ID   HCY6_ANDAU              Reviewed;         626 AA.
AC   P80476;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Hemocyanin AA6 chain;
OS   Androctonus australis (Sahara scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Androctonus.
OX   NCBI_TaxID=6858;
RN   [1]
RP   PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RC   STRAIN=Hector; TISSUE=Hemolymph;
RX   PubMed=7588779; DOI=10.1111/j.1432-1033.1995.093_1.x;
RA   Buzy A., Gagnon J., Lamy J., Thibault P., Forest E., Hudry-Clergeon G.;
RT   "Complete amino acid sequence of the Aa6 subunit of the scorpion
RT   Androctonus australis hemocyanin determined by Edman degradation and mass
RT   spectrometry.";
RL   Eur. J. Biochem. 233:93-101(1995).
CC   -!- FUNCTION: Hemocyanins are copper-containing oxygen carriers occurring
CC       freely dissolved in the hemolymph of many mollusks and arthropods.
CC   -!- SUBUNIT: Scorpion hemocyanin is a 24-chain polymer with 8 different
CC       chains identified, assembled in hexameric substructures.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC   -!- TISSUE SPECIFICITY: Hemolymph.
CC   -!- PTM: Three disulfide bonds are present.
CC   -!- MASS SPECTROMETRY: Mass=71890; Mass_error=7; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:7588779};
CC   -!- MISCELLANEOUS: The two copper ions bound each have 3 nitrogen ligands
CC       (presumably contributed by His residues) and share a bridging ligand
CC       (possibly contributed by a Tyr residue) in addition to binding oxygen.
CC   -!- SIMILARITY: Belongs to the tyrosinase family. Hemocyanin subfamily.
CC       {ECO:0000305}.
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DR   PIR; S67964; S67964.
DR   PDB; 3IXV; EM; 6.80 A; A/C/D/E/F/G/H/I/J/K/L/M=1-626.
DR   PDB; 3IXW; EM; 8.00 A; A/C/D/E/F/G/H/I/J/K/L/M=1-626.
DR   PDBsum; 3IXV; -.
DR   PDBsum; 3IXW; -.
DR   AlphaFoldDB; P80476; -.
DR   SMR; P80476; -.
DR   EvolutionaryTrace; P80476; -.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0031404; F:chloride ion binding; ISS:UniProtKB.
DR   GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1280.10; -; 1.
DR   Gene3D; 1.20.1370.10; -; 1.
DR   Gene3D; 2.60.40.1520; -; 1.
DR   InterPro; IPR008922; Di-copper_centre_dom_sf.
DR   InterPro; IPR013788; Hemocyanin/hexamerin.
DR   InterPro; IPR000896; Hemocyanin/hexamerin_mid_dom.
DR   InterPro; IPR005203; Hemocyanin_C.
DR   InterPro; IPR037020; Hemocyanin_C_sf.
DR   InterPro; IPR005204; Hemocyanin_N.
DR   InterPro; IPR036697; Hemocyanin_N_sf.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR002227; Tyrosinase_Cu-bd.
DR   PANTHER; PTHR11511; PTHR11511; 1.
DR   Pfam; PF03723; Hemocyanin_C; 1.
DR   Pfam; PF00372; Hemocyanin_M; 1.
DR   Pfam; PF03722; Hemocyanin_N; 1.
DR   PRINTS; PR00187; HAEMOCYANIN.
DR   SUPFAM; SSF48050; SSF48050; 1.
DR   SUPFAM; SSF48056; SSF48056; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   PROSITE; PS00209; HEMOCYANIN_1; 1.
DR   PROSITE; PS00210; HEMOCYANIN_2; 1.
DR   PROSITE; PS00498; TYROSINASE_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Copper; Direct protein sequencing; Disulfide bond;
KW   Metal-binding; Oxygen transport; Phosphoprotein; Secreted; Transport.
FT   CHAIN           1..626
FT                   /note="Hemocyanin AA6 chain"
FT                   /id="PRO_0000204253"
FT   BINDING         170
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         174
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         201
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305"
FT   BINDING         321
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         325
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         361
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         374
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   626 AA;  71786 MW;  E788136AE3DEF0D2 CRC64;
     TVADKQARLM PLFKHLTALT REKLPLDQRD ERLKGVGILP RGTLFSCFHA RHLAEATELY
     VALYGAKDFN DFIHLCEQAR QIVNEGMFVY AVSVAVLHRE DCKGITVPPI QEVFPDRFVP
     AETINRANKE ASNHPDQQSI VVEAEETGNI LDPEYKLSYF REDIGINAHH WHWHIVYPAT
     WNPTVMGKEK DRKGELFFYM HQQMCARYDS ERLSNGLQRM IPFHNFDEPL EGYAPHLTSL
     VSGLQYASRP EGYSIHDLSD VDVQDMVRWR ERILDAINMH YIVDKDNNKI PLDIEHGTDI
     LGDIIESSDE SKNVEYYGSL HNWGHVMMAN ITDPDHRFQE NPGVMSDTST SLRDPIFYRW
     HRFIDNIFQE HKKSFHPYTK EELSFPGVEV VGVSINSKTA NVITTLIKES LLELSHGINF
     GTDQSVKVKY HHLDHEPFTY NIVVENNSGA EKHSTVRIFL APKYDELNNK LEPDEQRRLF
     IELDKFFYTL TPGKNTIVRN HQDSSVTISK VRTFDQLGAG EGVSEDSTEY CSCGWPEHML
     IPRGSHKGME FELFVMLTDH DEDTVAGLSE NAVCSDAVSY CGARDDRYPD KKAMGFPFDR
     KIEARTAAEF LTPNMGLTDI KIKFHG