CLH1_MOUSE
ID CLH1_MOUSE Reviewed; 1675 AA.
AC Q68FD5;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Clathrin heavy chain 1;
GN Name=Cltc;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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 [3]
RP PROTEIN SEQUENCE OF 44-63; 87-96; 101-112; 145-157; 164-188; 190-205;
RP 228-245; 270-278; 298-320; 355-366; 377-382; 430-444; 446-453; 457-481;
RP 626-637; 768-780; 799-806; 838-852 AND 857-881.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-184; TYR-634; TYR-899;
RP TYR-1206; TYR-1477 AND TYR-1487, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; THR-105; SER-1167 AND
RP SER-1494, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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).
RN [6]
RP INTERACTION WITH OCRL.
RX PubMed=20133602; DOI=10.1073/pnas.0914658107;
RA Swan L.E., Tomasini L., Pirruccello M., Lunardi J., De Camilli P.;
RT "Two closely related endocytic proteins that share a common OCRL-binding
RT motif with APPL1.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:3511-3516(2010).
RN [7]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-737 AND LYS-1441, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [8]
RP INTERACTION WITH USP2.
RX PubMed=26756164; DOI=10.1371/journal.pone.0145155;
RA Pouly D., Chenaux S., Martin V., Babis M., Koch R., Nagoshi E.,
RA Katanaev V.L., Gachon F., Staub O.;
RT "USP2-45 is a circadian clock output effector regulating calcium absorption
RT at the post-translational level.";
RL PLoS ONE 11:E0145155-E0145155(2016).
CC -!- FUNCTION: Clathrin is the major protein of the polyhedral coat of
CC coated pits and vesicles. Two different adapter protein complexes link
CC the clathrin lattice either to the plasma membrane or to the trans-
CC Golgi network. Acts as component of the TACC3/ch-TOG/clathrin complex
CC proposed to contribute to stabilization of kinetochore fibers of the
CC mitotic spindle by acting as inter-microtubule bridge. The TACC3/ch-
CC TOG/clathrin complex is required for the maintenance of kinetochore
CC fiber tension. Plays a role in early autophagosome formation.
CC {ECO:0000250|UniProtKB:P11442, ECO:0000250|UniProtKB:Q00610}.
CC -!- SUBUNIT: Clathrin triskelions, composed of 3 heavy chains and 3 light
CC chains, are the basic subunits of the clathrin coat (By similarity). In
CC the presence of light chains, hub assembly is influenced by both the pH
CC and the concentration of calcium (By similarity). Interacts with HIP1
CC (By similarity). Interacts with DENND1A, DENND1B and DENND1C (By
CC similarity). Interacts with ERBB2 (By similarity). Interacts with FKBP6
CC (By similarity). Interacts with OCRL (PubMed:20133602). Interacts with
CC CKAP5 and TACC3 forming the TACC3/ch-TOG/clathrin complex located at
CC spindle inter-microtubules bridges; the complex implicates clathrin
CC triskelions; TACC3 and CLTC are proposed to form a composite
CC microtubule interaction surface (By similarity). Plays a role in early
CC autopahgosome formation (By similarity). Interacts with ATG16L1 (via N-
CC terminus) (By similarity). Interacts with RFTN1; the interaction occurs
CC in response to pathogens (By similarity). Interacts with USP2 isoform 2
CC (PubMed:26756164). {ECO:0000250|UniProtKB:P49951,
CC ECO:0000250|UniProtKB:Q00610, ECO:0000269|PubMed:20133602,
CC ECO:0000269|PubMed:26756164}.
CC -!- INTERACTION:
CC Q68FD5; Q01968: OCRL; Xeno; NbExp=2; IntAct=EBI-769168, EBI-6148898;
CC Q68FD5; Q15637: SF1; Xeno; NbExp=3; IntAct=EBI-769168, EBI-744603;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Membrane, coated pit {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Melanosome
CC {ECO:0000250}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q00610}. Note=Cytoplasmic face of coated pits
CC and vesicles. In complex with TACC3 and CKAP5 (forming the TACC3/ch-
CC TOG/clathrin complex) localized to inter-microtubule bridges in mitotic
CC spindles. {ECO:0000250, ECO:0000250|UniProtKB:Q00610}.
