Reviewed, UniProtKB/Swiss-Prot O61363 (HCYG_ENTDO)

Names and origin

Protein names

Recommended name:
    Hemocyanin G-type, units Oda to Odg

Gene names

Name:

ODHCY

Organism

Octopus dofleini (Giant octopus)

Taxonomic identifier

267067 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Mollusca › Cephalopoda › Coleoidea › Neocoleoidea › Octopodiformes › Octopoda › Incirrata › Octopodidae › Enteroctopus

Protein attributes

Sequence length	2896 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods.
Cofactor	Binds 2 copper ions per heterodimer.
Subunit structure	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. Ref.2
Sequence similarities	Belongs to the tyrosinase family. Hemocyanin subfamily.

Ontologies

Keywords
Biological process	Oxygen transport Transport
Domain	Repeat
Ligand	Copper Metal-binding
PTM	Disulfide bond Glycoprotein Thioether bond
Technical term	3D-structure
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: InterPro oxygen transport Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity Inferred from electronic annotation. Source: InterPro oxygen transporter activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2896

2896

Hemocyanin G-type, units Oda to Odg

PRO_0000204301

Regions

Region

1 – 419

419

ODA

Region

420 – 834

415

ODB

Region

835 – 1254

420

ODC

Region

1255 – 1667

413

ODD

Region

1668 – 2085

418

ODE

Region

2086 – 2502

417

ODF

Region

2503 – 2896

394

ODG

Sites

Metal binding

41

1

Copper A By similarity

Metal binding

60

1

Copper A By similarity

Metal binding

69

1

Copper A By similarity

Metal binding

178

1

Copper B By similarity

Metal binding

182

1

Copper B By similarity

Metal binding

209

1

Copper B By similarity

Metal binding

460

1

Copper A By similarity

Metal binding

480

1

Copper A By similarity

Metal binding

489

1

Copper A By similarity

Metal binding

601

1

Copper B By similarity

Metal binding

605

1

Copper B By similarity

Metal binding

632

1

Copper B By similarity

Metal binding

875

1

Copper A By similarity

Metal binding

895

1

Copper A By similarity

Metal binding

904

1

Copper A By similarity

Metal binding

1013

1

Copper B By similarity

Metal binding

1017

1

Copper B By similarity

Metal binding

1044

1

Copper B By similarity

Metal binding

1292

1

Copper A By similarity

Metal binding

1312

1

Copper A By similarity

Metal binding

1321

1

Copper A By similarity

Metal binding

1425

1

Copper B By similarity

Metal binding

1429

1

Copper B By similarity

Metal binding

1456

1

Copper B By similarity

Metal binding

1708

1

Copper A By similarity

Metal binding

1728

1

Copper A By similarity

Metal binding

1737

1

Copper A By similarity

Metal binding

1849

1

Copper B By similarity

Metal binding

1853

1

Copper B By similarity

Metal binding

1880

1

Copper B By similarity

Metal binding

2126

1

Copper A By similarity

Metal binding

2144

1

Copper A By similarity

Metal binding

2153

1

Copper A By similarity

Metal binding

2262

1

Copper B By similarity

Metal binding

2266

1

Copper B By similarity

Metal binding

2293

1

Copper B By similarity

Metal binding

2543

1

Copper A

Metal binding

2562

1

Copper A

Metal binding

2571

1

Copper A

Metal binding

2671

1

Copper B

Metal binding

2675

1

Copper B

Metal binding

2702

1

Copper B

Amino acid modifications

Glycosylation

386

1

N-linked (GlcNAc...) Potential

Glycosylation

804

1

N-linked (GlcNAc...) Potential

Glycosylation

1496

1

N-linked (GlcNAc...) Potential

Glycosylation

1634

1

N-linked (GlcNAc...) Potential

Glycosylation

2055

1

N-linked (GlcNAc...) Potential

Glycosylation

2201

1

N-linked (GlcNAc...) Potential

Glycosylation

2553

1

N-linked (GlcNAc...)

