HCY1_MEGCR
ID HCY1_MEGCR Reviewed; 3414 AA.
AC Q10583; Q53IP9; Q6KC56;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 17-JUN-2020, sequence version 2.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Hemocyanin 1 {ECO:0000312|EMBL:CAG28309.2};
DE AltName: Full=Keyhole limpet hemocyanin A {ECO:0000303|PubMed:8829804};
DE Short=KLH-A {ECO:0000303|PubMed:8829804};
DE Flags: Precursor;
GN Name=KLH1 {ECO:0000303|PubMed:15036312};
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:CAG28307.2}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15036312; DOI=10.1016/j.micron.2003.10.035;
RA Lieb B., Markl J.;
RT "Evolution of molluscan hemocyanins as deduced from DNA sequencing.";
RL Micron 35:117-119(2004).
RN [2] {ECO:0000312|EMBL:CAG28309.2}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lieb B., Streit K., Markl J.;
RT "KLH1 and KLH2: cDNAs, genes and evolutionary implications.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 17-30, 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 [4]
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 [5] {ECO:0007744|PDB:4BED}
RP STRUCTURE BY ELECTRON MICROSCOPY (9.00 ANGSTROMS) OF 17-3414 IN COMPLEX
RP WITH COPPER, AND DISULFIDE BONDS.
RX PubMed=19013468; DOI=10.1016/j.jmb.2008.10.080;
RA Gatsogiannis C., Markl J.;
RT "Keyhole limpet hemocyanin: 9-A CryoEM structure and molecular model of the
RT KLH1 didecamer reveal the interfaces and intricate topology of the 160
RT functional units.";
RL J. Mol. Biol. 385:963-983(2009).
RN [6] {ECO:0007744|PDB:3L6W}
RP X-RAY CRYSTALLOGRAPHY (4.00 ANGSTROMS) OF 2922-3412.
RX PubMed=20025608; DOI=10.1042/bj20091501;
RA Jaenicke E., Buchler K., Markl J., Decker H., Barends T.R.;
RT "Cupredoxin-like domains in haemocyanins.";
RL Biochem. J. 426:373-378(2010).
RN [7] {ECO:0007744|PDB:3QJO}
RP X-RAY CRYSTALLOGRAPHY (4.00 ANGSTROMS) OF 2922-3412 IN COMPLEX WITH COPPER,
RP AND DISULFIDE BONDS.
RX PubMed=21445849; DOI=10.1002/iub.435;
RA Jaenicke E., Buchler K., Decker H., Markl J., Schroder G.F.;
RT "The refined structure of functional unit h of keyhole limpet hemocyanin
RT (KLH1-h) reveals disulfide bridges.";
RL IUBMB Life 63:183-187(2011).
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, with two decamers assembled face-to-face at
CC their open ends. This didecamer form a stable 25 nM cylinder wall.
CC {ECO:0000269|PubMed:19013468}.
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:0000305|PubMed:19013468}.
CC -!- PTM: Probably N-glycosylated (Probable). Asn-1280 and Asn-2484 are
CC buried deeply in the protein which make them inaccessible for sugar
CC attachment (Probable). Asn-3278 N-glycan is likely to represent a
CC diantennate carbohydrate tree (Probable). The didecamer is almost
CC evenly tagged by a total of 120 sugar trees (Probable).
CC {ECO:0000305|PubMed:19013468}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAG28307.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAG28309.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ698341; CAG28309.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AJ698339; CAG28307.2; ALT_SEQ; mRNA.
DR PDB; 3L6W; X-ray; 4.00 A; A/B=2922-3412.
DR PDB; 3QJO; X-ray; 4.00 A; A/B=2922-3412.
DR PDB; 4BED; EM; 9.00 A; A/C=17-1680, B/D=1681-3414.
DR PDBsum; 3L6W; -.
DR PDBsum; 3QJO; -.
DR PDBsum; 4BED; -.
DR SMR; Q10583; -.
DR ChEMBL; CHEMBL4662943; -.
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; 8.