CC -!- DOMAIN: The N-terminal seven-bladed beta-propeller is formed by WD40-
CC like repeats, and projects inward from the polyhedral outer clathrin
CC coat. It constitutes a major protein-protein interaction node (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the clathrin heavy chain family. {ECO:0000305}.
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DR EMBL; AL592222; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC079897; AAH79897.1; -; mRNA.
DR CCDS; CCDS25204.1; -.
DR RefSeq; NP_001003908.1; NM_001003908.1.
DR PDB; 5ODS; X-ray; 3.09 A; A/B/C/D=1-574.
DR PDBsum; 5ODS; -.
DR AlphaFoldDB; Q68FD5; -.
DR SMR; Q68FD5; -.
DR BioGRID; 212086; 63.
DR CORUM; Q68FD5; -.
DR DIP; DIP-31947N; -.
DR IntAct; Q68FD5; 28.
DR MINT; Q68FD5; -.
DR STRING; 10090.ENSMUSP00000099475; -.
DR iPTMnet; Q68FD5; -.
DR PhosphoSitePlus; Q68FD5; -.
DR SwissPalm; Q68FD5; -.
DR EPD; Q68FD5; -.
DR jPOST; Q68FD5; -.
DR MaxQB; Q68FD5; -.
DR PaxDb; Q68FD5; -.
DR PRIDE; Q68FD5; -.
DR ProteomicsDB; 283383; -.
DR Antibodypedia; 4164; 488 antibodies from 40 providers.
DR DNASU; 67300; -.
DR Ensembl; ENSMUST00000103186; ENSMUSP00000099475; ENSMUSG00000047126.
DR GeneID; 67300; -.
DR KEGG; mmu:67300; -.
DR UCSC; uc007kta.1; mouse.
DR CTD; 1213; -.
DR MGI; MGI:2388633; Cltc.
DR VEuPathDB; HostDB:ENSMUSG00000047126; -.
DR eggNOG; KOG0985; Eukaryota.
DR GeneTree; ENSGT00950000183166; -.
DR HOGENOM; CLU_002136_0_0_1; -.
DR InParanoid; Q68FD5; -.
DR OMA; QVNEACV; -.
DR OrthoDB; 17940at2759; -.
DR TreeFam; TF300059; -.
DR Reactome; R-MMU-177504; Retrograde neurotrophin signalling.
DR Reactome; R-MMU-190873; Gap junction degradation.
DR Reactome; R-MMU-196025; Formation of annular gap junctions.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-MMU-437239; Recycling pathway of L1.
DR Reactome; R-MMU-5099900; WNT5A-dependent internalization of FZD4.
DR Reactome; R-MMU-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-MMU-8866427; VLDLR internalisation and degradation.
DR Reactome; R-MMU-8964038; LDL clearance.
DR Reactome; R-MMU-9013420; RHOU GTPase cycle.
DR Reactome; R-MMU-9013424; RHOV GTPase cycle.
DR BioGRID-ORCS; 67300; 28 hits in 80 CRISPR screens.
DR ChiTaRS; Cltc; mouse.
DR PRO; PR:Q68FD5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q68FD5; protein.
DR Bgee; ENSMUSG00000047126; Expressed in stroma of bone marrow and 248 other tissues.
DR ExpressionAtlas; Q68FD5; baseline and differential.
DR Genevisible; Q68FD5; MM.
DR GO; GO:0030118; C:clathrin coat; ISO:MGI.
DR GO; GO:0030132; C:clathrin coat of coated pit; IEA:InterPro.
DR GO; GO:0030130; C:clathrin coat of trans-Golgi network vesicle; IEA:InterPro.
DR GO; GO:0071439; C:clathrin complex; ISO:MGI.
DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; IBA:GO_Central.
DR GO; GO:0005905; C:clathrin-coated pit; IDA:MGI.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0098850; C:extrinsic component of synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IMP:ParkinsonsUK-UCL.
DR GO; GO:0030117; C:membrane coat; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:1990498; C:mitotic spindle microtubule; ISO:MGI.
DR GO; GO:0031523; C:Myb complex; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0098684; C:photoreceptor ribbon synapse; IDA:SynGO.