Disulfide bond

47 ↔ 57

By similarity

Disulfide bond

168 ↔ 234

By similarity

Disulfide bond

321 ↔ 333

By similarity

Disulfide bond

466 ↔ 477

By similarity

Disulfide bond

591 ↔ 657

By similarity

Disulfide bond

881 ↔ 892

By similarity

Disulfide bond

1003 ↔ 1070

By similarity

Disulfide bond

1298 ↔ 1309

By similarity

Disulfide bond

1415 ↔ 1482

By similarity

Disulfide bond

1571 ↔ 1581

By similarity

Disulfide bond

1714 ↔ 1725

By similarity

Disulfide bond

1839 ↔ 1906

By similarity

Disulfide bond

1997 ↔ 2003

By similarity

Disulfide bond

2131 ↔ 2141

By similarity

Disulfide bond

2252 ↔ 2319

By similarity

Disulfide bond

2406 ↔ 2411

By similarity

Disulfide bond

2549 ↔ 2559

Disulfide bond

2661 ↔ 2728

Disulfide bond

2815 ↔ 2821

Cross-link

58 ↔ 60

2'-(S-cysteinyl)-histidine (Cys-His) By similarity

Cross-link

478 ↔ 480

2'-(S-cysteinyl)-histidine (Cys-His) By similarity

Cross-link

893 ↔ 895

2'-(S-cysteinyl)-histidine (Cys-His) By similarity

Cross-link

1310 ↔ 1312

2'-(S-cysteinyl)-histidine (Cys-His) By similarity

Cross-link

1726 ↔ 1728

2'-(S-cysteinyl)-histidine (Cys-His) By similarity

Cross-link

2142 ↔ 2144

2'-(S-cysteinyl)-histidine (Cys-His) By similarity

Cross-link

2560 ↔ 2562

2'-(S-cysteinyl)-histidine (Cys-His)

Secondary structure

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2896

Helix Strand Turn

Details...

