ID   HCYC_SCUCO              Reviewed;         673 AA.
AC   Q8T115;
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 C;
DE   Flags: Precursor;
GN   Name=HCC; Synonyms=HC4;
OS   Scutigera coleoptrata (House centipede).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC   Notostigmophora; Scutigeromorpha; Scutigeridae; Scutigera.
OX   NCBI_TaxID=29022 {ECO:0000312|EMBL:CAD24086.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
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   -!- SUBUNIT: 36-chain polymer consisting of 6 hexamers, each of which
CC       includes 4 different chains, A, B, C and D.
CC       {ECO:0000269|PubMed:12823556}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC       {ECO:0000269|PubMed:12823556}.
CC   -!- TISSUE SPECIFICITY: Hemolymph. {ECO:0000269|PubMed:12823556}.
CC   -!- SIMILARITY: Belongs to the tyrosinase family. Hemocyanin subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AJ431379; CAD24086.1; -; mRNA.
DR   AlphaFoldDB; Q8T115; -.
DR   SMR; Q8T115; -.
DR   GO; GO:0005576; C:extracellular region; IDA: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; PS00209; HEMOCYANIN_1; 1.
DR   PROSITE; PS00210; HEMOCYANIN_2; 1.
DR   PROSITE; PS00498; TYROSINASE_2; 1.
PE   1: Evidence at protein 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..673
FT                   /note="Hemocyanin subunit C"
FT                   /id="PRO_0000013347"
FT   BINDING         207
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:P10787"
FT   BINDING         211
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:P10787"
FT   BINDING         237
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:P10787"
FT   BINDING         358
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P10787"
FT   BINDING         362
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P10787"
FT   BINDING         398
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P10787"
FT   CARBOHYD        323
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   DISULFID        568..616
FT                   /evidence="ECO:0000250|UniProtKB:P10787"
SQ   SEQUENCE   673 AA;  78098 MW;  F66B7E64C57D7E55 CRC64;
     MGAWKVWTFF AIALVVAVKA YDEEAKCMSH DEDSQVKERQ ILHIVDSINK PISPDFRAPR
     GVIDEHKLRG LGTLKKREIF SLFDERNWDE ASKVVRLLLD AKDFDDFIDV AEVIRLRVNE
     ELFLYAFSVA VMHRGDTQGL QVPRIHDIFP DKFLKEDVIH RLLELSNRGE HYDRIPIIDA
     TQISHNYLDP NSELEYFLED LGLNSHHHHW HVIHPAIWVS ELGNEKDRKG EFFYWMHHQM
     LARYEAERMS NGLARTRTFQ NWNDPIDEGY APHISIMKTG YTYAYRPPGY TLRDLPNLPK
     NKMVEWAKRV LYSIHSGIFH FSNGTDAHLD TEHGIDELGN IVESSLTSLN RDYYGNLHCY
     AHVIAGRIAD PEGKYGEDNG VMYDVATSAR DPLFYRWHKY IDNIFQEYKN TLPPYTTEEL
     TPQNSEFRVQ GISVVGETSA RDTVHTYWQH SLLKVGQGFE FTKHTPAYVK VKHLQHESFT
     YVIDVENRGR TRTGFFRIFA APKYNELGQK WHINDQRLIM VEMDKFIEKL YPGKNTIERH
     SEDSTVTMSS ASIFSDISSE QSEDHCSCGW PDYLLVPKGN FEGFPMEVFV IVTDYEEDKV
     EGPDEGCACH DALTYCGGID YHFPDKRAMG FPFDRPIKQR NFNAFKTKNM GKVTVDVKFT
     GETIAPEDFH NQH