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Hemocyanin G-type, units Oda to Odg

 HCYG_ENTDO              Reviewed;        2896 AA.
O61363;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
10-MAY-2017, entry version 87.
RecName: Full=Hemocyanin G-type, units Oda to Odg;
Name=ODHCY;
Enteroctopus dofleini (North Pacific giant octopus) (Octopus
dofleini).
Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Cephalopoda; Coleoidea;
Neocoleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae;
Enteroctopus.
NCBI_TaxID=267067;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
TISSUE=Branchial gland;
PubMed=9614945; DOI=10.1006/jmbi.1998.1648;
Miller K.I., Cuff M.E., Lang W.F., Varga-Weisz P., Field K.G.,
van Holde K.E.;
"Sequence of the Octopus dofleini hemocyanin subunit: structural and
evolutionary implications.";
J. Mol. Biol. 278:827-842(1998).
[2]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF SUBUNIT ODG.
PubMed=9614947; DOI=10.1006/jmbi.1998.1647;
Cuff M.E., Miller K.I., van Holde K.E., Hendrickson W.A.;
"Crystal structure of a functional unit from Octopus hemocyanin.";
J. Mol. Biol. 278:855-870(1998).
-!- FUNCTION: Hemocyanins are copper-containing oxygen carriers
occurring freely dissolved in the hemolymph of many mollusks and
arthropods.
-!- COFACTOR:
Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
Note=Binds 2 copper ions per heterodimer.;
-!- SUBUNIT: Decamers of large identical subunits (350 kDa), each
containing 7 globular oxygen-binding functional units: ODA, ODB,
ODC, ODD, ODE, ODF, and ODG. Decamer formation requires the
presence of magnesium ions.
-!- SIMILARITY: Belongs to the tyrosinase family. Hemocyanin
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF020548; AAC39018.1; -; mRNA.
PIR; S13442; S13442.
PIR; T30939; T30939.
PDB; 1JS8; X-ray; 2.30 A; A/B=2503-2896.
PDBsum; 1JS8; -.
ProteinModelPortal; O61363; -.
SMR; O61363; -.
PRIDE; O61363; -.
EvolutionaryTrace; O61363; -.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
GO; GO:0005344; F:oxygen transporter activity; IEA:UniProtKB-KW.
Gene3D; 1.10.1280.10; -; 7.
Gene3D; 2.60.310.10; -; 7.
InterPro; IPR028999; Haemocyanin_beta-sandwich.
InterPro; IPR002227; Tyrosinase_Cu-bd.
InterPro; IPR008922; Unchr_di-copper_centre.
Pfam; PF14830; Haemocyan_bet_s; 7.
Pfam; PF00264; Tyrosinase; 7.
PRINTS; PR00092; TYROSINASE.
SUPFAM; SSF48056; SSF48056; 7.
SUPFAM; SSF81277; SSF81277; 7.
PROSITE; PS00497; TYROSINASE_1; 7.
PROSITE; PS00498; TYROSINASE_2; 6.
1: Evidence at protein level;
3D-structure; Copper; Disulfide bond; Glycoprotein; Metal-binding;
Oxygen transport; Repeat; Thioether bond; Transport.
CHAIN 1 2896 Hemocyanin G-type, units Oda to Odg.
/FTId=PRO_0000204301.
REGION 1 419 ODA.
REGION 420 834 ODB.
REGION 835 1254 ODC.
REGION 1255 1667 ODD.
REGION 1668 2085 ODE.
REGION 2086 2502 ODF.
REGION 2503 2896 ODG.
METAL 41 41 Copper A. {ECO:0000250}.
METAL 60 60 Copper A. {ECO:0000250}.
METAL 69 69 Copper A. {ECO:0000250}.
METAL 178 178 Copper B. {ECO:0000250}.
METAL 182 182 Copper B. {ECO:0000250}.
METAL 209 209 Copper B. {ECO:0000250}.
METAL 460 460 Copper A. {ECO:0000250}.
METAL 480 480 Copper A. {ECO:0000250}.
METAL 489 489 Copper A. {ECO:0000250}.
METAL 601 601 Copper B. {ECO:0000250}.
METAL 605 605 Copper B. {ECO:0000250}.
METAL 632 632 Copper B. {ECO:0000250}.
METAL 875 875 Copper A. {ECO:0000250}.
METAL 895 895 Copper A. {ECO:0000250}.
METAL 904 904 Copper A. {ECO:0000250}.
