ID   HCYA_CONCC              Reviewed;          11 AA.
AC   P84619;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   22-APR-2020, entry version 30.
DE   RecName: Full=Hemocyanin subunit A;
DE   AltName: Full=CCH-A;
DE   Flags: Fragment;
OS   Concholepas concholepas (Barnacle rock-shell).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Muricoidea; Muricidae; Concholepas.
OX   NCBI_TaxID=137544;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Hemolymph {ECO:0000269|PubMed:15075320};
RX   PubMed=15075320; DOI=10.1074/jbc.m400903200;
RA   De Ioannes P., Moltedo B., Oliva H., Pacheco R., Faunes F.,
RA   De Ioannes A.E., Becker M.I.;
RT   "Hemocyanin of the molluscan Concholepas concholepas exhibits an unusual
RT   heterodecameric array of subunits.";
RL   J. Biol. Chem. 279:26134-26142(2004).
CC   -!- FUNCTION: Hemocyanins are copper-containing oxygen carriers occurring
CC       freely dissolved in the hemolymph of many mollusks and arthropods.
CC       {ECO:0000305}.
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000269|PubMed:15075320};
CC       Note=Binds 2 copper ions per heterodimer.
CC       {ECO:0000269|PubMed:15075320};
CC   -!- SUBUNIT: Heterodidecamer composed of A and B subunits, each containing
CC       8 globular oxygen-binding functional units. Heterogenous decameric or
CC       multidecameric structures may also be formed.
CC       {ECO:0000269|PubMed:15075320}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC       {ECO:0000269|PubMed:15075320}.
CC   -!- TISSUE SPECIFICITY: Hemolymph. {ECO:0000269|PubMed:15075320}.
CC   -!- PTM: Forms a thioether bond between 2 amino acids. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the tyrosinase family. Hemocyanin subfamily.
CC       {ECO:0000255}.
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DR   SABIO-RK; P84619; -.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Copper; Direct protein sequencing; Metal-binding; Oxygen transport;
KW   Secreted; Thioether bond; Transport.
FT   CHAIN           1..>11
FT                   /note="Hemocyanin subunit A"
FT                   /id="PRO_0000204263"
FT   NON_TER         11
FT                   /evidence="ECO:0000303|PubMed:15075320"
SQ   SEQUENCE   11 AA;  1306 MW;  5A74C04DAAB2CAA3 CRC64;
     LMRKDVDTLT D