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Protein

Alpha-lactalbumin

Gene

LALBA

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi97 – 10812PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • identical protein binding Source: IntAct
  • lactose synthase activity Source: InterPro

GO - Biological processi

  • lactose biosynthetic process Source: UniProtKB-KW
  • response to 11-deoxycorticosterone Source: AgBase
  • response to dehydroepiandrosterone Source: AgBase
  • response to estradiol Source: AgBase
  • response to progesterone Source: AgBase
Complete GO annotation...

Keywords - Molecular functioni

Milk protein

Keywords - Biological processi

Lactose biosynthesis

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-BTA-5653890. Lactose synthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-lactalbumin
Alternative name(s):
Lactose synthase B protein
Allergen: Bos d 4
Gene namesi
Name:LALBA
Synonyms:ALACTA
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 5

Subcellular locationi

GO - Cellular componenti

  • extracellular space Source: AgBase
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Allergenic propertiesi

Causes an allergic reaction in human. Is one of the causes of cow's milk allergy.

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei163. Bos d 4.
3165. Bos d 4.0101.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Chaini20 – 142123Alpha-lactalbuminPRO_0000018439Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi25 ↔ 139PROSITE-ProRule annotation1 Publication
Disulfide bondi47 ↔ 130PROSITE-ProRule annotation1 Publication
Glycosylationi64 – 641N-linked (GlcNAc...)Sequence analysis
Disulfide bondi80 ↔ 96PROSITE-ProRule annotation1 Publication
Disulfide bondi92 ↔ 110PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP00711.
PRIDEiP00711.

Expressioni

Tissue specificityi

Mammary gland specific. Secreted in milk.

Interactioni

Subunit structurei

Lactose synthase (LS) is a heterodimer of a catalytic component, beta1,4-galactosyltransferase (beta4Gal-T1) and a regulatory component, alpha-lactalbumin (LA).

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-7080486,EBI-7080486

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi159201. 1 interaction.
IntActiP00711. 3 interactions.
MINTiMINT-1487560.
STRINGi9913.ENSBTAP00000007701.

Structurei

Secondary structure

1
142
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 307Combined sources
Helixi32 – 343Combined sources
Helixi37 – 393Combined sources
Helixi42 – 5312Combined sources
Beta strandi60 – 623Combined sources
Beta strandi67 – 693Combined sources
Turni70 – 734Combined sources
Turni76 – 794Combined sources
Beta strandi80 – 823Combined sources
Helixi96 – 1005Combined sources
Helixi105 – 11713Combined sources
Helixi120 – 1223Combined sources
Helixi124 – 1296Combined sources
Beta strandi130 – 1323Combined sources
Helixi134 – 1374Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F6RX-ray2.20A/B/C/D/E/F20-142[»]
1F6SX-ray2.20A/B/C/D/E/F20-142[»]
1HFZX-ray2.30A/B/C/D20-142[»]
2G4NX-ray2.30A/B/C/D/E/F20-142[»]
ProteinModelPortaliP00711.
SMRiP00711. Positions 20-142.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00711.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 22 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IX41. Eukaryota.
ENOG410ZQK6. LUCA.
GeneTreeiENSGT00550000074398.
HOGENOMiHOG000037357.
HOVERGENiHBG052297.
InParanoidiP00711.
KOiK00704.
OMAiLAHKPLC.
OrthoDBiEOG7BW0M5.
TreeFamiTF324882.

Family and domain databases

InterProiIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000545. Lactalbumin.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamiPF00062. Lys. 1 hit.
[Graphical view]
PRINTSiPR00136. LACTALBUMIN.
PR00135. LYZLACT.
SMARTiSM00263. LYZ1. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
PROSITEiPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00711-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMSFVSLLLV GILFHATQAE QLTKCEVFRE LKDLKGYGGV SLPEWVCTTF
60 70 80 90 100
HTSGYDTQAI VQNNDSTEYG LFQINNKIWC KDDQNPHSSN ICNISCDKFL
110 120 130 140
DDDLTDDIMC VKKILDKVGI NYWLAHKALC SEKLDQWLCE KL
Length:142
Mass (Da):16,247
Last modified:July 1, 1989 - v2
Checksum:i810CDB1145901405
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti49 – 491T → A (PubMed:3120795).Curated
Sequence conflicti49 – 491T → A (Ref. 5) Curated
Sequence conflicti58 – 581Q → E AA sequence (PubMed:5532231).Curated
Sequence conflicti82 – 854DDQN → NDQD AA sequence (PubMed:5532231).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti29 – 291R → Q in an allele of Droughtmaster cattle; an Australian breed.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06366 Genomic DNA. Translation: CAA29664.1.
M18780 mRNA. Translation: AAA30615.1.
J05147 mRNA. Translation: AAA30367.1.
AB052163 Genomic DNA. Translation: BAB18921.1.
AB052164 Genomic DNA. Translation: BAB18922.1.
AB052165 Genomic DNA. Translation: BAB18923.1.
AB052166 Genomic DNA. Translation: BAB18924.1.
AB052167 Genomic DNA. Translation: BAB18925.1.
AF249896 Genomic DNA. Translation: AAF63624.1.
BT025469 mRNA. Translation: ABF57425.1.
BC102173 mRNA. Translation: AAI02174.1.
M90645 Genomic DNA. Translation: AAA30614.1.
PIRiA27360. LABO.
RefSeqiNP_776803.1. NM_174378.2.
UniGeneiBt.87412.

