ID   HCYG_HELPO              Reviewed;         404 AA.
AC   P56823;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Hemocyanin, beta-C chain unit G;
DE   Flags: Fragment;
OS   Helix pomatia (Roman snail) (Edible snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Eupulmonata; Stylommatophora;
OC   Helicina; Helicoidea; Helicidae; Helix.
OX   NCBI_TaxID=6536;
RN   [1]
RP   PROTEIN SEQUENCE OF 1-139.
RA   Xin X.-Q., Vanhoegaerden R., Gielens C., Witters R., van Beeumen J.,
RA   Preaux G.;
RT   "Amino-acid sequence of the N-terminal part of the functional unit g of
RT   beta-c-haemocyanin of the mollusc Helix pomatia.";
RL   Arch. Int. Physiol. Biochim. 97:B194-B195(1989).
RN   [2]
RP   PROTEIN SEQUENCE OF 140-404.
RA   Xin X.-Q., Gielens C., Witters R., Preaux G.;
RT   "Amino-acid sequence of functional unit g from the beta-c-haemocyanin of
RT   Helix pomatia.";
RL   (In) Preaux G., Lontie R. (eds.);
RL   Invertebrate Dioxygen Carriers, pp.113-118, Leuven University Press, Leuven
RL   (1990).
RN   [3]
RP   PARTIAL PROTEIN SEQUENCE, SEQUENCE REVISION, THIOETHER BOND, AND
RP   IDENTIFICATION BY 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 (450 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; P56823; -.
DR   SMR; P56823; -.
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   PRINTS; PR00092; TYROSINASE.
DR   SUPFAM; SSF48056; SSF48056; 1.
DR   SUPFAM; SSF81277; SSF81277; 1.
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..>404
FT                   /note="Hemocyanin, beta-C chain unit G"
FT                   /id="PRO_0000204303"
FT   BINDING         50
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250"
FT   BINDING         61
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250"
FT   BINDING         77
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250"
FT   BINDING         176
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250"
FT   BINDING         180
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250"
FT   BINDING         207
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        38
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        60
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   CARBOHYD        378
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        56..65
FT   DISULFID        166..233
FT   DISULFID        320..326
FT   CROSSLNK        66..68
FT                   /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT                   /evidence="ECO:0000269|PubMed:9342242"
FT   NON_TER         1
FT   NON_TER         404
SQ   SEQUENCE   404 AA;  46210 MW;  AEF937948AD12ED5 CRC64;
     DIHTTAVAGV GVRKDVTRLT VSETENLREA LRRIKADNGS DGFQSIASFH GSPPGCEHEN
     HSVACCIHGM ANFPQWHRLY VKQWEDALTA QGAKIGIPYW DWTTAFTELP ALVTEEVDNP
     FHHGTIYNGE ITTRAPRDKL FNDPEFGKES FFYRQVLLAL EQTDYCDFEV QYEISHNAIH
     SWTGGQSPYG MSTLEYTAYD PLFLLHHSNV DRQFAIWQAL QKFRGLPYNS ANCAIQLLHQ
     PMRPFSDADN VNPVTRTNSR ARDVFNYDRL NYQYDDLNFH GLSISELNDV LERRKEKARI
     FAEFLLHGIG ASADVTFDLC DSHDHCEFAG TFAILGGPLE HPWAFDRLFK YDVTDVFSKL
     HLRPDSEYHF NIHIVSVNGT ELDSHLIRSP TVQFVPGVKD YYEK