DYN3_HUMAN
ID DYN3_HUMAN Reviewed; 869 AA.
AC Q9UQ16; A9Z1Y1; O14982; O95555; Q1MTM8; Q5W129; Q6P2G1; Q9H0P3; Q9H548;
AC Q9NQ68; Q9NQN6;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 4.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Dynamin-3;
DE EC=3.6.5.5;
DE AltName: Full=Dynamin, testicular;
DE AltName: Full=T-dynamin;
GN Name=DNM3; Synonyms=KIAA0820;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Kidney;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Brain;
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 [7] {ECO:0007744|PDB:3L43}
RP X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 6-306 IN COMPLEX WITH GTP ANALOG.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the dynamin 3 GTPase domain bound with GDP.";
RL Submitted (DEC-2009) to the PDB data bank.
CC -!- FUNCTION: Microtubule-associated force-producing protein involved in
CC producing microtubule bundles and able to bind and hydrolyze GTP. Most
CC probably involved in vesicular trafficking processes, in particular
CC endocytosis (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.5;
CC -!- INTERACTION:
CC Q9UQ16-2; Q9UQ16-2: DNM3; NbExp=4; IntAct=EBI-3959311, EBI-3959311;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Cytoplasm, cytoskeleton
CC {ECO:0000305}. Note=Microtubule-associated. {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9UQ16-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UQ16-2; Sequence=VSP_034053;
CC Name=3;
CC IsoId=Q9UQ16-3; Sequence=VSP_034053, VSP_034054;
CC Name=4;
CC IsoId=Q9UQ16-4; Sequence=VSP_034054;
CC Name=5;
CC IsoId=Q9UQ16-5; Sequence=VSP_034053, VSP_054546, VSP_054547;
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE-
CC ProRule:PRU01055}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA74843.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB020627; BAA74843.2; ALT_INIT; mRNA.
DR EMBL; AL136712; CAB66647.1; -; mRNA.
DR EMBL; AL031864; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL121984; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL133514; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL137157; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445990; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL512843; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z97195; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW90918.1; -; Genomic_DNA.
DR EMBL; BC064546; AAH64546.1; -; mRNA.
DR CCDS; CCDS44276.1; -. [Q9UQ16-2]
DR CCDS; CCDS53431.1; -. [Q9UQ16-3]
DR CCDS; CCDS60356.1; -. [Q9UQ16-5]
DR CCDS; CCDS86032.1; -. [Q9UQ16-1]
DR RefSeq; NP_001129599.1; NM_001136127.2. [Q9UQ16-2]
DR RefSeq; NP_001265181.1; NM_001278252.1. [Q9UQ16-5]
DR RefSeq; NP_056384.2; NM_015569.4. [Q9UQ16-3]
DR RefSeq; XP_005245136.1; XM_005245079.1. [Q9UQ16-4]
DR RefSeq; XP_005245137.1; XM_005245080.1.
DR PDB; 3L43; X-ray; 2.27 A; A/B/C/D=6-306.
DR PDB; 5A3F; X-ray; 3.70 A; A/B/C/D=1-764.
DR PDBsum; 3L43; -.
DR PDBsum; 5A3F; -.
DR AlphaFoldDB; Q9UQ16; -.
DR SMR; Q9UQ16; -.
DR BioGRID; 117515; 97.
DR DIP; DIP-36244N; -.
DR IntAct; Q9UQ16; 44.
DR MINT; Q9UQ16; -.
DR STRING; 9606.ENSP00000356705; -.
DR iPTMnet; Q9UQ16; -.
DR PhosphoSitePlus; Q9UQ16; -.
DR BioMuta; DNM3; -.
DR DMDM; 190358934; -.
DR EPD; Q9UQ16; -.
DR jPOST; Q9UQ16; -.
DR MassIVE; Q9UQ16; -.
DR MaxQB; Q9UQ16; -.
DR PaxDb; Q9UQ16; -.
DR PeptideAtlas; Q9UQ16; -.
DR PRIDE; Q9UQ16; -.
DR ProteomicsDB; 66900; -.
DR ProteomicsDB; 85492; -. [Q9UQ16-1]
DR ProteomicsDB; 85493; -. [Q9UQ16-2]
DR ProteomicsDB; 85494; -. [Q9UQ16-3]
DR ProteomicsDB; 85495; -. [Q9UQ16-4]
DR Antibodypedia; 34382; 223 antibodies from 32 providers.
DR DNASU; 26052; -.
