ID CLH1_BOVIN Reviewed; 1675 AA. AC P49951; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 169. DE RecName: Full=Clathrin heavy chain 1 {ECO:0000250|UniProtKB:Q00610}; GN Name=CLTC {ECO:0000250|UniProtKB:Q00610}; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Kidney; RX PubMed=7585943; DOI=10.1016/0092-8674(95)90167-1; RA Liu S.-H., Wong M.L., Craik C.S., Brodsky F.M.; RT "Regulation of clathrin assembly and trimerization defined using RT recombinant triskelion hubs."; RL Cell 83:257-267(1995). RN [2] RP FUNCTION, AND INTERACTION WITH DNAJC6. RX PubMed=8524399; DOI=10.1038/378632a0; RA Ungewickell E., Ungewickell H., Holstein S.E., Lindner R., Prasad K., RA Barouch W., Martin B., Greene L.E., Eisenberg E.; RT "Role of auxilin in uncoating clathrin-coated vesicles."; RL Nature 378:632-635(1995). RN [3] RP FUNCTION, AND INTERACTION WITH DNAJC6. RX PubMed=11470803; DOI=10.1074/jbc.m106511200; RA Scheele U., Kalthoff C., Ungewickell E.; RT "Multiple interactions of auxilin 1 with clathrin and the AP-2 adaptor RT complex."; RL J. Biol. Chem. 276:36131-36138(2001). RN [4] RP INTERACTION WITH DENND1A; DENND1B AND DENND1C. RX PubMed=20154091; DOI=10.1074/jbc.m109.050930; RA Marat A.L., McPherson P.S.; RT "The connecdenn family, Rab35 guanine nucleotide exchange factors RT interfacing with the clathrin machinery."; RL J. Biol. Chem. 285:10627-10637(2010). RN [5] {ECO:0007744|PDB:1XI5} RP STRUCTURE BY ELECTRON MICROSCOPY (12.00 ANGSTROMS) OF 1-1630 IN COMPLEX RP WITH DNAJC6, AND FUNCTION. RX PubMed=15502813; DOI=10.1038/nature03078; RA Fotin A., Cheng Y., Grigorieff N., Walz T., Harrison S.C., Kirchhausen T.; RT "Structure of an auxilin-bound clathrin coat and its implications for the RT mechanism of uncoating."; RL Nature 432:649-653(2004). 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 a 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 Interaction with DNAJC6 mediates the recruitment of HSPA8 to the CC clathrin lattice and creates local destabilization of the lattice CC promoting uncoating (PubMed:8524399, PubMed:15502813, PubMed:11470803). CC {ECO:0000250|UniProtKB:P11442, ECO:0000250|UniProtKB:Q00610, CC ECO:0000269|PubMed:11470803, ECO:0000269|PubMed:15502813, CC ECO:0000269|PubMed:8524399}. CC -!- SUBUNIT: Clathrin triskelions, composed of 3 heavy chains and 3 light CC chains, are the basic subunits of the clathrin coat. In the presence of CC light chains, hub assembly is influenced by both the pH and the CC concentration of calcium. Interacts with HIP1. Interacts with DENND1A, CC DENND1B and DENND1C. Interacts with OCRL. Interacts with ERBB2. CC Interacts with FKBP6 (By similarity). Interacts with CKAP5 and TACC3 CC forming the TACC3/ch-TOG/clathrin complex located at spindle inter- CC microtubules bridges; the complex implicates clathrin triskelions; CC TACC3 and CLTC are proposed to form a composite microtubule interaction CC surface (By similarity). Interacts with ATG16L1 (via N-terminus). CC Interacts with RFTN1; the interaction occurs in response to pathogens CC (By similarity). Interacts with TMEM106B (via N-terminus) (By CC similarity). Interacts with DNAJC6; this interaction produces a local CC change in heavy-chain contacts, creating a detectable global distortion CC of the clathrin coat and leads to the recruitment of HSPA8 CC (PubMed:15502813, PubMed:11470803, PubMed:8524399). CC {ECO:0000250|UniProtKB:Q00610, ECO:0000250|UniProtKB:Q68FD5, CC ECO:0000269|PubMed:11470803, ECO:0000269|PubMed:15502813, CC ECO:0000269|PubMed:8524399}. CC -!