PE 1: Evidence at protein level;
KW 3D-structure; Copper; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Metal-binding; Oxygen transport; Repeat; Secreted; Signal;
KW Thioether bond; Transport; WD repeat.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..3414
FT /note="Hemocyanin 1"
FT /id="PRO_0000204304"
FT REPEAT 628..669
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 1041..1082
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 1450..1491
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 1873..1914
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 2163..2199
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 2696..2737
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 3101..3142
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REGION 17..437
FT /note="Functional unit a (wall)"
FT /evidence="ECO:0000305|PubMed:19013468"
FT REGION 438..851
FT /note="Functional unit b (wall)"
FT /evidence="ECO:0000305|PubMed:19013468"
FT REGION 852..1271
FT /note="Functional unit c (wall)"
FT /evidence="ECO:0000305|PubMed:19013468"
FT REGION 1272..1680
FT /note="Functional unit d (wall)"
FT /evidence="ECO:0000305|PubMed:19013468"
FT REGION 1681..2097
FT /note="Functional unit e (wall)"
FT /evidence="ECO:0000305|PubMed:19013468"
FT REGION 2098..2517
FT /note="Functional unit f (wall)"
FT /evidence="ECO:0000305|PubMed:19013468"
FT REGION 2518..2921
FT /note="Functional unit g (internal arc)"
FT /evidence="ECO:0000305|PubMed:19013468"
FT REGION 2922..3414
FT /note="Functional unit h (internal slab)"
FT /evidence="ECO:0000305|PubMed:19013468"
FT BINDING 17
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="structural"
FT /evidence="ECO:0000305|PubMed:19013468"
FT BINDING 58
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 76
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 85
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 195
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 199
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 226
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 478
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 498
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 507
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 618
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 622
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 649
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 737
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="structural"
FT /evidence="ECO:0000305|PubMed:19013468"
FT BINDING 892
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="5"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 912
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="5"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 921
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="5"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 1031
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="6"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 1035
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="6"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 1062
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="6"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 1309
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="7"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 1327
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="7"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 1336
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="7"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 1440
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="8"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 1444
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="8"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 1471
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="8"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 1721
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="9"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 1741
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="9"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 1750
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="9"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 1863
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="10"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 1867
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="10"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 1894
