HCY2_MEGCR
ID HCY2_MEGCR Reviewed; 3421 AA.
AC Q10584; Q1MVA1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 17-JUN-2020, sequence version 2.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Hemocyanin 2 {ECO:0000312|EMBL:CAG28310.1};
DE AltName: Full=Keyhole limpet hemocyanin B {ECO:0000303|PubMed:8829804};
DE Short=KLH-B {ECO:0000303|PubMed:8829804};
DE Flags: Precursor;
GN Name=KLH2 {ECO:0000303|Ref.1};
OS Megathura crenulata (Giant keyhole limpet).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Vetigastropoda; Lepetellida; Fissurelloidea; Fissurellidae; Megathura.
OX NCBI_TaxID=55429;
RN [1] {ECO:0000312|EMBL:CAG28310.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lieb B., Streit K., Markl J.;
RT "KLH1 and KLH2: cDNAs, genes and evolutionary implications.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 20-31, AND TISSUE SPECIFICITY.
RX PubMed=8829804; DOI=10.1016/0305-0491(95)02091-8;
RA Swerdlow R.D., Ebert R.F., Lee P., Bonaventura C., Miller K.I.;
RT "Keyhole limpet hemocyanin: structural and functional characterization of
RT two different subunits and multimers.";
RL Comp. Biochem. Physiol. 113B:537-548(1996).
RN [3]
RP REVIEW, AND BIOTECHNOLOGY.
RX PubMed=10544506; DOI=10.1016/s0968-4328(99)00036-0;
RA Harris J.R., Markl J.;
RT "Keyhole limpet hemocyanin (KLH): a biomedical review.";
RL Micron 30:597-623(1999).
RN [4]
RP SUBUNIT.
RX PubMed=10838022; DOI=10.1016/s0968-4328(99)00145-6;
RA Harris J.R., Scheffler D., Gebauer W., Lehnert R., Markl J.;
RT "Haliotis tuberculata hemocyanin (HtH): analysis of oligomeric stability of
RT HtH1 and HtH2, and comparison with keyhole limpet hemocyanin KLH1 and
RT KLH2.";
RL Micron 31:613-622(2000).
CC -!- FUNCTION: Hemocyanins are copper-containing oxygen carriers occurring
CC freely dissolved in the hemolymph of many mollusks and arthropods.
CC {ECO:0000305|PubMed:8829804}.
CC -!- SUBUNIT: Homo-didecamer and homo-multidecamer.
CC {ECO:0000269|PubMed:10838022}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- TISSUE SPECIFICITY: Hemolymph. {ECO:0000269|PubMed:8829804}.
CC -!- DOMAIN: The protein is composed of 8 globular functional units (a->h),
CC forming a 'pearl chain'. Each unit is separated from the next by a
CC linker. Since the lengths but not the exact positions are known,
CC lengths are indicated here in free text. Linker lengths in amino acids
CC are: 20 (a->b), 13 (b->c), 19 (c->d), 16 (d->e), 14 (e->f), 17 (f->g),
CC and 17 (g->h). {ECO:0000250|UniProtKB:Q10583}.
CC -!- PTM: Probably N-glycosylated. Asn-2489 is buried deeply in the protein
CC which make it inaccessible for sugar attachment.
CC {ECO:0000250|UniProtKB:Q10583}.
CC -!- BIOTECHNOLOGY: Potent immunogen used classically as a carrier protein
CC for haptens and more recently in human vaccines and for immunotherapy
CC of bladder cancer. {ECO:0000305|PubMed:10544506}.
CC -!- SIMILARITY: Belongs to the tyrosinase family. Hemocyanin subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ698342; CAG28310.1; -; Genomic_DNA.
DR GlyConnect; 211; 15 N-Linked glycans.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1280.10; -; 8.
DR Gene3D; 2.60.310.10; -; 8.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR028999; Haemocyanin_beta-sandwich.
DR InterPro; IPR036848; Haemocyanin_C_sf.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR Pfam; PF14830; Haemocyan_bet_s; 8.
DR Pfam; PF00264; Tyrosinase; 9.
DR PRINTS; PR00092; TYROSINASE.
