HCYD_APHSP
ID HCYD_APHSP Reviewed; 627 AA.
AC P02241; Q9NFH8;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Hemocyanin D chain;
DE Short=HcD;
GN Name=HCD;
OS Aphonopelma sp. (American tarantula).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC Mygalomorphae; Theraphosidae; Aphonopelma; unclassified Aphonopelma.
OX NCBI_TaxID=29932;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=10961996; DOI=10.1074/jbc.m005442200;
RA Voit R., Feldmaier-Fuchs G., Schweikardt T., Decker H., Burmester T.;
RT "Complete sequence of the 24-mer hemocyanin of the tarantula Eurypelma
RT californicum. Structure and intramolecular evolution of the subunits.";
RL J. Biol. Chem. 275:39339-39344(2000).
RN [2]
RP PROTEIN SEQUENCE OF 2-627.
RX PubMed=6642428; DOI=10.1515/bchm2.1983.364.2.1383;
RA Schartau W., Eyerle F., Reisinger P., Geisert H., Storz H., Linzen B.;
RT "Hemocyanins in spiders, XIX. Complete amino-acid sequence of subunit d
RT from Eurypelma californicum hemocyanin, and comparison to chain e.";
RL Hoppe-Seyler's Z. Physiol. Chem. 364:1383-1409(1983).
CC -!- FUNCTION: Hemocyanins are copper-containing oxygen carriers occurring
CC freely dissolved in the hemolymph of many mollusks and arthropods.
CC -!- SUBUNIT: Tarantula hemocyanin is a 24-chain polymer with seven
CC different chains identified.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- TISSUE SPECIFICITY: Hemolymph.
CC -!- MISCELLANEOUS: The two copper ions bound each have 3 nitrogen ligands
CC (presumably contributed by His residues) and share a bridging ligand
CC (possibly contributed by a Tyr residue) in addition to binding oxygen.
CC -!- SIMILARITY: Belongs to the tyrosinase family. Hemocyanin subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ290430; CAB89499.1; -; mRNA.
DR PIR; A02565; BHTLD.
DR AlphaFoldDB; P02241; -.
DR SMR; P02241; -.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0031404; F:chloride ion binding; ISS:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
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; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6642428"
FT CHAIN 2..627
FT /note="Hemocyanin D chain"
FT /id="PRO_0000204268"
FT BINDING 171
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 322
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 362
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 531..579
FT /evidence="ECO:0000250"
FT CONFLICT 47..48
FT /note="SC -> GS (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 58..66
FT /note="ETLAEALVE -> IVFIEIIHD (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="I -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="I -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="L -> I (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="V -> I (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="I -> F (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="I -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="L -> I (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="R -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="L -> I (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 299..302
FT /note="LNIL -> INVI (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="F -> Y (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 403..404
FT /note="LI -> IL (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 419..421
FT /note="INL -> LNI (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="Y -> YNY (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="I -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 531..533
FT /note="CGW -> DGK (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 562
FT /note="K -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 572..573
FT /note="CS -> DQ (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 627 AA; 72123 MW; B8C9E9D2960518F7 CRC64;
MTIADHQARI LPLFKKLTSL SPDPLPEAER DPRLKGVGFL PRGTLFSCFH EEHLAEAETL
AEALVEAKNF DDFIALATNA RAVVNEGLYA FAMSVAILSR DDCNGVVLPP IQEVFPDRFV
PAETINRALK VDKVSDPNKD TVVPIQKTGN IRDPEYNVAY FREDIGINSH HWHWHLVYPA
FYDADIFGKI KDRKGELFYY MHQQMCARYD CERLSVGLQR MIPFQNLDDE LEGYSPHLRS
LVSGLSYGSR PAGMHLRDIN DCSVQDMERW RERILDAIHT GLVTDSHGKE IKLTEENGLN
ILGALIESSH DSVNKPFYGT LHNWGHVMIA RIHDADGRYR TNPGVMDDTS TSLRDPIFYR
YHRWMDNIFQ EYKHRLPSYT HQQLDFPGVR ISRVTVRSKV PNLIHTYSKD SLLELSHGIN
LKGHIQVKYE HLDHEPYNYE IEVDNRTGEA RETCVRIFLA PKYDELGNRL ILEEQRRLYI
ELDKFHRRLE PGKNVLVRAS GDSSVTLSKV PTFEELESGN ANVNPNEYCS CGWPEHMLVP
RGKERGMDFY LFVMLTDYEE DKVQGAGEQT ICSDAVSYCG AKDQKYPDKK AMGYPFDRPI
QVRTPSQFKT PNMAFQEIII QYEGHKH