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="10"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 2138
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="11"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 2157
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="11"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 2166
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="11"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 2276
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="12"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 2280
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="12"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 2307
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="12"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 2424
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="structural"
FT /evidence="ECO:0000305|PubMed:19013468"
FT BINDING 2558
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="13"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 2577
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="13"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 2586
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="13"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 2686
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="14"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 2690
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="14"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 2717
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="14"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 2962
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="15"
FT /evidence="ECO:0007744|PDB:3QJO, ECO:0007744|PDB:4BED"
FT BINDING 2981
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="15"
FT /evidence="ECO:0007744|PDB:3QJO, ECO:0007744|PDB:4BED"
FT BINDING 2990
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="15"
FT /evidence="ECO:0007744|PDB:3QJO, ECO:0007744|PDB:4BED"
FT BINDING 3091
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="16"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 3095
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="16"
FT /evidence="ECO:0007744|PDB:4BED"
FT BINDING 3122
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="16"
FT /evidence="ECO:0007744|PDB:4BED"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 545
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1648
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2571
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 3278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 64..73
FT /evidence="ECO:0007744|PDB:4BED"
FT DISULFID 185..252
FT /evidence="ECO:0007744|PDB:4BED"
FT DISULFID 339..351
FT /evidence="ECO:0007744|PDB:4BED"
FT DISULFID 484..495
FT /evidence="ECO:0007744|PDB:4BED"
FT DISULFID 608..674
FT /evidence="ECO:0007744|PDB:4BED"
FT DISULFID 898..909
FT /evidence="ECO:0007744|PDB:4BED"
FT DISULFID 1021..1088
FT /evidence="ECO:0007744|PDB:4BED"
FT DISULFID 1178..1184
FT /evidence="ECO:0007744|PDB:4BED"
FT DISULFID 1315..1324
FT /evidence="ECO:0007744|PDB:4BED"
FT DISULFID 1430..1497
FT /evidence="ECO:0007744|PDB:4BED"
FT DISULFID 1585..1595
FT /evidence="ECO:0007744|PDB:4BED"
FT DISULFID 1727..1738
FT /evidence="ECO:0007744|PDB:4BED"
FT DISULFID 1853..1920
FT /evidence="ECO:0007744|PDB:4BED"
FT DISULFID 2009..2015
FT /evidence="ECO:0007744|PDB:4BED"
FT DISULFID 2144..2154
FT /evidence="ECO:0007744|PDB:4BED"
FT DISULFID 2266..2333
FT /evidence="ECO:0007744|PDB:4BED"
FT DISULFID 2420..2426
FT /evidence="ECO:0007744|PDB:4BED"
FT DISULFID 2564..2574
FT /evidence="ECO:0007744|PDB:4BED"
FT DISULFID 2676..2743
FT /evidence="ECO:0007744|PDB:4BED"
FT DISULFID 2830..2836
FT /evidence="ECO:0007744|PDB:4BED"
FT DISULFID 2968..2978
FT /evidence="ECO:0007744|PDB:3QJO, ECO:0007744|PDB:4BED"
FT DISULFID 3081..3148
FT /evidence="ECO:0007744|PDB:3QJO, ECO:0007744|PDB:4BED"
FT DISULFID 3367..3400
FT /evidence="ECO:0007744|PDB:3QJO, ECO:0007744|PDB:4BED"
FT CROSSLNK 74..76
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000250|UniProtKB:P56824,
FT ECO:0000305|PubMed:19013468"
FT CROSSLNK 287..290
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000305|PubMed:19013468"
FT CROSSLNK 496..498
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000250|UniProtKB:P56824,
FT ECO:0000305|PubMed:19013468"
FT CROSSLNK 910..912
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000250|UniProtKB:P56824,
FT ECO:0000305|PubMed:19013468"
FT CROSSLNK 1325..1327
