ID   HCYG_APHSP              Reviewed;         629 AA.
AC   Q9NFL4;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Hemocyanin G chain;
DE            Short=HcG;
GN   Name=HCG;
OS   Aphonopelma sp. (American tarantula).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Mygalomorphae; Theraphosidae; Aphonopelma; unclassified Aphonopelma.
OX   NCBI_TaxID=29932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Heart;
RX   PubMed=10961996; DOI=10.1074/jbc.m005442200;
RA   Voit R., Feldmaier-Fuchs G., Schweikardt T., Decker H., Burmester T.;
RT   "Complete sequence of the 24-mer hemocyanin of the tarantula Eurypelma
RT   californicum. Structure and intramolecular evolution of the subunits.";
RL   J. Biol. Chem. 275:39339-39344(2000).
CC   -!- FUNCTION: Hemocyanins are copper-containing oxygen carriers occurring
CC       freely dissolved in the hemolymph of many mollusks and arthropods.
CC   -!- SUBUNIT: Tarantula hemocyanin is a 24-chain polymer with seven
CC       different chains identified.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC   -!- TISSUE SPECIFICITY: Hemolymph.
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   EMBL; AJ277492; CAB89497.1; -; mRNA.
DR   AlphaFoldDB; Q9NFL4; -.
DR   SMR; Q9NFL4; -.
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   2: Evidence at transcript level;
KW   Copper; Disulfide bond; Glycoprotein; Metal-binding; Oxygen transport;
KW   Secreted; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..629
FT                   /note="Hemocyanin G chain"
FT                   /id="PRO_0000204271"
FT   BINDING         171
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         175
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         202
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         322
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         326
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         362
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        447
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        506
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        615
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        534..582
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   629 AA;  71811 MW;  0B3E2F117A9FFD56 CRC64;
     MASIPEKQAL ILPLFEKLTS LTKETPPRAQ WDPRLAGVGV LPRGTLFSCF HEKHLLEATK
     LFKVLYSPES FNDFLQLARE ARVVVNEGLF AYAFSVAVIH RDDCKGVTLP PIQEVFPDRF
     VPSETINLAM KEAKNDPNSD IVVDVQETGN ILDPEYKLAY FREDIGANAH HWYWHVVYPA
     NWDAVFTGKT KDRKGELFYY MHQQMCARYD CERLSNGLTR MIPFHNFKEK LEGYAPHLTS
     LVSGLHYASR PAGLCLRDLS ELEVQDVERW RDRILDAYHL NHVHDRENND VVLDAEHGAD
     ILGAIIESSS DSVNRRFYGS LHNWGHVMMA RMTDPDRSFE ENPGVMSDTS TSLRDPIFYR
     WHRFVDNIFQ EYKATLPSYT ADDLNFPGLR IVSVQVNAKS QNRVRTFLKQ EELVLSHGIN
     FGTEHTVKVH YNHLDHEPFS YTINVDNSSG AVKHATVRIF LGPKCDELGN ILEPNEQRRL
     FIELDKFHKE LGPGLNTINR NSVESNVTVA HTYTFDELRE GKLAPEDATE YCNCGWPRHM
     LIPKGTHRGM EFQLFVMLTD YTVDNPCGGA GKIVCADAVS YCGAKDQKYP DTKPMGFPFD
     RPTKIHTAEE ILTPNMSLTD VVIQYVGHE