ID   HCYE_SEPOF              Reviewed;         208 AA.
AC   P56825;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Hemocyanin, units E and F;
DE   Flags: Fragments;
OS   Sepia officinalis (Common cuttlefish).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC   Coleoidea; Decapodiformes; Sepiida; Sepiina; Sepiidae; Sepia.
OX   NCBI_TaxID=6610;
RN   [1]
RP   PROTEIN SEQUENCE OF 27-68 AND 98-208.
RA   Top A., Gielens C., Witters R., van Beeumen J., Preaux G.;
RT   "Partial amino-acid sequence and location of the carbohydrate chain in
RT   functional unit f of Sepia officinalis haemocyanin.";
RL   (In) Preaux G., Lontie R. (eds.);
RL   Invertebrate Dioxygen Carriers, pp.119-123, Leuven University Press, Leuven
RL   (1990).
RN   [2]
RP   PROTEIN SEQUENCE OF 69-125.
RA   Top A., Witters R., Gielens C., van Beeumen J., Preaux G.;
RT   "Amino-acid sequence determination of an N-terminal fragment from
RT   functional unit f of Sepia officinalis haemocyanin.";
RL   Arch. Int. Physiol. Biochim. 96:B187-B187(1988).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-26 AND 113-134, THIOETHER BOND, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=9342242; DOI=10.1111/j.1432-1033.1997.00879.x;
RA   Gielens C., de Geest N., Xin X.-Q., Devreese B., van Beeumen J., Preaux G.;
RT   "Evidence for a cysteine-histidine thioether bridge in functional units of
RT   molluscan haemocyanins and location of the disulfide bridges in functional
RT   units d and g of the beta-c-haemocyanin of Helix pomatia.";
RL   Eur. J. Biochem. 248:879-888(1997).
CC   -!- FUNCTION: Hemocyanins are copper-containing oxygen carriers occurring
CC       freely dissolved in the hemolymph of many mollusks and arthropods.
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC       Note=Binds 2 copper ions per heterodimer.;
CC   -!- SUBUNIT: Decamers of large identical subunits (390 kDa), each
CC       containing 8 globular oxygen-binding functional units.
CC   -!- SIMILARITY: Belongs to the tyrosinase family. Hemocyanin subfamily.
CC       {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   AlphaFoldDB; P56825; -.
DR   SMR; P56825; -.
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; -; 1.
DR   InterPro; IPR008922; Di-copper_centre_dom_sf.
DR   InterPro; IPR002227; Tyrosinase_Cu-bd.
DR   Pfam; PF00264; Tyrosinase; 1.
DR   SUPFAM; SSF48056; SSF48056; 1.
DR   PROSITE; PS00497; TYROSINASE_1; 1.
PE   1: Evidence at protein level;
KW   Copper; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Metal-binding; Oxygen transport; Repeat; Thioether bond; Transport.
FT   CHAIN           <1..>208
FT                   /note="Hemocyanin, units E and F"
FT                   /id="PRO_0000204309"
FT   REGION          <1..74
FT                   /note="Unit E"
FT   REGION          75..>208
FT                   /note="Unit F"
FT   BINDING         1
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250"
FT   BINDING         133
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        43
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   DISULFID        7..18
FT   DISULFID        119..130
FT   CROSSLNK        19..21
FT                   /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT                   /evidence="ECO:0000269|PubMed:9342242"
FT   CROSSLNK        131..133
FT                   /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT                   /evidence="ECO:0000269|PubMed:9342242"
FT   NON_CONS        26..27
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         208
SQ   SEQUENCE   208 AA;  23341 MW;  43292ECECF4385D8 CRC64;
     HGLPAQCPNA DGTMVHTCCL HGMPTFKLNF DSHFTIKTVV AQNGTELPES ILPEATIDRI
     PPSSHDLESV RGNLVRKNVD RLSLQEVNSL VHALKRMQKD RSSDGFESIA CFHALPPLCP
     NPTAKHRYAC CLHGMATFPQ WHRLYVVQFE QSLNRHGATV GVPYTDWTYP MKEVPHLLTS
     EKYTDPFTAV ETFNPFNHGH LSLLSPET