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P00713 (LALBA_CAVPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Alpha-lactalbumin
Alternative name(s):
Lactose synthase B protein
Gene names
Name:LALBA
OrganismCavia porcellus (Guinea pig) [Reference proteome]
Taxonomic identifier10141 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia

Protein attributes

Sequence length142 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Secreted.

Tissue specificity

Mammary gland specific. Secreted in milk.

Sequence similarities

Belongs to the glycosyl hydrolase 22 family.

Ontologies

Keywords
   Biological processLactose biosynthesis
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionMilk protein
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processlactose biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

lactose synthase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.3
Chain20 – 142123Alpha-lactalbumin
PRO_0000018443

Regions

Calcium binding97 – 10812

Amino acid modifications

Disulfide bond25 ↔ 139
Disulfide bond47 ↔ 130
Disulfide bond80 ↔ 96
Disulfide bond92 ↔ 110

Experimental info

Sequence conflict811E → D in AAA60337. Ref.2
Sequence conflict1241L → F in AAA60337. Ref.2

Secondary structure

......................... 142
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00713 [UniParc].

Last modified July 1, 1989. Version 2.
Checksum: E13FA2ACA8F1029E

FASTA14216,300
        10         20         30         40         50         60 
MMSFFPLLLV GILFPAVQAK QLTKCALSHE LNDLAGYRDI TLPEWLCIIF HISGYDTQAI 

        70         80         90        100        110        120 
VKNSDHKEYG LFQINDKDFC ESSTTVQSRN ICDISCDKLL DDDLTDDIMC VKKILDIKGI 

       130        140 
DYWLAHKPLC SDKLEQWYCE AQ 

« Hide

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.
PIRLAGP. S01144.
RefSeqNP_001166360.1. NM_001172889.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HFXX-ray1.90A20-142[»]
ProteinModelPortalP00713.
SMRP00713. Positions 20-142.
ModBaseSearch...

Protein-protein interaction databases

STRING10141.ENSCPOP00000019835.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSCPOT00000019635; ENSCPOP00000019835; ENSCPOG00000027342.
GeneID100379577.

Organism-specific databases

CTD3906.

Phylogenomic databases

eggNOGNOG72593.
GeneTreeENSGT00550000074398.
HOGENOMHOG000037357.
HOVERGENHBG052297.
InParanoidP00713.
OMAKCELSQV.
OrthoDBEOG43JC60.

Family and domain databases

InterProIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000545. Lactalbumin.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PANTHERPTHR11407:SF5. PTHR11407:SF5. 1 hit.
PfamPF00062. Lys. 1 hit.
[Graphical view]
PRINTSPR00136. LACTALBUMIN.
PR00135. LYZLACT.
SMARTSM00263. LYZ1. 1 hit.
[Graphical view]
SUPFAMSSF53955. SSF53955. 1 hit.
PROSITEPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00713.

Entry information

Entry nameLALBA_CAVPO
AccessionPrimary (citable) accession number: P00713
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1989
Last modified: April 3, 2013
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata 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