Genome annotation databases

EnsembliENSBTAT00000007701; ENSBTAP00000007701; ENSBTAG00000005859.
GeneIDi281894.
KEGGibta:281894.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06366 Genomic DNA. Translation: CAA29664.1.
M18780 mRNA. Translation: AAA30615.1.
J05147 mRNA. Translation: AAA30367.1.
AB052163 Genomic DNA. Translation: BAB18921.1.
AB052164 Genomic DNA. Translation: BAB18922.1.
AB052165 Genomic DNA. Translation: BAB18923.1.
AB052166 Genomic DNA. Translation: BAB18924.1.
AB052167 Genomic DNA. Translation: BAB18925.1.
AF249896 Genomic DNA. Translation: AAF63624.1.
BT025469 mRNA. Translation: ABF57425.1.
BC102173 mRNA. Translation: AAI02174.1.
M90645 Genomic DNA. Translation: AAA30614.1.
PIRiA27360. LABO.
RefSeqiNP_776803.1. NM_174378.2.
UniGeneiBt.87412.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F6RX-ray2.20A/B/C/D/E/F20-142[»]
1F6SX-ray2.20A/B/C/D/E/F20-142[»]
1HFZX-ray2.30A/B/C/D20-142[»]
2G4NX-ray2.30A/B/C/D/E/F20-142[»]
ProteinModelPortaliP00711.
SMRiP00711. Positions 20-142.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi159201. 1 interaction.
IntActiP00711. 3 interactions.
MINTiMINT-1487560.
STRINGi9913.ENSBTAP00000007701.

Protein family/group databases

Allergomei163. Bos d 4.
3165. Bos d 4.0101.

Proteomic databases

PaxDbiP00711.
PRIDEiP00711.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000007701; ENSBTAP00000007701; ENSBTAG00000005859.
GeneIDi281894.
KEGGibta:281894.

Organism-specific databases

CTDi3906.

Phylogenomic databases

eggNOGiENOG410IX41. Eukaryota.
ENOG410ZQK6. LUCA.
GeneTreeiENSGT00550000074398.
HOGENOMiHOG000037357.
HOVERGENiHBG052297.
InParanoidiP00711.
KOiK00704.
OMAiLAHKPLC.
OrthoDBiEOG7BW0M5.
TreeFamiTF324882.

Enzyme and pathway databases

ReactomeiR-BTA-5653890. Lactose synthesis.

Miscellaneous databases

EvolutionaryTraceiP00711.
NextBioi20805791.

Family and domain databases

InterProiIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000545. Lactalbumin.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamiPF00062. Lys. 1 hit.
[Graphical view]
PRINTSiPR00136. LACTALBUMIN.
PR00135. LYZLACT.
SMARTiSM00263. LYZ1. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
PROSITEiPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete nucleotide sequence of bovine alpha-lactalbumin gene: comparison with its rat counterpart."
    Vilotte J.-L., Soulier S., Mercier J.-C., Gaye P., Hue-Delahaie D., Furet J.-P.
    Biochimie 69:609-620(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Molecular cloning and nucleotide sequence of a bovine alpha-lactalbumin cDNA."
    Hurley W.L., Schuler L.A.
    Gene 61:119-122(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Recombinant bovine alpha-lactalbumin obtained by limited proteolysis of a fusion protein expressed at high levels in Escherichia coli."
    Wang M., Scott W.A., Rao K.R., Udey J., Conner G.E., Brew K.
    J. Biol. Chem. 264:21116-21121(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Bos taurus alpha lactalbumin gene."
    Yamamoto N.
    Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Angus, Hereford, Holstein, Japanese black and Jersey.
    Tissue: Blood.
  5. "Bovine gene for alpha lactalbumin."
    Dhinakar Raj G., Kumanan K.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Mammary gland.
  8. "The complete amino acid sequence of bovine alpha-lactalbumin."
    Brew K., Castellino F.J., Vanaman T.C., Hill R.L.
    J. Biol. Chem. 245:4570-4582(1970) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 20-142.
  9. "Evolution of alpha-lactalbumins. The complete amino acid sequence of the alpha-lactalbumin from a marsupial (Macropus rufogriseus) and corrections to regions of sequence in bovine and goat alpha-lactalbumins."
    Shewale J.G., Sinha S.K., Brew K.
    J. Biol. Chem. 259:4947-4956(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  10. "Sequence and single-base polymorphisms of the bovine alpha-lactalbumin 5'-flanking region."
    Bleck G.T., Bremel R.D.
    Gene 126:213-218(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
  11. "The disulfide bonds of bovine alpha-lactalbumin."
    Vanaman T.C., Brew K., Hill R.L.
    J. Biol. Chem. 245:4583-4590(1970) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS.
  12. "A comparison of bovine alpha-lactalbumin A and B of Droughtmaster."
    Bell K., Hopper K.E., McKenzie H.A., Murphy W.H., Shaw D.C.
    Biochim. Biophys. Acta 214:437-444(1970) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY PROTEIN SEQUENCE (VARIANTS ALLELIC).
    Strain: Droughtmaster.
  13. "Amino acid composition of several alpha-lactalbumins."
    Gordon W.G., Aschaffenburg R., Sen A., Ghosh S.K.
    J. Dairy Sci. 51:947-947(1968)
    Cited for: PRELIMINARY PROTEIN SEQUENCE OF 20-142 (VARIANT A).
    Strain: Zebu cattle.
  14. Cited for: CALCIUM-BINDING DATA.
  15. "Characteristics of the binding of Ca2+ and other divalent metal ions to bovine alpha-lactalbumin."
    Kronman M.J., Sinha S.K., Brew K.
    J. Biol. Chem. 256:8582-8587(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: CALCIUM-BINDING DATA.
  16. "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 (2.3 ANGSTROMS).

Entry informationi

Entry nameiLALBA_BOVIN
AccessioniPrimary (citable) accession number: P00711
Secondary accession number(s): Q3T111, Q95NE4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1989
Last modified: May 11, 2016
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Allergens
    Nomenclature of allergens and list of entries
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.