Reviewed, UniProtKB/Swiss-Prot P04253 (HCY2_LIMPO)

Names and origin

Protein names	Recommended name:     Hemocyanin II
Organism	Limulus polyphemus (Atlantic horseshoe crab)
Taxonomic identifier	6850 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Arthropoda › Chelicerata › Merostomata › Xiphosura › Limulidae › Limulus

Protein attributes

Sequence length	628 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.
Subunit structure	Hexamer or a multiple thereof.
Subcellular location	Secreted › extracellular space.
Tissue specificity	Hemolymph.
Sequence similarities	Belongs to the tyrosinase family. Hemocyanin subfamily.

Ontologies

Keywords
Biological process	Oxygen transport Transport
Cellular component	Secreted
Ligand	Copper Metal-binding
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: InterPro oxygen transport Ref.1 Non-traceable author statement. Source: UniProtKB protein oligomerization Ref.1 Traceable author statement. Source: UniProtKB
Cellular component	extracellular space Ref.1 Inferred by curator. Source: UniProtKB
Molecular function	chloride ion binding Ref.4 Inferred from direct assay. Source: UniProtKB copper ion binding Ref.4 Inferred from direct assay. Source: UniProtKB oxidoreductase activity Inferred from electronic annotation. Source: InterPro oxygen transporter activity Ref.1 Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 628

628

Hemocyanin II

PRO_0000204281

Sites

Metal binding

173

1

Copper 1 Ref.4

Metal binding

177

1

Copper 1 Ref.4

Metal binding

204

1

Copper 1 Ref.4

Metal binding

324

1

Copper 2 Ref.4

Metal binding

328

1

Copper 2 Ref.4

Metal binding

364

1

Copper 2 Ref.4

Amino acid modifications

Modified residue

1

1

Blocked amino end (Thr); partial Ref.1

Glycosylation

449

1

N-linked (GlcNAc...) Potential

Disulfide bond

534 ↔ 576

Disulfide bond

536 ↔ 583

Secondary structure

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628

Helix Strand Turn

Details...