- INTERACTION: CC P49951; P49951: CLTC; NbExp=2; IntAct=EBI-448355, EBI-448355; CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Peripheral membrane CC protein; Cytoplasmic side. Membrane, coated pit; Peripheral membrane CC protein; Cytoplasmic side. Melanosome {ECO:0000250}. Cytoplasm, CC cytoskeleton, spindle {ECO:0000250|UniProtKB:Q00610}. Note=Cytoplasmic CC face of coated pits and vesicles. In complex with TACC3 and CKAP5 CC (forming the TACC3/ch-TOG/clathrin complex) localized to inter- CC microtubule bridges in mitotic spindles. CC {ECO:0000250|UniProtKB:Q00610}. CC -!- DOMAIN: The C-terminal third of the heavy chains forms the hub of the CC triskelion. This region contains the trimerization domain and the CC light-chain binding domain involved in the assembly of the clathrin CC lattice. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U31757; AAC48524.1; -; mRNA. DR RefSeq; NP_776448.1; NM_174023.2. DR PDB; 1B89; X-ray; 2.60 A; A=1074-1522. DR PDB; 1UTC; X-ray; 2.30 A; A/B=1-363. DR PDB; 1XI4; EM; 7.90 A; A/B/C/D/E/F/G/H/I=1-1630. DR PDB; 1XI5; EM; 12.00 A; A/B/C/D/E/F/G/H/I=1-1630. DR PDB; 3GC3; X-ray; 2.20 A; B=1-363. DR PDB; 3GD1; X-ray; 3.50 A; I=1-363. DR PDB; 3IYV; EM; 7.90 A; A/B/C/D/E/F/G/H/I=1-1630. DR PDB; 3LVG; X-ray; 7.94 A; A/B/C=1074-1675. DR PDB; 3LVH; X-ray; 9.00 A; A/B/C=1074-1675. DR PDB; 3QIL; X-ray; 3.92 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1521-1624. DR PDB; 5M5R; X-ray; 1.76 A; A=1-363. DR PDB; 5M5S; X-ray; 1.88 A; A/B=1-363. DR PDB; 5M5T; X-ray; 1.70 A; A/B=1-363. DR PDB; 5M5U; X-ray; 2.15 A; A/B=1-363. DR PDB; 5M5V; X-ray; 1.96 A; A/B=1-363. DR PDB; 5M61; X-ray; 1.84 A; A/B=1-363. DR PDB; 6WCJ; EM; 6.30 A; A/C/D/G/H/I/K/L/M=1-1675. DR PDBsum; 1B89; -. DR PDBsum; 1UTC; -. DR PDBsum; 1XI4; -. DR PDBsum; 1XI5; -. DR PDBsum; 3GC3; -. DR PDBsum; 3GD1; -. DR PDBsum; 3IYV; -. DR PDBsum; 3LVG; -. DR PDBsum; 3LVH; -. DR PDBsum; 3QIL; -. DR PDBsum; 5M5R; -. DR PDBsum; 5M5S; -. DR PDBsum; 5M5T; -. DR PDBsum; 5M5U; -. DR PDBsum; 5M5V; -. DR PDBsum; 5M61; -. DR PDBsum; 6WCJ; -. DR AlphaFoldDB; P49951; -. DR EMDB; EMD-21608; -. DR EMDB; EMD-21611; -. DR SMR; P49951; -. DR BioGRID; 158448; 4. DR DIP; DIP-31603N; -. DR IntAct; P49951; 8. DR MINT; P49951; -. DR STRING; 9913.ENSBTAP00000060092; -. DR PaxDb; 9913-ENSBTAP00000022210; -. DR PeptideAtlas; P49951; -. DR Ensembl; ENSBTAT00000077192.1; ENSBTAP00000060092.1; ENSBTAG00000016708.6. DR GeneID; 281080; -. DR KEGG; bta:281080; -. DR CTD; 1213; -. DR VEuPathDB; HostDB:ENSBTAG00000016708; -. DR VGNC; VGNC:27471; CLTC. DR eggNOG; KOG0985; Eukaryota. DR GeneTree; ENSGT00950000183166; -. DR InParanoid; P49951; -. DR OMA; XLECSEE; -. DR OrthoDB; 5474327at2759; -. DR Reactome; R-BTA-177504; Retrograde neurotrophin signalling. DR Reactome; R-BTA-190873; Gap junction degradation. DR Reactome; R-BTA-196025; Formation of annular gap junctions. DR Reactome; R-BTA-2132295; MHC class II antigen presentation. DR Reactome; R-BTA-432720; Lysosome Vesicle Biogenesis. DR Reactome; R-BTA-432722; Golgi Associated Vesicle Biogenesis. DR Reactome; R-BTA-437239; Recycling pathway of L1. DR Reactome; R-BTA-5099900; WNT5A-dependent internalization of FZD4. DR Reactome; R-BTA-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2. DR Reactome; R-BTA-8856825; Cargo recognition for clathrin-mediated endocytosis. DR Reactome; R-BTA-8856828; Clathrin-mediated endocytosis. DR Reactome; R-BTA-8866427; VLDLR internalisation and degradation. DR Reactome; R-BTA-8964038; LDL clearance. DR Reactome; R-BTA-9013420; RHOU GTPase cycle. DR Reactome; R-BTA-9013424; RHOV GTPase cycle. DR EvolutionaryTrace; P49951; -. DR Proteomes; UP000009136; Chromosome 19. DR Bgee; ENSBTAG00000016708; Expressed in prefrontal cortex and 109 other cell types or tissues. DR ExpressionAtlas; P49951; baseline and differential. 