HCYE_APHSP
ID HCYE_APHSP Reviewed; 624 AA.
AC P02242;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Hemocyanin E chain;
DE Short=HcE;
GN Name=HCE;
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 [GENOMIC DNA].
RX PubMed=2371273; DOI=10.1073/pnas.87.14.5312;
RA Voll W., Voit R.;
RT "Characterization of the gene encoding the hemocyanin subunit e from the
RT tarantula Eurypelma californicum.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:5312-5316(1990).
RN [2]
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 [3]
RP PROTEIN SEQUENCE OF 2-624.
RX PubMed=6357986; DOI=10.1515/bchm2.1983.364.2.1357;
RA Schneider H.-J., Drexel R., Feldmaier G., Linzen B., Lottspeich F.,
RA Henschen A.;
RT "Hemocyanins in Spiders, XVIII. Complete amino-acid sequence of subunit e
RT from Eurypelma californicum hemocyanin.";
RL Hoppe-Seyler's Z. Physiol. Chem. 364:1357-1381(1983).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 75-600.
RX PubMed=3017715; DOI=10.1111/j.1432-1033.1986.tb09828.x;
RA Voit R., Schneider H.-J.;
RT "Tarantula hemocyanin mRNA. In vitro translation, cDNA cloning and
RT nucleotide sequence corresponding to subunit e.";
RL Eur. J. Biochem. 159:23-29(1986).
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; X16894; CAA34772.1; -; mRNA.
DR EMBL; X04291; CAA27838.1; -; mRNA.
DR EMBL; X16650; CAA34643.1; -; Genomic_DNA.
DR EMBL; X16651; CAA34643.1; JOINED; Genomic_DNA.
DR EMBL; X16652; CAA34643.1; JOINED; Genomic_DNA.
DR EMBL; X16653; CAA34643.1; JOINED; Genomic_DNA.
DR EMBL; X16654; CAA34643.1; JOINED; Genomic_DNA.
DR EMBL; X16655; CAA34643.1; JOINED; Genomic_DNA.
DR EMBL; X16656; CAA34643.1; JOINED; Genomic_DNA.
DR EMBL; X16657; CAA34643.1; JOINED; Genomic_DNA.
DR PIR; S06701; BHTLE.
DR AlphaFoldDB; P02242; -.
DR SMR; P02242; -.
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:6357986"
FT CHAIN 2..624
FT /note="Hemocyanin E chain"
FT /id="PRO_0000204269"
FT BINDING 169
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 173
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 200
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 320
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 324
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 360
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 529..577
FT /evidence="ECO:0000250"
FT CONFLICT 30
FT /note="D -> R (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="C -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="R -> K (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="A -> H (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="Missing (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="K -> R (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="R -> H (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="H -> M (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="F -> H (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="M -> MK (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 529..531
FT /note="CGW -> DGK (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 562..564
FT /note="NGH -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 603
FT /note="F -> L (in Ref. 2; CAA34772/CAA34643)"
FT /evidence="ECO:0000305"
FT CONFLICT 609
FT /note="V -> P (in Ref. 2; CAA34772/CAA34643)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 624 AA; 71676 MW; 7D0BE0AC5BF95A72 CRC64;
MPDKQKQLRV ISLFEHMTSI NTPLPRDQID ARLHHLGRLP QGELFSCFHE EDLEEATELY
KILYTAKDFD EVINLAKQSR TFVNEGLFVY AVSVALLHRD DCKGIVVPAI QEIFPDRFVP
TETINLAVKE AANHPDQDIS VHVVETGNIL DEEYKLAYFK EDVGTNAHHW HWHIVYPATW
DPAFMGRMKD RKGELFYYMH QQMCARYDCE RLSNGMRRMI PFSNFDEKLE GYSAHLTSLV
SGLPYAFRPD GLCLHDLKDI DLKEMFRWRE RILDAIDSGY YIDNEGHQVK LDIVDGINVL
GALIESSFET KNKLYYGSLH NWGHVMMARL QDPDHRFNEN PGVMSDTSTS LRDPIFYRYH
RFIDNIFQKY IATLPHYTPE DLTCPGVHVV NVTVNAKVPN VVTTFMKEAE LELSYGIDFG
SDHSVKVLYR HLDHEPFTYN ISVENSSGGA KDVTMRIFLG PKYDELGNRL QPEQQRTLNI
ELDKFKATLD PGKNVVTRDH RNSTVTVEQS VPVKKLREEG GVAGEYCSCG WPEHMLIPKG
NHRGMDFELF VIVTDYAQDA VNGHGENAEC VDAVSYCGAK DQKYPDKKPM GFPFDRVIEG
LTFEEFLTVS MSCTDVRIKY TDIK
