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P35747 (ALBU_HORSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Serum albumin
Alternative name(s):
Allergen=Equ c 3
Gene names
Name:ALB
OrganismEquus caballus (Horse) [Reference proteome]
Taxonomic identifier9796 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Perissodactyla › Equidae › Equus ›

Protein attributes

Sequence length607 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca2+, Na+, K+, fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc.

Subcellular location

Secreted.

Tissue specificity

Plasma.

Post-translational modification

Phosphorylation sites are present in the extracellular medium By similarity.

Allergenic properties

Causes an allergic reaction in human. Binds to IgE.

Sequence similarities

Belongs to the ALB/AFP/VDB family.

Contains 3 albumin domains.

Ontologies

Keywords
   Cellular componentSecreted
   DiseaseAllergen
   DomainRepeat
Signal
   LigandCopper
Lipid-binding
Metal-binding
Zinc
   PTMCleavage on pair of basic residues
Disulfide bond
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to starvation

Inferred from sequence or structural similarity. Source: UniProtKB

hemolysis by symbiont of host erythrocytes

Inferred from sequence or structural similarity. Source: UniProtKB

maintenance of mitochondrion location

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

transport

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular space

Inferred from electronic annotation. Source: InterPro

protein complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

drug binding

Inferred from sequence or structural similarity. Source: UniProtKB

fatty acid binding

Inferred from sequence or structural similarity. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

pyridoxal phosphate binding

Inferred from sequence or structural similarity. Source: UniProtKB

toxin binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 By similarity
Propeptide19 – 224 By similarity
PRO_0000001065
Chain25 – 607583Serum albumin
PRO_0000001066

Regions

Domain19 – 209191Albumin 1
Domain210 – 402193Albumin 2
Domain403 – 600198Albumin 3

Sites

Metal binding271Copper By similarity
Metal binding911Zinc By similarity
Metal binding1231Zinc By similarity
Metal binding2701Zinc By similarity
Metal binding2721Zinc By similarity

Amino acid modifications

Modified residue821Phosphoserine By similarity
Modified residue4421Phosphoserine By similarity
Modified residue4431Phosphothreonine By similarity
Modified residue4451Phosphothreonine By similarity
Disulfide bond77 ↔ 86
Disulfide bond99 ↔ 115
Disulfide bond114 ↔ 125
Disulfide bond147 ↔ 192
Disulfide bond191 ↔ 200
Disulfide bond223 ↔ 269
Disulfide bond268 ↔ 276
Disulfide bond288 ↔ 302
Disulfide bond301 ↔ 312
Disulfide bond339 ↔ 384
Disulfide bond383 ↔ 392
Disulfide bond415 ↔ 461
Disulfide bond460 ↔ 471
Disulfide bond484 ↔ 500
Disulfide bond499 ↔ 510
Disulfide bond537 ↔ 582
Disulfide bond581 ↔ 590

Secondary structure

1 ......................................................................... 607
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P35747 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 256F6E830A1B90C5

FASTA60768,599
        10         20         30         40         50         60 
MKWVTFVSLL FLFSSAYSRG VLRRDTHKSE IAHRFNDLGE KHFKGLVLVA FSQYLQQCPF 

        70         80         90        100        110        120 
EDHVKLVNEV TEFAKKCAAD ESAENCDKSL HTLFGDKLCT VATLRATYGE LADCCEKQEP 

       130        140        150        160        170        180 
ERNECFLTHK DDHPNLPKLK PEPDAQCAAF QEDPDKFLGK YLYEVARRHP YFYGPELLFH 

       190        200        210        220        230        240 
AEEYKADFTE CCPADDKLAC LIPKLDALKE RILLSSAKER LKCSSFQNFG ERAVKAWSVA 

       250        260        270        280        290        300 
RLSQKFPKAD FAEVSKIVTD LTKVHKECCH GDLLECADDR ADLAKYICEH QDSISGKLKA 

       310        320        330        340        350        360 
CCDKPLLQKS HCIAEVKEDD LPSDLPALAA DFAEDKEICK HYKDAKDVFL GTFLYEYSRR 

       370        380        390        400        410        420 
HPDYSVSLLL RIAKTYEATL EKCCAEADPP ACYRTVFDQF TPLVEEPKSL VKKNCDLFEE 

       430        440        450        460        470        480 
VGEYDFQNAL IVRYTKKAPQ VSTPTLVEIG RTLGKVGSRC CKLPESERLP CSENHLALAL 

       490        500        510        520        530        540 
NRLCVLHEKT PVSEKITKCC TDSLAERRPC FSALELDEGY VPKEFKAETF TFHADICTLP 

       550        560        570        580        590        600 
EDEKQIKKQS ALAELVKHKP KATKEQLKTV LGNFSAFVAK CCGREDKEAC FAEEGPKLVA 


SSQLALA

« Hide

References

[1]"X-ray and primary structure of horse serum albumin (Equus caballus) at 0.27-nm resolution."
Ho J.X., Holowachuk E.W., Norton E.J., Twigg P.D., Carter D.C.
Eur. J. Biochem. 215:205-212(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X74045 mRNA. Translation: CAA52194.1.
PIRABHOS. S34053.
RefSeqNP_001075972.1. NM_001082503.1.
UniGeneEca.1455.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3V08X-ray2.45A25-607[»]
4F5TX-ray2.32A25-607[»]
4F5UX-ray2.04A25-607[»]
ProteinModelPortalP35747.
SMRP35747. Positions 27-606.
ModBaseSearch...

Protein-protein interaction databases

STRING9796.ENSECAP00000009171.

Protein family/group databases

Allergome3302. Equ c 3.0101.
335. Equ c 3.

Proteomic databases

PRIDEP35747.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100034206.
KEGGecb:100034206.

Organism-specific databases

CTD213.

Phylogenomic databases

eggNOGNOG45992.
HOGENOMHOG000293137.
HOVERGENHBG004207.
InParanoidP35747.
KOK16141.
OrthoDBEOG4Z0B55.

Family and domain databases

InterProIPR000264. ALB/AFP/VDB.
IPR020858. Serum_albumin-like.
IPR021177. Serum_albumin/AFP.
IPR020857. Serum_albumin_CS.
IPR014760. Serum_albumin_N.
[Graphical view]
PfamPF00273. Serum_albumin. 3 hits.
[Graphical view]
PIRSFPIRSF002520. Serum_albumin_subgroup. 1 hit.
PRINTSPR00802. SERUMALBUMIN.
SMARTSM00103. ALBUMIN. 3 hits.
[Graphical view]
SUPFAMSSF48552. Serum_albumin. 3 hits.
PROSITEPS00212. ALBUMIN_1. 3 hits.
PS51438. ALBUMIN_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALBU_HORSE
AccessionPrimary (citable) accession number: P35747
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: May 1, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Allergens

Nomenclature of allergens and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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