DR SUPFAM; SSF48056; SSF48056; 8.
DR SUPFAM; SSF81277; SSF81277; 8.
DR PROSITE; PS00497; TYROSINASE_1; 7.
DR PROSITE; PS00498; TYROSINASE_2; 7.
PE 1: Evidence at protein level;
KW Copper; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Metal-binding; Oxygen transport; Repeat; Secreted; Signal; Thioether bond;
KW Transport; WD repeat.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..3421
FT /note="Hemocyanin 2"
FT /id="PRO_0000204305"
FT REPEAT 632..673
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 1043..1084
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 1387..1425
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 1454..1495
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 1878..1919
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 2168..2204
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 2700..2742
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REPEAT 3109..3150
FT /note="WD 8"
FT /evidence="ECO:0000255"
FT REGION 20..442
FT /note="Functional unit a (wall)"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT REGION 443..853
FT /note="Functional unit b (wall)"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT REGION 854..1275
FT /note="Functional unit c (wall)"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT REGION 969..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1276..1685
FT /note="Functional unit d (wall)"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT REGION 1686..2102
FT /note="Functional unit e (wall)"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT REGION 2103..2522
FT /note="Functional unit f (wall)"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT REGION 2523..2929
FT /note="Functional unit g (internal arc)"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT REGION 2896..2928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2930..3421
FT /note="Functional unit h (internal slab)"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT COMPBIAS 972..988
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2902..2928
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 62
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 81
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 90
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 200
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 204
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 231
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 483
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 503
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 512
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 622
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 626
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 653
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 894
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 914
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 923
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 1033
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 1037
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 1063
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q10583, ECO:0000305"
FT BINDING 1313
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="7"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 1331
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="7"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 1340
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="7"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 1444
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="8"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 1448
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="8"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 1475
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="8"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 1726
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="9"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 1746
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="9"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 1755
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="9"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 1868
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="10"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 1872
