Egftnjytyk

ALB
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1AO6, 1BJ5, 1BKE, 1BM0, 1E78, 1E7A, 1E7B, 1E7C, 1E7E, 1E7F, 1E7G, 1E7H, 1E7I, 1GNI, 1GNJ, 1H9Z, 1HA2, 1HK1, 1HK2, 1HK3, 1HK4, 1HK5, 1N5U, 1O9X, 1TF0, 1UOR, 1YSX, 2BX8, 2BXA, 2BXB, 2BXC, 2BXD, 2BXF, 2BXG, 2BXH, 2BXI, 2BXK, 2BXL, 2BXM, 2BXN, 2BXO, 2BXP, 2BXQ, 2I2Z, 2I30, 2VDB, 2VUE, 2VUF, 2XSI, 2XVQ, 2XVU, 2XVV, 2XVW, 2XW0, 2XW1, 2YDF, 3A73, 3B9L, 3B9M, 3CX9, 3JQZ, 3JRY, 3LU6, 3LU7, 3LU8, 3SQJ, 3TDL, 3UIV, 4E99, 4EMX, 4G03, 4G04, 4HGK, 4HGM, 4IW1, 4IW2, 4K2C, 4L8U, 4L9K, 4L9Q, 4LA0, 4LB9, 4LB2, 2N0X, 2ESG, 4S1Y, 4N0F, 4Z69, 4N0U, 4K71, 2BXE, 4BKE, 5IJF, 5ID7, 5IFO, 5FUO
Identifiers
Aliases	ALB, blood albumin, ANALBA, FDAH, PRO0883, PRO0903, PRO1341, albumin, Serum albumin, HSA
External IDs	OMIM: 103600 MGI: 87991 HomoloGene: 405 GeneCards: ALB
Gene location (Human) Chr. Chromosome 4 (human)[1] Band 4q13.3 Start 73,397,114 bp[1] End 73,421,412 bp[1]
Gene location (Mouse) Chr. Chromosome 5 (mouse)[2] Band 5 E1|5 44.7 cM Start 90,460,897 bp[2] End 90,476,602 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • DNA binding • oxygen binding • chaperone binding • metal ion binding • antioxidant activity • protein binding • identical protein binding • pyridoxal phosphate binding • copper ion binding • lipid binding • toxic substance binding • fatty acid binding • drug binding Cellular component • cytoplasm • Golgi apparatus • blood microparticle • myelin • protein complex • extracellular region • endoplasmic reticulum • extracellular exosome • platelet alpha granule lumen • cell nucleus • extracellular space • endoplasmic reticulum lumen Biological process • sodium-independent organic anion transport • hemolysis by symbiont of host erythrocytes • cellular response to starvation • platelet degranulation • negative regulation of apoptotic process • receptor-mediated endocytosis • maintenance of mitochondrion location • retina homeostasis • bile acid and bile salt transport • negative regulation of programmed cell death • cellular oxidant detoxification • high-density lipoprotein particle remodeling • post-translational protein modification • cellular protein metabolic process • transport Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	213	11657
Ensembl	ENSG00000163631	ENSMUSG00000029368
UniProt	P02768	P07724
RefSeq (mRNA)	NM_000477	NM_009654
RefSeq (protein)	NP_000468	NP_033784
Location (UCSC)	Chr 4: 73.4 – 73.42 Mb	Chr 5: 90.46 – 90.48 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Serum albumin, often referred to simply as blood albumin, is an albumin (a type of globular protein) found in vertebrate blood. Human serum albumin is encoded by the ALB gene.^[5][6][7] Other mammalian forms, such as bovine serum albumin, are chemically similar.

Serum albumin is produced by the liver, occurs dissolved in blood plasma and is the most abundant blood protein in mammals. Albumin is essential for maintaining the oncotic pressure needed for proper distribution of body fluids between blood vessels and body tissues; without albumin, the high pressure in the blood vessels would force more fluids out into the tissues. It also acts as a plasma carrier by non-specifically binding several hydrophobic steroid hormones and as a transport protein for hemin and fatty acids. Too much or too little circulating serum albumin may be harmful. Albumin in the urine usually denotes the presence of kidney disease. Occasionally albumin appears in the urine of normal persons following long standing (postural albuminuria).

Function

Albumin functions primarily as a carrier protein for steroids, fatty acids, and thyroid hormones in the blood and plays a major role in stabilizing extracellular fluid volume by contributing to oncotic pressure (known also as colloid osmotic pressure) of plasma.

Because smaller animals (for example rats) function at a lower blood pressure, they need less oncotic pressure to balance this^{[citation needed]}, and thus need less albumin to maintain proper fluid distribution.

Synthesis

Albumin is synthesized in the liver as preproalbumin which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. The product, proalbumin, is in turn cleaved in the Golgi vesicles to produce the secreted albumin.^[7]

Properties

Albumin is a globular, water-soluble, un-glycosylated serum protein of approximate molecular weight of 65,000 Daltons.

Albumin (when ionized in water at pH 7.4, as found in the body) is negatively charged. The glomerular basement membrane is also negatively charged in the body; some studies suggest that this prevents the filtration of albumin in the urine. According to this theory, that charge plays a major role in the selective exclusion of albumin from the glomerular filtrate. A defect in this property results in nephrotic syndrome leading to albumin loss in the urine. Nephrotic syndrome patients are sometimes given albumin to replace the lost albumin.

Structure

The general structure of albumin is characterized by several long α helices allowing it to maintain a relatively static shape, which is essential for regulating blood pressure.

Serum albumin contains eleven distinct binding domains for hydrophobic compounds. One hemin and six long-chain fatty acids can bind to serum albumin at the same time.^[8]

Serum albumin family Structure of human serum albumin.[9] Identifiers Symbol Serum_albumin Pfam PF00273 Pfam clan CL0282 InterPro IPR014760 SMART SM00103 PROSITE PS51438 SCOP 1ao6 SUPERFAMILY 1ao6 Available protein structures: Pfam structures PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Types

Serum albumin is widely distributed in mammals.

• The human version is human serum albumin.


• 
  Bovine serum albumin, or BSA, is commonly used in immunodiagnostic procedures, clinical chemistry reagents, cell culture media, protein chemistry research (including venom toxicity), and molecular biology laboratories (usually to leverage its non-specific protein binding properties).

See also

• Human serum albumin


• Bovine serum albumin


• Blood plasma fractionation


• Chromatography in blood processing


• Lactalbumin


• Ovalbumin

References

External links

• RCSB Protein Data Bank : Molecule of the Month – Serum Albumin


• Albumin binding prediction