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Protein

Alpha-lactalbumin

Gene

LALBA

Organism
Cavia porcellus (Guinea pig)
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
OrganismiCavia porcellus (Guinea pig)
Taxonomic identifieri10141 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia
Proteomesi
  • UP000005447 Componenti: Unassembled WGS sequence

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_0000018443Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi25 ↔ 139
Disulfide bondi47 ↔ 130
Disulfide bondi80 ↔ 96
Disulfide bondi92 ↔ 110

Keywords - PTMi

Disulfide bond

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).

Protein-protein interaction databases

STRINGi10141.ENSCPOP00000019835.

Structurei

Secondary structure

1
142
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 307Combined sources
Turni31 – 366Combined sources
Helixi37 – 393Combined sources
Helixi42 – 5312Combined sources
Beta strandi60 – 634Combined sources
Beta strandi66 – 694Combined sources
Turni70 – 734Combined sources
Turni76 – 794Combined sources
Beta strandi83 – 853Combined sources
Helixi96 – 994Combined sources
Beta strandi100 – 1023Combined sources
Helixi105 – 11713Combined sources
Helixi121 – 1244Combined sources
Helixi134 – 1374Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HFXX-ray1.90A20-142[»]
ProteinModelPortaliP00713.
SMRiP00713. Positions 20-142.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00713.

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.
InParanoidiP00713.
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.

P00713-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMSFFPLLLV GILFPAVQAK QLTKCALSHE LNDLAGYRDI TLPEWLCIIF
60 70 80 90 100
HISGYDTQAI VKNSDHKEYG LFQINDKDFC ESSTTVQSRN ICDISCDKLL
110 120 130 140
DDDLTDDIMC VKKILDIKGI DYWLAHKPLC SDKLEQWYCE AQ
Length:142
Mass (Da):16,300
Last modified:July 1, 1989 - v2
Checksum:iE13FA2ACA8F1029E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti81 – 811E → D in AAA60337 (PubMed:6285305).Curated
Sequence conflicti124 – 1241L → F in AAA60337 (PubMed:6285305).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00051 mRNA. Translation: AAA60337.1.
Y00726 Genomic DNA. Translation: CAA68710.1.
PIRiS01144. LAGP.
RefSeqiNP_001166360.1. NM_001172889.1.

Genome annotation databases

EnsembliENSCPOT00000019635; ENSCPOP00000019835; ENSCPOG00000027342.
GeneIDi100379577.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00051 mRNA. Translation: AAA60337.1.
Y00726 Genomic DNA. Translation: CAA68710.1.
PIRiS01144. LAGP.
RefSeqiNP_001166360.1. NM_001172889.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HFXX-ray1.90A20-142[»]
ProteinModelPortaliP00713.
SMRiP00713. Positions 20-142.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10141.ENSCPOP00000019835.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSCPOT00000019635; ENSCPOP00000019835; ENSCPOG00000027342.
GeneIDi100379577.

Organism-specific databases

CTDi3906.

Phylogenomic databases

eggNOGiENOG410IX41. Eukaryota.
ENOG410ZQK6. LUCA.
GeneTreeiENSGT00550000074398.
HOGENOMiHOG000037357.
HOVERGENiHBG052297.
InParanoidiP00713.
OMAiLAHKPLC.
OrthoDBiEOG7BW0M5.
TreeFamiTF324882.

Miscellaneous databases

EvolutionaryTraceiP00713.

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. "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).

Entry informationi

Entry nameiLALBA_CAVPO
AccessioniPrimary (citable) accession number: P00713
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1989
Last modified: November 11, 2015
This is version 109 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. 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.