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="10"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 1899
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="10"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 2143
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="11"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 2162
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="11"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 2171
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="11"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 2281
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="12"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 2285
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="12"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 2312
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="12"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 2563
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="13"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 2582
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="13"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 2591
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="13"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 2691
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="14"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 2695
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="14"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 2722
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="14"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 2970
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="15"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 2989
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="15"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 2998
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="15"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 3099
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="16"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 3103
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="16"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT BINDING 3130
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="16"
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1653
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 68..78
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT DISULFID 190..257
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT DISULFID 344..356
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT DISULFID 489..500
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT DISULFID 612..678
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT DISULFID 900..911
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT DISULFID 1023..1090
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT DISULFID 1180..1187
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT DISULFID 1319..1328
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT DISULFID 1434..1501
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT DISULFID 1590..1599
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT DISULFID 1732..1743
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT DISULFID 1858..1925
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT DISULFID 2014..2020
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT DISULFID 2149..2159
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT DISULFID 2271..2338
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT DISULFID 2425..2431
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT DISULFID 2569..2579
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT DISULFID 2681..2748
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT DISULFID 2835..2841
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT DISULFID 2976..2986
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT DISULFID 3089..3156
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT DISULFID 3374..3407
FT /evidence="ECO:0000250|UniProtKB:Q10583"
FT CROSSLNK 79..81
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000250|UniProtKB:P56824"
FT CROSSLNK 501..503
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000250|UniProtKB:P56824"
FT CROSSLNK 912..914
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000250|UniProtKB:P56824"
