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Protein

Albumin-2

Gene
N/A
Organism
Lathyrus sativus (Chickling vetch)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

May play a role in response to oxidative stress and polyamine biosynthesis. The monomeric form binds one hemin per monomer. In the dimeric form, about half of the dimers bind one molecule of spermine each under physiological conditions. Ligand binding is mutually exclusive as binding of hemin leads to dissociation of the dimer.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi7Calcium1 Publication1
Metal bindingi65Calcium; via carbonyl oxygen1 Publication1
Binding sitei118Spermine1 PublicationSequence analysis1
Metal bindingi121Calcium; via carbonyl oxygen1 Publication1
Metal bindingi175Calcium; via carbonyl oxygen1 Publication1

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • heme binding Source: UniProtKB
  • nutrient reservoir activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Seed storage protein, Storage protein

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Albumin-2By similarity
Alternative name(s):
24 kDa albumin1 Publication
Short name:
LS-241 Publication
PA2By similarity
OrganismiLathyrus sativus (Chickling vetch)
Taxonomic identifieri3860 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaeLathyrus

Subcellular locationi

  • Cytoplasmcytosol By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004087671 – 227Albumin-2Add BLAST227

Interactioni

Subunit structurei

Monomer and homodimer. Dimers are prevalent in solution.1 Publication

Structurei

Secondary structure

1227
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 11Combined sources7
Beta strandi17 – 22Combined sources6
Beta strandi25 – 30Combined sources6
Beta strandi39 – 46Combined sources8
Helixi47 – 50Combined sources4
Helixi52 – 54Combined sources3
Helixi58 – 62Combined sources5
Beta strandi65 – 69Combined sources5
Beta strandi74 – 79Combined sources6
Beta strandi82 – 87Combined sources6
Turni90 – 92Combined sources3
Beta strandi96 – 103Combined sources8
Helixi104 – 107Combined sources4
Helixi109 – 111Combined sources3
Turni115 – 118Combined sources4
Beta strandi121 – 125Combined sources5
Beta strandi131 – 136Combined sources6
Beta strandi139 – 144Combined sources6
Turni145 – 148Combined sources4
Beta strandi149 – 154Combined sources6
Helixi158 – 161Combined sources4
Helixi163 – 165Combined sources3
Helixi169 – 172Combined sources4
Beta strandi175 – 179Combined sources5
Beta strandi185 – 190Combined sources6
Beta strandi193 – 198Combined sources6
Beta strandi201 – 203Combined sources3
Beta strandi206 – 209Combined sources4
Helixi214 – 217Combined sources4
Helixi219 – 221Combined sources3
Turni222 – 224Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3LP9X-ray2.20A/B/C/D1-227[»]
SMRiD4AEP7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiD4AEP7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati3 – 46Hemopexin 1Add BLAST44
Repeati61 – 111Hemopexin 2Add BLAST51
Repeati117 – 165Hemopexin 3Add BLAST49
Repeati171 – 221Hemopexin 4Add BLAST51

Sequence similaritiesi

Contains 4 hemopexin repeats.Curated

Keywords - Domaini

Repeat

Family and domain databases

CDDicd00094. HX. 1 hit.
Gene3Di2.110.10.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
[Graphical view]
PfamiPF00045. Hemopexin. 3 hits.
[Graphical view]
SMARTiSM00120. HX. 3 hits.
[Graphical view]
SUPFAMiSSF50923. SSF50923. 1 hit.
PROSITEiPS51642. HEMOPEXIN_2. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

D4AEP7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
TKPGYINAAF RSSKNNEAYF FINDKYVLLD YAPGSSRDKV LYGPTPVRDG
60 70 80 90 100
FKSLNQTIFG SYGIDCSFDT ENNEAFIFYE NFCALIDYAP HSKKDKIILG
110 120 130 140 150
PKKIADVFPF FEGTVFESGI DAAYRSTRGK EVYLFKGDQY ARIDYGSNSM
160 170 180 190 200
VNKEIKSISS GYPCFRNTIF ESGADAAFAS HKTNEVYFFK DDHYARVKVT
210 220
PGGKLAIMDG VREIVDYWPS LKDIVPL
Length:227
Mass (Da):25,621
Last modified:May 31, 2011 - v2
Checksum:i9FAD69E8D9E7F8E7
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3LP9X-ray2.20A/B/C/D1-227[»]
SMRiD4AEP7.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiD4AEP7.

Family and domain databases

CDDicd00094. HX. 1 hit.
Gene3Di2.110.10.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
[Graphical view]
PfamiPF00045. Hemopexin. 3 hits.
[Graphical view]
SMARTiSM00120. HX. 3 hits.
[Graphical view]
SUPFAMiSSF50923. SSF50923. 1 hit.
PROSITEiPS51642. HEMOPEXIN_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiALB2_LATSA
AccessioniPrimary (citable) accession number: D4AEP7
Secondary accession number(s): P86190
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 31, 2011
Last sequence update: May 31, 2011
Last modified: November 30, 2016
This is version 24 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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.