CLH1_BOVIN
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 03-AUG-2022, entry version 161.
DE RecName: Full=Clathrin heavy chain 1;
GN Name=CLTC;
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 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).
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. 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). {ECO:0000250|UniProtKB:Q00610,
CC ECO:0000250|UniProtKB:Q68FD5}.
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}.
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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 SMR; P49951; -.
DR BioGRID; 158448; 4.
DR DIP; DIP-31603N; -.
DR IntAct; P49951; 8.
DR MINT; P49951; -.
DR STRING; 9913.ENSBTAP00000022210; -.
DR PaxDb; P49951; -.
DR PeptideAtlas; P49951; -.
DR PRIDE; P49951; -.
DR Ensembl; ENSBTAT00000077192; ENSBTAP00000060092; ENSBTAG00000016708.
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; QVNEACV; -.
DR OrthoDB; 17940at2759; -.
DR EvolutionaryTrace; P49951; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000016708; Expressed in prefrontal cortex and 109 other 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:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005768; C:endosome; IEA:Ensembl.
DR GO; GO:0005764; C:lysosome; IEA:Ensembl.
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:1990498; C:mitotic spindle microtubule; IEA:Ensembl.
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:0003725; F:double-stranded RNA binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:1990381; F:ubiquitin-specific protease binding; IEA:Ensembl.
DR GO; GO:0150093; P:amyloid-beta clearance by transcytosis; IEA:Ensembl.
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:0072583; P:clathrin-dependent endocytosis; IEA:Ensembl.
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:1903077; P:negative regulation of protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0031623; P:receptor internalization; IEA:Ensembl.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IBA:GO_Central.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; IEA:Ensembl.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IEA:Ensembl.
DR GO; GO:0033572; P:transferrin transport; IEA:Ensembl.
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; 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
