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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi7 – 71Calcium1 Publication
Metal bindingi65 – 651Calcium; via carbonyl oxygen1 Publication
Binding sitei118 – 1181Spermine1 PublicationSequence analysis
Metal bindingi121 – 1211Calcium; via carbonyl oxygen1 Publication
Metal bindingi175 – 1751Calcium; via carbonyl oxygen1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 227227Albumin-2PRO_0000408767Add
BLAST

Interactioni

Subunit structurei

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

Structurei

Secondary structure

1
227
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 117Combined sources
Beta strandi17 – 226Combined sources
Beta strandi25 – 306Combined sources
Beta strandi39 – 468Combined sources
Helixi47 – 504Combined sources
Helixi52 – 543Combined sources
Helixi58 – 625Combined sources
Beta strandi65 – 695Combined sources
Beta strandi74 – 796Combined sources
Beta strandi82 – 876Combined sources
Turni90 – 923Combined sources
Beta strandi96 – 1038Combined sources
Helixi104 – 1074Combined sources
Helixi109 – 1113Combined sources
Turni115 – 1184Combined sources
Beta strandi121 – 1255Combined sources
Beta strandi131 – 1366Combined sources
Beta strandi139 – 1446Combined sources
Turni145 – 1484Combined sources
Beta strandi149 – 1546Combined sources
Helixi158 – 1614Combined sources
Helixi163 – 1653Combined sources
Helixi169 – 1724Combined sources
Beta strandi175 – 1795Combined sources
Beta strandi185 – 1906Combined sources
Beta strandi193 – 1986Combined sources
Beta strandi201 – 2033Combined sources
Beta strandi206 – 2094Combined sources
Helixi214 – 2174Combined sources
Helixi219 – 2213Combined sources
Turni222 – 2243Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiD4AEP7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati3 – 4644Hemopexin 1Add
BLAST
Repeati61 – 11151Hemopexin 2Add
BLAST
Repeati117 – 16549Hemopexin 3Add
BLAST
Repeati171 – 22151Hemopexin 4Add
BLAST

Sequence similaritiesi

Contains 4 hemopexin repeats.Curated

Keywords - Domaini

Repeat

Family and domain databases

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
EntryMethodResolution (Å)ChainPositionsPDBsum
3LP9X-ray2.20A/B/C/D1-227[»]
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiD4AEP7.

Family and domain databases

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...

Publicationsi

  1. "Crystal structure and functional insights of hemopexin fold protein from grass pea."
    Gaur V., Qureshi I.A., Singh A., Chanana V., Salunke D.M.
    Plant Physiol. 152:1842-1850(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, FUNCTION, SUBUNIT, HEME-BINDING, X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH CALCIUM.
    Tissue: Seed1 Publication.
  2. "Purification, identification and preliminary crystallographic studies of an allergenic protein from Lathyrus sativus."
    Qureshi I.A., Sethi D.K., Salunke D.M.
    Acta Crystallogr. F 62:869-872(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-40, CRYSTALLIZATION, PRELIMINARY X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
    Tissue: Seed1 Publication.

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: January 7, 2015
This is version 22 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.