ID CLH1_RAT Reviewed; 1675 AA. AC P11442; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 188. DE RecName: Full=Clathrin heavy chain 1 {ECO:0000250|UniProtKB:Q00610}; GN Name=Cltc {ECO:0000312|RGD:2364}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3480512; DOI=10.1073/pnas.84.24.8805; RA Kirchhausen T., Harrison S.C., Chow E.P., Mattaliano R.J., RA Ramachandran K.L., Smart J., Brosius J.; RT "Clathrin heavy chain: molecular cloning and complete primary structure."; RL Proc. Natl. Acad. Sci. U.S.A. 84:8805-8809(1987). RN [2] RP PROTEIN SEQUENCE OF 2-8; 87-96; 177-205; 270-278; 355-382; 838-851; RP 882-892; 896-903; 1011-1034; 1095-1101; 1123-1130; 1216-1226; 1398-1406; RP 1435-1441; 1444-1453; 1502-1508; 1536-1545 AND 1610-1620, CLEAVAGE OF RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Pheochromocytoma; RA Bienvenut W.V., von Kriegsheim A.F., Kolch W.; RL Submitted (AUG-2006) to UniProtKB. RN [3] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=15858577; DOI=10.1038/nature03502; RA Royle S.J., Bright N.A., Lagnado L.; RT "Clathrin is required for the function of the mitotic spindle."; RL Nature 434:1152-1157(2005). RN [4] RP FUNCTION, AND SUBUNIT. RX PubMed=16968737; DOI=10.1242/jcs.03192; RA Royle S.J., Lagnado L.; RT "Trimerisation is important for the function of clathrin at the mitotic RT spindle."; RL J. Cell Sci. 119:4071-4078(2006). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-105; THR-394 AND SER-1494, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-493, AND WD40-LIKE REPEATS. RX PubMed=9827808; DOI=10.1016/s0092-8674(00)81623-2; RA Ter Haar E., Musacchio A., Harrison S.C., Kirchhausen T.; RT "Atomic structure of clathrin: a beta propeller terminal domain joins an RT alpha zigzag linker."; RL Cell 95:563-573(1998). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-359, AND WD40-LIKE REPEATS. RX PubMed=10655490; DOI=10.1073/pnas.97.3.1096; RA ter Haar E., Harrison S.C., Kirchhausen T.; RT "Peptide-in-groove interactions link target proteins to the beta-propeller RT of clathrin."; RL Proc. Natl. Acad. Sci. U.S.A. 97:1096-1100(2000). 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 (By similarity). Acts as a component of the TACC3/ch- CC TOG/clathrin complex proposed to contribute to stabilization of CC kinetochore fibers of the mitotic spindle by acting as inter- CC microtubule bridge (PubMed:15858577, PubMed:16968737). The TACC3/ch- CC TOG/clathrin complex is required for the maintenance of kinetochore CC fiber tension (By similarity). Plays a role in early autophagosome CC formation (By similarity). Interaction with DNAJC6 mediates the CC recruitment of HSPA8 to the clathrin lattice and creates local CC destabilization of the lattice promoting uncoating (By similarity). CC {ECO:0000250|UniProtKB:P49951, ECO:0000250|UniProtKB:Q00610, CC ECO:0000269|PubMed:15858577, ECO:0000269|PubMed:16968737}. CC -!- SUBUNIT: Clathrin triskelions, composed of 3 heavy chains and 3 light CC chains, are the basic subunits of the clathrin coat (PubMed:16968737). CC In the presence of light chains, hub assembly is influenced by both the CC pH and the concentration of calcium (By similarity). Interacts with CC HIP1 (By similarity). Interacts with DENND1A, DENND1B and DENND1C (By CC similarity). Interacts with OCRL (By similarity). Interacts with ERBB2 CC (By similarity). Interacts with FKBP6 (By similarity). 