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Protein

Alpha-lactalbumin

Gene

LALBA

Organism
Capra hircus (Goat)
Status
Reviewed-Annotation score: Annotation score: 4 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 – 10812Add
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Milk protein

Keywords - Biological processi

Lactose biosynthesis

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-lactalbumin
Alternative name(s):
Lactose synthase B protein
Gene namesi
Name:LALBA
OrganismiCapra hircus (Goat)
Taxonomic identifieri9925 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeCapra

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Chaini20 – 142123Alpha-lactalbuminPRO_0000018442Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi25 ↔ 139
Disulfide bondi47 ↔ 130
Glycosylationi64 – 641N-linked (GlcNAc...)Sequence analysis
Disulfide bondi80 ↔ 96
Disulfide bondi92 ↔ 110
Glycosylationi93 – 931N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

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).

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
Helixi96 – 1005Combined sources
Helixi105 – 11814Combined sources
Helixi120 – 1223Combined sources
Helixi127 – 1304Combined sources
Beta strandi131 – 1333Combined sources
Helixi134 – 1374Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FKQX-ray1.80A20-142[»]
1FKVX-ray2.00A20-142[»]
1HFYX-ray2.30A/B20-142[»]
1HMKX-ray2.00A19-142[»]
3B0KX-ray1.60A/B21-142[»]
ProteinModelPortaliP00712.
SMRiP00712. Positions 20-139.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00712.

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG052297.
KOiK00704.

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.

P00712-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMSFVSLLLV GILFHATQAE QLTKCEVFQK LKDLKDYGGV SLPEWVCTAF
60 70 80 90 100
HTSGYDTQAI VQNNDSTEYG LFQINNKIWC KDDQNPHSRN ICNISCDKFL
110 120 130 140
DDDLTDDIVC AKKILDKVGI NYWLAHKALC SEKLDQWLCE KL
Length:142
Mass (Da):16,255
Last modified:November 1, 1988 - v1
Checksum:iABA2C83D821BE493
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05149 mRNA. Translation: CAA28797.1.
M63868 Genomic DNA. No translation available.
PIRiJU0455. LAGT.
RefSeqiNP_001272564.1. NM_001285635.1.
UniGeneiChi.599.

Genome annotation databases

GeneIDi100860779.
KEGGichx:100860779.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05149 mRNA. Translation: CAA28797.1.
M63868 Genomic DNA. No translation available.
PIRiJU0455. LAGT.
RefSeqiNP_001272564.1. NM_001285635.1.
UniGeneiChi.599.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FKQX-ray1.80A20-142[»]
1FKVX-ray2.00A20-142[»]
1HFYX-ray2.30A/B20-142[»]
1HMKX-ray2.00A19-142[»]
3B0KX-ray1.60A/B21-142[»]
ProteinModelPortaliP00712.
SMRiP00712. Positions 20-139.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100860779.
KEGGichx:100860779.

Organism-specific databases

CTDi3906.

Phylogenomic databases

HOVERGENiHBG052297.
KOiK00704.

Miscellaneous databases

EvolutionaryTraceiP00712.

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

  1. "Molecular cloning and sequencing of cDNA encoding goat pre alpha-lactalbumin."
    Kumagai I., Tamaki E., Kakinuma S., Miura K.
    J. Biochem. 101:511-517(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Sequence of the goat alpha-lactalbumin-encoding gene: comparison with the bovine gene and evidence of related sequences in the goat genome."
    Vilotte J.-L., Soulier S., Printz C., Mercier J.-C.
    Gene 98:271-276(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  3. Cited for: PROTEIN SEQUENCE OF 20-142.
  4. "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.
  5. "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).
  6. "Effect of the extra N-terminal methionine residue on the stability and folding of recombinant alpha-lactalbumin expressed in Escherichia coli."
    Chaudhuri T.K., Horii K., Yoda T., Arai M., Nagata S., Terada T.P., Uchiyama H., Ikura T., Tsumoto K., Kataoka H., Matsushima M., Kuwajima K., Kumagai I.
    J. Mol. Biol. 285:1179-1194(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Entry informationi

Entry nameiLALBA_CAPHI
AccessioniPrimary (citable) accession number: P00712
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1988
Last modified: November 11, 2015
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.