CLH1_RAT
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 03-AUG-2022, entry version 181.
DE RecName: Full=Clathrin heavy chain 1;
GN Name=Cltc;
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 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). {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). {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}.
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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 SMR; P11442; -.
DR BioGRID; 248464; 22.
DR CORUM; P11442; -.
DR DIP; DIP-36966N; -.
DR IntAct; P11442; 8.
DR MINT; P11442; -.
DR STRING; 10116.ENSRNOP00000005987; -.
DR iPTMnet; P11442; -.
DR PhosphoSitePlus; P11442; -.
DR World-2DPAGE; 0004:P11442; -.
DR jPOST; P11442; -.
DR PaxDb; P11442; -.
DR PRIDE; P11442; -.
DR GeneID; 54241; -.
DR KEGG; rno:54241; -.
DR CTD; 1213; -.
DR RGD; 2364; Cltc.
DR eggNOG; KOG0985; Eukaryota.
DR InParanoid; P11442; -.
DR OrthoDB; 17940at2759; -.
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:0008022; F:protein C-terminus binding; IPI:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO: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: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; 1.25.40.10; -; 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; 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
