ID   HCYF_APHSP              Reviewed;         629 AA.
AC   Q9NFL5;
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 F chain;
DE            Short=HcF;
GN   Name=HCF;
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; AJ277491; CAB89496.1; -; mRNA.
DR   AlphaFoldDB; Q9NFL5; -.
DR   SMR; Q9NFL5; -.
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 F chain"
FT                   /id="PRO_0000204270"
FT   REGION          503..522
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         172
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         176
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         203
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        395
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        447
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        527
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;  72149 MW;  8E9C881138F1CE11 CRC64;
     MTVQDKQRQI LPLFEHLTSL TRGGLDRTES DVRLRRVGRL PRGTLFSCFH SEHLKEATEL
     YQILYKADSF ADFIHLAQQA RDIVNEGLFV YSVSVAILHR DDCRGVTVPP IQEIFPDRFV
     PAETVNQAVK ADLKRQSSDE DVLVEIQETG NILDPEHKLA YFREDIGANA HHWHWHIVYP
     PTWDASVMSK VKDRKGELFY YMHQQMCARY DCDRLSTGLR RMIPFHNFDE KLEGYSPHLT
     SLVSGLNYAS RPAGLHLRDL VDFVDVQDMA RWRERLLYSI DIGHVIDHEG QEIPLDAEHG
     IDVLGALLES SHDSLNDDYY GNLHNSGHVM MARIHDPDGR FRENPGVMSD TSTSLRDPIF
     YRYHRFIDNI FQEYKATLPC YEKKDLEFSG VEIVNCTVNA KAPNVINTYM KESTLEMSHG
     ISFKGAVKVK YQHLDHDPFT YSISVENTTG DVKHATVRIF LGPTQDELGN RLRLNEQRRF
     YIELDKFHAE LAAGKNTITR KSSESSVTVS HTPTFEELQR GEGVDENTTE FCSCGWPEHL
     LVPRGTYKGM DFQLFVMLTD YEDDHVGSHN GQTLCADAVS YCGAKDSKYP DKRAMGFPFD
     RVIKARTVAD FRTTNMSFTD VKIQFKDQV