DR GO; GO:0098835; C:presynaptic endocytic zone membrane; IDA:SynGO.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0042383; C:sarcolemma; ISO:MGI.
DR GO; GO:0005819; C:spindle; ISO:MGI.
DR GO; GO:0030315; C:T-tubule; ISO:MGI.
DR GO; GO:0030506; F:ankyrin binding; ISO:MGI.
DR GO; GO:0032051; F:clathrin light chain binding; ISO:MGI.
DR GO; GO:0097718; F:disordered domain specific binding; ISO:MGI.
DR GO; GO:0003725; F:double-stranded RNA binding; ISO:MGI.
DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; ISO:MGI.
DR GO; GO:0042277; F:peptide binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:1990381; F:ubiquitin-specific protease binding; ISO:MGI.
DR GO; GO:0150093; P:amyloid-beta clearance by transcytosis; ISO:MGI.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0048268; P:clathrin coat assembly; ISO:MGI.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; ISO:MGI.
DR GO; GO:0007030; P:Golgi organization; ISO:MGI.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0000278; P:mitotic cell cycle; ISO:MGI.
DR GO; GO:0090307; P:mitotic spindle assembly; ISO:MGI.
DR GO; GO:1900126; P:negative regulation of hyaluronan biosynthetic process; ISS:UniProtKB.
DR GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0031623; P:receptor internalization; ISO:MGI.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISO:MGI.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; ISO:MGI.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISO:MGI.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; ISO:MGI.
DR GO; GO:0033572; P:transferrin transport; ISO:MGI.
DR Gene3D; 1.25.40.10; -; 4.
DR Gene3D; 2.130.10.110; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR InterPro; IPR015348; Clathrin_H-chain_linker_core.
DR InterPro; IPR016025; Clathrin_H-chain_N.
DR InterPro; IPR022365; Clathrin_H-chain_propeller_rpt.
DR InterPro; IPR016341; Clathrin_heavy_chain.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR Pfam; PF00637; Clathrin; 7.
DR Pfam; PF09268; Clathrin-link; 1.
DR Pfam; PF01394; Clathrin_propel; 5.
DR PIRSF; PIRSF002290; Clathrin_H_chain; 1.
DR SMART; SM00299; CLH; 7.
DR SUPFAM; SSF48371; SSF48371; 6.
DR SUPFAM; SSF50989; SSF50989; 1.
DR PROSITE; PS50236; CHCR; 7.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Autophagy; Cell cycle; Cell division;
KW Coated pit; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Direct protein sequencing; Membrane; Mitosis; Phosphoprotein;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q00610"
FT CHAIN 2..1675
FT /note="Clathrin heavy chain 1"
FT /id="PRO_0000205779"
FT REPEAT 537..683
FT /note="CHCR 1"
FT REPEAT 686..828
FT /note="CHCR 2"
FT REPEAT 833..972
FT /note="CHCR 3"
FT REPEAT 979..1124
FT /note="CHCR 4"
FT REPEAT 1128..1269
FT /note="CHCR 5"
FT REPEAT 1274..1420
FT /note="CHCR 6"
FT REPEAT 1423..1566
FT /note="CHCR 7"
FT REGION 2..479
FT /note="Globular terminal domain"
FT REGION 24..67
FT /note="WD40-like repeat 1"
FT REGION 68..107
FT /note="WD40-like repeat 2"
FT REGION 108..149
FT /note="WD40-like repeat 3"
FT REGION 150..195
FT /note="WD40-like repeat 4"
FT REGION 196..257
FT /note="WD40-like repeat 5"
FT REGION 258..301
FT /note="WD40-like repeat 6"
FT REGION 302..330
FT /note="WD40-like repeat 7"
