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UniProtKB - O61363 (HCYG_ENTDO)
Protein
Hemocyanin G-type, units Oda to Odg
Gene
ODHCY
Organism
Enteroctopus dofleini (North Pacific giant octopus) (Octopus dofleini)
Status
Functioni
Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods.
Cofactori
Cu2+Note: Binds 2 copper ions per heterodimer.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 41 | Copper ABy similarity | 1 | |
Metal bindingi | 60 | Copper ABy similarity | 1 | |
Metal bindingi | 69 | Copper ABy similarity | 1 | |
Metal bindingi | 178 | Copper BBy similarity | 1 | |
Metal bindingi | 182 | Copper BBy similarity | 1 | |
Metal bindingi | 209 | Copper BBy similarity | 1 | |
Metal bindingi | 460 | Copper ABy similarity | 1 | |
Metal bindingi | 480 | Copper ABy similarity | 1 | |
Metal bindingi | 489 | Copper ABy similarity | 1 | |
Metal bindingi | 601 | Copper BBy similarity | 1 | |
Metal bindingi | 605 | Copper BBy similarity | 1 | |
Metal bindingi | 632 | Copper BBy similarity | 1 | |
Metal bindingi | 875 | Copper ABy similarity | 1 | |
Metal bindingi | 895 | Copper ABy similarity | 1 | |
Metal bindingi | 904 | Copper ABy similarity | 1 | |
Metal bindingi | 1013 | Copper BBy similarity | 1 | |
Metal bindingi | 1017 | Copper BBy similarity | 1 | |
Metal bindingi | 1044 | Copper BBy similarity | 1 | |
Metal bindingi | 1292 | Copper ABy similarity | 1 | |
Metal bindingi | 1312 | Copper ABy similarity | 1 | |
Metal bindingi | 1321 | Copper ABy similarity | 1 | |
Metal bindingi | 1425 | Copper BBy similarity | 1 | |
Metal bindingi | 1429 | Copper BBy similarity | 1 | |
Metal bindingi | 1456 | Copper BBy similarity | 1 | |
Metal bindingi | 1708 | Copper ABy similarity | 1 | |
Metal bindingi | 1728 | Copper ABy similarity | 1 | |
Metal bindingi | 1737 | Copper ABy similarity | 1 | |
Metal bindingi | 1849 | Copper BBy similarity | 1 | |
Metal bindingi | 1853 | Copper BBy similarity | 1 | |
Metal bindingi | 1880 | Copper BBy similarity | 1 | |
Metal bindingi | 2126 | Copper ABy similarity | 1 | |
Metal bindingi | 2144 | Copper ABy similarity | 1 | |
Metal bindingi | 2153 | Copper ABy similarity | 1 | |
Metal bindingi | 2262 | Copper BBy similarity | 1 | |
Metal bindingi | 2266 | Copper BBy similarity | 1 | |
Metal bindingi | 2293 | Copper BBy similarity | 1 | |
Metal bindingi | 2543 | Copper ACombined sources | 1 | |
Metal bindingi | 2562 | Copper ACombined sources | 1 | |
Metal bindingi | 2571 | Copper ACombined sources | 1 | |
Metal bindingi | 2671 | Copper BCombined sources | 1 | |
Metal bindingi | 2675 | Copper BCombined sources | 1 | |
Metal bindingi | 2702 | Copper BCombined sources | 1 |
GO - Molecular functioni
- metal ion binding Source: UniProtKB-KW
- oxidoreductase activity Source: InterPro
- oxygen carrier activity Source: UniProtKB-KW
Keywordsi
Biological process | Oxygen transport, Transport |
Ligand | Copper, Metal-binding |
Names & Taxonomyi
Protein namesi | Recommended name: Hemocyanin G-type, units Oda to Odg |
Gene namesi | Name:ODHCY |
Organismi | Enteroctopus dofleini (North Pacific giant octopus) (Octopus dofleini) |
Taxonomic identifieri | 267067 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Spiralia › Lophotrochozoa › Mollusca › Cephalopoda › Coleoidea › Octopodiformes › Octopoda › Incirrata › Octopodidae › Enteroctopus |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000204301 | 1 – 2896 | Hemocyanin G-type, units Oda to OdgAdd BLAST | 2896 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 47 ↔ 57 | By similarity | ||
Cross-linki | 58 ↔ 60 | 2'-(S-cysteinyl)-histidine (Cys-His)By similarity | ||
Disulfide bondi | 168 ↔ 234 | By similarity | ||
Disulfide bondi | 321 ↔ 333 | By similarity | ||
Glycosylationi | 386 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 466 ↔ 477 | By similarity | ||
Cross-linki | 478 ↔ 480 | 2'-(S-cysteinyl)-histidine (Cys-His)By similarity | ||
Disulfide bondi | 591 ↔ 657 | By similarity | ||
Glycosylationi | 804 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 881 ↔ 892 | By similarity | ||
Cross-linki | 893 ↔ 895 | 2'-(S-cysteinyl)-histidine (Cys-His)By similarity | ||
Disulfide bondi | 1003 ↔ 1070 | By similarity | ||
Disulfide bondi | 1298 ↔ 1309 | By similarity | ||
Cross-linki | 1310 ↔ 1312 | 2'-(S-cysteinyl)-histidine (Cys-His)By similarity | ||
Disulfide bondi | 1415 ↔ 1482 | By similarity | ||
Glycosylationi | 1496 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1571 ↔ 1581 | By similarity | ||
Glycosylationi | 1634 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1714 ↔ 1725 | By similarity | ||
Cross-linki | 1726 ↔ 1728 | 2'-(S-cysteinyl)-histidine (Cys-His)By similarity | ||
Disulfide bondi | 1839 ↔ 1906 | By similarity | ||
Disulfide bondi | 1997 ↔ 2003 | By similarity | ||
Glycosylationi | 2055 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 2131 ↔ 2141 | By similarity | ||
Cross-linki | 2142 ↔ 2144 | 2'-(S-cysteinyl)-histidine (Cys-His)By similarity | ||
Glycosylationi | 2201 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 2252 ↔ 2319 | By similarity | ||
Disulfide bondi | 2406 ↔ 2411 | By similarity | ||
Disulfide bondi | 2549 ↔ 2559 | Combined sources1 Publication | ||
Glycosylationi | 2553 | N-linked (GlcNAc...) asparagine | 1 | |
Cross-linki | 2560 ↔ 2562 | 2'-(S-cysteinyl)-histidine (Cys-His) | ||
Disulfide bondi | 2661 ↔ 2728 | Combined sources1 Publication | ||
Disulfide bondi | 2815 ↔ 2821 | Combined sources1 Publication |
Keywords - PTMi
Disulfide bond, Glycoprotein, Thioether bondProteomic databases
PRIDEi | O61363 |
Interactioni
Subunit structurei
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.
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | O61363 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | O61363 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 419 | Functional unit Oda1 PublicationAdd BLAST | 419 | |
Regioni | 420 – 834 | Functional unit Odb1 PublicationAdd BLAST | 415 | |
Regioni | 835 – 1254 | Functional unit Odc1 PublicationAdd BLAST | 420 | |
Regioni | 1255 – 1667 | Functional unit Odd1 PublicationAdd BLAST | 413 | |
Regioni | 1668 – 2085 | Functional unit Ode1 PublicationAdd BLAST | 418 | |
Regioni | 2086 – 2502 | Functional unit Odf1 PublicationAdd BLAST | 417 | |
Regioni | 2503 – 2896 | Functional unit Odg1 PublicationAdd BLAST | 394 |
Sequence similaritiesi
Keywords - Domaini
RepeatFamily and domain databases
Gene3Di | 1.10.1280.10, 7 hits 2.60.310.10, 7 hits |
InterProi | View protein in InterPro IPR028999, Haemocyanin_beta-sandwich IPR036848, Haemocyanin_C_sf IPR002227, Tyrosinase_Cu-bd IPR008922, Unchr_di-copper_centre |
Pfami | View protein in Pfam PF14830, Haemocyan_bet_s, 7 hits PF00264, Tyrosinase, 8 hits |
PRINTSi | PR00092, TYROSINASE |
SUPFAMi | SSF48056, SSF48056, 7 hits SSF81277, SSF81277, 7 hits |
PROSITEi | View protein in PROSITE PS00497, TYROSINASE_1, 7 hits PS00498, TYROSINASE_2, 6 hits |
i Sequence
Sequence statusi: Complete.
