ID   HCYA_ENTDO              Reviewed;        1233 AA.
AC   P12659; Q25585;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 2.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Hemocyanin A-type, units Ode to Odg;
DE   Flags: Fragment;
OS   Enteroctopus dofleini (North Pacific giant octopus) (Octopus dofleini).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC   Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Enteroctopus.
OX   NCBI_TaxID=267067;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-834.
RX   PubMed=1898774; DOI=10.1073/pnas.88.1.244;
RA   Lang W.H., van Holde K.E.;
RT   "Cloning and sequencing of Octopus dofleini hemocyanin cDNA: derived
RT   sequences of functional units Ode and Odf.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:244-248(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 835-1233.
RX   PubMed=3207675; DOI=10.1021/bi00419a015;
RA   Lang W.H.;
RT   "cDNA cloning of the Octopus dofleini hemocyanin: sequence of the carboxyl-
RT   terminal domain.";
RL   Biochemistry 27:7276-7282(1988).
CC   -!- FUNCTION: Hemocyanins are copper-containing oxygen carriers occurring
CC       freely dissolved in the hemolymph of many mollusks and arthropods.
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC       Note=Binds 2 copper ions per heterodimer.;
CC   -!- SUBUNIT: Decamers of large identical subunits (350 kDa), each
CC       containing 7 globular oxygen-binding domains: ODA, ODB, ODC, ODD, ODE,
CC       ODF, and ODG.
CC   -!- SIMILARITY: Belongs to the tyrosinase family. Hemocyanin subfamily.
CC       {ECO:0000305}.
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DR   EMBL; M57288; AAA29391.1; -; mRNA.
DR   EMBL; J02835; AAA29390.1; -; mRNA.
DR   PIR; A31137; A31137.
DR   PIR; S13442; S13442.
DR   AlphaFoldDB; P12659; -.
DR   SMR; P12659; -.
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; -; 3.
DR   Gene3D; 2.60.310.10; -; 3.
DR   InterPro; IPR008922; Di-copper_centre_dom_sf.
DR   InterPro; IPR028999; Haemocyanin_beta-sandwich.
DR   InterPro; IPR036848; Haemocyanin_C_sf.
DR   InterPro; IPR002227; Tyrosinase_Cu-bd.
DR   Pfam; PF14830; Haemocyan_bet_s; 3.
DR   Pfam; PF00264; Tyrosinase; 4.
DR   PRINTS; PR00092; TYROSINASE.
DR   SUPFAM; SSF48056; SSF48056; 3.
DR   SUPFAM; SSF81277; SSF81277; 3.
DR   PROSITE; PS00497; TYROSINASE_1; 3.
DR   PROSITE; PS00498; TYROSINASE_2; 3.
PE   2: Evidence at transcript level;
KW   Copper; Disulfide bond; Glycoprotein; Metal-binding; Oxygen transport;
KW   Repeat; Thioether bond; Transport.