FT REGION 449..465
FT /note="Binding site for the uncoating ATPase, involved in
FT lattice disassembly"
FT /evidence="ECO:0000255"
FT REGION 480..523
FT /note="Flexible linker"
FT REGION 524..1675
FT /note="Heavy chain arm"
FT REGION 524..634
FT /note="Distal segment"
FT REGION 639..1675
FT /note="Proximal segment"
FT REGION 1213..1522
FT /note="Involved in binding clathrin light chain"
FT /evidence="ECO:0000250"
FT REGION 1550..1675
FT /note="Trimerization"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q00610"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 105
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 184
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 394
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q00610"
FT MOD_RES 634
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 737
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 856
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q00610"
FT MOD_RES 899
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 1167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1206
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 1229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00610"
FT MOD_RES 1441
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00610"
FT MOD_RES 1441
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1477
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 1487
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 1494
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1501
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q00610"
FT STRAND 6..14
FT /evidence="ECO:0007829|PDB:5ODS"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:5ODS"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:5ODS"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:5ODS"
FT STRAND 33..44
FT /evidence="ECO:0007829|PDB:5ODS"
FT STRAND 47..57
FT /evidence="ECO:0007829|PDB:5ODS"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:5ODS"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:5ODS"
FT STRAND 75..84
FT /evidence="ECO:0007829|PDB:5ODS"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:5ODS"
FT TURN 93..96
FT /evidence="ECO:0007829|PDB:5ODS"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:5ODS"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:5ODS"
FT STRAND 118..133
FT /evidence="ECO:0007829|PDB:5ODS"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:5ODS"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:5ODS"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:5ODS"
FT STRAND 164..172
FT /evidence="ECO:0007829|PDB:5ODS"
FT STRAND 174..185
FT /evidence="ECO:0007829|PDB:5ODS"
FT TURN 186..189
FT /evidence="ECO:0007829|PDB:5ODS"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:5ODS"
FT STRAND 197..204
FT /evidence="ECO:0007829|PDB:5ODS"
FT STRAND 213..222
FT /evidence="ECO:0007829|PDB:5ODS"
FT STRAND 225..232
FT /evidence="ECO:0007829|PDB:5ODS"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:5ODS"
FT STRAND 261..267
FT /evidence="ECO:0007829|PDB:5ODS"
FT TURN 268..271
FT /evidence="ECO:0007829|PDB:5ODS"
FT STRAND 272..277
FT /evidence="ECO:0007829|PDB:5ODS"
FT STRAND 280..286
FT /evidence="ECO:0007829|PDB:5ODS"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:5ODS"
