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P00709

- LALBA_HUMAN

UniProt

P00709 - LALBA_HUMAN

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Protein

Alpha-lactalbumin

Gene

LALBA

Organism
Homo sapiens (Human)
Status
Reviewed - 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 – 10812Add
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. lactose synthase activity Source: InterPro

GO - Biological processi

  1. apoptotic process Source: ProtInc
  2. cell-cell signaling Source: ProtInc
  3. defense response to bacterium Source: ProtInc
  4. lactose biosynthetic process Source: ProtInc
  5. signal transduction Source: ProtInc
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
Lysozyme-like protein 7
Gene namesi
Name:LALBA
Synonyms:LYZL7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:6480. LALBA.

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30269.

Protein family/group databases

Allergomei1289. Hom s ALA.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Chaini20 – 142123Alpha-lactalbuminPRO_0000018444Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi25 ↔ 139
Disulfide bondi47 ↔ 130
Glycosylationi64 – 641N-linked (GlcNAc...)1 Publication
Disulfide bondi80 ↔ 96
Glycosylationi90 – 901N-linked (GlcNAc...); partial; atypical1 Publication
Disulfide bondi92 ↔ 110

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP00709.

Expressioni

Tissue specificityi

Mammary gland specific. Secreted in milk.

Gene expression databases

BgeeiP00709.
CleanExiHS_LALBA.
ExpressionAtlasiP00709. baseline.
GenevestigatoriP00709.

Organism-specific databases

HPAiHPA029856.

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

BioGridi110101. 6 interactions.
STRINGi9606.ENSP00000301046.

Structurei

Secondary structure

1
142
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 307
Helixi32 – 343
Helixi37 – 393
Helixi42 – 5312
Beta strandi60 – 623
Beta strandi67 – 693
Turni70 – 734
Turni76 – 783
Beta strandi79 – 813
Beta strandi83 – 853
Beta strandi91 – 955
Helixi96 – 1005
Helixi105 – 11713
Turni118 – 1203
Helixi121 – 1244
Helixi128 – 1303
Helixi134 – 1374

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP00709.
SMRiP00709. Positions 21-139.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00709.

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG72593.
GeneTreeiENSGT00550000074398.
HOGENOMiHOG000037357.
HOVERGENiHBG052297.
InParanoidiP00709.
KOiK00704.
OMAiLAHKPLC.
OrthoDBiEOG7BW0M5.
PhylomeDBiP00709.
TreeFamiTF324882.

Family and domain databases

InterProiIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000545. Lactalbumin.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PANTHERiPTHR11407:SF5. PTHR11407:SF5. 1 hit.
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.

P00709-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRFFVPLFLV GILFPAILAK QFTKCELSQL LKDIDGYGGI ALPELICTMF
60 70 80 90 100
HTSGYDTQAI VENNESTEYG LFQISNKLWC KSSQVPQSRN ICDISCDKFL
110 120 130 140
DDDITDDIMC AKKILDIKGI DYWLAHKALC TEKLEQWLCE KL
Length:142
Mass (Da):16,225
Last modified:July 21, 1986 - v1
Checksum:i647F448733B06D65
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti99 – 991F → K AA sequence (PubMed:1401360)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti46 – 461I → V.1 Publication
Corresponds to variant rs2232565 [ dbSNP | Ensembl ].
VAR_024526

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS8765.1.
PIRiA27880. LAHU.
RefSeqiNP_002280.1. NM_002289.2.
UniGeneiHs.72938.

Genome annotation databases

EnsembliENST00000301046; ENSP00000301046; ENSG00000167531.
GeneIDi3906.
KEGGihsa:3906.
UCSCiuc001rrt.3. human.

Polymorphism databases

DMDMi126001.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS8765.1.
PIRi A27880. LAHU.
RefSeqi NP_002280.1. NM_002289.2.
UniGenei Hs.72938.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A4V X-ray 1.80 A 20-142 [» ]
1B9O X-ray 1.15 A 20-142 [» ]
1CB3 NMR - A 120-129 [» ]
1HML X-ray 1.70 A 1-142 [» ]
3B0I X-ray 1.80 A 20-142 [» ]
3B0O X-ray 1.61 A/B 21-142 [» ]
4L41 X-ray 2.70 A/B 19-142 [» ]
ProteinModelPortali P00709.
SMRi P00709. Positions 21-139.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110101. 6 interactions.
STRINGi 9606.ENSP00000301046.

Protein family/group databases

Allergomei 1289. Hom s ALA.

Polymorphism databases

DMDMi 126001.

Proteomic databases

PRIDEi P00709.

Protocols and materials databases

DNASUi 3906.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000301046 ; ENSP00000301046 ; ENSG00000167531 .
GeneIDi 3906.
KEGGi hsa:3906.
UCSCi uc001rrt.3. human.

Organism-specific databases

CTDi 3906.
GeneCardsi GC12M048927.
HGNCi HGNC:6480. LALBA.
HPAi HPA029856.
MIMi 149750. gene.
neXtProti NX_P00709.
PharmGKBi PA30269.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG72593.
GeneTreei ENSGT00550000074398.
HOGENOMi HOG000037357.
HOVERGENi HBG052297.
InParanoidi P00709.
KOi K00704.
OMAi LAHKPLC.
OrthoDBi EOG7BW0M5.
PhylomeDBi P00709.
TreeFami TF324882.

Miscellaneous databases

EvolutionaryTracei P00709.
GeneWikii Alpha-lactalbumin.
GenomeRNAii 3906.
NextBioi 15335.
PROi P00709.
SOURCEi Search...

Gene expression databases

Bgeei P00709.
CleanExi HS_LALBA.
ExpressionAtlasi P00709. baseline.
Genevestigatori P00709.

Family and domain databases

InterProi IPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000545. Lactalbumin.
IPR023346. Lysozyme-like_dom.
[Graphical view ]
PANTHERi PTHR11407:SF5. PTHR11407:SF5. 1 hit.
Pfami PF00062. Lys. 1 hit.
[Graphical view ]
PRINTSi PR00136. LACTALBUMIN.
PR00135. LYZLACT.
SMARTi SM00263. LYZ1. 1 hit.
[Graphical view ]
SUPFAMi SSF53955. SSF53955. 1 hit.
PROSITEi PS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiLALBA_HUMAN
AccessioniPrimary (citable) accession number: P00709
Secondary accession number(s): Q6FGX0, Q9UDK4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 29, 2014
This is version 149 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

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. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3