Helix

3 – 13

11

Helix

16 – 18

3

Helix

33 – 36

4

Beta strand

48 – 50

3

Helix

51 – 65

15

Helix

70 – 80

11

Turn

81 – 83

3

Helix

86 – 99

14

Helix

101 – 103

3

Helix

111 – 114

4

Helix

116 – 118

3

Helix

122 – 130

9

Beta strand

143 – 146

4

Helix

156 – 160

5

Helix

161 – 164

4

Helix

167 – 179

13

Helix

186 – 189

4

Helix

196 – 217

22

Turn

243 – 245

3

Helix

266 – 282

17

Beta strand

284 – 286

3

Beta strand

292 – 294

3

Turn

297 – 299

3

Helix

300 – 309

10

Helix

317 – 320

4

Helix

323 – 332

10

Turn

333 – 335

3

Helix

347 – 349

3

Turn

351 – 353

3

Helix

354 – 356

3

Helix

358 – 375

18

Helix

383 – 386

4

Beta strand

391 – 402

12

Beta strand

405 – 416

12

Turn

418 – 420

3

Beta strand

429 – 438

10

Beta strand

442 – 449

8

Beta strand

451 – 453

3

Beta strand

455 – 467

13

Helix

476 – 482

7

Beta strand

484 – 493

10

Beta strand

495 – 503

9

Helix

504 – 506

3

Helix

517 – 521

5

Beta strand

537 – 539

3

Helix

540 – 542

3

Beta strand

552 – 562

11

Helix

563 – 566

4

Helix

580 – 583

4

Turn

596 – 599

4

Beta strand

600 – 602

3

Beta strand

606 – 608

3

Helix

609 – 611

3

Beta strand

617 – 626

10

Sequences

	Sequence		Length	Mass (Da)
	P04253-1 [UniParc]. Last modified July 1, 1989. Version 2. Checksum: 6B8B4C6D8B1225BE	FASTA	628	72,629
	10 20 30 40 50 60 TLHDKQIRVC HLFEQLSSAT VIGDGDKHKH SDRLKNVGKL QPGAIFSCFH PDHLEEARHL 70 80 90 100 110 120 YEVFWEAGDF NDFIEIAKEA RTFVNEGLFA FAAEVAVLHR DDCKGLYVPP VQEIFPDKFI 130 140 150 160 170 180 PSAAINEAFK KAHVRPEFDE SPILVDVQDT GNILDPEYRL AYYREDVGIN AHHWHWHLVY 190 200 210 220 230 240 PSTWNPKYFG KKKDRKGELF YYMHQQMCAR YDCERLSNGM HRMLPFNNFD EPLAGYAPHL 250 260 270 280 290 300 THVASGKYYS PRPDGLKLRD LGDIEISEMV RMRERILDSI HLGYVISEDG SHKTLDELHG 310 320 330 340 350 360 TDILGALVES SYESVNHEYY GNLHNWGHVT MARIHDPDGR FHEEPGVMSD TSTSLRDPIF 370 380 390 400 410 420 YNWHRFIDNI FHEYKNTLKP YDHDVLNFPD IQVQDVTLHA RVDNVVHFTM REQELELKHG 430 440 450 460 470 480 INPGNARSIK ARYYHLDHEP FSYAVNVQNN SASDKHATVR IFLAPKYDEL GNEIKADELR 490 500 510 520 530 540 RTAIELDKFK TDLHPGKNTV VRHSLDSSVT LSHQPTFEDL LHGVGLNEHK SEYCSCGWPS 550 560 570 580 590 600 HLLVPKGNIK GMEYHLFVML TDWDKDKVDG SESVACVDAV SYCGARDHKY PDKKPMGFPF 610 620 DRPIHTEHIS DFLTNNMFIK DIKIKFHE

References

[1]	"Structure of hemocyanin II from the horseshoe crab, Limulus polyphemus. Sequences of the overlapping peptides, ordering the CNBr fragments, and the complete amino acid sequence." Nakashima H., Behrens P.Q., Moore M.D., Yokota E., Riggs A.F. J. Biol. Chem. 261:10526-10533(1986) [PubMed: 3525550] [Abstract] Cited for: PROTEIN SEQUENCE.
[2]	"The structure of the hemocyanin from the horseshoe crab, Limulus polyphemus. The amino acid sequence of the largest cyanogen bromide fragment." Yokota E., Riggs A.F. J. Biol. Chem. 259:4739-4749(1984) [PubMed: 6715319] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-203.
[3]	"Hexamers of subunit II from Limulus hemocyanin (a 48-mer) have the same quaternary structure as whole Panulirus hemocyanin molecules." Magnus K.A., Lattman E.E., Volbeda A., Hol W.G.J. Proteins 9:240-247(1991) [PubMed: 1866430] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[4]	"Crystal structure of deoxygenated Limulus polyphemus subunit II hemocyanin at 2.18-A resolution: clues for a mechanism for allosteric regulation." Hazes B., Magnus K.A., Bonaventura C., Bonaventura J., Dauter Z., Kalk K.H., Hol W.G.J. Protein Sci. 2:597-619(1993) [PubMed: 8518732] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

PIR

BHHC2A. A26713.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LL1	X-ray	2.55	A	1-628	[»]
1LLA	X-ray	2.18	A	1-628	[»]
1NOL	X-ray	2.40	A	1-628	[»]
1OXY	X-ray	2.40	A	1-628	[»]

ModBase

Search...

Family and domain databases

InterPro

IPR008922. Di-copper_centre.
IPR013788. Hemocyanin.
IPR005203. Hemocyanin_C.
IPR000896. Hemocyanin_Cu.
IPR005204. Hemocyanin_N.
IPR002227. Tyrosinase.
[Graphical view]

Gene3D

G3DSA:1.10.1280.10. Di-copper_centre. 1 hit.
G3DSA:2.60.40.1520. hemocyanin_C. 1 hit.
G3DSA:1.20.1370.10. hemocyanin_N. 1 hit.

PANTHER

PTHR11511. Hemocyanin. 1 hit.

Pfam

PF03723. Hemocyanin_C. 1 hit.
PF00372. Hemocyanin_M. 1 hit.
PF03722. Hemocyanin_N. 1 hit.
[Graphical view]

PRINTS

PR00187. HAEMOCYANIN.

PROSITE

PS00209. HEMOCYANIN_1. 1 hit.
PS00210. HEMOCYANIN_2. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

HCY2_LIMPO

Accession

Primary (citable) accession number: P04253

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 1987
Last sequence update:	July 1, 1989
Last modified:	June 16, 2009
This is version 75 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)