METAL 1013 1013 Copper B. {ECO:0000250}.
METAL 1017 1017 Copper B. {ECO:0000250}.
METAL 1044 1044 Copper B. {ECO:0000250}.
METAL 1292 1292 Copper A. {ECO:0000250}.
METAL 1312 1312 Copper A. {ECO:0000250}.
METAL 1321 1321 Copper A. {ECO:0000250}.
METAL 1425 1425 Copper B. {ECO:0000250}.
METAL 1429 1429 Copper B. {ECO:0000250}.
METAL 1456 1456 Copper B. {ECO:0000250}.
METAL 1708 1708 Copper A. {ECO:0000250}.
METAL 1728 1728 Copper A. {ECO:0000250}.
METAL 1737 1737 Copper A. {ECO:0000250}.
METAL 1849 1849 Copper B. {ECO:0000250}.
METAL 1853 1853 Copper B. {ECO:0000250}.
METAL 1880 1880 Copper B. {ECO:0000250}.
METAL 2126 2126 Copper A. {ECO:0000250}.
METAL 2144 2144 Copper A. {ECO:0000250}.
METAL 2153 2153 Copper A. {ECO:0000250}.
METAL 2262 2262 Copper B. {ECO:0000250}.
METAL 2266 2266 Copper B. {ECO:0000250}.
METAL 2293 2293 Copper B. {ECO:0000250}.
METAL 2543 2543 Copper A.
METAL 2562 2562 Copper A.
METAL 2571 2571 Copper A.
METAL 2671 2671 Copper B.
METAL 2675 2675 Copper B.
METAL 2702 2702 Copper B.
CARBOHYD 386 386 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 804 804 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1496 1496 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1634 1634 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2055 2055 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2201 2201 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2553 2553 N-linked (GlcNAc...) asparagine.
DISULFID 47 57 {ECO:0000250}.
DISULFID 168 234 {ECO:0000250}.
DISULFID 321 333 {ECO:0000250}.
DISULFID 466 477 {ECO:0000250}.
DISULFID 591 657 {ECO:0000250}.
DISULFID 881 892 {ECO:0000250}.
DISULFID 1003 1070 {ECO:0000250}.
DISULFID 1298 1309 {ECO:0000250}.
DISULFID 1415 1482 {ECO:0000250}.
DISULFID 1571 1581 {ECO:0000250}.
DISULFID 1714 1725 {ECO:0000250}.
DISULFID 1839 1906 {ECO:0000250}.
DISULFID 1997 2003 {ECO:0000250}.
DISULFID 2131 2141 {ECO:0000250}.
DISULFID 2252 2319 {ECO:0000250}.
DISULFID 2406 2411 {ECO:0000250}.
DISULFID 2549 2559
DISULFID 2661 2728
DISULFID 2815 2821
CROSSLNK 58 60 2'-(S-cysteinyl)-histidine (Cys-His).
{ECO:0000250}.
CROSSLNK 478 480 2'-(S-cysteinyl)-histidine (Cys-His).
{ECO:0000250}.
CROSSLNK 893 895 2'-(S-cysteinyl)-histidine (Cys-His).
{ECO:0000250}.
CROSSLNK 1310 1312 2'-(S-cysteinyl)-histidine (Cys-His).
{ECO:0000250}.
CROSSLNK 1726 1728 2'-(S-cysteinyl)-histidine (Cys-His).
{ECO:0000250}.
CROSSLNK 2142 2144 2'-(S-cysteinyl)-histidine (Cys-His).
{ECO:0000250}.
CROSSLNK 2560 2562 2'-(S-cysteinyl)-histidine (Cys-His).
STRAND 2504 2506 {ECO:0000244|PDB:1JS8}.
HELIX 2509 2511 {ECO:0000244|PDB:1JS8}.
HELIX 2514 2529 {ECO:0000244|PDB:1JS8}.
HELIX 2536 2540 {ECO:0000244|PDB:1JS8}.
TURN 2541 2543 {ECO:0000244|PDB:1JS8}.
STRAND 2544 2546 {ECO:0000244|PDB:1JS8}.
HELIX 2567 2584 {ECO:0000244|PDB:1JS8}.
HELIX 2605 2608 {ECO:0000244|PDB:1JS8}.
TURN 2621 2624 {ECO:0000244|PDB:1JS8}.
HELIX 2633 2635 {ECO:0000244|PDB:1JS8}.
