Alpha-lactalbumin precursor - Mus musculus (Mouse)

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P29752 (LALBA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 116. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Alpha-lactalbumin

Alternative name(s):
Lactose synthase B protein

Gene names

Name:

Lalba

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	143 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 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 process	Lactose biosynthesis
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Milk protein
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome 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 activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
B4GALT1	P08037	10	EBI-1031454,EBI-1031436	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

Chain

21 – 143

123

Alpha-lactalbumin

PRO_0000018446

Regions

Calcium binding

98 – 109

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Secondary structure

143

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P29752 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 0322892711FF4309
Show »

FASTA

143

16,260

        10         20         30         40         50         60 
MMHFVPLFLV CILSLPAFQA TELTKCKVSH AIKDIDGYQG ISLLEWACVL FHTSGYDTQA 

        70         80         90        100        110        120 
VVNDNGSTEY GLFQISDRFW CKSSEFPESE NICGISCDKL LDDELDDDIA CAKKILAIKG 

       130        140 
IDYWKAYKPM CSEKLEQWRC EKP

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence of the murine alpha-lactalbumin-encoding cDNA: interspecies comparison of the coding frame and deduced pre-protein." Vilotte J.-L., Soulier S., Mercier J.-C. Gene 112:251-255(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c.
[2]	"Isolation and characterization of the mouse alpha-lactalbumin-encoding gene: interspecies comparison, tissue- and stage-specific expression." Vilotte J.-L., Soulier S. Gene 119:287-292(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"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]. Strain: FVB/N. Tissue: Mammary gland.
[4]	"Crystal structure of lactose synthase reveals a large conformational change in its catalytic component, the beta1,4-galactosyltransferase-I." Ramakrishnan B., Qasba P.K. J. Mol. Biol. 310:205-218(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 21-143 IN COMPLEX WITH B4GALT1.
[5]	"The role of tryptophan 314 in the conformational changes of beta1,4-galactosyltransferase-I." Ramasamy V., Ramakrishnan B., Boeggeman E., Qasba P.K. J. Mol. Biol. 331:1065-1076(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 21-143 IN COMPLEX WITH B4GALT1.
[6]	"Alpha-lactalbumin (LA) stimulates milk beta-1,4-galactosyltransferase I (beta 4Gal-T1) to transfer glucose from UDP-glucose to N-acetylglucosamine. Crystal structure of beta 4Gal-T1 x LA complex with UDP-Glc." Ramakrishnan B., Shah P.S., Qasba P.K. J. Biol. Chem. 276:37665-37671(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) OF 21-143 IN COMPLEX WITH B4GALT1 AND UDP-GLC.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M80909 mRNA. Translation: AAA37208.1.
M87863 Genomic DNA. Translation: AAA37209.1.
BC006922 mRNA. Translation: AAH06922.1.
BC069916 mRNA. Translation: AAH69916.1.

IPI

IPI00129166.

PIR

JC1302.

RefSeq

NP_034809.1. NM_010679.1.

UniGene

Mm.5074.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NF5	X-ray	2.00	A/C	21-143	[»]
1NHE	X-ray	2.50	A/C	21-143	[»]
1NKH	X-ray	2.00	A/C	21-143	[»]
1NMM	X-ray	2.00	A/C	21-143	[»]
1NQI	X-ray	2.00	A/C	21-143	[»]
1NWG	X-ray	2.32	A/C	21-143	[»]
1O23	X-ray	2.32	A/C	21-143	[»]
1OQM	X-ray	2.10	A/C	21-143	[»]
1PZY	X-ray	2.30	A/C	21-143	[»]
1YRO	X-ray	1.90	A/C	21-143	[»]
2FYC	X-ray	2.00	A/C	21-143	[»]
2FYD	X-ray	2.00	A/C	21-143	[»]

ProteinModelPortal

P29752.

SMR

P29752. Positions 21-143.

ModBase

Search...

Protein-protein interaction databases

IntAct

P29752. 1 interaction.

STRING

10090.ENSMUSP00000023726.

Proteomic databases

PaxDb

P29752.

PRIDE

P29752.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000023726; ENSMUSP00000023726; ENSMUSG00000022991.

GeneID

16770.

KEGG

mmu:16770.

UCSC

uc007xmo.1. mouse.

Organism-specific databases

CTD

3906.

MGI

MGI:96742. Lalba.

Phylogenomic databases

eggNOG

NOG72593.

GeneTree

ENSGT00550000074398.

HOGENOM

HOG000037357.

HOVERGEN

HBG052297.

InParanoid

P29752.

K00704.

OMA

KCELSQV.

OrthoDB

EOG43JC60.

Gene expression databases

Bgee

P29752.

CleanEx

MM_LALBA.

Genevestigator

P29752.

GermOnline

ENSMUSG00000022991. Mus musculus.

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

ChiTaRS

LALBA. mouse.

EvolutionaryTrace

P29752.

NextBio

290598.

SOURCE

Search...

Entry information

Entry name

LALBA_MOUSE

Accession

Primary (citable) accession number: P29752

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	April 3, 2013
This is version 116 of the entry and version 1 of the sequence. [Complete history]

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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents