Hemocyanin II - Limulus polyphemus (Atlantic horseshoe crab)

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P04253 (HCY2_LIMPO) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 83. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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.
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	protein oligomerization Traceable author statement Ref.1. Source: UniProtKB
Cellular component	extracellular space Inferred by curator Ref.1. Source: UniProtKB
Molecular function	chloride ion binding Inferred from direct assay Ref.4. Source: UniProtKB copper ion binding Inferred from direct assay Ref.4. Source: UniProtKB oxidoreductase activity Inferred from electronic annotation. Source: InterPro oxygen transporter activity Non-traceable author statement Ref.1. 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

Copper 1 Ref.4

Metal binding

177

Copper 1 Ref.4

Metal binding

204

Copper 1 Ref.4

Metal binding

324

Copper 2 Ref.4

Metal binding

328

Copper 2 Ref.4

Metal binding

364

Copper 2 Ref.4

Amino acid modifications

Modified residue

Blocked amino end (Thr); partial Ref.1

Glycosylation

449

N-linked (GlcNAc...) Potential

Disulfide bond

534 ↔ 576

Disulfide bond

536 ↔ 583

Secondary structure

628

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P04253 [UniParc].

Last modified July 1, 1989. Version 2.
Checksum: 6B8B4C6D8B1225BE
Show »

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

« Hide

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

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P04253.

SMR

P04253. Positions 1-628.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR013788. Hemocyanin.
IPR005203. Hemocyanin_C.
IPR000896. Hemocyanin_Cu.
IPR005204. Hemocyanin_N.
IPR014756. Ig_E-set.
IPR002227. Tyrosinase.
IPR008922. Unchr_di-copper_centre.
[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.

SUPFAM

SSF48056. Di-copper_centre. 1 hit.
SSF48050. Hemocyanin_N. 1 hit.
SSF81296. Ig_E-set. 1 hit.

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:	October 19, 2011
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Family and domain databases

Entry information

Relevant documents