UniProtKB - P35747 (ALBU_HORSE)
Protein
Albumin
Gene
ALB
Organism
Equus caballus (Horse)
Status
Functioni
Binds 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 (By similarity). Major calcium and magnesium transporter in plasma, binds approximately 45% of circulating calcium and magnesium in plasma (By similarity). Potentially has more than two calcium-binding sites and might additionally bind calcium in a non-specific manner (By similarity). The shared binding site between zinc and calcium at residue Asp-272 suggests a crosstalk between zinc and calcium transport in the blood (By similarity). The rank order of affinity is zinc > calcium > magnesium (By similarity). Binds to the bacterial siderophore enterobactin and inhibits enterobactin-mediated iron uptake of E.coli from ferric transferrin, and may thereby limit the utilization of iron and growth of enteric bacteria such as E.coli (By similarity). Does not prevent iron uptake by the bacterial siderophore aerobactin (By similarity).By similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 27 | CopperBy similarity | 1 | |
Metal bindingi | 30 | Calcium 1By similarity | 1 | |
Metal bindingi | 37 | Calcium 2By similarity | 1 | |
Metal bindingi | 91 | Zinc; via tele nitrogenCombined sources1 Publication | 1 | |
Metal bindingi | 267 | Calcium 1By similarity | 1 | |
Metal bindingi | 270 | Zinc; via pros nitrogenCombined sources1 Publication | 1 | |
Metal bindingi | 272 | Calcium 1By similarity | 1 | |
Metal bindingi | 272 | ZincCombined sources1 Publication | 1 | |
Metal bindingi | 275 | Calcium 1By similarity | 1 | |
Metal bindingi | 278 | Calcium 2By similarity | 1 | |
Metal bindingi | 282 | Calcium 2By similarity | 1 |
GO - Molecular functioni
- DNA binding Source: UniProtKB
- enterobactin binding Source: UniProtKB
- fatty acid binding Source: UniProtKB
- pyridoxal phosphate binding Source: UniProtKB
- toxic substance binding Source: UniProtKB
- zinc ion binding Source: GO_Central
GO - Biological processi
- cellular response to starvation Source: UniProtKB
- maintenance of mitochondrion location Source: UniProtKB
- negative regulation of apoptotic process Source: UniProtKB
Keywordsi
Ligand | Calcium, Copper, Lipid-binding, Metal-binding, Zinc |
Names & Taxonomyi
Protein namesi | Recommended name: AlbuminAlternative name(s): Allergen: Equ c 3 |
Gene namesi | Name:ALB |
Organismi | Equus caballus (Horse) |
Taxonomic identifieri | 9796 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Perissodactyla › Equidae › Equus › |
Proteomesi |
|
Subcellular locationi
Extracellular region or secreted
Extracellular region or secreted
- extracellular space Source: InterPro
Other locations
- cytoplasm Source: GO_Central
- protein-containing complex Source: UniProtKB
Keywords - Cellular componenti
SecretedPathology & Biotechi
Allergenic propertiesi
Can cause allergic reactions in humans. Binds to IgE.
Keywords - Diseasei
AllergenProtein family/group databases
Allergomei | 3302, Equ c 3.0101 335, Equ c 3 |
Chemistry databases
ChEMBLi | CHEMBL3751645 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 18 | Sequence analysisAdd BLAST | 18 | |
PropeptideiPRO_0000001065 | 19 – 24 | By similarity | 6 | |
ChainiPRO_0000001066 | 25 – 607 | AlbuminAdd BLAST | 583 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 29 | PhosphoserineBy similarity | 1 | |
Disulfide bondi | 77 ↔ 86 | Combined sources4 Publications | ||
Modified residuei | 82 | PhosphoserineBy similarity | 1 | |
Modified residuei | 89 | PhosphoserineBy similarity | 1 | |
Disulfide bondi | 99 ↔ 115 | Combined sources4 Publications | ||