HELIX 2646 2656 {ECO:0000244|PDB:1JS8}.
HELIX 2660 2679 {ECO:0000244|PDB:1JS8}.
TURN 2689 2691 {ECO:0000244|PDB:1JS8}.
HELIX 2692 2694 {ECO:0000244|PDB:1JS8}.
HELIX 2697 2719 {ECO:0000244|PDB:1JS8}.
STRAND 2727 2729 {ECO:0000244|PDB:1JS8}.
HELIX 2732 2734 {ECO:0000244|PDB:1JS8}.
TURN 2738 2741 {ECO:0000244|PDB:1JS8}.
HELIX 2748 2752 {ECO:0000244|PDB:1JS8}.
HELIX 2756 2758 {ECO:0000244|PDB:1JS8}.
HELIX 2762 2765 {ECO:0000244|PDB:1JS8}.
STRAND 2767 2770 {ECO:0000244|PDB:1JS8}.
HELIX 2779 2789 {ECO:0000244|PDB:1JS8}.
STRAND 2794 2799 {ECO:0000244|PDB:1JS8}.
STRAND 2808 2816 {ECO:0000244|PDB:1JS8}.
STRAND 2821 2829 {ECO:0000244|PDB:1JS8}.
STRAND 2844 2847 {ECO:0000244|PDB:1JS8}.
HELIX 2849 2854 {ECO:0000244|PDB:1JS8}.
STRAND 2863 2874 {ECO:0000244|PDB:1JS8}.
HELIX 2879 2881 {ECO:0000244|PDB:1JS8}.
STRAND 2886 2890 {ECO:0000244|PDB:1JS8}.
SEQUENCE 2896 AA; 331922 MW; BE1F35C8C987FBFC CRC64;
NLIRKDVDAL SEDEVLNLQV ALRAMQDDET PTGYQAIAAY HGEPADCKAP DGSTVVCCLH
GMPTFPLWHR LYTVQFEQTM VAHGSKLGVP YWDWTQPLNH LPELVSHPLF MDPTAHKAKK
NVFYSGDIAF EKKTTARAVD TRLFQASKGG KNFLLEGVLS ALEQDDYCHF EVQFEVAHNP
IHYLVGGRFT HSMSSLEYTS YDPLFFLHHS NVERLFTIWQ ALQKHRGLDG NANCGLNMFH
KPMEPFGRDT NPISLTKEHA KAVDVFNYNE LGYDYDDLHL NGMDIPELDT MLKERQQHPR
SFANFRLGGI KTSANVRVAV CIPSEDKRHS DNCNNHVGSF FILGGVHEMT WDFGYPFLFE
ITDVVKSLGI PLDGNYYVHA DVTEINGTLL PDGTIPRPTV SYIPHNFKDA DMVVVDKTGL
NVRKDLQSLT TEEEYELRVA MERFMDDKSI DGYQALAEFH GLPAKCPEPD AINRVACCVH
GMSTFPHWHR LVVMQFEDAL LARGSPIGVP YWDWTTPSSS LPHLVAVETY EDPYTKEVKP
NPFYHAQIEF LHNDVFTARN VDSRLFEKPT KGHHGYLHDG MLLAFEQEDF CDFEVQFEVT
HNAIHAWVGG NEPYSMSSLH YTSFDPLFWL HHSQVDRLWA VWQALQIYRG KPYKPYCALS
EVHRPLKPFA FEPPLNNNKH THSHSVPTHV YDYQSDLHYT YDTLFFGGMS VRELQRHIEE
DKAKDRVFVG FLLMGIKTSA NVVINVESAG NTYMAGTITI LGGSKEMEWR FDRLYKYEIT
DALAELGVDM HAEYSINLQI NDINGTALPP TSIPDPIVIF SPGKKESGVV FDELYRSRRD
VSSLTDADMN ALRKALQAYE DDKDASGYQQ VAAFHGSTKW CPSPDAEVKY ACCHHGMATF
PHWHRLLTVN FENGLRHNGY QNGIPYWDWT RPLSELPTLV KDETYADENG ETHPNPFFSG
VIDEIGEHTT RSPNPTLFLK PPFGHFTPLG DEVMYALEQE DFCSFEVQFE IAHNHIHALV
GGTEPYSMSS LEYTTFDPIF ILHHSNVDRI WAIWQALQKF RGHRYNSANC AIETLRKPMS