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; IBA:GO_Central. DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; IBA:GO_Central. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0030117; C:membrane coat; ISS:AgBase. DR GO; GO:0005739; C:mitochondrion; ISS:AgBase. DR GO; GO:0005819; C:spindle; IBA:GO_Central. DR GO; GO:1990763; F:arrestin family protein binding; IPI:CAFA. DR GO; GO:0032051; F:clathrin light chain binding; IBA:GO_Central. DR GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. 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; IMP:CAFA. DR GO; GO:0072318; P:clathrin coat disassembly; IDA:UniProtKB. DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro. DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central. DR GO; GO:1900126; P:negative regulation of hyaluronan biosynthetic process; ISS:UniProtKB. DR GO; GO:0006898; P:receptor-mediated endocytosis; IBA:GO_Central. DR Gene3D; 1.25.40.730; -; 1. DR Gene3D; 2.130.10.110; Clathrin heavy-chain terminal domain; 1. DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 4. 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 PANTHER; PTHR10292:SF7; CLATHRIN HEAVY CHAIN 1; 1. DR PANTHER; PTHR10292; CLATHRIN HEAVY CHAIN RELATED; 1. DR Pfam; PF00637; Clathrin; 7. DR Pfam; PF09268; Clathrin-link; 1. DR Pfam; PF13838; Clathrin_H_link; 1. DR Pfam; PF01394; Clathrin_propel; 5. DR PIRSF; PIRSF002290; Clathrin_H_chain; 1. DR SMART; SM00299; CLH; 7. DR SUPFAM; SSF48371; ARM repeat; 6. DR SUPFAM; SSF50989; Clathrin heavy-chain terminal domain; 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; Membrane; KW Mitosis; Phosphoprotein; 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_0000205777" 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 REGION 1550..1675 FT /note="Trimerization" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:Q00610" FT MOD_RES 67 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q00610" FT MOD_RES 105 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q68FD5" FT MOD_RES 184 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q68FD5" FT MOD_RES 394 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q00610" FT MOD_RES 634 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q00610" FT MOD_RES 737 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q68FD5" FT MOD_RES 856 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q00610" FT MOD_RES 899 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q68FD5" FT MOD_RES 1167 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q68FD5" FT MOD_RES 1206 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q68FD5" 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:0000250|UniProtKB:Q68FD5" FT MOD_RES 1477 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q00610" FT MOD_RES 1487 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q68FD5" FT MOD_RES 1494 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q00610" FT MOD_RES 1501 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q00610" FT STRAND 6..14 FT /evidence="ECO:0007829|PDB:5M5T" FT HELIX 15..18 FT /evidence="ECO:0007829|PDB:5M5T" FT HELIX 22..24 FT /evidence="ECO:0007829|PDB:5M5T" FT TURN 27..29 FT /evidence="ECO:0007829|PDB:5M5T" FT STRAND 30..34 FT /evidence="ECO:0007829|PDB:5M5T" FT STRAND 37..44 FT /evidence="ECO:0007829|PDB:5M5T" FT STRAND 47..54 FT /evidence="ECO:0007829|PDB:5M5T" FT STRAND 62..66 FT /evidence="ECO:0007829|PDB:5M5T" FT STRAND 69..73 FT /evidence="ECO:0007829|PDB:5M5T" FT STRAND 75..84 FT /evidence="ECO:0007829|PDB:5M5T" FT STRAND 87..92 FT /evidence="ECO:0007829|PDB:5M5T" FT TURN 93..96 FT /evidence="ECO:0007829|PDB:5M5T" FT STRAND 97..103 FT /evidence="ECO:0007829|PDB:5M5T" FT STRAND 108..113 FT /evidence="ECO:0007829|PDB:5M5T" FT STRAND 115..131 FT /evidence="ECO:0007829|PDB:5M5T" FT STRAND 139..143 FT /evidence="ECO:0007829|PDB:5M5T" FT HELIX 146..148 FT /evidence="ECO:0007829|PDB:5M5T" FT STRAND 152..158 FT /evidence="ECO:0007829|PDB:5M5T" FT STRAND 164..173 FT /evidence="ECO:0007829|PDB:5M5T" FT STRAND 176..185 FT /evidence="ECO:0007829|PDB:5M5T" FT TURN 186..189 FT /evidence="ECO:0007829|PDB:5M5T" FT STRAND 190..195 FT /evidence="ECO:0007829|PDB:5M5T" FT STRAND 197..204 FT /evidence="ECO:0007829|PDB:5M5T" FT STRAND 213..221 FT /evidence="ECO:0007829|PDB:5M5T" FT STRAND 226..232 FT /evidence="ECO:0007829|PDB:5M5T" FT STRAND 246..250 FT /evidence="ECO:0007829|PDB:5M5T" FT HELIX 254..256 FT /evidence="ECO:0007829|PDB:5M5T" FT STRAND 261..267 FT /evidence="ECO:0007829|PDB:5M5T" FT TURN 268..271 FT /evidence="ECO:0007829|PDB:5M5T" FT STRAND 272..277 FT /evidence="ECO:0007829|PDB:5M5T" FT STRAND 280..286 FT /evidence="ECO:0007829|PDB:5M5T" FT TURN 287..289 FT /evidence="ECO:0007829|PDB:5M5T" FT STRAND 292..297 FT /evidence="ECO:0007829|PDB:5M5T" FT STRAND 303..309 FT /evidence="ECO:0007829|PDB:5M5T" FT TURN 310..313 FT /evidence="ECO:0007829|PDB:5M5T" FT STRAND 314..319 FT /evidence="ECO:0007829|PDB:5M5T" FT STRAND 323..329 FT /evidence="ECO:0007829|PDB:5M5T" FT TURN 331..333 FT /evidence="ECO:0007829|PDB:5M5T" FT HELIX 334..340 FT /evidence="ECO:0007829|PDB:5M5T" FT HELIX 345..354 FT /evidence="ECO:0007829|PDB:5M5T" FT HELIX 1183..1186 FT /evidence="ECO:0007829|PDB:1B89" FT TURN 1187..1191 FT /evidence="ECO:0007829|PDB:1B89" FT TURN 1211..1213 FT /evidence="ECO:0007829|PDB:1B89" FT HELIX 1214..1220 FT /evidence="ECO:0007829|PDB:1B89" FT HELIX 1224..1232 FT /evidence="ECO:0007829|PDB:1B89" FT TURN 1233..1235 FT /evidence="ECO:0007829|PDB:1B89" FT HELIX 1237..1247 FT /evidence="ECO:0007829|PDB:1B89" FT HELIX 1250..1262 FT /evidence="ECO:0007829|PDB:1B89" FT HELIX 1266..1271 FT /evidence="ECO:0007829|PDB:1B89" FT TURN 1272..1278 FT /evidence="ECO:0007829|PDB:1B89" FT HELIX 1280..1292 FT /evidence="ECO:0007829|PDB:1B89" FT HELIX 1296..1306 FT /evidence="ECO:0007829|PDB:1B89" FT HELIX 1314..1325 FT /evidence="ECO:0007829|PDB:1B89" FT HELIX 1329..1339 FT /evidence="ECO:0007829|PDB:1B89" FT HELIX 1345..1353 FT /evidence="ECO:0007829|PDB:1B89" FT TURN 1354..1356 FT /evidence="ECO:0007829|PDB:1B89" FT HELIX 1358..1367 FT /evidence="ECO:0007829|PDB:1B89" FT HELIX 1371..1380 FT /evidence="ECO:0007829|PDB:1B89" FT TURN 1382..1385 FT /evidence="ECO:0007829|PDB:1B89" FT HELIX 1388..1397 FT /evidence="ECO:0007829|PDB:1B89" FT HELIX 1402..1414 FT /evidence="ECO:0007829|PDB:1B89" FT HELIX 1416..1418 FT /evidence="ECO:0007829|PDB:1B89" FT HELIX 1419..1426 FT /evidence="ECO:0007829|PDB:1B89" FT HELIX 1427..1429 FT /evidence="ECO:0007829|PDB:1B89" FT HELIX 1432..1441 FT /evidence="ECO:0007829|PDB:1B89" FT TURN 1445..1448 FT /evidence="ECO:0007829|PDB:1B89" FT HELIX 1449..1456 FT /evidence="ECO:0007829|PDB:1B89" FT HELIX 1461..1473 FT /evidence="ECO:0007829|PDB:1B89" FT HELIX 1477..1486 FT /evidence="ECO:0007829|PDB:1B89" FT HELIX 1492..1499 FT /evidence="ECO:0007829|PDB:1B89" FT HELIX 1505..1515 FT /evidence="ECO:0007829|PDB:1B89" SQ SEQUENCE 1675 AA; 191589 MW; 6C4F2D54801579E2 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 VQAANTSGNW 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 VELYYRAIQF 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 APAYGQPQPG FGYSM //