DR Ensembl; ENST00000355305.9; ENSP00000347457.5; ENSG00000197959.15. [Q9UQ16-1]
DR Ensembl; ENST00000367731.5; ENSP00000356705.1; ENSG00000197959.15. [Q9UQ16-2]
DR Ensembl; ENST00000367733.6; ENSP00000356707.2; ENSG00000197959.15. [Q9UQ16-5]
DR Ensembl; ENST00000627582.3; ENSP00000486701.1; ENSG00000197959.15. [Q9UQ16-3]
DR GeneID; 26052; -.
DR KEGG; hsa:26052; -.
DR MANE-Select; ENST00000627582.3; ENSP00000486701.1; NM_015569.5; NP_056384.2. [Q9UQ16-3]
DR UCSC; uc001gid.6; human. [Q9UQ16-1]
DR CTD; 26052; -.
DR DisGeNET; 26052; -.
DR GeneCards; DNM3; -.
DR HGNC; HGNC:29125; DNM3.
DR HPA; ENSG00000197959; Tissue enriched (brain).
DR MIM; 611445; gene.
DR neXtProt; NX_Q9UQ16; -.
DR OpenTargets; ENSG00000197959; -.
DR PharmGKB; PA134954683; -.
DR VEuPathDB; HostDB:ENSG00000197959; -.
DR eggNOG; KOG0446; Eukaryota.
DR GeneTree; ENSGT00940000158056; -.
DR HOGENOM; CLU_008964_5_2_1; -.
DR InParanoid; Q9UQ16; -.
DR OMA; XVLLLID; -.
DR OrthoDB; 264244at2759; -.
DR PhylomeDB; Q9UQ16; -.
DR TreeFam; TF300362; -.
DR BRENDA; 3.6.5.5; 2681.
DR PathwayCommons; Q9UQ16; -.
DR Reactome; R-HSA-166016; Toll Like Receptor 4 (TLR4) Cascade.
DR Reactome; R-HSA-177504; Retrograde neurotrophin signalling.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-437239; Recycling pathway of L1.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR SignaLink; Q9UQ16; -.
DR BioGRID-ORCS; 26052; 8 hits in 1070 CRISPR screens.
DR ChiTaRS; DNM3; human.
DR EvolutionaryTrace; Q9UQ16; -.
DR GeneWiki; DNM3; -.
DR GenomeRNAi; 26052; -.
DR Pharos; Q9UQ16; Tbio.
DR PRO; PR:Q9UQ16; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9UQ16; protein.
DR Bgee; ENSG00000197959; Expressed in lateral nuclear group of thalamus and 140 other tissues.
DR ExpressionAtlas; Q9UQ16; baseline and differential.
DR Genevisible; Q9UQ16; HS.
DR GO; GO:0061828; C:apical tubulobulbar complex; IEA:Ensembl.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0061829; C:basal tubulobulbar complex; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
DR GO; GO:0044327; C:dendritic spine head; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0098844; C:postsynaptic endocytic zone membrane; IEA:Ensembl.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0043083; C:synaptic cleft; IEA:Ensembl.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0050998; F:nitric-oxide synthase binding; IEA:Ensembl.
DR GO; GO:0099186; F:structural constituent of postsynapse; IEA:Ensembl.
DR GO; GO:0031798; F:type 1 metabotropic glutamate receptor binding; IEA:Ensembl.
DR GO; GO:0031802; F:type 5 metabotropic glutamate receptor binding; IEA:Ensembl.
DR GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
DR GO; GO:0046847; P:filopodium assembly; ISS:UniProtKB.
DR GO; GO:0061002; P:negative regulation of dendritic spine morphogenesis; IEA:Ensembl.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IEA:Ensembl.
DR GO; GO:1903423; P:positive regulation of synaptic vesicle recycling; IEA:Ensembl.
DR GO; GO:0098884; P:postsynaptic neurotransmitter receptor internalization; IEA:Ensembl.
DR GO; GO:0031623; P:receptor internalization; IBA:GO_Central.
DR GO; GO:0007416; P:synapse assembly; ISS:UniProtKB.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central.
DR CDD; cd08771; DLP_1; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR022812; Dynamin.
DR InterPro; IPR001401; Dynamin_GTPase.
DR InterPro; IPR019762; Dynamin_GTPase_CS.
DR InterPro; IPR045063; Dynamin_N.
DR InterPro; IPR000375; Dynamin_stalk.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR003130; GED.
DR InterPro; IPR020850; GED_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR11566; PTHR11566; 1.
DR Pfam; PF01031; Dynamin_M; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR Pfam; PF02212; GED; 1.
DR Pfam; PF00169; PH; 1.
DR PRINTS; PR00195; DYNAMIN.
DR SMART; SM00053; DYNc; 1.