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). Interacts with ATG16L1 CC (via N-terminus) (By similarity). Interacts with RFTN1; the interaction CC occurs in response to pathogens (By similarity). Interacts with USP2 CC isoform 2 (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 (By CC similarity). {ECO:0000250|UniProtKB:P49951, CC ECO:0000250|UniProtKB:Q00610, ECO:0000250|UniProtKB:Q68FD5, CC ECO:0000269|PubMed:16968737}. CC -!- INTERACTION: CC P11442; Q01968: OCRL; Xeno; NbExp=5; IntAct=EBI-397997, EBI-6148898; 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:0000269|PubMed:15858577}. 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 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. 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; J03583; AAA40874.1; -; mRNA. DR PIR; A39941; LRRTH. DR RefSeq; NP_062172.1; NM_019299.1. DR PDB; 1BPO; X-ray; 2.60 A; A/B/C=1-494. DR PDB; 1C9I; X-ray; 2.90 A; A/B=1-359. DR PDB; 1C9L; X-ray; 2.90 A; A/B=3-359. DR PDBsum; 1BPO; -. DR PDBsum; 1C9I; -. DR PDBsum; 1C9L; -. DR AlphaFoldDB; P11442; -. DR EMDB; EMD-3442; -. DR SMR; P11442; -. DR BioGRID; 248464; 22. DR CORUM; P11442; -. DR DIP; DIP-36966N; -. DR IntAct; P11442; 9. DR MINT; P11442; -. DR STRING; 10116.ENSRNOP00000005987; -. DR GlyGen; P11442; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P11442; -. DR PhosphoSitePlus; P11442; -. DR SwissPalm; P11442; -. DR jPOST; P11442; -. DR PaxDb; 10116-ENSRNOP00000005987; -. DR GeneID; 54241; -. DR KEGG; rno:54241; -. DR AGR; RGD:2364; -. DR CTD; 1213; -. DR RGD; 2364; Cltc. DR eggNOG; KOG0985; Eukaryota. DR InParanoid; P11442; -. DR OrthoDB; 5474327at2759; -. DR PhylomeDB; P11442; -. DR Reactome; R-RNO-177504; Retrograde neurotrophin signalling. DR Reactome; R-RNO-190873; Gap junction degradation. DR Reactome; R-RNO-196025; Formation of annular gap junctions. DR Reactome; R-RNO-2132295; MHC class II antigen presentation. DR Reactome; R-RNO-432720; Lysosome Vesicle Biogenesis. DR Reactome; R-RNO-432722; Golgi Associated Vesicle Biogenesis. DR Reactome; R-RNO-437239; Recycling pathway of L1. DR Reactome; R-RNO-5099900; WNT5A-dependent internalization of FZD4. DR Reactome; R-RNO-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2. DR Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis. DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis. DR Reactome; R-RNO-8866427; VLDLR internalisation and degradation. DR Reactome; R-RNO-8964038; LDL clearance. DR Reactome; R-RNO-9013420; RHOU GTPase cycle. DR Reactome; R-RNO-9013424; RHOV GTPase cycle. DR EvolutionaryTrace; P11442; -. DR PRO; PR:P11442; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0030118; C:clathrin coat; IDA:RGD. 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:RGD. DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; IBA:GO_Central. DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0005905; C:clathrin-coated pit; ISO:RGD. DR GO; GO:0030136; C:clathrin-coated vesicle; ISO:RGD. DR GO; GO:0005829; C:cytosol; IEA:GOC. DR GO; GO:0098850; C:extrinsic component of synaptic vesicle membrane; IDA:SynGO. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; ISO:RGD. DR GO; GO:0030117; C:membrane coat; ISO:RGD. DR GO; GO:1990498; C:mitotic spindle microtubule; ISO:RGD. DR GO; GO:0031523; C:Myb complex; ISO:RGD. DR GO; GO:0098684; C:photoreceptor ribbon synapse; ISO:RGD. DR GO; GO:0098835; C:presynaptic endocytic zone membrane; ISO:RGD. DR GO; GO:0032991; C:protein-containing complex; ISO:RGD. DR GO; GO:0042383; C:sarcolemma; IDA:RGD. DR GO; GO:0005819; C:spindle; IDA:UniProtKB. DR GO; GO:0030315; C:T-tubule; IDA:RGD. DR GO; GO:0043195; C:terminal bouton; HDA:ParkinsonsUK-UCL. DR GO; GO:0030506; F:ankyrin binding; IDA:RGD. DR GO; GO:0032051; F:clathrin light chain binding; ISO:RGD. DR GO; GO:0097718; F:disordered domain specific binding; ISO:RGD. DR GO; GO:0003725; F:double-stranded RNA binding; ISO:RGD. DR GO; GO:0031072; F:heat shock protein binding; IDA:RGD. DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; ISO:RGD. DR GO; GO:0042277; F:peptide binding; IDA:RGD. DR GO; GO:0019901; F:protein kinase binding; ISO:RGD. DR GO; GO:0120283; F:protein serine/threonine kinase binding; IPI:RGD. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:1990381; F:ubiquitin-specific protease binding; ISO:RGD. DR GO; GO:0150093; P:amyloid-beta clearance by transcytosis; ISO:RGD. DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW. DR GO; GO:0048268; P:clathrin coat assembly; ISO:RGD. DR GO; GO:0072318; P:clathrin coat disassembly; ISS:UniProtKB. DR GO; GO:0072583; P:clathrin-dependent endocytosis; ISO:RGD. DR GO; GO:0007030; P:Golgi organization; IMP:RGD. DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro. DR GO; GO:0000278; P:mitotic cell cycle; IMP:UniProtKB. DR GO; GO:0090307; P:mitotic spindle assembly; ISO:RGD. 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:RGD. DR GO; GO:0031623; P:receptor internalization; ISO:RGD. DR GO; GO:0006898; P:receptor-mediated endocytosis; IMP:UniProtKB. DR GO; GO:0060236; P:regulation of mitotic spindle organization; ISO:RGD. DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISO:RGD. DR GO; GO:0048488; P:synaptic vesicle endocytosis; IDA:SynGO. DR GO; GO:0033572; P:transferrin transport; ISO:RGD. 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. DR World-2DPAGE; 0004:P11442; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Autophagy; Coated pit; Cytoplasm; KW Cytoplasmic vesicle; Cytoskeleton; Direct protein sequencing; Membrane; KW Phosphoprotein; Reference proteome; Repeat. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.2" FT CHAIN 2..1675 FT /note="Clathrin heavy chain 1" FT /id="PRO_0000205780" 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:0000269|Ref.2" FT MOD_RES 67 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q00610" FT MOD_RES 105 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 184 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q68FD5" FT MOD_RES 394 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:22673903" 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:0007744|PubMed:22673903" FT MOD_RES 1501 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q00610" FT STRAND 7..14 FT /evidence="ECO:0007829|PDB:1BPO" FT HELIX 