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P02770 (ALBU_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serum albumin
Gene names
Name:Alb
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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.

Sequence similarities

Belongs to the ALB/AFP/VDB family.

Contains 3 albumin domains.

Caution

A peptide arising from positions 166 to 174 was originally (Ref.5) termed neurotensin-related peptide (NRP) and was thought to regulate fat digestion, lipid absorption, and blood flow.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   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

positive regulation of circadian sleep/wake cycle, non-REM sleep

Inferred from direct assay PubMed 9748091. Source: RGD

response to mercury ion

Inferred from expression pattern PubMed 17184894. Source: RGD

response to nutrient

Inferred from expression pattern PubMed 20227002. Source: RGD

response to organic substance

Inferred from expression pattern PubMed 12051991. Source: RGD

response to platinum ion

Inferred from expression pattern PubMed 19425235. Source: RGD

transport

Inferred from electronic annotation. Source: InterPro

vasodilation

Non-traceable author statement PubMed 11983891. Source: RGD

   Cellular_componentbasement membrane

Inferred from direct assay PubMed 1723977. Source: RGD

cytoplasm

Inferred from electronic annotation. Source: Ensembl

extracellular space

Inferred from direct assay PubMed 17010194. Source: RGD

extracellular vesicular exosome

Inferred from electronic annotation. Source: Ensembl

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

enzyme binding

Inferred from physical interaction PubMed 10350214. Source: RGD

fatty acid binding

Inferred from sequence or structural similarity. Source: UniProtKB

oxygen binding

Inferred from electronic annotation. Source: Ensembl

pyridoxal phosphate binding

Inferred from sequence or structural similarity. Source: UniProtKB

toxic substance binding

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from direct assay PubMed 540055. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.3
Propeptide19 – 224
PRO_0000001079
Chain25 – 608584Serum albumin
PRO_0000001080

Regions

Domain19 – 211193Albumin 1
Domain212 – 403192Albumin 2
Domain404 – 601198Albumin 3

Sites

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

Amino acid modifications

Modified residue4431Phosphoserine By similarity
Modified residue4441Phosphothreonine By similarity
Modified residue4461Phosphothreonine By similarity
Modified residue4601N6-succinyllysine By similarity
Modified residue5431N6-succinyllysine By similarity
Modified residue5881N6-succinyllysine 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

Natural variations

Natural variant2621V → L. Ref.2

Experimental info

Sequence conflict1741Y → L AA sequence Ref.5
Sequence conflict3171I → T in CAA24532. Ref.1
Sequence conflict4311V → I in AAH85359. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P02770 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 07475796EA94938C

FASTA60868,731
        10         20         30         40         50         60 
MKWVTFLLLL FISGSAFSRG VFRREAHKSE IAHRFKDLGE QHFKGLVLIA FSQYLQKCPY 

        70         80         90        100        110        120 
EEHIKLVQEV TDFAKTCVAD ENAENCDKSI HTLFGDKLCA IPKLRDNYGE LADCCAKQEP 

       130        140        150        160        170        180 
ERNECFLQHK DDNPNLPPFQ RPEAEAMCTS FQENPTSFLG HYLHEVARRH PYFYAPELLY 

       190        200        210        220        230        240 
YAEKYNEVLT QCCTESDKAA CLTPKLDAVK EKALVAAVRQ RMKCSSMQRF GERAFKAWAV 

       250        260        270        280        290        300 
ARMSQRFPNA EFAEITKLAT DVTKINKECC HGDLLECADD RAELAKYMCE NQATISSKLQ 

       310        320        330        340        350        360 
ACCDKPVLQK SQCLAEIEHD NIPADLPSIA ADFVEDKEVC KNYAEAKDVF LGTFLYEYSR 

       370        380        390        400        410        420 
RHPDYSVSLL LRLAKKYEAT LEKCCAEGDP PACYGTVLAE FQPLVEEPKN LVKTNCELYE 

       430        440        450        460        470        480 
KLGEYGFQNA VLVRYTQKAP QVSTPTLVEA ARNLGRVGTK CCTLPEAQRL PCVEDYLSAI 

       490        500        510        520        530        540 
LNRLCVLHEK TPVSEKVTKC CSGSLVERRP CFSALTVDET YVPKEFKAET FTFHSDICTL 

       550        560        570        580        590        600 
PDKEKQIKKQ TALAELVKHK PKATEDQLKT VMGDFAQFVD KCCKAADKDN CFATEGPNLV 


ARSKEALA 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of cloned rat serum albumin messenger RNA."
Sargent T.D., Yang M., Bonner J.
Proc. Natl. Acad. Sci. U.S.A. 78:243-246(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT LEU-262.
Tissue: Ovary.
[3]"Rat liver pre-proalbumin: complete amino acid sequence of the pre-piece. Analysis of the direct translation product of albumin messenger RNA."
Strauss A.W., Bennett C.D., Donohue A.M., Rodkey J.A., Alberts A.W.
J. Biol. Chem. 252:6846-6855(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-38, PROTEOLYTIC PROCESSING.
[4]"Amino acid sequences of fragments I and II obtained by cyanogen bromide cleavage of rat serum albumin."
Isemura S., Ikenaka T.
J. Biochem. 83:35-48(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-222.
[5]"Structure of a biologically active neurotensin-related peptide obtained from pepsin-treated albumin(s)."
Carraway R.E., Mitra S.P., Cochrane D.E.
J. Biol. Chem. 262:5968-5973(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 166-174.
Tissue: Plasma.
[6]Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 35-57; 66-75; 89-97; 168-181; 247-264; 287-298; 361-372; 376-383; 414-434; 439-452; 470-483; 509-524; 528-545; 570-581 AND 585-602, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain, Hippocampus and Spinal cord.
[7]"Fragmentation of rat serum albumin by cyanogen bromide cleavage and the amino acid sequences of four fragments."
Isemura S., Ikenaka T.
J. Biochem. 79:1183-1196(1976) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 223-288 AND 572-608.
[8]"Copper(II)-binding ability of human alpha-fetoprotein."
Aoyagi Y., Ikenaka T., Ichida F.
Cancer Res. 38:3483-3486(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: COPPER-BINDING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V01222 mRNA. Translation: CAA24532.1.
BC085359 mRNA. Translation: AAH85359.1.
PIRABRTS. A93872.
RefSeqNP_599153.2. NM_134326.2.
UniGeneRn.202968.

3D structure databases

ProteinModelPortalP02770.
SMRP02770. Positions 26-608.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP02770. 2 interactions.
MINTMINT-4542462.

Chemistry

BindingDBP02770.
ChEMBLCHEMBL4817.

Protein family/group databases

Allergome756. Rat n 4.

PTM databases

PhosphoSiteP02770.

2D gel databases

UCD-2DPAGEP02770.
World-2DPAGE0004:P02770.

Proteomic databases

PaxDbP02770.
PRIDEP02770.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000003921; ENSRNOP00000003921; ENSRNOG00000002911.
GeneID24186.
KEGGrno:24186.
UCSCRGD:2085. rat.

Organism-specific databases

CTD213.
RGD2085. Alb.

Phylogenomic databases

eggNOGNOG45992.
GeneTreeENSGT00390000000113.
HOGENOMHOG000293137.
HOVERGENHBG004207.
InParanoidP02770.
KOK16141.
OrthoDBEOG7S4X5C.
PhylomeDBP02770.
TreeFamTF335561.

Gene expression databases

GenevestigatorP02770.

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. SSF48552. 3 hits.
PROSITEPS00212. ALBUMIN_1. 3 hits.
PS51438. ALBUMIN_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio602549.
PROP02770.

Entry information

Entry nameALBU_RAT
AccessionPrimary (citable) accession number: P02770
Secondary accession number(s): P11382, Q5U3X3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families