HCYA_APHSP
ID HCYA_APHSP Reviewed; 631 AA.
AC P14750;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Hemocyanin A chain;
DE Short=HcA;
GN Name=HCA;
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].
RX PubMed=2246235; DOI=10.1016/s0021-9258(17)45393-2;
RA Voit R., Feldmaier-Fuchs G.;
RT "Arthropod hemocyanins. Molecular cloning and sequencing of cDNAs encoding
RT the tarantula hemocyanin subunits a and e.";
RL J. Biol. Chem. 265:19447-19452(1990).
RN [2]
RP PROTEIN SEQUENCE OF 2-631.
RX PubMed=2222854; DOI=10.1515/bchm3.1990.371.2.557;
RA Schartau W., Metzger W., Sonner P., Geisert H., Storz H.;
RT "Hemocyanins in spiders, XXIII. Complete amino-acid sequence of subunit a
RT of Eurypelma californicum hemocyanin.";
RL Biol. Chem. Hoppe-Seyler 371:557-565(1990).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X16893; CAA34771.1; -; mRNA.
DR AlphaFoldDB; P14750; -.
DR SMR; P14750; -.
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:2222854"
FT CHAIN 2..631
FT /note="Hemocyanin A chain"
FT /id="PRO_0000204265"
FT BINDING 175
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 179
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 206
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 326
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 330
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 366
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 621
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 538..586
FT /evidence="ECO:0000250"
SQ SEQUENCE 631 AA; 72318 MW; 5A0C2496208963AA CRC64;
MTILHDKQVQ ALKLFEKLSV AATGEPVPAD QIDERLRNIT TLGPNEFFSC FYPDHLEQAK
RVYEVFCHAA NFDDFVSLAK QARSFMNSTL FAFSAEVALL HREDCRGVIV PPVQEVFADR
FIPADSLIKA FTLATTTQPG DESDIIVDVK DTGNILDPEY KLAYFREDIG VNAHHWHWHV
VYPSTYDPAF FGKVKDRKGE LFYYMHQQMC ARYDCERLSN GLNRMIPFHN FNEPLGGYAA
HLTHVASGRH YAQRPDGLAM HDVREVDVQD MERWTERIME AIDLRRVISP TGEYIPLDEE
HGADILGALI ESSYESKNRG YYGSLHNWGH VMMAYIHDPD GRFRETPGVM TDTATSLRDP
IFYRYHRFID NVFQEYKKTL PVYSKDNLDF PQVTITDVKV KAKIPNVVHT FIREDELELS
HCLHFAKPGS VRARYHHLDH ESFSYIISAQ NNSNADKQAT VRIFLAPTYD ELGNDISLDE
QRRLYIEMDK FYHTLRPGKN TIVRSSTDSS VTLSSVHTFK ELLRGEDLVE GQTEFCSCGW
PQHLLVPKGN EKGMQFDLFV MLTDASVDRV QSGDGTPLCA DALSYCGVLD QKYPDKRAMG
YPFDRKITAD THEEFLTGNM NISHVTVRFQ D