Beta strand

2504 – 2506

3

Helix

2509 – 2511

3

Helix

2514 – 2529

16

Helix

2536 – 2540

5

Turn

2541 – 2543

3

Beta strand

2544 – 2546

3

Helix

2567 – 2584

18

Helix

2605 – 2608

4

Turn

2621 – 2624

4

Helix

2633 – 2635

3

Helix

2646 – 2656

11

Helix

2660 – 2679

20

Turn

2689 – 2691

3

Helix

2692 – 2694

3

Helix

2697 – 2719

23

Beta strand

2727 – 2729

3

Helix

2732 – 2734

3

Turn

2738 – 2741

4

Helix

2748 – 2752

5

Helix

2756 – 2758

3

Helix

2762 – 2765

4

Beta strand

2767 – 2770

4

Helix

2779 – 2789

11

Beta strand

2794 – 2799

6

Beta strand

2808 – 2816

9

Beta strand

2821 – 2829

9

Beta strand

2844 – 2847

4

Helix

2849 – 2854

6

Beta strand

2863 – 2874

12

Helix

2879 – 2881

3

Beta strand

2886 – 2890

5

Sequences

	Sequence		Length	Mass (Da)
	O61363-1 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: BE1F35C8C987FBFC	FASTA	2,896	331,922
	10 20 30 40 50 60 NLIRKDVDAL SEDEVLNLQV ALRAMQDDET PTGYQAIAAY HGEPADCKAP DGSTVVCCLH 70 80 90 100 110 120 GMPTFPLWHR LYTVQFEQTM VAHGSKLGVP YWDWTQPLNH LPELVSHPLF MDPTAHKAKK 130 140 150 160 170 180 NVFYSGDIAF EKKTTARAVD TRLFQASKGG KNFLLEGVLS ALEQDDYCHF EVQFEVAHNP 190 200 210 220 230 240 IHYLVGGRFT HSMSSLEYTS YDPLFFLHHS NVERLFTIWQ ALQKHRGLDG NANCGLNMFH 250 260 270 280 290 300 KPMEPFGRDT NPISLTKEHA KAVDVFNYNE LGYDYDDLHL NGMDIPELDT MLKERQQHPR 310 320 330 340 350 360 SFANFRLGGI KTSANVRVAV CIPSEDKRHS DNCNNHVGSF FILGGVHEMT WDFGYPFLFE 370 380 390 400 410 420 ITDVVKSLGI PLDGNYYVHA DVTEINGTLL PDGTIPRPTV SYIPHNFKDA DMVVVDKTGL 430 440 450 460 470 480 NVRKDLQSLT TEEEYELRVA MERFMDDKSI DGYQALAEFH GLPAKCPEPD AINRVACCVH 490 500 510 520 530 540 GMSTFPHWHR LVVMQFEDAL LARGSPIGVP YWDWTTPSSS LPHLVAVETY EDPYTKEVKP 550 560 570 580 590 600 NPFYHAQIEF LHNDVFTARN VDSRLFEKPT KGHHGYLHDG MLLAFEQEDF CDFEVQFEVT 610 620 630 640 650 660 HNAIHAWVGG NEPYSMSSLH YTSFDPLFWL HHSQVDRLWA VWQALQIYRG KPYKPYCALS 670 680 690 700 710 720 EVHRPLKPFA FEPPLNNNKH THSHSVPTHV YDYQSDLHYT YDTLFFGGMS VRELQRHIEE 730 740 750 760 770 780 DKAKDRVFVG FLLMGIKTSA NVVINVESAG NTYMAGTITI LGGSKEMEWR FDRLYKYEIT 790 800 810 820 830 840 DALAELGVDM HAEYSINLQI NDINGTALPP TSIPDPIVIF SPGKKESGVV FDELYRSRRD 850 860 870 880 890 900 VSSLTDADMN ALRKALQAYE DDKDASGYQQ VAAFHGSTKW CPSPDAEVKY ACCHHGMATF 910 920 930 940 950 960 PHWHRLLTVN FENGLRHNGY QNGIPYWDWT RPLSELPTLV KDETYADENG ETHPNPFFSG 970 980 990 1000 1010 1020 VIDEIGEHTT RSPNPTLFLK PPFGHFTPLG DEVMYALEQE DFCSFEVQFE IAHNHIHALV 1030 1040 1050 1060 1070 1080 GGTEPYSMSS LEYTTFDPIF ILHHSNVDRI WAIWQALQKF RGHRYNSANC AIETLRKPMS 1090 1100 1110 1120 1130 1140 PFSLTSDINI DPMTREHSVP FDVFDYKKNF HYEYDLLELN GLSIPQLHRE ISRRRAKSRI 1150 1160 1170 1180 1190 1200 FATFMLEGIK QSALVEYYIR AHGSTDQLKA GEFYILGSAN EMPWKFDRVY KADITQQMKE 1210 1220 1230 1240 1250 1260 ANLHFNDQYH IEYHLKDLSG NEIAGVHLET AIIYEPGLGN FGEAGIWVEP VTSANRIRKN 1270 1280 1290 1300 1310 1320 LNALTDGDME SLRKAFKDMT TDGRYEEIAS FHGLPAQCPN KDGSKVYTCC IHGMPTFPHW 1330 1340 1350 1360 1370 1380 HRLYVALVEN ELLARGSGVA VPYWDWVQPF DHLPALVNRA TYYNSRTLLV EPNPFFKGKI 1390 1400 1410 1420 1430 1440 SFLNSETNRD PQEELFGNKY LYEHTLFVLE QTDFCDFEVH FEVLHNTIHS WLGGRDPHSM 1450 1460 1470 1480 1490 1500 SSLDFAAYDP IFFLHHSNID RIWAIWQELQ RYRKLPYNEA NCALPLLNVP MRPFSNTTAN 1510 1520 1530 1540 1550 1560 HDRMTLTHSA PNDVFDYQNV LHYKYDTLSF YDLTITQLDH LIEERKSHDR IFAGFLLHGV 1570 1580 1590 1600 1610 1620 QASADIHVFI CVPTSKHEEN CAHDVGVFSV LGGKSEMPWQ FASVFQYEIT DQLKLLGLNQ 1630 1640 1650 1660 1670 1680 NSHFRGVTEV TAVNGSSINS DIFPHPTIIY VPKQDHSADI KSEEGNEYLV RKNVERLSLS 1690 1700 1710 1720 1730 1740 EMNSLIHAFR RMQRDKSSDG FEAIASFHAL PPLCPSPTAK HRHACCLHGM ATFPHWHRLY 1750 1760 1770 1780 1790 1800 VVQFEQALHR HGATVGVPYW DWTRPISKIP DFIASKRYSD PFTKIEDYNP FNQGQISFIS 1810 1820 1830 1840 1850 1860 EDTETKREVS EYLFEHPVLG KQTWLFDNIA LALEQTDYCD FEIQLEIVHN AIHSWIGGKE 1870 1880 1890 1900 1910 1920 EHSLNHLHYA AYDPIFYLHH SNVDRLWVIW QELQKLRGLN AYESHCALEL MKVPLKPFSF 1930 1940 1950 1960 1970 1980 GAPYNLNDLT TKLSKPEDMF RYKDNFHYEY DILDINSMSI NQIESSYIRH QRDHDRVFAG 1990 2000 2010 2020 2030 2040 FLLSGFGSSA YATFEICIEG GECHEGSHFS VLGGSTEMPW AFDRLYKIEI TDILSDMNLA 2050 2060 2070 2080 2090 2100 FDSAFTIKTK LVAQNGTELP ASILPEATVI RIPPSNEDAD IDTPLNHIRR NVESLDERDI 2110 2120 2130 2140 2150 2160 QNLMAALTRV KEDESDHGFQ TIASYHGSTL CPSPEEPKYA CCLHGMPVFP HWHRVYLLHF 2170 2180 2190 2200 2210 2220 EDSMRRHGSS VATPYWDWTQ PGTKLPRLLA DSDYYDAWTD NVTENPFLRG YIKTEDTYTV 2230 2240 2250 2260 2270 2280 RDVKPELFEI GGGEGSTLYQ QVLLMLEQED YCDFEVQFEV VHNSIHYLVG GHQKYAMSSL 2290 2300 2310 2320 2330 2340 VYSSFDPIFY VHHSMVDRLW AIWQALQEHR HLPFDKAYCA LEQLSFPMKP FVWESNPNLH 2350 2360 2370 2380 2390 2400 TRAASTPQHL FDDNKLGYKY DNLEFHGMNI DQLENAIHKQ QNKDRVFASF LLFGIKTSAD 2410 2420 2430 2440 2450 2460 VHLKLCKDET CEDAGVVFIL GGDNEMPWHF DRTYKKDITH VLHQMHIPLE DLYVHGSTIL 2470 2480 2490 2500 2510 2520 LEVEIETVDG KVLDSSSLPA PSMIYVPAKD FKREVHKKTV GDAIIRKNVN SLTPSDIKEL 2530 2540 2550 2560 2570 2580 RDAMAKVQAD TSDNGYQKIA SYHGIPLSCH YENGTAYACC QHGMVTFPNW HRLLTKQMED 2590 2600 2610 2620 2630 2640 ALVAKGSHVG IPYWDWTTTF ANLPVLVTEE KDNSFHHAHI DVANTDTTRS PRAQLFDDPD 2650 2660 2670 2680 2690 2700 KGDKSFFYRQ IALALEQTDF CDFEIQFEIG HNAIHSWVGG SSPYGMSTLH YTSYDPLFYL 2710 2720 2730 2740 2750 2760 HHSNTDRIWS VWQALQKYRG LPYNTANCEI NKLVKPLKPF NLDTNPNAVT KAHSTGATSF 2770 2780 2790 2800 2810 2820 DYHKLGYDYD NLNFHGMTIP ELEEHLKEIQ HEDRVFAGFL LRTIGQSADV NFDVCTKDGE 2830 2840 2850 2860 2870 2880 CTFGGTFCIL GGEHEMFWAF DRPFKYDITT SLKHLRLDAH DDFDIKVTIK GIDGHVLSNK 2890 YLSPPTVFLA PAKTTH

