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