"
FT CONFLICT 2699
FT /note="Q -> K (in Ref. 2; BAC38914)"
FT /evidence="ECO:0000305"
FT CONFLICT 2734
FT /note="E -> K (in Ref. 4; AAS15578)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 4306 AA; 492339 MW; 0899EEC8224F4B04 CRC64;
MAGSLGDVRK LFLFTTTQNY FGLRPELWDQ PPLSNCPEVN NFLDDGNQML LRVQRSEAGL
AFSNTIDFDD AKDKVLVFFK LRPEVITDGN LHNNILVSSM LESPINSLYQ AVRQVFAPML
LKDQEWSRNF DPKLQNLLSE LEAGLGIVLR KSDTNLPKLK LKEDDTRGIL TPSDEFQFWI
EQAHRGSKQI SKERASYFKE LFETISREFY NLDSLSLLEV VDLVETTRDV VDDVWRQTEH
DHYPESRMLH LLDVIGGSFG RFVQKKLGSL KLWEDPYYLV KENLKAGISI CEQWVIVCSH
LTGQVWQRYV PHPWKSGKYF PETLDKLGKR LEEVLAIRTI HEKLLYFLPA SEERIVCLSR
VFEPFTGVNP VQYNPYTEPL WKAAVSQYEK IIAPAEQKIA GKLKNYISEI QDSPQQLLQA
FLKYKELVKR PTISKELMLE RETLLARLGD SAKDFRLDFE NRCRGIPGDP SGPLSGKNLS
EVVNNIVWVR QLELKVDDTI KIAEALLSDL SGFRSFHRSA EDLLDQFKLY EQEQFDDWSR
EVQSGLSDSR SGLCIEANSR IMELDPNDGA LKVHYSDRLV ILLREVRQLS ALGFVIPAKI
QQVANVAQKF CKQAIILKQV AHFYNSIDQQ MIQSQRPMML QSALAFEQII KNSKAGSGGK
SQITWDNPKE LEGYIQKLQN AAERLATENR RLRKWHTTFC EKVVILMNID LLRQQQRWKD
GLQELRTGLA TVAAQGFQAS DMRAWRQHWN HQLYKALEHQ YQVGLEALNE NLPEINVDLT
YKQGRLQFRP PFEEIRAKYY REMKRFIGIP NQFKGVGEAG DESIFSVMID RNASGFLTIY
SKAEDLFRRL SAVLHQHKEW VVIGQVDMEA LVEKNLSTVH DWEKNFKALK IKGKEVERLP
SAVKVDCLNI NCSPVKTVID DLIQKLFDLL VLSLKKSIQT HIHEIDTFVT EAMKVLTVIP
QSVEEIGDTN VQYSNLQDRR PEILPLFQEA EDKNRLLRTV AGGGVETVSN LRAKWDKFEL
MMESHQLMIK DQIEVMKGNV KSRLQIYYQE LDKFKARWDQ LKPGDDIIET GQQNTMDQSA
KSIKEKKIEF DDLEVIRKKL VDDCHHFGLE EPNFSLAYSI SKDIESCAQI WALYEEFQQG
LQDMAKEDWI TYRAKIYLFE EFLINWHERL RKIEEHSVMT VKLQSEVDRY KMIIPILKYV
RGEHLSPDHW LDLFRLLGLP RGTSLEKLLF GDLLRVADTI VEKASELKDL NSRAQGEVTI
REALRELDLW GVGAVFSLID YEDSQNHTIK LIKDWKDIVN QVGDNRCLLQ SLKDSPYYKG
FEDKVSIWER KLAQLDEYLQ NLNHIQRKWV YLEPIFGRGA LPKEQTRFNK VDEDFRSIMM
DIRKDSRVTT LTTHAGIRNT LLTILDQLQR CQKSLNEFLE EKRSAFPRFY FIGDDDLLEI
LGQSTNPSVI QSHLKKLFAG INSVCFDEES KHITAMKSLE GEVVPFKSKV LLSNNVEAWL
NDLALEMKQT LKQLLKECVT AGRSSQGAID PSLFPSQILC LAEQIKFTED VENAIKDHSL
HQIEAQLVAK LERYTSVDTS SEDPGNSESG ILELKLKALI LDIIHNIDIV KQLNQVQVHT
TDDWAWKKQV RFYMKSDHTC YVQMVDSELQ YTYEYQGNAP KLVYTPLTDK CYLTLTQAMK
MGLGGNPYGP AGTGKTESVK ALGGLLGRQV LVFNCDEGID VKSMGRIFVG LVKCGAWGCF
DEFNRLEEAV LSAVSMQIQT IQDALKNHRT VCELLGKEVE INANSGIFIT MNPAGKGYGG
RQKLPDNLKQ LFRPVAMSRP DNDLIAEVIL YSEGFKDAKE LGRKLVAIFN LSRELLTPQQ
HYDWGLRALK TVLRGSGNLL RQLKKNSTKQ DVNENHIVVQ ALRLNTMSKF TFADCTRFDA
LIKDVFPGID FKEVEYDELS SALKQVFEEA NYEVIPNQMK KALELYEQLR QRTGVVIVGP
SGAGKSTLWR MLRAALCKIG KVVKQYTMNP KAMPRHQLLG HIDMDTREWS DGVLTNSARQ
