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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
 
 
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