DR SMART; SM00302; GED; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00410; G_DYNAMIN_1; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
DR PROSITE; PS51388; GED; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Endocytosis; GTP-binding; Hydrolase; Microtubule; Motor protein;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..869
FT /note="Dynamin-3"
FT /id="PRO_0000206573"
FT DOMAIN 28..294
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 515..621
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 659..750
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 38..45
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 64..66
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 136..139
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 205..208
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 235..238
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 747..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..826
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..858
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 38..46
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|Ref.7"
FT BINDING 205..211
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|Ref.7"
FT BINDING 236..239
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|Ref.7"
FT MOD_RES 231
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P39052"
FT MOD_RES 299
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P39054"
FT MOD_RES 603
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P39052"
FT MOD_RES 604
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P50570"
FT MOD_RES 769
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08877"
FT MOD_RES 773
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39052"
FT MOD_RES 853
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08877"
FT VAR_SEQ 516..525
FT /note="Missing (in isoform 2, isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:10048485,
FT ECO:0000303|PubMed:11230166, ECO:0000303|PubMed:15489334"
FT /id="VSP_034053"
FT VAR_SEQ 564..565
FT /note="EK -> NI (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054546"
FT VAR_SEQ 566..869
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054547"
FT VAR_SEQ 637
FT /note="V -> VGNNK (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11230166"
FT /id="VSP_034054"
FT CONFLICT 323
FT /note="T -> S (in Ref. 3; CAB66647)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="I -> T (in Ref. 3; CAB66647)"
FT /evidence="ECO:0000305"
FT CONFLICT 844
FT /note="S -> R (in Ref. 3; CAB66647)"
FT /evidence="ECO:0000305"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:3L43"
FT HELIX 44..52
FT /evidence="ECO:0007829|PDB:3L43"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:3L43"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:3L43"
FT HELIX 94..105
FT /evidence="ECO:0007829|PDB:3L43"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:3L43"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:3L43"
FT HELIX 152..164
FT /evidence="ECO:0007829|PDB:3L43"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:3L43"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:3L43"
FT HELIX 185..193
FT /evidence="ECO:0007829|PDB:3L43"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:3L43"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:3L43"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:3L43"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:3L43"
FT HELIX 239..243
FT /evidence="ECO:0007829|PDB:3L43"
FT HELIX 248..261
FT /evidence="ECO:0007829|PDB:3L43"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:3L43"
FT HELIX 266..271
FT /evidence="ECO:0007829|PDB:3L43"
FT HELIX 274..285
FT /evidence="ECO:0007829|PDB:3L43"
SQ SEQUENCE 869 AA; 97746 MW; 01B376CF1AE6F2FE CRC64;
MGNREMEELI PLVNRLQDAF SALGQSCLLE LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG
SGIVTRRPLV LQLVTSKAEY AEFLHCKGKK FTDFDEVRLE IEAETDRVTG MNKGISSIPI
NLRVYSPHVL NLTLIDLPGI TKVPVGDQPP DIEYQIREMI MQFITRENCL ILAVTPANTD
LANSDALKLA KEVDPQGLRT IGVITKLDLM DEGTDARDVL ENKLLPLRRG YVGVVNRSQK
DIDGKKDIKA AMLAERKFFL SHPAYRHIAD RMGTPHLQKV LNQQLTNHIR DTLPNFRNKL
QGQLLSIEHE VEAYKNFKPE DPTRKTKALL QMVQQFAVDF EKRIEGSGDQ VDTLELSGGA
KINRIFHERF PFEIVKMEFN EKELRREISY AIKNIHGIRT GLFTPDMAFE AIVKKQIVKL
KGPSLKSVDL VIQELINTVK KCTKKLANFP RLCEETERIV ANHIREREGK TKDQVLLLID
IQVSYINTNH EDFIGFANAQ QRSSQVHKKT TVGNQGTNLP PSRQIVIRKG WLTISNIGIM
KGGSKGYWFV LTAESLSWYK DDEEKEKKYM LPLDNLKVRD VEKSFMSSKH IFALFNTEQR
NVYKDYRFLE LACDSQEDVD SWKASLLRAG VYPDKSVAEN DENGQAENFS MDPQLERQVE
TIRNLVDSYM SIINKCIRDL IPKTIMHLMI NNVKDFINSE LLAQLYSSED QNTLMEESAE
QAQRRDEMLR MYQALKEALG IIGDISTATV STPAPPPVDD SWIQHSRRSP PPSPTTQRRP
TLSAPLARPT SGRGPAPAIP SPGPHSGAPP VPFRPGPLPP FPSSSDSFGA PPQVPSRPTR
APPSVPSRRP PPSPTRPTII RPLESSLLD