15..18 FT /evidence="ECO:0007829|PDB:1BPO" FT HELIX 22..24 FT /evidence="ECO:0007829|PDB:1C9I" FT TURN 27..29 FT /evidence="ECO:0007829|PDB:1BPO" FT STRAND 30..34 FT /evidence="ECO:0007829|PDB:1BPO" FT STRAND 37..42 FT /evidence="ECO:0007829|PDB:1BPO" FT STRAND 49..54 FT /evidence="ECO:0007829|PDB:1BPO" FT STRAND 62..65 FT /evidence="ECO:0007829|PDB:1BPO" FT STRAND 71..73 FT /evidence="ECO:0007829|PDB:1BPO" FT STRAND 75..78 FT /evidence="ECO:0007829|PDB:1BPO" FT STRAND 80..84 FT /evidence="ECO:0007829|PDB:1BPO" FT STRAND 87..92 FT /evidence="ECO:0007829|PDB:1BPO" FT TURN 93..96 FT /evidence="ECO:0007829|PDB:1BPO" FT STRAND 97..103 FT /evidence="ECO:0007829|PDB:1BPO" FT STRAND 110..115 FT /evidence="ECO:0007829|PDB:1BPO" FT STRAND 118..122 FT /evidence="ECO:0007829|PDB:1BPO" FT STRAND 124..135 FT /evidence="ECO:0007829|PDB:1BPO" FT STRAND 139..143 FT /evidence="ECO:0007829|PDB:1BPO" FT HELIX 146..148 FT /evidence="ECO:0007829|PDB:1BPO" FT STRAND 152..158 FT /evidence="ECO:0007829|PDB:1BPO" FT STRAND 162..173 FT /evidence="ECO:0007829|PDB:1BPO" FT STRAND 176..186 FT /evidence="ECO:0007829|PDB:1BPO" FT STRAND 191..194 FT /evidence="ECO:0007829|PDB:1BPO" FT STRAND 197..205 FT /evidence="ECO:0007829|PDB:1BPO" FT STRAND 210..220 FT /evidence="ECO:0007829|PDB:1BPO" FT STRAND 227..232 FT /evidence="ECO:0007829|PDB:1BPO" FT STRAND 246..249 FT /evidence="ECO:0007829|PDB:1BPO" FT STRAND 261..267 FT /evidence="ECO:0007829|PDB:1BPO" FT TURN 268..271 FT /evidence="ECO:0007829|PDB:1BPO" FT STRAND 272..277 FT /evidence="ECO:0007829|PDB:1BPO" FT STRAND 280..286 FT /evidence="ECO:0007829|PDB:1BPO" FT TURN 287..289 FT /evidence="ECO:0007829|PDB:1BPO" FT STRAND 292..297 FT /evidence="ECO:0007829|PDB:1BPO" FT STRAND 303..309 FT /evidence="ECO:0007829|PDB:1BPO" FT TURN 310..313 FT /evidence="ECO:0007829|PDB:1BPO" FT STRAND 314..319 FT /evidence="ECO:0007829|PDB:1BPO" FT TURN 320..322 FT /evidence="ECO:0007829|PDB:1C9L" FT STRAND 323..329 FT /evidence="ECO:0007829|PDB:1BPO" FT TURN 331..333 FT /evidence="ECO:0007829|PDB:1BPO" FT HELIX 334..340 FT /evidence="ECO:0007829|PDB:1BPO" FT HELIX 345..354 FT /evidence="ECO:0007829|PDB:1BPO" FT HELIX 361..373 FT /evidence="ECO:0007829|PDB:1BPO" FT HELIX 377..386 FT /evidence="ECO:0007829|PDB:1BPO" FT HELIX 388..390 FT /evidence="ECO:0007829|PDB:1BPO" FT HELIX 395..401 FT /evidence="ECO:0007829|PDB:1BPO" FT HELIX 413..424 FT /evidence="ECO:0007829|PDB:1BPO" FT HELIX 429..441 FT /evidence="ECO:0007829|PDB:1BPO" FT HELIX 445..454 FT /evidence="ECO:0007829|PDB:1BPO" FT HELIX 461..470 FT /evidence="ECO:0007829|PDB:1BPO" FT HELIX 473..482 FT /evidence="ECO:0007829|PDB:1BPO" SQ SEQUENCE 1675 AA; 191599 MW; C10F54C7ED8C5A61 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 IWVQVASKYH EQLSTQSLIE LFESFKSFEG LFYFLGSIVN FSQDPDVHFK YIQAACKTGQ IKEVERICRE SNCYDPERVK NFLKEAKLTD QLPLIIVCDR FDFVHDLVLY LYRNSLQKYI 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 VELYYKAIQF YLEFKPLLLN DLLMVLSPRL AHTRAVNYFS KVKQLPLVKP YLRSVQNHNN KSVNESLNNL FITEEDYQAL RTSIDAYDNF DNISLAQRLE KHELIEFRRI AAYLFKGNNR WKQSVELCKK DSLYKDAMQY ASESKDTELA EELLQWFLQE EKRECFGACL FTCYDLLRPD VVLETAWRHN IMDFAMPYFI QVMKEYLTKV DKLDASESLR KEEEQATETQ PIVYGQPQLM LTAGPSVAVP PQAPFGYGYT APPYGQPQPG FGYSM //