References

[1]	"Sequence of the Octopus dofleini hemocyanin subunit: structural and evolutionary implications." Miller K.I., Cuff M.E., Lang W.F., Varga-Weisz P., Field K.G., van Holde K.E. J. Mol. Biol. 278:827-842(1998) [PubMed: 9614945] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION. Tissue: Branchial gland.
[2]	"Crystal structure of a functional unit from Octopus hemocyanin." Cuff M.E., Miller K.I., van Holde K.E., Hendrickson W.A. J. Mol. Biol. 278:855-870(1998) [PubMed: 9614947] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF SUBUNIT ODG.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF020548 mRNA. Translation: AAC39018.1.

PIR

S13442.
T30939.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JS8	X-ray	2.30	A/B	2503-2896	[»]

ModBase

Search...

Family and domain databases

InterPro

IPR008922. Di-copper_centre.
IPR002227. Tyrosinase.
[Graphical view]

Gene3D

G3DSA:1.10.1280.10. Di-copper_centre. 7 hits.

Pfam

PF00264. Tyrosinase. 7 hits.
[Graphical view]

PRINTS

PR00092. TYROSINASE.

PROSITE

PS00497. TYROSINASE_1. 7 hits.
PS00498. TYROSINASE_2. 6 hits.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

HCYG_ENTDO

Accession

Primary (citable) accession number: O61363

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	August 1, 1998
Last modified:	June 16, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)