HCYA_CHEDE
ID HCYA_CHEDE Reviewed; 35 AA.
AC P83173;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 11-DEC-2019, entry version 36.
DE RecName: Full=Hemocyanin A chain;
DE Flags: Fragment;
OS Cherax destructor (Common yabby crayfish).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Astacidea;
OC Parastacoidea; Parastacidae; Cherax.
OX NCBI_TaxID=6723 {ECO:0000305};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE.
RC TISSUE=Hemolymph;
RX PubMed=2620501; DOI=10.1016/0305-0491(89)90200-9;
RA Neuteboom B., Sierdsema S.J., Beintema J.J.;
RT "The relationship between N-terminal sequences and immunological
RT characterization of crustacean hemocyanins.";
RL Comp. Biochem. Physiol. 94B:587-592(1989).
CC -!- FUNCTION: Hemocyanins are copper-containing oxygen carriers occurring
CC freely dissolved in the hemolymph of many mollusks and arthropods.
CC {ECO:0000269|PubMed:2620501}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- TISSUE SPECIFICITY: Hemolymph.
CC -!- SIMILARITY: Belongs to the tyrosinase family. Hemocyanin subfamily.
CC {ECO:0000305}.
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DR PIR; G60529; G60529.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0005344; F:oxygen carrier activity; IDA:UniProtKB.
DR GO; GO:0015671; P:oxygen transport; TAS:UniProtKB.
PE 1: Evidence at protein level;
KW Copper; Direct protein sequencing; Oxygen transport; Secreted; Transport.
FT CHAIN 1..>35
FT /note="Hemocyanin A chain"
FT /id="PRO_0000204261"
FT NON_TER 35
FT /evidence="ECO:0000303|PubMed:2620501"
SQ SEQUENCE 35 AA; 4014 MW; 1D1BE799B9CBE237 CRC64;
GVPGDVHDEQ KQHDINFLLF KVYEVLXDIX LKXVA