O61363-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
NLIRKDVDAL SEDEVLNLQV ALRAMQDDET PTGYQAIAAY HGEPADCKAP
60 70 80 90 100
DGSTVVCCLH GMPTFPLWHR LYTVQFEQTM VAHGSKLGVP YWDWTQPLNH
110 120 130 140 150
LPELVSHPLF MDPTAHKAKK NVFYSGDIAF EKKTTARAVD TRLFQASKGG
160 170 180 190 200
KNFLLEGVLS ALEQDDYCHF EVQFEVAHNP IHYLVGGRFT HSMSSLEYTS
210 220 230 240 250
YDPLFFLHHS NVERLFTIWQ ALQKHRGLDG NANCGLNMFH KPMEPFGRDT
260 270 280 290 300
NPISLTKEHA KAVDVFNYNE LGYDYDDLHL NGMDIPELDT MLKERQQHPR
310 320 330 340 350
SFANFRLGGI KTSANVRVAV CIPSEDKRHS DNCNNHVGSF FILGGVHEMT
360 370 380 390 400
WDFGYPFLFE ITDVVKSLGI PLDGNYYVHA DVTEINGTLL PDGTIPRPTV
410 420 430 440 450
SYIPHNFKDA DMVVVDKTGL NVRKDLQSLT TEEEYELRVA MERFMDDKSI
460 470 480 490 500
DGYQALAEFH GLPAKCPEPD AINRVACCVH GMSTFPHWHR LVVMQFEDAL
510 520 530 540 550
LARGSPIGVP YWDWTTPSSS LPHLVAVETY EDPYTKEVKP NPFYHAQIEF
560 570 580 590 600
LHNDVFTARN VDSRLFEKPT KGHHGYLHDG MLLAFEQEDF CDFEVQFEVT
610 620 630 640 650
HNAIHAWVGG NEPYSMSSLH YTSFDPLFWL HHSQVDRLWA VWQALQIYRG
660 670 680 690 700
KPYKPYCALS EVHRPLKPFA FEPPLNNNKH THSHSVPTHV YDYQSDLHYT
710 720 730 740 750
YDTLFFGGMS VRELQRHIEE DKAKDRVFVG FLLMGIKTSA NVVINVESAG
760 770 780 790 800
NTYMAGTITI LGGSKEMEWR FDRLYKYEIT DALAELGVDM HAEYSINLQI
810 820 830 840 850
NDINGTALPP TSIPDPIVIF SPGKKESGVV FDELYRSRRD VSSLTDADMN
860 870 880 890 900
ALRKALQAYE DDKDASGYQQ VAAFHGSTKW CPSPDAEVKY ACCHHGMATF
910 920 930 940 950
PHWHRLLTVN FENGLRHNGY QNGIPYWDWT RPLSELPTLV KDETYADENG
960 970 980 990 1000
ETHPNPFFSG VIDEIGEHTT RSPNPTLFLK PPFGHFTPLG DEVMYALEQE
1010 1020 1030 1040 1050
DFCSFEVQFE IAHNHIHALV GGTEPYSMSS LEYTTFDPIF ILHHSNVDRI
1060 1070 1080 1090 1100
WAIWQALQKF RGHRYNSANC AIETLRKPMS PFSLTSDINI DPMTREHSVP
1110 1120 1130 1140 1150
FDVFDYKKNF HYEYDLLELN GLSIPQLHRE ISRRRAKSRI FATFMLEGIK
1160 1170 1180 1190 1200
QSALVEYYIR AHGSTDQLKA GEFYILGSAN EMPWKFDRVY KADITQQMKE
1210 1220 1230 1240 1250
ANLHFNDQYH IEYHLKDLSG NEIAGVHLET AIIYEPGLGN FGEAGIWVEP
1260 1270 1280 1290 1300
VTSANRIRKN LNALTDGDME SLRKAFKDMT TDGRYEEIAS FHGLPAQCPN
1310 1320 1330 1340 1350
KDGSKVYTCC IHGMPTFPHW HRLYVALVEN ELLARGSGVA VPYWDWVQPF
1360 1370 1380 1390 1400
DHLPALVNRA TYYNSRTLLV EPNPFFKGKI SFLNSETNRD PQEELFGNKY
1410 1420 1430 1440 1450
LYEHTLFVLE QTDFCDFEVH FEVLHNTIHS WLGGRDPHSM SSLDFAAYDP
1460 1470 1480 1490 1500
IFFLHHSNID RIWAIWQELQ RYRKLPYNEA NCALPLLNVP MRPFSNTTAN
1510 1520 1530 1540 1550
HDRMTLTHSA PNDVFDYQNV LHYKYDTLSF YDLTITQLDH LIEERKSHDR
1560 1570 1580 1590 1600
IFAGFLLHGV QASADIHVFI CVPTSKHEEN CAHDVGVFSV LGGKSEMPWQ
1610 1620 1630 1640 1650
FASVFQYEIT DQLKLLGLNQ NSHFRGVTEV TAVNGSSINS DIFPHPTIIY
1660 1670 1680 1690 1700
VPKQDHSADI KSEEGNEYLV RKNVERLSLS EMNSLIHAFR RMQRDKSSDG
1710 1720 1730 1740 1750
FEAIASFHAL PPLCPSPTAK HRHACCLHGM ATFPHWHRLY VVQFEQALHR
1760 1770 1780 1790 1800
HGATVGVPYW DWTRPISKIP DFIASKRYSD PFTKIEDYNP FNQGQISFIS
1810 1820 1830 1840 1850
EDTETKREVS EYLFEHPVLG KQTWLFDNIA LALEQTDYCD FEIQLEIVHN
1860 1870 1880 1890 1900
AIHSWIGGKE EHSLNHLHYA AYDPIFYLHH SNVDRLWVIW QELQKLRGLN
1910 1920 1930 1940 1950
