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HCYC_SEPOF
ID   HCYC_SEPOF              Reviewed;         250 AA.
AC   P56824;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Hemocyanin, units C and D;
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   NUCLEOTIDE SEQUENCE.
RA   Declercq L., Witters R., Preaux G.;
RT   "Partial sequence determination of Sepia officinalis haemocyanin via
RT   cDNA.";
RL   (In) Preaux G., Lontie R. (eds.);
RL   Invertebrate Dioxygen Carriers, pp.131-134, Leuven University Press, Leuven
RL   (1990).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-19 AND 230-249, 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}.
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DR   AlphaFoldDB; P56824; -.
DR   SMR; P56824; -.
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   Gene3D; 2.60.310.10; -; 1.
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; 1.
DR   Pfam; PF00264; Tyrosinase; 1.
DR   SUPFAM; SSF48056; SSF48056; 1.
DR   SUPFAM; SSF81277; SSF81277; 1.
DR   PROSITE; PS00497; TYROSINASE_1; 1.
PE   1: Evidence at protein level;
KW   Copper; Direct protein sequencing; Disulfide bond; Metal-binding;
KW   Oxygen transport; Repeat; Thioether bond; Transport.
FT   CHAIN           <1..>250
FT                   /note="Hemocyanin, units C and D"
FT                   /id="PRO_0000204308"
FT   REGION          <1..106
FT                   /note="Unit C"
FT   REGION          107..>250
FT                   /note="Unit D"
FT   BINDING         1
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250"
FT   BINDING         21
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250"
FT   BINDING         172
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250"
FT   DISULFID        7..18
FT                   /evidence="ECO:0000269|PubMed:9342242"
FT   DISULFID        149..160
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        19..21
FT                   /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT                   /evidence="ECO:0000269|PubMed:9342242"
FT   CROSSLNK        161..163
FT                   /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT                   /evidence="ECO:0000250"
FT   NON_CONS        25..26
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         250
SQ   SEQUENCE   250 AA;  28715 MW;  2020FC9A329DBCDC CRC64;
     HGSTKWCPSP DAAQKYACCH HGMATYVLGS ENEMPWKFDR AYKSDITHVM DEMKLHYTDK
     YHVEYKISDM TGAEVTDIKL ESSVVFEPGL GKYGEGRAWI EPVTSAVRIR KNLNDLSGDE
     LILRNYIKQM TKDGSYQQIA AFHGLPAQCP SEDGTTVHTC CLHGMPTFPH WHRLYVALVE
     DELLSRGSRS GRPYWDWIDP FDRLPDFFND ATYYNSRTLH IESNPFFRGS MSFANTLTDR
     DAQDVIYNNH
 
 
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