FT CROSSLNK 1329..1331
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000250|UniProtKB:P56824"
FT CROSSLNK 1744..1746
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000250|UniProtKB:P56824"
FT CROSSLNK 2160..2162
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000250|UniProtKB:P56824"
FT CROSSLNK 2580..2582
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000250|UniProtKB:P56824"
FT CROSSLNK 2987..2989
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000250|UniProtKB:P56824"
SQ SEQUENCE 3421 AA; 391513 MW; 94915A26F0870962 CRC64;
MWTILALLTA TLLFEGAFSV DTVVRKNVDS LSSDEVLALE KALDDLQQDD SNQGYQAIAG
YHGVPTMCVD KHEKNVACCL HGMPSFPLWH RLYVVQLERA LIRKKATISI PYWDWTSELT
HLPELVSHPL FVGTEGGKAH DNSWYRADIT FLNKKTSRAV DDRLFEKVQP GHHTRLMEGI
LDALEQDEFC KFEIQFELAH NAIHYLVGGR HTYSMSHLEY TSYDPLFFLH HSNTDRIFAI
WQRLQQLRGK DPNSADCAHN LIHTPMEPFD RDTNPLDLTR EHAKPADSFD YGRLGYQYDD
LSLNGMSPEE LNVYLGERAA KERTFASFIL SGFGGSANVV VYVCRPAHDE ISDDQCIKAG
DFFLLGGPTE MKWGFYRAYH FDVTDSVASI DDDGHGHYYV KSELFSVNGS ALSNDILRQP
TLVHRPAKGH FDKPPVPVAQ ANLAVRKNIN DLTAEETYSL RKAMERFQND KSVDGYQATV
EFHALPARCP RPDAKDRFAC CVHGMATFPH WHRLFVTQVE DALLRRGSTI GLPNWDWTMP
MDHLPELATS ETYLDPVTGE TKNNPFHHAQ VAFENGVTSR NPDAKLFMKP TYGDHTYLFD
SMIYAFEQED FCDFEVQYEL THNAIHAWVG GSEKYSMSSL HYTAFDPIFY LHHSNVDRLW
AIWQALQIRR GKSYKAHCAS SQEREPLKPF AFSSPLNNNE KTYHNSVPTN VYDYVGVLHY
RYDDLQFGGM TMSELEEYIH KQTQHDRTFA GFFLSYIGTS ASVDIFINRE GHDKYKVGSF
VVLGGSKEMK WGFDRMYKYE ITEALKTLNV AVDDGFSITV EITDVDGSPP SADLIPPPAI
IFERADAKDF GHSRKIRKAV DSLTVEEQTS LRRAMADLQD DKTSGGFQQI AAFHGEPKWC
PSPEAEKKFA CCVHGMAVFP HWHRLLTVQG ENALRKHGFT GGLPYWDWTR SMSALPHFVA
DPTYNDAISS QEEDNPWHHG HIDSVGHDTT RDVRDDLYQS PGFGHYTDIA KQVLLAFEQD
DFCDFEVQFE IAHNFIHALV GGNEPYSMSS LRYTTYDPIF FLHRSNTDRL WAIWQALQKY
RGKPYNTANC AIASMRKPLQ PFGLDSVINP DDETREHSVP FRVFDYKNNF DYEYESLAFN
GLSIAQLDRE LQRRKSHDRV FAGFLLHEIG QSALVKFYVC KHNVSDCDHY AGEFYILGDE
AEMPWRYDRV YKYEITQQLH DLDLHVGDNF FLKYEAFDLN GGSLGGSIFS QPSVIFEPAA
GSHQADEYRE AVTSASHIRK NIRDLSEGEI ESIRSAFLQI QKEGIYENIA KFHGKPGLCE
HDGHPVACCV HGMPTFPHWH RLYVLQVENA LLERGSAVAV PYWDWTEKAD SLPSLINDAT
YFNSRSQTFD PNPFFRGHIA FENAVTSRDP QPELWDNKDF YENVMLALEQ DNFCDFEIQL
ELIHNALHSR LGGRAKYSLS SLDYTAFDPV FFLHHANVDR IWAIWQDLQR YRKKPYNEAD
CAVNEMRKPL QPFNNPELNS DSMTLKHNLP QDSFDYQNRF RYQYDNLQFN HFSIQKLDQT
IQARKQHDRV FAGFILHNIG TSAVVDIYIC VEQGGEQNCK TKAGSFTILG GETEMPFHFD
RLYKFDITSA LHKLGVPLDG HGFDIKVDVR AVNGSHLDQH ILNEPSLLFV PGERKNIYYD
GLSQHNLVRK EVSSLTTLEK HFLRKALKNM QADDSPDGYQ AIASFHALPP LCPSPSAAHR
HACCLHGMAT FPQWHRLYTV QFEDSLKRHG SIVGLPYWDW LKPQSALPDL VTQETYEHLF
SHKTFPNPFL KANIEFEGEG VTTERDVDAE HLFAKGNLVY NNWFCNQALY ALEQENYCDF
EIQFEILHNG IHSWVGGSKT HSIGHLHYAS YDPLFYIHHS QTDRIWAIWQ ALQEHRGLSG
KEAHCALEQM KDPLKPFSFG SPYNLNKRTQ EFSKPEDTFD YHRFGYEYDS LEFVGMSVSS
LHNYIKQQQE ADRVFAGFLL KGFGQSASVS FDICRPDQSC QEAGYFSVLG GSSEMPWQFD
RLYKYDITKT LKDMKLRYDD TFTIKVHIKD IAGAELDSDL IPTPSVLLEE GKHGINVRHV
GRNRIRMELS ELTERDLASL KSAMRSLQAD DGVNGYQAIA SFHGLPASCH DDEGHEIACC
IHGMPVFPHW HRLYTLQMDM ALLSHGSAVA IPYWDWTKPI SKLPDLFTSP EYYDPWRDAV
VNNPFAKGYI KSEDAYTVRD PQDILYHLQD ETGTSVLLDQ TLLALEQTDF CDFEVQFEVV
HNAIHYLVGG RQVYALSSQH YASYDPAFFI HHSFVDKIWA VWQALQKKRK RPYHKADCAL
NMMTKPMRPF AHDFNHNGFT KMHAVPNTLF DFQDLFYTYD NLEIAGMNVN QLEAEINRRK
SQTRVFAGFL LHGIGRSADV RFWICKTADD CHASGMIFIL GGSKEMHWAY DRNFKYDITQ
ALKAQSIHPE DVFDTDAPFF IKVEVHGVNK TALPSSAIPA PTIIYSAGEG HTDDHGSDHI
AGSGVRKDVT SLTASEIENL RHALQSVMDD DGPNGFQAIA AYHGSPPMCH MXDGRDVACC
THGMASFPHW HRLFVKQMED ALAAHGAHIG IPYWDWTSAF SHLPALVTDH EHNPFHHGHI
AHRNVDTSRS PRDMLFNDPE HGSESFFYRQ VLLALEQTDF CQFEVQFEIT HNAIHSWTGG
HTPYGMSSLE YTAYDPLFYL HHSNTDRIWA IWQALQKYRG FQYNAAHCDI QVLKQPLKPF
SESRNPNPVT RANSRAVDSF DYERLNYQYD TLTFHGHSIS ELDAMLQERK KEERTFAAFL
LHGFGASADV SFDVCTPDGH CAFAGTFAVL GGELEMPWSF ERLFRYDITK VLKQMNLHYD
SEFHFELKIV GTDGTELPSD RIKSPTIEHH GGDHHGGDTS GHDHSERHDG FFRKEVGSLS
LDEANDLKNA LYKLQNDQGP NGYESIAGYH GYPFLCPEHG EDQYACCVHG MPVFPHWHRL
HTIQFERALK EHGSHLGIPY WDWTKSMIAL PAFFADSSNS NPFYKYHIMK AGHDTARSPS
DLLFNQPQLH GYDYLYYLAL STLEEDNYCD FEVHYEILHN AVHLWLGGTE TYSMSSLAFS
AYDPVFMILH SGLDRLWIIW QELQKLRKKP YNAAKCAGHM MDEPLHPFNY ESANHDSFTR
ANAKPSTVFD SHKFNYHYDN PDVRGNSIQE ISAIIHDLRN QPRVFAGFVL SGIYTSANVK
IYLVREGHDD ENVGSFVVLG GPKEMPWAYE RIFKYDITEV ANRLNMHHDD TFNFRLEVQS
YTGEMVTHHL PEPLIIYRPA KQEYDVLVIP LGSGHKLPPK VIVKRGTRIM FHPVDDTVNR
PVVDLGSHTA LYNCVVPPFT YNGYELDHAY SLRDGHYYIA GPTKDLCTSG NVRIHIHIED
E