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000250|UniProtKB:P56824,
FT ECO:0000305|PubMed:19013468"
FT CROSSLNK 1739..1741
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000250|UniProtKB:P56824,
FT ECO:0000305|PubMed:19013468"
FT CROSSLNK 2155..2157
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000250|UniProtKB:P56824,
FT ECO:0000305|PubMed:19013468"
FT CROSSLNK 2575..2577
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000250|UniProtKB:P56824,
FT ECO:0000305|PubMed:19013468"
FT CROSSLNK 2979..2981
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000250|UniProtKB:P56824,
FT ECO:0000305|PubMed:19013468"
FT CONFLICT 17
FT /note="E -> G (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3414 AA; 392246 MW; 1DE70B29A343AD01 CRC64;
MLSVRLLIVV LALANAENLV RKSVEHLTQE ETLDLQAALR ELQMDSSSIG FQKIAAAHGA
PASCVHKDTS IACCIHGMPT FPHWHRAYVV HMERALQTKR RTSGLPYWDW TEPITQLPSL
AADPVYIDSQ GGKAHTNYWY RGNIDFLDKK TNRAVDDRLF EKVKPGQHTH LMESVLDALE
QDEFCKFEIQ FELAHNAIHY LVGGKHDYSM ANLEYTAYDP IFFLHHSNVD RIFAIWQRLQ
ELRNKDPKAM DCAQELLHQK MEPFSWEDND IPLTNEHSTP ADLFDYCELH YDYDTLNLNG
MTPEELKTYL DERSSRARAF ASFRLKGFGG SANVFVYVCI PDDNDRNDDH CEKAGDFFVL
GGPSEMKWQF YRPYLFDLSD TVHKMGMKLD GHYTVKAELF SVNGTALPDD LLPHPVVVHH
PEKGFTDPPV KHHQSANLLV RKNINDLTRE EVLNLREAFH KFQEDRSVDG YQATAEYHGL
PARCPRPDAK DRYACCVHGM PIFPHWHRLF VTQVEDALVG RGATIGIPYW DWTEPMTHIP
GLAGNKTYVD SHGASHTNPF HSSVIAFEEN APHTKRQIDQ RLFKPATFGH HTDLFNQILY
AFEQEDYCDF EVQFEITHNT IHAWTGGSEH FSMSSLHYTA FDPLFYFHHS NVDRLWAVWQ
ALQMRRHKPY RAHCAISLEH MHLKPFAFSS PLNNNEKTHA NAMPNKIYDY ENVLHYTYED
LTFGGISLEN IEKMIHENQQ EDRIYAGFLL AGIRTSANVD IFIKTTDSVQ HKAGTFAVLG
GSKEMKWGFD RVFKFDITHV LKDLDLTADG DFEVTVDITE VDGTKLASSL IPHASVIREH
ARVKFDKVPR SRLIRKNVDR LSPEEMNELR KALALLKEDK SAGGFQQLGA FHGEPKWCPS
PEASKKFACC VHGMSVFPHW HRLLTVQSEN ALRRHGYDGA LPYWDWTSPL NHLPELADHE
KYVDPEDGVE KHNPWFDGHI DTVDKTTTRS VQNKLFEQPE FGHYTSIAKQ VLLALEQDNF
CDFEIQYEIA HNYIHALVGG AQPYGMASLR YTAFDPLFYL HHSNTDRIWA IWQALQKYRG
KPYNVANCAV TSMREPLQPF GLSANINTDH VTKEHSVPFN VFDYKTNFNY EYDTLEFNGL
SISQLNKKLE AIKSQDRFFA GFLLSGFKKS SLVKFNICTD SSNCHPAGEF YLLGDENEMP
WAYDRVFKYD ITEKLHDLKL HAEDHFYIDY EVFDLKPASL GKDLFKQPSV IHEPRIGHHE
GEVYQAEVTS ANRIRKNIEN LSLGELESLR AAFLEIENDG TYESIAKFHG SPGLCQLNGN
PISCCVHGMP TFPHWHRLYV VVVENALLKK GSSVAVPYWD WTKRIEHLPH LISDATYYNS
RQHHYETNPF HHGKITHENE ITTRDPKDSL FHSDYFYEQV LYALEQDNFC DFEIQLEILH
NALHSLLGGK GKYSMSNLDY AAFDPVFFLH HATTDRIWAI WQDLQRFRKR PYREANCAIQ
LMHTPLQPFD KSDNNDEATK THATPHDGFE YQNSFGYAYD NLELNHYSIP QLDHMLQERK
RHDRVFAGFL LHNIGTSADG HVFVCLPTGE HTKDCSHEAG MFSILGGQTE MSFVFDRLYK
LDITKALKKN GVHLQGDFDL EIEITAVNGS HLDSHVIHSP TILFEAGTDS AHTDDGHTEP
VMIRKDITQL DKRQQLSLVK ALESMKADHS SDGFQAIASF HALPPLCPSP AASKRFACCV
HGMATFPQWH RLYTVQFQDS LRKHGAVVGL PYWDWTLPRS ELPELLTVST IHDPETGRDI
PNPFIGSKIE FEGENVHTKR DINRDRLFQG STKTHHNWFI EQALLALEQT NYCDFEVQFE
IMHNGVHTWV GGKEPYGIGH LHYASYDPLF YIHHSQTDRI WAIWQSLQRF RGLSGSEANC
AVNLMKTPLK PFSFGAPYNL NDHTHDFSKP EDTFDYQKFG YIYDTLEFAG WSIRGIDHIV
RNRQEHSRVF AGFLLEGFGT SATVDFQVCR TAGDCEDAGY FTVLGGEKEM PWAFDRLYKY
DITETLDKMN LRHDEIFQIE VTITSYDGTV LDSGLIPTPS IIYDPAHHDI SSHHLSLNKV
RHDLSTLSER DIGSLKYALS SLQADTSADG FAAIASFHGL PAKCNDSHNN EVACCIHGMP
TFPHWHRLYT LQFEQALRRH GSSVAVPYWD WTKPIHNIPH LFTDKEYYDV WRNKVMPNPF
ARGYVPSHDT YTVRDVQEGL FHLTSTGEHS ALLNQALLAL EQHDYCDFAV QFEVMHNTIH
YLVGGPQVYS LSSLHYASYD PIFFIHHSFV DKVWAVWQAL QEKRGLPSDR ADCAVSLMTQ
NMRPFHYEIN HNQFTKKHAV PNDVFKYELL GYRYDNLEIG GMNLHEIEKE IKDKQHHVRV
FAGFLLHGIR TSADVQFQIC KTSEDCHHGG QIFVLGGTKE MAWAYNRLFK YDITHALHDA
HITPEDVFHP SEPFFIKVSV TAVNGTVLPA SILHAPTIIY EPGLDHHEDH HSSSMAGHGV
RKEINTLTTA EVDNLKDAMR AVMADHGPNG YQAIAAFHGN PPMCPMPDGK NYSCCTHGMA
TFPHWHRLYT KQMEDALTAH GARVGLPYWD GTTAFTALPT FVTDEEDNPF HHGHIDYLGV
DTTRSPRDKL FNDPERGSES FFYRQVLLAL EQTDFCQFEV QFEITHNAIH SWTGGLTPYG
MSTLEYTTYD PLFWLHHANT DRIWAIWQAL QEYRGLPYDH ANCEIQAMKR PLRPFSDPIN
HNAFTHSNAK PTDVFEYSRF NFQYDNLRFH GMTIKKLEHE LEKQKEEDRT FAAFLLHGIK
KSADVSFDVC NHDGECHFAG TFAILGGEHE MPWSFDRLFR YDITQVLKQM HLEYDSDFTF
HMRIIDTSGK QLPSDLIKMP TVEHSPGGKH HEKHHEDHHE DILVRKNIHS LSHHEAEELR
DALYKLQNDE SHGGYEHIAG FHGYPNLCPE KGDEKYPCCV HGMSIFPHWH RLHTIQFERA
LKKHGSHLGI PYWDWTQTIS SLPTFFADSG NNNPFFKYHI RSINQDTVRD VNEAIFQQTK
FGEFSSIFYL ALQALEEDNY CDFEVQYEIL HNEVHALIGG AEKYSMSTLE YSAFDPYFMI
HHASLDKIWI IWQELQKRRV KPAHAGSCAG DIMHVPLHPF NYESVNNDDF TRENSLPNAV
VDSHRFNYKY DNLNLHGHNI EELEEVLRSL RLKSRVFAGF VLSGIRTTAV VKVYIKSGTD
SDDEYAGSFV ILGGAKEMPW AYERLYRFDI TETVHNLNLT DDHVKFRFDL KKYDHTELDA
SVLPAPIIVR RPNNAVFDII EIPIGKDVNL PPKVVVKRGT KIMFMSVDEA VTTPMLNLGS
YTAMFKCKVP PFSFHAFELG KMYSVESGDY FMTASTTELC NDNNLRIHVH VDDE