VVREPQDVSS WIICDGDIDP EWIESLNSVL DDNRLLTMPS GERIQFGPNV NFVFETHDLS
CASPATISRM GMIFLSDEET DLNSLIKSWL RNQPLEYRSN LENWIGDYFS KALQWVLKQN
DYVVETSLVG TVMNGLSHLH GCKYHDQFII NLIRGLGGNL NMKSRLEFTK EVFNWARETP
PDSHRPMDTY YDCDRGQLAS YMLKKPESLT ADDFSNGHIL PVIQTPDMQR GLDYFKPWLS
SDTKQPFILV GPEGCGKGML LRYAFSQLRS TEIATIHCSA QTTSRHLLQK LSQTCMVIST
NTGRVYRPKD CERLVLYLKD INLPKLDKWG TSTLVAFLQQ VLTYQGFYDE NLEWVGLENI
QIVASMSAGG RLGRHKLTTR FTSIVRLCAI DYPEREQLQT IYGAYLEAVL HKNLKNHSIW
GSSSKIYLLA GSMVQVYEQV RAKFTVDEYS HYFFTPCILT QWVLGLFRYD LEGGSSNHPL
DYVLEIVAYE ARRLFRDKIV GVKELHLFDN ILTSVLQGDW GSDILDNMAD SFYVTWGAHH
VSGGKTAPGQ PLPPHGKPLG KLTSADLKDV IKKGLIHYGR DNQNLDILLF QEVLEYMSRI
DRVLSFPGGS LLLAGRSGVG RRTVTSLVSH MHGAVLFSPK ISRGYEPKQF RNDLKHVLQL
AGIEAQQVVL LLEDYQFVHP TFLEMINSLL ASGEVPGLYT LEELEPLLLP LKDQASQDGF
FGPVFNYFTY RIQQNLHIVL IMDSANLNFI VNCESNPALH KKCQVLWMEG WSDSSMKKIP
EMLFSETDGE EKYEKKRKDE KKRNSVDPDF IKSFLLIHES CKAYGATPSR YMTFLHVYSA
ISSSKKKELL KRQSHLQAGV SKLNEAKALV DELNRKAGEQ SILLRIKQDE ADSALQEITV
SMQDASEQKT ELERLKQRIA EEVVKIEERK SKIDDELKEV QPLVNEAKLA VGNIRPESLS
EIRSLRMPPD VIRDILEGVL RLMGIFDTSW VSMKSFLAKR GVREDIATFD ARNIPKEIRE
SVEELLFKNK ASFDPKNAKR ASTAAAPLAA WVKANVQYSH VLERIQPLET EQSGLELNLK
KTEDRKRKLE DLLNSVGQKV SELKEKFQSR TSEAAKLEAE VSKAQETIKA AEVLISQLDR
EHRRWNAQVA EIAEELATLP KRAQLAAAFI TYLSAAPEGL RKNCLEEWTK AAGLEKFDLR
RFLCTESEQL IWKSEGLPSD DLSIENALVI LQSRVCPFLI DPSSQATEWL KTHLKDSHLE
VINQQDSNFI TALELAVRFG KTLIIQEMDG VEPVLYPLLR RDLVAQGPRY VVQIGDKIID
YNEDFRLFLS TRNPNPFIPP DAASIVTEVN FTTTRSGLRG QLLALTIQHE KPDLEEQKTK
LLQQEEDKKI QLARLEESLL ETLATSQGNI LENKDLIESL NQTKASSALI QDSLKESYKL
QISLDQERDA YLPLAESASK MYFIISDLSK INNMYRFSLA SFLRLFQRAL QNKQDSENTE
ERIQCLVNSL KHMVYEYICR CLFKADQLMF ALHFVRGMHP ELFQENEWDT FTGVVVGDML
RKADSQQRIR DQLPSWIDQE RSWAVATLKI SLPSLYQTLC LEDGAFWRTY YHHSMCEQEF
PSILAKKVSL FQQVLVVQAL RPDRLQSAMA LFACKALGLK ELSPLPLNLK RLYKETLEIE
PILIIISPGA DPSQELQELA SAERSSECYH QVAMGQGQAD LAIQMLKECA RNGDWLCLKN
LHLVVSWLPV LEKELNTLQP KDSFRLWLTA EVHPNFTPIL LQSSLKITYE SPPGLKKNLM
RTYESWTPEQ ISKRDNIHRA HALFSLAWFH AACQERRNYI PQGWTKFYEF SLSDLRAGYH
VIDRLFDGTK DVQWEFVHGL LENSIYGGRV DNYFDLRVLQ SYLKQFFNSS IIDVLNQRNK
KSIFPYSISL PNSCSILDYR AVIEKLPEDD KPSFFGLPAN IARSSQRMIS SQVISQLRIL
GRSVTAGCKF DREIWSNELS PVLNLWKKLN QNSNLIHQKV SPPNDRQGSP ILSFIILEQF
NAIRLVQSVH QSLAALSKVI RGTTLLSSEV QKLASALLNQ KCPLTWQSRW EGPEDPLQYL
RGLVARTLAI QNWVEKAEKQ VLLADTLDLS ELFHPDTFLN ALRQETARAT GCSVDSLKFV
ASWKGRLQEA KLQIKISGLL LEGCSFDGNR LSENQHDSPS VSSVLPCYMG WTPQGSYGPY
SPDECISLPV YTSAERERVV TNIDVPCGGN QDQWIQCGAA LFLKNQ