FT STRAND 292..297
FT /evidence="ECO:0007829|PDB:5ODS"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:5ODS"
FT TURN 310..313
FT /evidence="ECO:0007829|PDB:5ODS"
FT STRAND 314..318
FT /evidence="ECO:0007829|PDB:5ODS"
FT STRAND 322..329
FT /evidence="ECO:0007829|PDB:5ODS"
FT TURN 331..333
FT /evidence="ECO:0007829|PDB:5ODS"
FT HELIX 334..340
FT /evidence="ECO:0007829|PDB:5ODS"
FT HELIX 345..354
FT /evidence="ECO:0007829|PDB:5ODS"
FT HELIX 361..373
FT /evidence="ECO:0007829|PDB:5ODS"
FT HELIX 377..385
FT /evidence="ECO:0007829|PDB:5ODS"
FT HELIX 395..402
FT /evidence="ECO:0007829|PDB:5ODS"
FT STRAND 408..410
FT /evidence="ECO:0007829|PDB:5ODS"
FT HELIX 413..424
FT /evidence="ECO:0007829|PDB:5ODS"
FT HELIX 429..441
FT /evidence="ECO:0007829|PDB:5ODS"
FT HELIX 446..453
FT /evidence="ECO:0007829|PDB:5ODS"
FT HELIX 461..468
FT /evidence="ECO:0007829|PDB:5ODS"
FT HELIX 472..481
FT /evidence="ECO:0007829|PDB:5ODS"
FT HELIX 485..494
FT /evidence="ECO:0007829|PDB:5ODS"
FT HELIX 498..508
FT /evidence="ECO:0007829|PDB:5ODS"
FT HELIX 514..524
FT /evidence="ECO:0007829|PDB:5ODS"
FT HELIX 526..536
FT /evidence="ECO:0007829|PDB:5ODS"
FT STRAND 539..541
FT /evidence="ECO:0007829|PDB:5ODS"
FT HELIX 546..555
FT /evidence="ECO:0007829|PDB:5ODS"
FT HELIX 559..573
FT /evidence="ECO:0007829|PDB:5ODS"
SQ SEQUENCE 1675 AA; 191557 MW; 6C41EBD89EB7D56B CRC64;
MAQILPIRFQ EHLQLQNLGI NPANIGFSTL TMESDKFICI REKVGEQAQV VIIDMNDPSN
PIRRPISADS AIMNPASKVI ALKAGKTLQI FNIEMKSKMK AHTMTDDVTF WKWISLNTVA
LVTDNAVYHW SMEGESQPVK MFDRHSSLAG CQIINYRTDA KQKWLLLTGI SAQQNRVVGA
MQLYSVDRKV SQPIEGHAAS FAQFKMEGNA EESTLFCFAV RGQAGGKLHI IEVGTPPTGN
QPFPKKAVDV FFPPEAQNDF PVAMQISEKH DVVFLITKYG YIHLYDLETG TCIYMNRISG
ETIFVTAPHE ATAGIIGVNR KGQVLSVCVE EENIIPYITN VLQNPDLALR MAVRNNLAGA
EELFARKFNA LFAQGNYSEA AKVAANAPKG ILRTPDTIRR FQSVPAQPGQ TSPLLQYFGI
LLDQGQLNKY ESLELCRPVL QQGRKQLLEK WLKEDKLECS EELGDLVKSV DPTLALSVYL
RANVPNKVIQ CFAETGQVQK IVLYAKKVGY TPDWIFLLRN VMRISPDQGQ QFAQMLVQDE
EPLADITQIV DVFMEYNLIQ QCTAFLLDAL KNNRPSEGPL QTRLLEMNLM HAPQVADAIL
GNQMFTHYDR AHIAQLCEKA GLLQRALEHF TDLYDIKRAV VHTHLLNPEW LVNYFGSLSV
EDSLECLRAM LSANIRQNLQ ICVQVASKYH EQLSTQSLIE LFESFKSFEG LFYFLGSIVN
FSQDPDVHFK YIQAACKTGQ IKEVERICRE SNCYDPERVK NFLKEAKLTD QLPLIIVCDR
FDFVHDLVLY LYRNNLQKYI EIYVQKVNPS RLPVVIGGLL DVDCSEDVIK NLILVVRGQF
STDELVAEVE KRNRLKLLLP WLEARIHEGC EEPATHNALA KIYIDSNNNP ERFLRENPYY
DSRVVGKYCE KRDPHLACVA YERGQCDLEL INVCNENSLF KSLSRYLVRR KDPELWGSVL
LESNPYRRPL IDQVVQTALS ETQDPEEVSV TVKAFMTADL PNELIELLEK IVLDNSVFSE
HRNLQNLLIL TAIKADRTRV MEYINRLDNY DAPDIANIAI SNELFEEAFA IFRKFDVNTS
AVQVLIEHIG NLDRAYEFAE RCNEPAVWSQ LAKAQLQKGM VKEAIDSYIK ADDPSSYMEV
VQAANASGNW EELVKYLQMA RKKARESYVE TELIFALAKT NRLAELEEFI NGPNNAHIQQ
VGDRCYDEKM YDAAKLLYNN VSNFGRLAST LVHLGEYQAA VDGARKANST RTWKEVCFAC
VDGKEFRLAQ MCGLHIVVHA DELEELINYY QDRGYFEELI TMLEAALGLE RAHMGMFTEL
AILYSKFKPQ KMREHLELFW SRVNIPKVLR AAEQAHLWAE LVFLYDKYEE YDNAIITMMN
HPTDAWKEGQ FKDIITKVAN VELYYKAIQF YLEFKPLLLN DLLMVLSPRL DHTRAVNYFS
KVKQLPLVKP YLRSVQNHNN KSVNESLNNL FITEEDYQAL RTSIDAYDNF DNISLAQRLE
KHELIEFRRI AAYLFKGNNR WKQSVELCKK DSLYKDAMQY ASESKDTELA EELLQWFLQE
EKRECFGACL FTCYDLLRPD VVLETAWRHN IMDFAMPYFI QVMKEYLTKV DKLDASESLR
KEEEQATETQ PIVYGQPQLM LTAGPSVAVP PQAPFGYGYT APPYGQPQPG FGYSM
