HCY1_LIODE
ID HCY1_LIODE Reviewed; 12 AA.
AC P84461;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 11-DEC-2019, entry version 25.
DE RecName: Full=Hemocyanin subunit 1;
DE Flags: Fragment;
OS Liocarcinus depurator (Harbour crab) (Portunus depurator).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura;
OC Eubrachyura; Portunoidea; Polybiidae; Liocarcinus.
OX NCBI_TaxID=313354;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, AND TISSUE SPECIFICITY.
RC TISSUE=Hemolymph {ECO:0000269|Ref.1};
RX DOI=10.1007/s00227-006-0537-4;
RA Giomi F., Raicevich S., Ferrarese A., Pranovi F., Di Muro P., Beltramin K.;
RT "Structural and functional heterogeneity of hemocyanin: intra- and inter-
RT specific comparison in four species of portunid crabs (Crustacea:
RT Portunidae).";
RL Mar. Biol. 151:1237-1247(2007).
CC -!- FUNCTION: Hemocyanins are copper-containing oxygen carriers occurring
CC freely dissolved in the hemolymph of many mollusks and arthropods.
CC {ECO:0000250|UniProtKB:P84293}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000250|UniProtKB:P84293}.
CC -!- TISSUE SPECIFICITY: Hemolymph. {ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the tyrosinase family. Hemocyanin subfamily.
CC {ECO:0000305}.
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DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Copper; Direct protein sequencing; Oxygen transport; Secreted; Transport.
FT CHAIN 1..>12
FT /note="Hemocyanin subunit 1"
FT /id="PRO_0000204278"
FT NON_TER 12
FT /evidence="ECO:0000303|Ref.1"
SQ SEQUENCE 12 AA; 1160 MW; 3A0D70568EB5BDD8 CRC64;
DSPGGASDAQ KQ