ID   HCY2_LIODE              Reviewed;          12 AA.
AC   P84462;
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 2;
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 2"
FT                   /id="PRO_0000204279"
FT   NON_TER         12
FT                   /evidence="ECO:0000303|Ref.1"
SQ   SEQUENCE   12 AA;  1144 MW;  3A0D668C8EB5BDD8 CRC64;
     DAPGGASDAQ KQ