Modified residuei | 107 | PhosphothreonineBy similarity | 1 | |
Disulfide bondi | 114 ↔ 125 | Combined sources4 Publications | ||
Disulfide bondi | 147 ↔ 192 | Combined sources4 Publications | ||
Disulfide bondi | 191 ↔ 200 | Combined sources4 Publications | ||
Disulfide bondi | 223 ↔ 269 | Combined sources4 Publications | ||
Disulfide bondi | 268 ↔ 276 | Combined sources4 Publications | ||
Disulfide bondi | 288 ↔ 302 | Combined sources4 Publications | ||
Disulfide bondi | 301 ↔ 312 | Combined sources4 Publications | ||
Disulfide bondi | 339 ↔ 384 | Combined sources4 Publications | ||
Disulfide bondi | 383 ↔ 392 | Combined sources4 Publications | ||
Disulfide bondi | 415 ↔ 461 | Combined sources4 Publications | ||
Modified residuei | 442 | PhosphoserineBy similarity | 1 | |
Modified residuei | 443 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 445 | PhosphothreonineBy similarity | 1 | |
Disulfide bondi | 460 ↔ 471 | Combined sources4 Publications | ||
Disulfide bondi | 484 ↔ 500 | Combined sources4 Publications | ||
Disulfide bondi | 499 ↔ 510 | Combined sources4 Publications | ||
Modified residuei | 512 | PhosphoserineBy similarity | 1 | |
Disulfide bondi | 537 ↔ 582 | Combined sources4 Publications | ||
Modified residuei | 557 | N6-methyllysineBy similarity | 1 | |
Modified residuei | 569 | PhosphothreonineBy similarity | 1 | |
Disulfide bondi | 581 ↔ 590 | Combined sources4 Publications | ||
Modified residuei | 587 | N6-succinyllysineBy similarity | 1 |
Post-translational modificationi
Phosphorylated by FAM20C in the extracellular medium.By similarity
Keywords - PTMi
Cleavage on pair of basic residues, Disulfide bond, Methylation, PhosphoproteinProteomic databases
PaxDbi | P35747 |
PeptideAtlasi | P35747 |
PRIDEi | P35747 |
Expressioni
Tissue specificityi
Plasma.
Interactioni
Subunit structurei
Interacts with FCGRT; this interaction regulates ALB homeostasis (By similarity).
Interacts with TASOR (By similarity).
By similarityStructurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P35747 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 19 – 209 | Albumin 1PROSITE-ProRule annotationAdd BLAST | 191 | |
Domaini | 210 – 402 | Albumin 2PROSITE-ProRule annotationAdd BLAST | 193 | |
Domaini | 403 – 600 | Albumin 3PROSITE-ProRule annotationAdd BLAST | 198 |
Sequence similaritiesi
Belongs to the ALB/AFP/VDB family.PROSITE-ProRule annotation
Keywords - Domaini
Repeat, SignalPhylogenomic databases
InParanoidi | P35747 |
OrthoDBi | 906547at2759 |
Family and domain databases
CDDi | cd00015, ALBUMIN, 3 hits |
InterProi | View protein in InterPro IPR000264, ALB/AFP/VDB IPR020858, Serum_albumin-like IPR021177, Serum_albumin/AFP/Afamin IPR020857, Serum_albumin_CS IPR014760, Serum_albumin_N |
PANTHERi | PTHR11385, PTHR11385, 1 hit |
Pfami | View protein in Pfam PF00273, Serum_albumin, 3 hits |
PIRSFi | PIRSF002520, Serum_albumin_subgroup, 1 hit |
PRINTSi | PR00802, SERUMALBUMIN |
SMARTi | View protein in SMART SM00103, ALBUMIN, 3 hits |
SUPFAMi | SSF48552, SSF48552, 3 hits |
PROSITEi | View protein in PROSITE PS00212, ALBUMIN_1, 3 hits PS51438, ALBUMIN_2, 3 hits |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P35747-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MKWVTFVSLL FLFSSAYSRG VLRRDTHKSE IAHRFNDLGE KHFKGLVLVA
60 70 80 90 100
FSQYLQQCPF EDHVKLVNEV TEFAKKCAAD ESAENCDKSL HTLFGDKLCT
110 120 130 140 150
VATLRATYGE LADCCEKQEP ERNECFLTHK DDHPNLPKLK PEPDAQCAAF
160 170 180 190 200
QEDPDKFLGK YLYEVARRHP YFYGPELLFH AEEYKADFTE CCPADDKLAC
210 220 230 240 250
