HCYA_SCUCO
ID HCYA_SCUCO Reviewed; 656 AA.
AC Q95P08;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Hemocyanin subunit A;
DE Flags: Precursor;
GN Name=HCA; Synonyms=HC1;
OS Scutigera coleoptrata (House centipede).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC Notostigmophora; Scutigeromorpha; Scutigeridae; Scutigera.
OX NCBI_TaxID=29022 {ECO:0000312|EMBL:CAC69246.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-36, SUBUNIT, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Hemolymph {ECO:0000269|PubMed:12823556};
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}.
CC -!- CAUTION: PubMed:12823556 conflicts between the peptide sequence
CC obtained by Edman degradation and that obtained from the cDNA sequence
CC may be due to contamination of the peptide sample with hemocyanin C.
CC {ECO:0000305}.
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DR EMBL; AJ344359; CAC69246.1; -; mRNA.
DR AlphaFoldDB; Q95P08; -.
DR SMR; Q95P08; -.
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; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Metal-binding; Oxygen transport; Secreted; Signal; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:12823556"
FT CHAIN 19..656
FT /note="Hemocyanin subunit A"
FT /id="PRO_0000013345"
FT BINDING 197
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:P10787"
FT BINDING 201
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:P10787"
FT BINDING 227
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:P10787"
FT BINDING 348
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P10787"
FT BINDING 352
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P10787"
FT BINDING 388
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P10787"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 558..606
FT /evidence="ECO:0000250|UniProtKB:P10787"
FT CONFLICT 21
FT /note="C -> E (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="P -> A (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 656 AA; 76382 MW; 78F06FE39140AE07 CRC64;
MWSLALATLF VLGTVIRADQ CPPVPADTKD KLEKILELIG HVNRPLTPET PEPAGYDETK
LKGLGILPQH EIFSLFDERT WPEATKAAEF LMEATDFEHF IQRADVLRHR INEDMFMYAL
NVAVLHRKDT RGVQVPRIHK IYPDKFLKQD ILVEVREKVN HGEEKPVVDA TELHQNQLDP
NYRLSYFLED IGMNSHHYHW HVVHPAVWLP KHGPRKDRKG ELFYYMHHQM VARYDSERLS
NNLPRTEPFE NWDDPLEEGY APHLTIHKTG YNYMFRPEGL IVRDLPELNK NKMRQWKSRI
LHGIHLNVLY AENGTKISLD NEHGIDLLGD AIESSLLSVN RAFYGNIHCY AHVMAARIAD
PDGRYGEDNG VMHDVATSAR DPLFYRWHKF IDNIFLEYKD NLDPYTQYEL TWPDVVLNDV
TVKPHKGDYD DEVHTYWEVD NYELGKGFDY TRKTTATVKV RHLQHEDYHY EIDIDNNAGK
AKKAVFRIFL APKYNEKGEL FPVNEQRQLL VELDKFVATL EPGHNVIERQ SKESSVTMSK
DHVFGEIRNL ADDHQCSCGW PDYLLLPKGK YEGMTYQLFV VATDYEEDHV EDAGEECQCR
DSMSYCGSVE HKLPDNKPLG YPFDRRIDGT GFEEFKTQNM YYGDVVIQFT GETVTH