PFSLTSDINI DPMTREHSVP FDVFDYKKNF HYEYDLLELN GLSIPQLHRE ISRRRAKSRI
FATFMLEGIK QSALVEYYIR AHGSTDQLKA GEFYILGSAN EMPWKFDRVY KADITQQMKE
ANLHFNDQYH IEYHLKDLSG NEIAGVHLET AIIYEPGLGN FGEAGIWVEP VTSANRIRKN
LNALTDGDME SLRKAFKDMT TDGRYEEIAS FHGLPAQCPN KDGSKVYTCC IHGMPTFPHW
HRLYVALVEN ELLARGSGVA VPYWDWVQPF DHLPALVNRA TYYNSRTLLV EPNPFFKGKI
SFLNSETNRD PQEELFGNKY LYEHTLFVLE QTDFCDFEVH FEVLHNTIHS WLGGRDPHSM
SSLDFAAYDP IFFLHHSNID RIWAIWQELQ RYRKLPYNEA NCALPLLNVP MRPFSNTTAN
HDRMTLTHSA PNDVFDYQNV LHYKYDTLSF YDLTITQLDH LIEERKSHDR IFAGFLLHGV
QASADIHVFI CVPTSKHEEN CAHDVGVFSV LGGKSEMPWQ FASVFQYEIT DQLKLLGLNQ
NSHFRGVTEV TAVNGSSINS DIFPHPTIIY VPKQDHSADI KSEEGNEYLV RKNVERLSLS
EMNSLIHAFR RMQRDKSSDG FEAIASFHAL PPLCPSPTAK HRHACCLHGM ATFPHWHRLY
VVQFEQALHR HGATVGVPYW DWTRPISKIP DFIASKRYSD PFTKIEDYNP FNQGQISFIS
EDTETKREVS EYLFEHPVLG KQTWLFDNIA LALEQTDYCD FEIQLEIVHN AIHSWIGGKE
EHSLNHLHYA AYDPIFYLHH SNVDRLWVIW QELQKLRGLN AYESHCALEL MKVPLKPFSF
GAPYNLNDLT TKLSKPEDMF RYKDNFHYEY DILDINSMSI NQIESSYIRH QRDHDRVFAG
FLLSGFGSSA YATFEICIEG GECHEGSHFS VLGGSTEMPW AFDRLYKIEI TDILSDMNLA
FDSAFTIKTK LVAQNGTELP ASILPEATVI RIPPSNEDAD IDTPLNHIRR NVESLDERDI
QNLMAALTRV KEDESDHGFQ TIASYHGSTL CPSPEEPKYA CCLHGMPVFP HWHRVYLLHF
EDSMRRHGSS VATPYWDWTQ PGTKLPRLLA DSDYYDAWTD NVTENPFLRG YIKTEDTYTV
RDVKPELFEI GGGEGSTLYQ QVLLMLEQED YCDFEVQFEV VHNSIHYLVG GHQKYAMSSL
VYSSFDPIFY VHHSMVDRLW AIWQALQEHR HLPFDKAYCA LEQLSFPMKP FVWESNPNLH
TRAASTPQHL FDDNKLGYKY DNLEFHGMNI DQLENAIHKQ QNKDRVFASF LLFGIKTSAD
VHLKLCKDET CEDAGVVFIL GGDNEMPWHF DRTYKKDITH VLHQMHIPLE DLYVHGSTIL
LEVEIETVDG KVLDSSSLPA PSMIYVPAKD FKREVHKKTV GDAIIRKNVN SLTPSDIKEL
RDAMAKVQAD TSDNGYQKIA SYHGIPLSCH YENGTAYACC QHGMVTFPNW HRLLTKQMED
ALVAKGSHVG IPYWDWTTTF ANLPVLVTEE KDNSFHHAHI DVANTDTTRS PRAQLFDDPD
KGDKSFFYRQ IALALEQTDF CDFEIQFEIG HNAIHSWVGG SSPYGMSTLH YTSYDPLFYL
HHSNTDRIWS VWQALQKYRG LPYNTANCEI NKLVKPLKPF NLDTNPNAVT KAHSTGATSF
DYHKLGYDYD NLNFHGMTIP ELEEHLKEIQ HEDRVFAGFL LRTIGQSADV NFDVCTKDGE
CTFGGTFCIL GGEHEMFWAF DRPFKYDITT SLKHLRLDAH DDFDIKVTIK GIDGHVLSNK
YLSPPTVFLA PAKTTH


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