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P49822 (ALBU_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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=Can f 3
Gene names
Name:ALB
OrganismCanis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis ›

Protein attributes

Sequence length608 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. Ref.2 Ref.6

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 termComplete proteome
Direct protein sequencing
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 Potential
Propeptide19 – 224
PRO_0000001059
Chain25 – 608584Serum albumin
PRO_0000001060

Regions

Domain19 – 210192Albumin 1
Domain211 – 403193Albumin 2
Domain404 – 601198Albumin 3

Sites

Metal binding271Copper By similarity
Metal binding911Zinc By similarity
Metal binding1231Zinc By similarity
Metal binding2711Zinc By similarity
Metal binding2731Zinc By similarity

Amino acid modifications

Modified residue821Phosphoserine By similarity
Modified residue4431Phosphoserine By similarity
Modified residue4441Phosphothreonine By similarity
Modified residue4461Phosphothreonine By similarity
Disulfide bond77 ↔ 86 By similarity
Disulfide bond99 ↔ 115 By similarity
Disulfide bond114 ↔ 125 By similarity
Disulfide bond148 ↔ 193 By similarity
Disulfide bond192 ↔ 201 By similarity
Disulfide bond224 ↔ 270 By similarity
Disulfide bond269 ↔ 277 By similarity
Disulfide bond289 ↔ 303 By similarity
Disulfide bond302 ↔ 313 By similarity
Disulfide bond340 ↔ 385 By similarity
Disulfide bond384 ↔ 393 By similarity
Disulfide bond416 ↔ 462 By similarity
Disulfide bond461 ↔ 472 By similarity
Disulfide bond485 ↔ 501 By similarity
Disulfide bond500 ↔ 511 By similarity
Disulfide bond538 ↔ 583 By similarity
Disulfide bond582 ↔ 591 By similarity

Experimental info

Sequence conflict1 – 2626MKWVT…VRREA → MDT in CAA76841. Ref.2
Sequence conflict1461A → R in CAA76841. Ref.2
Sequence conflict2061I → T in CAA76841. Ref.2
Sequence conflict3491V → A in CAA76841. Ref.2
Sequence conflict3591A → S in CAA76841. Ref.2
Sequence conflict3591A → S in AAB30434. Ref.6
Sequence conflict4481V → VV in AAB30434. Ref.6
Sequence conflict4741E → D in CAA76841. Ref.2
Sequence conflict4741E → D in AAB30434. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P49822 [UniParc].

Last modified December 21, 2004. Version 3.
Checksum: 3DB012FF7C979CF3

FASTA60868,605
        10         20         30         40         50         60 
MKWVTFISLF FLFSSAYSRG LVRREAYKSE IAHRYNDLGE EHFRGLVLVA FSQYLQQCPF 

        70         80         90        100        110        120 
EDHVKLAKEV TEFAKACAAE ESGANCDKSL HTLFGDKLCT VASLRDKYGD MADCCEKQEP 

       130        140        150        160        170        180 
DRNECFLAHK DDNPGFPPLV APEPDALCAA FQDNEQLFLG KYLYEIARRH PYFYAPELLY 

       190        200        210        220        230        240 
YAQQYKGVFA ECCQAADKAA CLGPKIEALR EKVLLSSAKE RFKCASLQKF GDRAFKAWSV 

       250        260        270        280        290        300 
ARLSQRFPKA DFAEISKVVT DLTKVHKECC HGDLLECADD RADLAKYMCE NQDSISTKLK 

       310        320        330        340        350        360 
ECCDKPVLEK SQCLAEVERD ELPGDLPSLA ADFVEDKEVC KNYQEAKDVF LGTFLYEYAR 

       370        380        390        400        410        420 
RHPEYSVSLL LRLAKEYEAT LEKCCATDDP PTCYAKVLDE FKPLVDEPQN LVKTNCELFE 

       430        440        450        460        470        480 
KLGEYGFQNA LLVRYTKKAP QVSTPTLVEV SRKLGKVGTK CCKKPESERM SCAEDFLSVV 

       490        500        510        520        530        540 
LNRLCVLHEK TPVSERVTKC CSESLVNRRP CFSGLEVDET YVPKEFNAET FTFHADLCTL 

       550        560        570        580        590        600 
PEAEKQVKKQ TALVELLKHK PKATDEQLKT VMGDFGAFVE KCCAAENKEG CFSEEGPKLV 


AAAQAALV

« Hide

References

[1]Hilger C.
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Beagle.
Tissue: Liver.
[2]"Escherichia coli expression and purification of recombinant dog albumin, a cross-reactive animal allergen."
Pandjaitan B., Swoboda I., Brandejsky-Pichler F., Rumpold H., Valenta R., Spitzauer S.
J. Allergy Clin. Immunol. 105:279-285(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALLERGEN.
Tissue: Liver.
[3]"Isolation of a cDNA encoding canine serum albumin."
Miyake M., Okazaki M., Iwabuchi S.
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Beagle.
Tissue: Liver.
[4]"Isolation, amino acid sequence and copper(II)-binding properties of peptide (1-24) of dog serum albumin."
Dixon J.W., Sarkar B.
J. Biol. Chem. 249:5872-5877(1974) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-48.
[5]"HSC-2DPAGE and the two-dimensional gel electrophoresis database of dog heart proteins."
Dunn M.J., Corbett J.M., Wheeler C.H.
Electrophoresis 18:2795-2802(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-38.
Tissue: Heart.
[6]"Molecular characterization of dog albumin as a cross-reactive allergen."
Spitzauer S., Schweiger C., Sperr W.R., Pandjaitan B., Valent P., Muehl S., Ebner C., Scheiner O., Kraft D., Rumpold H.
J. Allergy Clin. Immunol. 93:614-627(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 215-478, ALLERGEN.
Tissue: Salivary gland.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ133489 mRNA. Translation: CAB64867.1.
Y17737 mRNA. Translation: CAA76841.1.
AB090854 mRNA. Translation: BAC10663.1.
S72946 mRNA. Translation: AAB30434.1.
PIRS29749.
RefSeqNP_001003026.1. NM_001003026.1.
UniGeneCfa.5991.

3D structure databases

ProteinModelPortalP49822.
SMRP49822. Positions 29-585.
ModBaseSearch...

Protein-protein interaction databases

STRING9615.ENSCAFP00000032573.

Protein family/group databases

Allergome176. Can f 3.
3171. Can f 3.0101.

2D gel databases

UCD-2DPAGEP49822.

Proteomic databases

PaxDbP49822.
PRIDEP49822.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID403550.
KEGGcfa:403550.

Organism-specific databases

CTD213.

Phylogenomic databases

eggNOGNOG45992.
HOGENOMHOG000293137.
HOVERGENHBG004207.
KOK16141.

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...

Other

NextBio20817059.

Entry information

Entry nameALBU_CANFA
AccessionPrimary (citable) accession number: P49822
Secondary accession number(s): O77705, Q9TSZ4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: December 21, 2004
Last modified: May 1, 2013
This is version 94 of the entry and version 3 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

SIMILARITY comments

Index of protein domains and families

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