Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Hemocyanin AA6 chain

Gene
N/A
Organism
Androctonus australis (Sahara scorpion)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi170Copper 1Curated1
Metal bindingi174Copper 1Curated1
Metal bindingi201Copper 1Curated1
Metal bindingi321Copper 2Curated1
Metal bindingi325Copper 2Curated1
Metal bindingi361Copper 2Curated1

GO - Molecular functioni

Complete GO annotation...

Keywords - Biological processi

Oxygen transport, Transport

Keywords - Ligandi

Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Hemocyanin AA6 chain
OrganismiAndroctonus australis (Sahara scorpion)
Taxonomic identifieri6858 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaScorpionesButhidaButhoideaButhidaeAndroctonus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002042531 – 626Hemocyanin AA6 chainAdd BLAST626

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei374PhosphoserineCurated1

Post-translational modificationi

Three disulfide bonds are present.

Keywords - PTMi

Disulfide bond, Phosphoprotein

Expressioni

Tissue specificityi

Hemolymph.

Interactioni

Subunit structurei

Scorpion hemocyanin is a 24-chain polymer with 8 different chains identified, assembled in hexameric substructures.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3IXVelectron microscopy6.80A/C/D/E/F/G/H/I/J/K/L/M1-626[»]
3IXWelectron microscopy8.00A/C/D/E/F/G/H/I/J/K/L/M1-626[»]
ProteinModelPortaliP80476.
SMRiP80476.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80476.

Family & Domainsi

Sequence similaritiesi

Belongs to the tyrosinase family. Hemocyanin subfamily.Curated

Family and domain databases

Gene3Di1.10.1280.10. 1 hit.
1.20.1370.10. 1 hit.
2.60.40.1520. 1 hit.
InterProiIPR013788. Hemocyanin/hexamerin.
IPR000896. Hemocyanin/hexamerin_mid_dom.
IPR005203. Hemocyanin_C.
IPR005204. Hemocyanin_N.
IPR014756. Ig_E-set.
IPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PANTHERiPTHR11511. PTHR11511. 1 hit.
PfamiPF03723. Hemocyanin_C. 1 hit.
PF00372. Hemocyanin_M. 1 hit.
PF03722. Hemocyanin_N. 1 hit.
[Graphical view]
PRINTSiPR00187. HAEMOCYANIN.
SUPFAMiSSF48050. SSF48050. 1 hit.
SSF48056. SSF48056. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00209. HEMOCYANIN_1. 1 hit.
PS00210. HEMOCYANIN_2. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P80476-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
TVADKQARLM PLFKHLTALT REKLPLDQRD ERLKGVGILP RGTLFSCFHA
60 70 80 90 100
RHLAEATELY VALYGAKDFN DFIHLCEQAR QIVNEGMFVY AVSVAVLHRE
110 120 130 140 150
DCKGITVPPI QEVFPDRFVP AETINRANKE ASNHPDQQSI VVEAEETGNI
160 170 180 190 200
LDPEYKLSYF REDIGINAHH WHWHIVYPAT WNPTVMGKEK DRKGELFFYM
210 220 230 240 250
HQQMCARYDS ERLSNGLQRM IPFHNFDEPL EGYAPHLTSL VSGLQYASRP
260 270 280 290 300
EGYSIHDLSD VDVQDMVRWR ERILDAINMH YIVDKDNNKI PLDIEHGTDI
310 320 330 340 350
LGDIIESSDE SKNVEYYGSL HNWGHVMMAN ITDPDHRFQE NPGVMSDTST
360 370 380 390 400
SLRDPIFYRW HRFIDNIFQE HKKSFHPYTK EELSFPGVEV VGVSINSKTA
410 420 430 440 450
NVITTLIKES LLELSHGINF GTDQSVKVKY HHLDHEPFTY NIVVENNSGA
460 470 480 490 500
EKHSTVRIFL APKYDELNNK LEPDEQRRLF IELDKFFYTL TPGKNTIVRN
510 520 530 540 550
HQDSSVTISK VRTFDQLGAG EGVSEDSTEY CSCGWPEHML IPRGSHKGME
560 570 580 590 600
FELFVMLTDH DEDTVAGLSE NAVCSDAVSY CGARDDRYPD KKAMGFPFDR
610 620
KIEARTAAEF LTPNMGLTDI KIKFHG
Length:626
Mass (Da):71,786
Last modified:November 1, 1995 - v1
Checksum:iE788136AE3DEF0D2
GO

Mass spectrometryi

Molecular mass is 71890±7 Da from positions 1 - 626. Determined by ESI. 1 Publication

Sequence databases

PIRiS67964.

Cross-referencesi

Sequence databases

PIRiS67964.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3IXVelectron microscopy6.80A/C/D/E/F/G/H/I/J/K/L/M1-626[»]
3IXWelectron microscopy8.00A/C/D/E/F/G/H/I/J/K/L/M1-626[»]
ProteinModelPortaliP80476.
SMRiP80476.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP80476.

Family and domain databases

Gene3Di1.10.1280.10. 1 hit.
1.20.1370.10. 1 hit.
2.60.40.1520. 1 hit.
InterProiIPR013788. Hemocyanin/hexamerin.
IPR000896. Hemocyanin/hexamerin_mid_dom.
IPR005203. Hemocyanin_C.
IPR005204. Hemocyanin_N.
IPR014756. Ig_E-set.
IPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PANTHERiPTHR11511. PTHR11511. 1 hit.
PfamiPF03723. Hemocyanin_C. 1 hit.
PF00372. Hemocyanin_M. 1 hit.
PF03722. Hemocyanin_N. 1 hit.
[Graphical view]
PRINTSiPR00187. HAEMOCYANIN.
SUPFAMiSSF48050. SSF48050. 1 hit.
SSF48056. SSF48056. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00209. HEMOCYANIN_1. 1 hit.
PS00210. HEMOCYANIN_2. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHCY6_ANDAU
AccessioniPrimary (citable) accession number: P80476
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 2, 2016
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Miscellaneous

The two copper ions bound each have 3 nitrogen ligands (presumably contributed by His residues) and share a bridging ligand (possibly contributed by a Tyr residue) in addition to binding oxygen.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.