FT   CHAIN           <1..1233
FT                   /note="Hemocyanin A-type, units Ode to Odg"
FT                   /id="PRO_0000204300"
FT   REGION          <1..4
FT                   /note="ODD"
FT   REGION          5..422
FT                   /note="ODE"
FT   REGION          423..839
FT                   /note="ODF"
FT   REGION          840..1233
FT                   /note="ODG"
FT   BINDING         45
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250"
FT   BINDING         65
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250"
FT   BINDING         74
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250"
FT   BINDING         186
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250"
FT   BINDING         190
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250"
FT   BINDING         217
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250"
FT   BINDING         463
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250"
FT   BINDING         481
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250"
FT   BINDING         490
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250"
FT   BINDING         599
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250"
FT   BINDING         603
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250"
FT   BINDING         630
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250"
FT   BINDING         880
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250"
FT   BINDING         899
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250"
FT   BINDING         908
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250"
FT   BINDING         1008
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250"
FT   BINDING         1012
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250"
FT   BINDING         1039
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        392
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        538
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        890
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        51..62
FT                   /evidence="ECO:0000250"
FT   DISULFID        176..243
FT                   /evidence="ECO:0000250"
FT   DISULFID        334..340
FT                   /evidence="ECO:0000250"
FT   DISULFID        468..478
FT                   /evidence="ECO:0000250"
FT   DISULFID        589..656
FT                   /evidence="ECO:0000250"
FT   DISULFID        743..748
FT                   /evidence="ECO:0000250"
FT   DISULFID        886..896
FT                   /evidence="ECO:0000250"
FT   DISULFID        998..1065
FT                   /evidence="ECO:0000250"
FT   DISULFID        1152..1158
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        63..65
FT                   /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        479..481
FT                   /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        897..899
FT                   /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   1233 AA;  141524 MW;  90B6C6063C95D524 CRC64;
     EGNEYLVRKN VERLSLSEMN SLIHAFRRMQ KDKSSDGFEA IASFHALPPL CPSPTAKHRH
     ACCLHGMATF PHWHRLYVVQ FEQALHRHGA TVGVPYWDWT RPISKIPDFI ASEKYSDPFT
     KIEVYNPFNH GHISFISEDT TTKREVSEYL FEHPVLGKQT WLFDNIALAL EQTDYCDFEI
     QLEIVHNAIH SWIGGKEEHS LNHLHYAAYD PIFYLHHSNV DRLWVIWQEL QKLRGLNAYE
     SHCALELMKV PLKPFSFGAP YNLNDLTTKL SKPEDMFRYK DNFHYEYDIL DINSMSINQI
     ESSYIRHQKD HDRVFAGFLL SGFGSSAYAT FEICIEGGEC HEGSHFAVLG GSTEMPWAFD
     RLYKIEITDV LSDMHLAFDS AFTIKTKIVA QNGTELPASI LPEATVIRIP PSKQDADIDI
     PLNHIRRNVE SLDERDIQNL MAALTRVKKD ESDHGFQTIA SYHGSTLCPS PEEPKYACCL
     HGMPVFPHWH RVYLLHFEDS MRRHGSSVAT PYWDWTQPGT KLPRLLADSD YYDAWTDNVT
     ENPFLRGYIT SEDTYTVRDV KPELFEIGGG EGSTLYQQVL LMLEQEDYCD FEVQFEVVHN
     SIHYLVGGHQ KYAMSSLVYS SFDPIFYVHH SMVDRLWAIW QALQEHRHLP FDKAYCALEQ
     LSFPMKPFVW ESNPNLHTRA ASTPQHLFDY NKLGYKYDDL EFHGMNIDQL ENAIHKTQNK
     DRVFASFLLF GIKTSADVHL KLCKDETCED AGVVFVLGGD NEMPWPFDRT YKMDITNVLH
     KMHIPLEDLY VHGSTIHLEV KIESVDGKVL DSSSLPVPSM IYVPAKEFTK EIEKEAVRGT
     IIRKNVNSLT PSDIKELRDA MAKVQADTSD NGYQKIASYH GIPLSCHYEN GTAYACCQHG
     MVTFPNWHRL LTKQMEDALV AKGSHVGIPY WDWTTTFANL PVLVTEEKDN SFHHAHIDVA
     NTDTTRSPRA QLFDDPEKGD KSFFYRQIAL ALEQTDFCDF EIQFEIGHNA IHSWVGGSSP
     YGMSTLHYTS YDPLFYLHHS NTDRIWSVWQ ALQKYRGLPY NTANCEINKL VKPLKPFNLD
     TNPNAVTKAH STGATSFDYH KLGYDYDNLN FHGMTIPELE EHLKEIQHED RVFAGFLLRT
     IGQSADVNFD VCTKDGECTF GGTFCILGGE HEMFWAFDRP FKYDITTSLK HLRLDAHDDF
     DIKVTIKGID GHVLSNKYLS PPTVFLAPAK TTH