HCYG_SEPOF
ID HCYG_SEPOF Reviewed; 560 AA.
AC P56826;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Hemocyanin, units G and H;
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 OF 20-436 AND 446-560.
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 PARTIAL PROTEIN SEQUENCE (H SUBUNIT).
RA Vanderzande M., Gielens C., Preaux G.;
RT "Isolation of functional units g and h from the haemocyanin of Sepia
RT officinalis and partial amino-acid sequence of functional unit h.";
RL (In) Preaux G., Lontie R. (eds.);
RL Invertebrate Dioxygen Carriers, pp.125-129, Leuven University Press, Leuven
RL (1990).
RN [3]
RP PROTEIN SEQUENCE OF 1-19 AND 230-249, AND THIOETHER BOND.
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; P56826; -.
DR SMR; P56826; -.
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; -; 2.
DR Gene3D; 2.60.310.10; -; 2.
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; 2.
DR Pfam; PF00264; Tyrosinase; 1.
DR PRINTS; PR00092; TYROSINASE.
DR SUPFAM; SSF48056; SSF48056; 2.
DR SUPFAM; SSF81277; SSF81277; 2.
DR PROSITE; PS00497; TYROSINASE_1; 1.
DR PROSITE; PS00498; TYROSINASE_2; 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..560
FT /note="Hemocyanin, units G and H"
FT /id="PRO_0000204310"
FT REGION <1..184
FT /note="Unit G"
FT REGION 185..560
FT /note="Unit H"
FT BINDING 230
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 358
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 362
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 389
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1..11
FT /evidence="ECO:0000250"
FT DISULFID 93..98
FT /evidence="ECO:0000250"
FT DISULFID 236..246
FT /evidence="ECO:0000250"
FT DISULFID 348..415
FT /evidence="ECO:0000250"
FT DISULFID 476..482
FT /evidence="ECO:0000250"
FT CROSSLNK 12..14
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000269|PubMed:9342242"
FT CROSSLNK 247..249
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT /evidence="ECO:0000269|PubMed:9342242"
FT NON_CONS 19..20
FT /evidence="ECO:0000305"
FT NON_CONS 445..446
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 560 AA; 63362 MW; BD966BE34307B387 CRC64;
CPTPDAPQYA CCLHGMPTFR ESNPNPATRA VSTPNKLFDF KSLGYNYDNL DFHGMDTAHL
EAAIKKQKQK DRVFAGFLLH GIKTSADVHL KVCNAADCHE AGVVFVLGAR TEMPWHFDRN
YKMDITDVLH EMHIPMEALF ENDSKIHLEV EIQSVDGAIL DSHSLPTPSL IYAPAKGLVS
QHIEDHDTET LIRKNVNSLS PSEIKNLRDA LVAVQADKSG NGYQKIASYH GMPLSCHYPN
GTAFACCQHG MVTFPHWHRL YMKQMEDAMK AKGAKIGIPY WDWTTTFSHL PFLVTEPKNN
PFHHGYIDVA DTKTTRNPRP QLFDDPEQGD QSFFYRQIAF ALEQRDFCDF EIQFEMGHNA
IHSWVGGSSP YGMSTLHYTS YDPLFYLHHS NTDRIWAIWQ ALQKYRGLPY NSANCEINKL
KKPMMPFSSD DNPNEVTKAH STGTKHLNKI QEKDRVFAGF LLRAIGQSAD VNFDICRKDG
ECKFGGTFCV LGGQHEMAWA FDRLFLYDIS RTLLQLRLDA HDDFDVKVTI MGIDGKSLPT
TLLPPPTILF KPGTGTQLTR
