HCYB_SCUCO
ID HCYB_SCUCO Reviewed; 659 AA.
AC Q8IFJ8;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Hemocyanin subunit B;
DE Flags: Precursor;
GN Name=HCB;
OS Scutigera coleoptrata (House centipede).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC Notostigmophora; Scutigeromorpha; Scutigeridae; Scutigera.
OX NCBI_TaxID=29022 {ECO:0000312|EMBL:CAD55132.1};
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 D.
CC {ECO:0000305}.
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DR EMBL; AJ512793; CAD55132.1; -; mRNA.
DR AlphaFoldDB; Q8IFJ8; -.
DR SMR; Q8IFJ8; -.
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..659
FT /note="Hemocyanin subunit B"
FT /id="PRO_0000013346"
FT BINDING 198
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:P10787"
FT BINDING 202
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:P10787"
FT BINDING 232
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:P10787"
FT BINDING 353
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
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 393
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P10787"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 562..609
FT /evidence="ECO:0000250|UniProtKB:P10787"
FT CONFLICT 21
FT /note="C -> E (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 659 AA; 75565 MW; D0B41C410069A467 CRC64;
MVAKWCVLAM CLLVAVGADK CPRATDQEAK QKRMLEVLQH VNKPYVAETK DPKIPAGSED
VFKHLGILEK HEVFSLFDER QWDEATTAAV YMLTAPSFDE FIDRAEIVRH RINEDMFYYA
FSVAAVHRDD TRGINLPRIH EIYPDKFLKH KVIVEVKNSI NSGQEDPLID ATHEFTDLRD
PNSKLHYFLE DVGLNSHHYH WHVIHPAVWQ ESLEELTHQH KDRKGELFYF MHHQMVNRYD
AERLSNGLPR STTFENWNDP IETGYAPHLT IDRTGYRYQF RPDNLVVRDL PELTKNHMRQ
WRDRILYAVH RGEALAANGS SVSLRDERGI DVLGNMVESS LQSINRPFYG NVHCYAHVIA
ARIADPDGKY GEDNGAMYDV ATSARDPLFY QWHKFIDNLF HEYKDALKAY SSEDLTYNDI
TIEEVNVQGE GGSPANTVTT FLENSIVHLD EGFSFTARGH ARVKVQHLQH EGFNYQIKVN
NAGGEHKVVF RVFLAPKYDE EHHEFDFNEQ RGMAIELDKF VATVPAGSST VEQHSSKSSV
TQSNDNFYGS SATRSSENHC SCGWPDYLLI PKGNHQGVQF NVYVIATSYD EDHVESDESC
HCGDSLSYCG ALYDKYPDRR PMGYPFDRHA DAQTFDEFKT KNMNSVTVTI KHTGEVKDA
