P00713 (LALBA_CAVPO) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 98.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Alpha-lactalbumin Alternative name(s): Lactose synthase B protein | ||
| Gene names |
| ||
| Organism | Cavia porcellus (Guinea pig) [Reference proteome] | ||
| Taxonomic identifier | 10141 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Hystricognathi › Caviidae › Cavia![]() |
Protein attributes
| Sequence length | 142 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose onto the N-acetylglucosamine of the oligosaccharide chains in glycoproteins. |
| Subunit structure | Lactose synthase (LS) is a heterodimer of a catalytic component, beta1,4-galactosyltransferase (beta4Gal-T1) and a regulatory component, alpha-lactalbumin (LA). |
| Subcellular location | |
| Tissue specificity | Mammary gland specific. Secreted in milk. |
| Sequence similarities | Belongs to the glycosyl hydrolase 22 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lactose biosynthesis |
| Cellular component | Secreted |
| Domain | Signal |
| Ligand | Calcium Metal-binding |
| Molecular function | Milk protein |
| PTM | Disulfide bond |
| Technical term | 3D-structure Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | lactose biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | calcium ion binding Inferred from electronic annotation. Source: InterPro lactose synthase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 19 | 19 | Ref.3 | ||||||||||||||||||||||||||||||
| Chain | 20 – 142 | 123 | Alpha-lactalbumin | PRO_0000018443 | |||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||
| Calcium binding | 97 – 108 | 12 | |||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||
| Disulfide bond | 25 ↔ 139 | ||||||||||||||||||||||||||||||||
| Disulfide bond | 47 ↔ 130 | ||||||||||||||||||||||||||||||||
| Disulfide bond | 80 ↔ 96 | ||||||||||||||||||||||||||||||||
| Disulfide bond | 92 ↔ 110 | ||||||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||
| Sequence conflict | 81 | 1 | E → D in AAA60337. Ref.2 | ||||||||||||||||||||||||||||||
| Sequence conflict | 124 | 1 | L → F in AAA60337. Ref.2 | ||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||
| Helix | 24 – 30 | 7 | |||||||||||||||||||||||||||||||
| Turn | 31 – 36 | 6 | |||||||||||||||||||||||||||||||
| Helix | 37 – 39 | 3 | |||||||||||||||||||||||||||||||
| Helix | 42 – 53 | 12 | |||||||||||||||||||||||||||||||
| Beta strand | 60 – 63 | 4 | |||||||||||||||||||||||||||||||
| Beta strand | 66 – 69 | 4 | |||||||||||||||||||||||||||||||
| Turn | 70 – 73 | 4 | |||||||||||||||||||||||||||||||
| Turn | 76 – 79 | 4 | |||||||||||||||||||||||||||||||
| Beta strand | 83 – 85 | 3 | |||||||||||||||||||||||||||||||
| Helix | 96 – 99 | 4 | |||||||||||||||||||||||||||||||
| Beta strand | 100 – 102 | 3 | |||||||||||||||||||||||||||||||
| Helix | 105 – 117 | 13 | |||||||||||||||||||||||||||||||
| Helix | 121 – 124 | 4 | |||||||||||||||||||||||||||||||
| Helix | 134 – 137 | 4 | |||||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Structure and expression of the guinea-pig alpha-lactalbumin gene." Laird J.E., Jack L., Hall L., Boulton A.P., Parker D., Craig R.K. Biochem. J. 254:85-94(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Comparison of the nucleotide sequence of cloned human and guinea-pig pre-alpha-lactalbumin cDNA with that of chick pre-lysozyme cDNA suggests evolution from a common ancestral gene." Hall L., Craig R.K., Edbrooke M.R., Campbell P.N. Nucleic Acids Res. 10:3503-3515(1982) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [3] | "The complete amino-acid sequence of guinea-pig alpha-lactalbumin." Brew K. Eur. J. Biochem. 27:341-353(1972) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-142. |
| [4] | "Crystal structures of guinea-pig, goat and bovine alpha-lactalbumin highlight the enhanced conformational flexibility of regions that are significant for its action in lactose synthase." Pike A.C.W., Brew K., Acharya K.R. Structure 4:691-703(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | J00051 mRNA. Translation: AAA60337.1. Y00726 Genomic DNA. Translation: CAA68710.1. | ||||||||||||
| PIR | LAGP. S01144. | ||||||||||||
| RefSeq | NP_001166360.1. NM_001172889.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P00713. | ||||||||||||
| SMR | P00713. Positions 20-142. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| STRING | 10141.ENSCPOP00000019835. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENSCPOT00000019635; ENSCPOP00000019835; ENSCPOG00000027342. | ||||||||||||
| GeneID | 100379577. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 3906. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | NOG72593. | ||||||||||||
| GeneTree | ENSGT00550000074398. | ||||||||||||
| HOGENOM | HOG000037357. | ||||||||||||
| HOVERGEN | HBG052297. | ||||||||||||
| InParanoid | P00713. | ||||||||||||
| OMA | KCELSQV. | ||||||||||||
| OrthoDB | EOG43JC60. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR001916. Glyco_hydro_22. IPR019799. Glyco_hydro_22_CS. IPR000545. Lactalbumin. IPR023346. Lysozyme-like_dom. [Graphical view] | ||||||||||||
| PANTHER | PTHR11407:SF5. PTHR11407:SF5. 1 hit. | ||||||||||||
| Pfam | PF00062. Lys. 1 hit. [Graphical view] | ||||||||||||
| PRINTS | PR00136. LACTALBUMIN. PR00135. LYZLACT. | ||||||||||||
| SMART | SM00263. LYZ1. 1 hit. [Graphical view] | ||||||||||||
| SUPFAM | SSF53955. SSF53955. 1 hit. | ||||||||||||
| PROSITE | PS00128. LACTALBUMIN_LYSOZYME_1. 1 hit. PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| EvolutionaryTrace | P00713. | ||||||||||||
Entry information
| Entry name | LALBA_CAVPO | ||||||||
| Accession | Primary (citable) accession number: P00713 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