AYESHCALEL MKVPLKPFSF GAPYNLNDLT TKLSKPEDMF RYKDNFHYEY
1960 1970 1980 1990 2000
DILDINSMSI NQIESSYIRH QRDHDRVFAG FLLSGFGSSA YATFEICIEG
2010 2020 2030 2040 2050
GECHEGSHFS VLGGSTEMPW AFDRLYKIEI TDILSDMNLA FDSAFTIKTK
2060 2070 2080 2090 2100
LVAQNGTELP ASILPEATVI RIPPSNEDAD IDTPLNHIRR NVESLDERDI
2110 2120 2130 2140 2150
QNLMAALTRV KEDESDHGFQ TIASYHGSTL CPSPEEPKYA CCLHGMPVFP
2160 2170 2180 2190 2200
HWHRVYLLHF EDSMRRHGSS VATPYWDWTQ PGTKLPRLLA DSDYYDAWTD
2210 2220 2230 2240 2250
NVTENPFLRG YIKTEDTYTV RDVKPELFEI GGGEGSTLYQ QVLLMLEQED
2260 2270 2280 2290 2300
YCDFEVQFEV VHNSIHYLVG GHQKYAMSSL VYSSFDPIFY VHHSMVDRLW
2310 2320 2330 2340 2350
AIWQALQEHR HLPFDKAYCA LEQLSFPMKP FVWESNPNLH TRAASTPQHL
2360 2370 2380 2390 2400
FDDNKLGYKY DNLEFHGMNI DQLENAIHKQ QNKDRVFASF LLFGIKTSAD
2410 2420 2430 2440 2450
VHLKLCKDET CEDAGVVFIL GGDNEMPWHF DRTYKKDITH VLHQMHIPLE
2460 2470 2480 2490 2500
DLYVHGSTIL LEVEIETVDG KVLDSSSLPA PSMIYVPAKD FKREVHKKTV
2510 2520 2530 2540 2550
GDAIIRKNVN SLTPSDIKEL RDAMAKVQAD TSDNGYQKIA SYHGIPLSCH
2560 2570 2580 2590 2600
YENGTAYACC QHGMVTFPNW HRLLTKQMED ALVAKGSHVG IPYWDWTTTF
2610 2620 2630 2640 2650
ANLPVLVTEE KDNSFHHAHI DVANTDTTRS PRAQLFDDPD KGDKSFFYRQ
2660 2670 2680 2690 2700
IALALEQTDF CDFEIQFEIG HNAIHSWVGG SSPYGMSTLH YTSYDPLFYL
2710 2720 2730 2740 2750
HHSNTDRIWS VWQALQKYRG LPYNTANCEI NKLVKPLKPF NLDTNPNAVT
2760 2770 2780 2790 2800
KAHSTGATSF DYHKLGYDYD NLNFHGMTIP ELEEHLKEIQ HEDRVFAGFL
2810 2820 2830 2840 2850
LRTIGQSADV NFDVCTKDGE CTFGGTFCIL GGEHEMFWAF DRPFKYDITT
2860 2870 2880 2890
SLKHLRLDAH DDFDIKVTIK GIDGHVLSNK YLSPPTVFLA PAKTTH
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF020548 mRNA Translation: AAC39018.1 |
PIRi | S13442 T30939 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF020548 mRNA Translation: AAC39018.1 |
PIRi | S13442 T30939 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1JS8 | X-ray | 2.30 | A/B | 2503-2896 | [»] | |
SMRi | O61363 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Proteomic databases
PRIDEi | O61363 |
Miscellaneous databases
EvolutionaryTracei | O61363 |
Family and domain databases
Gene3Di | 1.10.1280.10, 7 hits 2.60.310.10, 7 hits |
InterProi | View protein in InterPro IPR028999, Haemocyanin_beta-sandwich IPR036848, Haemocyanin_C_sf IPR002227, Tyrosinase_Cu-bd IPR008922, Unchr_di-copper_centre |
Pfami | View protein in Pfam PF14830, Haemocyan_bet_s, 7 hits PF00264, Tyrosinase, 8 hits |
PRINTSi | PR00092, TYROSINASE |
SUPFAMi | SSF48056, SSF48056, 7 hits SSF81277, SSF81277, 7 hits |
PROSITEi | View protein in PROSITE PS00497, TYROSINASE_1, 7 hits PS00498, TYROSINASE_2, 6 hits |
MobiDBi | Search... |
Entry informationi
Entry namei | HCYG_ENTDO | |
Accessioni | O61363Primary (citable) accession number: O61363 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 30, 2000 |
Last sequence update: | August 1, 1998 | |
Last modified: | February 23, 2022 | |
This is version 97 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) |
Miscellaneousi
Keywords - Technical termi
3D-structureDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families