ID   HCYB_HELPO              Reviewed;         410 AA.
AC   P12031;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Hemocyanin, beta-C chain unit D;
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.
RX   PubMed=3620107; DOI=10.1515/bchm3.1987.368.1.617;
RA   Drexel R., Siegmund S., Schneider H.J., Linzen B., Gielens C., Preaux G.,
RA   Lontie R., Kellermann J., Lottspeich F.;
RT   "Complete amino-acid sequence of a functional unit from a molluscan
RT   hemocyanin (Helix pomatia).";
RL   Biol. Chem. Hoppe-Seyler 368:617-635(1987).
RN   [2]
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   PIR; A29393; A29393.
DR   AlphaFoldDB; P12031; -.
DR   SMR; P12031; -.
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..>410
FT                   /note="Hemocyanin, beta-C chain unit D"
FT                   /id="PRO_0000204302"
FT   BINDING         44
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250"
FT   BINDING         55
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250"
FT   BINDING         71
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250"
FT   BINDING         175
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250"
FT   BINDING         179
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250"
FT   BINDING         206
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        253
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   DISULFID        50..59
FT   DISULFID        165..232
FT   DISULFID        321..332
FT   CROSSLNK        60..62
FT                   /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT                   /evidence="ECO:0000269|PubMed:9342242"
FT   CONFLICT        60
FT                   /note="C -> S (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        62
FT                   /note="H -> S (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        165
FT                   /note="C -> D (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         410
SQ   SEQUENCE   410 AA;  47019 MW;  E872743ED14E66BF CRC64;
     DAVTVASHVR KDLDTLTAGE IESLRSAFLD IQQDHTYENI ASFHGKPGLC QHEGHKVACC
     VHGMPTFPSW HRLYVEQVEE ALLDHGSSVA VPYFDWISPI QKLPDLISKA TYYNSREQRF
     DPNPFFSGKV AGEDAVTTRD PQPELFNNNY FYEQALYALE QDNFCDFEIQ FEVLHNALHS
     WLGGHAKYSF SSLDYTAFDP VFFLHHANTD RLWAIWQELQ RYRGLPYNEA DCAINLMRKP
     LQPFQDKKLN PRNITNIYSR PADTFDYRNH FHYEYDTLEL NHQTVPQLEN LLKRRQEYGR
     VFAGFLIHNN GLSADVTVYV CVPSGPKGKN DCNHKAGVFS VLGGELEMPF TFDRLYKLQI
     TDTIKQLGLK VNNAASYQLK VEIKAVPGTL LDPHILPDPS IIFEPGTKER