LIPKLDALKE RILLSSAKER LKCSSFQNFG ERAVKAWSVA RLSQKFPKAD
260 270 280 290 300
FAEVSKIVTD LTKVHKECCH GDLLECADDR ADLAKYICEH QDSISGKLKA
310 320 330 340 350
CCDKPLLQKS HCIAEVKEDD LPSDLPALAA DFAEDKEICK HYKDAKDVFL
360 370 380 390 400
GTFLYEYSRR HPDYSVSLLL RIAKTYEATL EKCCAEADPP ACYRTVFDQF
410 420 430 440 450
TPLVEEPKSL VKKNCDLFEE VGEYDFQNAL IVRYTKKAPQ VSTPTLVEIG
460 470 480 490 500
RTLGKVGSRC CKLPESERLP CSENHLALAL NRLCVLHEKT PVSEKITKCC
510 520 530 540 550
TDSLAERRPC FSALELDEGY VPKEFKAETF TFHADICTLP EDEKQIKKQS
560 570 580 590 600
ALAELVKHKP KATKEQLKTV LGNFSAFVAK CCGREDKEAC FAEEGPKLVA
SSQLALA
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X74045 mRNA Translation: CAA52194.1 |
PIRi | S34053, ABHOS |
RefSeqi | NP_001075972.1, NM_001082503.1 |
Genome annotation databases
GeneIDi | 100034206 |
KEGGi | ecb:100034206 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X74045 mRNA Translation: CAA52194.1 |
PIRi | S34053, ABHOS |
RefSeqi | NP_001075972.1, NM_001082503.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3V08 | X-ray | 2.45 | A | 25-607 | [»] | |
4F5T | X-ray | 2.32 | A | 25-607 | [»] | |
4F5U | X-ray | 2.04 | A | 25-607 | [»] | |
4J2V | X-ray | 2.12 | A | 25-607 | [»] | |
4OT2 | X-ray | 2.42 | A | 25-607 | [»] | |
4ZBQ | X-ray | 1.92 | A | 25-607 | [»] | |
4ZBR | X-ray | 2.19 | A | 25-607 | [»] | |
5DBY | X-ray | 2.35 | A | 25-607 | [»] | |
5DQF | X-ray | 2.15 | A | 28-607 | [»] | |
5HOZ | X-ray | 2.15 | A | 25-607 | [»] | |
5ID9 | X-ray | 2.48 | A | 25-607 | [»] | |
5IIH | X-ray | 2.40 | A | 25-607 | [»] | |
5IIU | X-ray | 2.30 | A | 25-607 | [»] | |
5IIX | X-ray | 2.20 | A | 25-607 | [»] | |
5IJ5 | X-ray | 2.55 | A | 25-607 | [»] | |
5IJE | X-ray | 2.40 | A | 25-607 | [»] | |
5V0V | X-ray | 2.45 | A | 25-607 | [»] | |
6CI6 | X-ray | 2.80 | A | 25-607 | [»] | |
6MDQ | X-ray | 2.15 | A | 25-607 | [»] | |
6OCI | X-ray | 2.54 | A | 25-607 | [»] | |
6OCJ | X-ray | 2.50 | A | 25-607 | [»] | |
6U4R | X-ray | 2.45 | A | 25-607 | [»] | |
6U4X | X-ray | 2.25 | A | 25-607 | [»] | |
6U5A | X-ray | 2.65 | A | 25-607 | [»] | |
6XK0 | X-ray | 2.40 | A | 25-607 | [»] | |
SMRi | P35747 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Chemistry databases
ChEMBLi | CHEMBL3751645 |
Protein family/group databases
Allergomei | 3302, Equ c 3.0101 335, Equ c 3 |
Proteomic databases
PaxDbi | P35747 |
PeptideAtlasi | P35747 |
PRIDEi | P35747 |
Genome annotation databases
GeneIDi | 100034206 |
KEGGi | ecb:100034206 |
Organism-specific databases
CTDi | 213 |
Phylogenomic databases
InParanoidi | P35747 |
OrthoDBi | 906547at2759 |
Family and domain databases
CDDi | cd00015, ALBUMIN, 3 hits |
InterProi | View protein in InterPro IPR000264, ALB/AFP/VDB IPR020858, Serum_albumin-like IPR021177, Serum_albumin/AFP/Afamin IPR020857, Serum_albumin_CS IPR014760, Serum_albumin_N |
PANTHERi | PTHR11385, PTHR11385, 1 hit |
Pfami | View protein in Pfam PF00273, Serum_albumin, 3 hits |
PIRSFi | PIRSF002520, Serum_albumin_subgroup, 1 hit |
PRINTSi | PR00802, SERUMALBUMIN |
SMARTi | View protein in SMART SM00103, ALBUMIN, 3 hits |
SUPFAMi | SSF48552, SSF48552, 3 hits |
PROSITEi | View protein in PROSITE PS00212, ALBUMIN_1, 3 hits PS51438, ALBUMIN_2, 3 hits |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | ALBU_HORSE | |
Accessioni | P35747Primary (citable) accession number: P35747 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 1, 1994 |
Last sequence update: | June 1, 1994 | |
Last modified: | December 2, 2020 | |
This is version 134 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Allergens
Nomenclature of allergens and list of entries