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P00709 (LALBA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | 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
Lysozyme-like protein 7
Gene names
Name:LALBA
Synonyms:LYZL7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.7
Chain20 – 142123Alpha-lactalbumin
PRO_0000018444

Regions

Calcium binding97 – 10812

Amino acid modifications

Glycosylation641N-linked (GlcNAc...) Ref.10
Glycosylation901N-linked (GlcNAc...); partial; atypical Ref.9
Disulfide bond25 ↔ 139
Disulfide bond47 ↔ 130
Disulfide bond80 ↔ 96
Disulfide bond92 ↔ 110

Natural variations

Natural variant461I → V. Ref.15
Corresponds to variant rs2232565 [ dbSNP | Ensembl ].
VAR_024526

Experimental info

Sequence conflict991F → K AA sequence Ref.8

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P00709 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 647F448733B06D65

FASTA14216,225
        10         20         30         40         50         60 
MRFFVPLFLV GILFPAILAK QFTKCELSQL LKDIDGYGGI ALPELICTMF HTSGYDTQAI 

        70         80         90        100        110        120 
VENNESTEYG LFQISNKLWC KSSQVPQSRN ICDISCDKFL DDDITDDIMC AKKILDIKGI 

       130        140 
DYWLAHKALC TEKLEQWLCE KL 

« Hide

References

« Hide 'large scale' references
[1]"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].
[2]"Organization and sequence of the human alpha-lactalbumin gene."
Hall L., Emery D.C., Davies M.S., Parker D., Craig R.K.
Biochem. J. 242:735-742(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Analysis of flanking sequence of human alpha-lactalbumin containing a putative locus control region."
Fujiwara Y., Takahashi R., Hirabayashi M., Ueda M., Muramatsu T., Yamanaka H., Sekikawa K.
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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].
Tissue: Brain.
[7]"The complete amino-acid sequence of human alpha-lactalbumin."
Findlay J.B.C., Brew K.
Eur. J. Biochem. 27:65-86(1972) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-142.
[8]"Identification of a new molecular form of human alpha-lactalbumin."
Maynard F.
J. Dairy Res. 59:425-429(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 78-81 AND 90-112.
Tissue: Milk.
[9]"An unusual glycosylation site in alpha-lactalbumin from human milk."
Cavaletto M., Giuffrida M.G., Giunta C., Conti A.
Protein Sci. 4 Suppl. 1:119-119(1995)
Cited for: GLYCOSYLATION AT ASN-90.
[10]"Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry."
Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.
Proteomics 8:3833-3847(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-64.
Tissue: Milk.
[11]"Crystal structure of human alpha-lactalbumin at 1.7-A resolution."
Acharya K.R., Ren J.S., Stuart D.I., Phillips D.C., Fenna R.E.
J. Mol. Biol. 221:571-581(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[12]"Alpha-lactalbumin possesses a distinct zinc binding site."
Ren J.S., Stuart D.I., Acharya K.R.
J. Biol. Chem. 268:19292-19298(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[13]"Structural evidence for the presence of a secondary calcium binding site in human alpha-lactalbumin."
Chandra N., Brew K., Acharya K.R.
Biochemistry 37:4767-4772(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[14]"Crystallographic evaluation of internal motion of human alpha-lactalbumin refined by full-matrix least-squares method."
Harata K., Abe Y., Muraki M.
J. Mol. Biol. 287:347-358(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS).
[15]"Detection of a single nucleotide polymorphism in the human alpha-lactalbumin gene: implications for human milk proteins."
Chowanadisai W., Kelleher S.L., Nemeth J.F., Yachetti S., Kuhlman C.F., Jackson J.G., Davis A.M., Lien E.L., Loennerdal B.
J. Nutr. Biochem. 16:272-278(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT VAL-46, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J00270 mRNA. Translation: AAA60345.1.
X05153 Genomic DNA. Translation: CAA28799.1.
X05153 Genomic DNA. Translation: CAA28800.1.
AB049976 Genomic DNA. Translation: BAC06860.1.
CR541987 mRNA. Translation: CAG46784.1.
CR542017 mRNA. Translation: CAG46814.1.
CH471111 Genomic DNA. Translation: EAW57990.1.
BC069103 mRNA. Translation: AAH69103.1.
BC112316 mRNA. Translation: AAI12317.1.
BC112318 mRNA. Translation: AAI12319.1.
PIRLAHU. A27880.
RefSeqNP_002280.1. NM_002289.2.
UniGeneHs.72938.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A4VX-ray1.80A20-142[»]
1B9OX-ray1.15A20-142[»]
1CB3NMR-A120-129[»]
1HMLX-ray1.70A1-142[»]
3B0IX-ray1.80A20-142[»]
3B0OX-ray1.61A/B21-142[»]
4L41X-ray2.70A/B19-142[»]
ProteinModelPortalP00709.
SMRP00709. Positions 21-139.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110101. 6 interactions.
STRING9606.ENSP00000301046.

Protein family/group databases

Allergome1289. Hom s ALA.

Polymorphism databases

DMDM126001.

Proteomic databases

PRIDEP00709.

Protocols and materials databases

DNASU3906.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000301046; ENSP00000301046; ENSG00000167531.
GeneID3906.
KEGGhsa:3906.
UCSCuc001rrt.3. human.

Organism-specific databases

CTD3906.
GeneCardsGC12M048927.
HGNCHGNC:6480. LALBA.
HPAHPA029856.
MIM149750. gene.
neXtProtNX_P00709.
PharmGKBPA30269.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG72593.
HOGENOMHOG000037357.
HOVERGENHBG052297.
InParanoidP00709.
KOK00704.
OMALAHKPLC.
OrthoDBEOG7BW0M5.
PhylomeDBP00709.
TreeFamTF324882.

Gene expression databases

ArrayExpressP00709.
BgeeP00709.
CleanExHS_LALBA.
GenevestigatorP00709.

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

EvolutionaryTraceP00709.
GeneWikiAlpha-lactalbumin.
GenomeRNAi3906.
NextBio15335.
PROP00709.
SOURCESearch...

Entry information

Entry nameLALBA_HUMAN
AccessionPrimary (citable) accession number: P00709
Secondary accession number(s): Q6FGX0, Q9UDK4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 16, 2014
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries