ID   HCYD_SCUCO              Reviewed;         668 AA.
AC   Q95P07;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Hemocyanin subunit D;
DE   Flags: Precursor;
GN   Name=HCD; Synonyms=HC2;
OS   Scutigera coleoptrata (House centipede).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC   Notostigmophora; Scutigeromorpha; Scutigeridae; Scutigera.
OX   NCBI_TaxID=29022 {ECO:0000312|EMBL:CAC69247.1};
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; AJ344360; CAC69247.1; -; mRNA.
DR   AlphaFoldDB; Q95P07; -.
DR   SMR; Q95P07; -.
DR   PRIDE; Q95P07; -.
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..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..668
FT                   /note="Hemocyanin subunit D"
FT                   /id="PRO_0000013348"
FT   BINDING         206
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:P10787"
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         236
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:P10787"
FT   BINDING         357
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P10787"
FT   BINDING         361
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P10787"
FT   BINDING         397
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P10787"
FT   CARBOHYD        322
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   DISULFID        567..614
FT                   /evidence="ECO:0000250|UniProtKB:P10787"
SQ   SEQUENCE   668 AA;  76841 MW;  FA20BFEBD7B9FD51 CRC64;
     MDTRVLRLTL ALVALSGVLA DSESCSSAIV NDYKLKQKEI QHLVDTINKP VYPDFKDTRG
     IIDESKLKGL GTLPRREVFS LFDERNWAEA AKVVELLLEP KTFREFIHLA DIIHHRVNED
     LFLYALSVAI AHRPDCQGVQ VPRVLDIYPD KFLRKEVIHK IKEVSNEGAY LDKVPVIDAT
     EVSDNHLDPN QELLYFLEDL GMNSHHHHWH VIHPAIWLPK HGGVKDRKGE LFFYMHKQMV
     ARYDTERLSN DLPRVRPFEN WNDPIDEGYS PHLIIDKTGY KYAYRPQGVI VHDLPNLPKT
     KMFEWKNRIM VGIRKGSLIS ANKTQVPLNN DHGIDLLGDV VESSLLSVNR VFYGNLHCYA
     HVIAGKVTDP QSTYGEKNGA MYDVATSARD PLFYSWHKFI DNIFQEHKET LQPYNKDELN
     FPDVQVDSLR INVANGTYEN IVRTYWQNSL FKIAKGFTFT TEGSVLVKVK HLNHETFYYN
     LEVTNNALEE KHGVVRIFGA VINDERGHPY ILNDQRHLVI ELDKFTVNLK PGKNSVRQPC
     YNSAVTAKYD VFYGDVESQK PQEGCNCGWP DYMLLPKGKY EGLRFRVFAI VTNHDEDKVS
     DQETCLCGDA VAYCGAHNQK YPDKKPMGFP FDRRIDERTF EHFHTPNMIA TDVIIKFTGE
     FLPPKGDI