ID   HCYB_APHSP              Reviewed;         627 AA.
AC   Q9NFH9;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Hemocyanin B chain;
DE            Short=HcB;
GN   Name=HCB;
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; AJ290429; CAB89498.1; -; mRNA.
DR   AlphaFoldDB; Q9NFH9; -.
DR   SMR; Q9NFH9; -.
DR   PRIDE; Q9NFH9; -.
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..627
FT                   /note="Hemocyanin B chain"
FT                   /id="PRO_0000204266"
FT   BINDING         173
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         177
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         204
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         324
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         328
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         364
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        312
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        316
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        534..582
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   627 AA;  72098 MW;  5B715F11D3FA1FAF CRC64;
     MPSTAEKQRR ILPFFQFTSL STKDKFGILV QRDPRLAGLG VLGRGVLFSC FHEEHLKEAT
     QLYEVLIECE SFEEFLDLCH QAREYVNEGL YVYAVSVAIL HRQDCRGVSL PPVQEVFPDK
     FVPSETLFKA FKEVRLHPDD EEIIVDIEKT GNVKDPEYNL AYYREDIGVN AHHWHWHLVY
     PATWRPEVVH RIKDRKGELF FYMHQQMCAR YDSERLSNGM APMVPFHNFH EPMEGYSSHL
     SSGINGMPYA FRPHGRILKD MREVSVQDLE RSRERLLDAI NLGYVVDPNG LETPLDELHG
     IDILGAIVES SNDSVNKSYY GSLHNWGHVI MSAVDDPDGR YQLNPGVMSD TATSLRDPIF
     YRWHRFIDDM FQEYKKSLTP YSSQLQFKGV IVKSVCVRAK TADVVETTFA NALLDISHAF
     NFGRTGPVKV RYNHLTHEPF TYKIVVDNAG TKTRKATVRI FLGPEHDNLG NEFDIGRLRR
     LMIELDKFTT VLEPGENVIE RDSIDSSVTI REQYTYRQLQ DGRSNREQTE YCSCGWPNDL
     LVPKGNEHGM KFRLFVMLTD AVQGQVGDHG ATGLCTDAVS YCGAKDQLYP DRYPMGFPFD
     RDIKADSIPE WLHPNMHFSE VTITHHQ