ID   HCYC_APHSP              Reviewed;         629 AA.
AC   Q9NFL6;
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 C chain;
DE            Short=HcC;
GN   Name=HCC;
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; AJ277489; CAB89495.1; -; mRNA.
DR   AlphaFoldDB; Q9NFL6; -.
DR   SMR; Q9NFL6; -.
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 C chain"
FT                   /id="PRO_0000204267"
FT   BINDING         175
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         179
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         206
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
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         330
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         366
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        451
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        618
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        537..585
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   629 AA;  72567 MW;  312F9245ED0CC558 CRC64;
     MPSDANEMQA RLLQLFEHST LSTKAKFGLR VIRDPKLAGI GILGRGKIFS CFHEDHLEEA
     SRLAEVLVGA ETFDEFIDLC HQCRDFVNEA LFVYSLSVAI LHRPDCHGIS LPPIQEIFPD
     KFVPVETIYK AFKEATRHAD KTDDIIVDME ATGTIMDPEY NLAYYREDIG INAHHWHWHV
     VYPSAWDSVK MHMRKDRKGE LFFYMHQQMC ARYDCERLSN GLARMIPFHN FHEPLEGYNP
     HLSSTQNGLP YAFRPEPMTL CDMHDVSVQD LERWRERILD AINLGEVTDP NGDEYALDET
     FGIDVLGAII ESSRDSKNRE SYGSLHNWGH VLMANIVDPD GKYQTNPGVM DDTATSLRDP
     IFYRWHRFID DMFQEFKRKL KPYTKDQLSF TGVEIKNVKV HAHEENVITT TFVEDLLEIS
     NAFNFGRTGA VKVRYQHLDH EPFVYDIEVE NHSARLRHGT CRIFLAPVHD ELQNQLTPEE
     LRRLMIELDR FRVELKPGVN HNHRHSRDSS VTISKQPKFD ELLKGKGTNN ANEYCSCGWP
     DHLLVPKGND RGMPFHLCVM ITDYLYDLVG DYGYDTPCVD AVSYCGAKDS LYPDRRAMGF
     PFDRPIPEGH ASNLHQPNVS FSQIKIQHH