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P00709

- LALBA_HUMAN

UniProt

P00709 - LALBA_HUMAN

Protein

Alpha-lactalbumin

Gene

LALBA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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

    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

    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

    ArrayExpressiP00709.
    BgeeiP00709.
    CleanExiHS_LALBA.
    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.
    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

    MRFFVPLFLV GILFPAILAK QFTKCELSQL LKDIDGYGGI ALPELICTMF    50
    HTSGYDTQAI VENNESTEYG LFQISNKLWC KSSQVPQSRN ICDISCDKFL 100
    DDDITDDIMC AKKILDIKGI DYWLAHKALC TEKLEQWLCE KL 142
    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.
    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

    ArrayExpressi P00709.
    Bgeei P00709.
    CleanExi HS_LALBA.
    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

    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 1, 2014
    This is version 148 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