ID   HCYX_SCUCO              Reviewed;         685 AA.
AC   Q8T116;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Hemocyanin subunit X;
DE   Flags: Precursor;
GN   Name=HCX; Synonyms=HC3;
OS   Scutigera coleoptrata (House centipede).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC   Notostigmophora; Scutigeromorpha; Scutigeridae; Scutigera.
OX   NCBI_TaxID=29022 {ECO:0000312|EMBL:CAD24085.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12823556; DOI=10.1046/j.1432-1033.2003.03664.x;
RA   Kusche K., Hembach A., Hagner-Holler S., Gebauer W., Burmester T.;
RT   "Complete subunit sequences, structure and evolution of the 6 x 6-mer
RT   hemocyanin from the common house centipede, Scutigera coleoptrata.";
RL   Eur. J. Biochem. 270:2860-2868(2003).
CC   -!- FUNCTION: Hemocyanins are copper-containing oxygen carriers occurring
CC       freely dissolved in the hemolymph of many mollusks and arthropods.
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the tyrosinase family. Hemocyanin subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AJ431378; CAD24085.1; -; mRNA.
DR   AlphaFoldDB; Q8T116; -.
DR   SMR; Q8T116; -.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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; Signal; Transport.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..685
FT                   /note="Hemocyanin subunit X"
FT                   /id="PRO_0000013349"
FT   BINDING         210
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:P10787"
FT   BINDING         214
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:P10787"
FT   BINDING         243
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:P10787"
FT   BINDING         367
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P10787"
FT   BINDING         371
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P10787"
FT   BINDING         407
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P10787"
FT   CARBOHYD        329
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   DISULFID        577..625
FT                   /evidence="ECO:0000250|UniProtKB:P10787"
SQ   SEQUENCE   685 AA;  79888 MW;  EC6EAF0DC04207DF CRC64;
     MKYCTESLIL ILAVIGCISA AINFKCPKGT AEEKHQKEIY DLVQRINRPL IPQFKEPNFP
     TSFLIKGKDP KEFFQAIGHL PKKEVFSLFD ERHWDEAMTA YEYLYEAETL DDFIDIAKIL
     YLHLNEDMFY YVFSFAVLYR KDTRNVRLPQ VHDVYPDKFL KTDIINKIKQ ANYQGKQHPV
     IDATKEFHDL RNPVSYLHYF LEDIGMNSHH YHWHVMNSAL RKAYPTEGEK KFYRKGELFY
     HMHHQMLNRY ELERLSNGLP RCPTFENWDD PIAEGYASHL AVDRTGYRYT FRPDNLHVRD
     LPELTKDNMR VWRDRIFDAA TSCSVLRENG SFVKICRTRF YGGLNILGNL IESNLRSINR
     MFYGNIHCYA HVIAARVTDP DGKYGQGNGV MYDVATSARD PLFYQWHKFL DHFFYEHLTK
     LPTNHLFHLQ NPDVSITNLE IISNGRKNEI HTFWENDIME ISKGHSFTLN SDAKVKIQHL
     QHEKFEIHLT VQNDKGEDTD LFVRIFLLPL EDEESHELSL EEMVRMAVDI EKRVIPAKPG
     SNDIVISSRS IGAPANKFFG SFEERYISED CNFHSHCGWP NYLLVPKGSS QGTPFAFVVM
     LTLAEDDFTP NMDDTCFCAD SWSHCGSLFI QYPENVEMGF PFQPIIECTK EEFFALPNIA
     KQEVIIKFTG ETKDSPLVIQ LENDS