HCYB_CONCC
ID HCYB_CONCC Reviewed; 7 AA.
AC P84620;
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 B;
DE AltName: Full=CCH-B;
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; P84620; -.
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..>7
FT /note="Hemocyanin subunit B"
FT /id="PRO_0000204264"
FT NON_TER 7
FT /evidence="ECO:0000303|PubMed:15075320"
SQ SEQUENCE 7 AA; 855 MW; 6AB2C443241AE740 CRC64;
LXRKNVD