LALBA_BOVIN
ID LALBA_BOVIN Reviewed; 142 AA.
AC P00711; Q3T111; Q95NE4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Alpha-lactalbumin;
DE AltName: Full=Lactose synthase B protein;
DE AltName: Allergen=Bos d 4;
DE Flags: Precursor;
GN Name=LALBA; Synonyms=ALACTA;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3120795; DOI=10.1016/0300-9084(87)90180-5;
RA Vilotte J.-L., Soulier S., Mercier J.-C., Gaye P., Hue-Delahaie D.,
RA Furet J.-P.;
RT "Complete nucleotide sequence of bovine alpha-lactalbumin gene: comparison
RT with its rat counterpart.";
RL Biochimie 69:609-620(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3443304; DOI=10.1016/0378-1119(87)90371-4;
RA Hurley W.L., Schuler L.A.;
RT "Molecular cloning and nucleotide sequence of a bovine alpha-lactalbumin
RT cDNA.";
RL Gene 61:119-122(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2687274; DOI=10.1016/s0021-9258(19)30054-7;
RA Wang M., Scott W.A., Rao K.R., Udey J., Conner G.E., Brew K.;
RT "Recombinant bovine alpha-lactalbumin obtained by limited proteolysis of a
RT fusion protein expressed at high levels in Escherichia coli.";
RL J. Biol. Chem. 264:21116-21121(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Angus, Hereford, Holstein, Japanese black, and Jersey; TISSUE=Blood;
RA Yamamoto N.;
RT "Bos taurus alpha lactalbumin gene.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Dhinakar Raj G., Kumanan K.;
RT "Bovine gene for alpha lactalbumin.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Mammary gland;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP PROTEIN SEQUENCE OF 20-142.
RX PubMed=5532231; DOI=10.1016/s0021-9258(19)63827-5;
RA Brew K., Castellino F.J., Vanaman T.C., Hill R.L.;
RT "The complete amino acid sequence of bovine alpha-lactalbumin.";
RL J. Biol. Chem. 245:4570-4582(1970).
RN [9]
RP SEQUENCE REVISION.
RX PubMed=6715332; DOI=10.1016/s0021-9258(17)42938-3;
RA Shewale J.G., Sinha S.K., Brew K.;
RT "Evolution of alpha-lactalbumins. The complete amino acid sequence of the
RT alpha-lactalbumin from a marsupial (Macropus rufogriseus) and corrections
RT to regions of sequence in bovine and goat alpha-lactalbumins.";
RL J. Biol. Chem. 259:4947-4956(1984).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
RX PubMed=8482536; DOI=10.1016/0378-1119(93)90369-e;
RA Bleck G.T., Bremel R.D.;
RT "Sequence and single-base polymorphisms of the bovine alpha-lactalbumin 5'-
RT flanking region.";
RL Gene 126:213-218(1993).
RN [11]
RP DISULFIDE BONDS.
RX PubMed=5532232; DOI=10.1016/s0021-9258(19)63828-7;
RA Vanaman T.C., Brew K., Hill R.L.;
RT "The disulfide bonds of bovine alpha-lactalbumin.";
RL J. Biol. Chem. 245:4583-4590(1970).
RN [12]
RP PRELIMINARY PROTEIN SEQUENCE (VARIANTS ALLELIC).
RC STRAIN=Droughtmaster;
RX PubMed=5534301; DOI=10.1016/0005-2795(70)90302-8;
RA Bell K., Hopper K.E., McKenzie H.A., Murphy W.H., Shaw D.C.;
RT "A comparison of bovine alpha-lactalbumin A and B of Droughtmaster.";
RL Biochim. Biophys. Acta 214:437-444(1970).
RN [13]
RP PRELIMINARY PROTEIN SEQUENCE OF 20-142 (VARIANT A).
RC STRAIN=Zebu cattle;
RA Gordon W.G., Aschaffenburg R., Sen A., Ghosh S.K.;
RT "Amino acid composition of several alpha-lactalbumins.";
RL J. Dairy Sci. 51:947-947(1968).
RN [14]
RP CALCIUM-BINDING DATA.
RX PubMed=6774718; DOI=10.1016/0006-291x(80)91585-5;
RA Hiraoka Y., Segawa T., Kuwajima K., Sugai S., Murai N.;
RT "Alpha-lactalbumin: a calcium metalloprotein.";
RL Biochem. Biophys. Res. Commun. 95:1098-1104(1980).
RN [15]
RP CALCIUM-BINDING DATA.
RX PubMed=7263672; DOI=10.1016/s0021-9258(19)68884-8;
RA Kronman M.J., Sinha S.K., Brew K.;
RT "Characteristics of the binding of Ca2+ and other divalent metal ions to
RT bovine alpha-lactalbumin.";
RL J. Biol. Chem. 256:8582-8587(1981).
RN [16] {ECO:0007744|PDB:1HFZ}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 20-142 IN COMPLEX WITH CALCIUM.
RX PubMed=8805552; DOI=10.1016/s0969-2126(96)00075-5;
RA Pike A.C.W., Brew K., Acharya K.R.;
RT "Crystal structures of guinea-pig, goat and bovine alpha-lactalbumin
RT highlight the enhanced conformational flexibility of regions that are
RT significant for its action in lactose synthase.";
RL Structure 4:691-703(1996).
CC -!- FUNCTION: Regulatory subunit of lactose synthase, changes the substrate
CC specificity of galactosyltransferase in the mammary gland making
CC glucose a good acceptor substrate for this enzyme. This enables LS to
CC synthesize lactose, the major carbohydrate component of milk. In other
CC tissues, galactosyltransferase transfers galactose onto the N-
CC acetylglucosamine of the oligosaccharide chains in glycoproteins.
CC -!- SUBUNIT: Lactose synthase (LS) is a heterodimer of a catalytic
CC component, beta1,4-galactosyltransferase (beta4Gal-T1) and a regulatory
CC component, alpha-lactalbumin (LA).
CC -!- INTERACTION:
CC P00711; P00711: LALBA; NbExp=3; IntAct=EBI-7080486, EBI-7080486;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Mammary gland specific. Secreted in milk.
CC -!- ALLERGEN: Causes an allergic reaction in human. Is one of the causes of
CC cow's milk allergy.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00680}.
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DR EMBL; X06366; CAA29664.1; -; Genomic_DNA.
DR EMBL; M18780; AAA30615.1; -; mRNA.
DR EMBL; J05147; AAA30367.1; -; mRNA.
DR EMBL; AB052163; BAB18921.1; -; Genomic_DNA.
DR EMBL; AB052164; BAB18922.1; -; Genomic_DNA.
DR EMBL; AB052165; BAB18923.1; -; Genomic_DNA.
DR EMBL; AB052166; BAB18924.1; -; Genomic_DNA.
DR EMBL; AB052167; BAB18925.1; -; Genomic_DNA.
DR EMBL; AF249896; AAF63624.1; -; Genomic_DNA.
DR EMBL; BT025469; ABF57425.1; -; mRNA.
DR EMBL; BC102173; AAI02174.1; -; mRNA.
DR EMBL; M90645; AAA30614.1; -; Genomic_DNA.
DR PIR; A27360; LABO.
DR RefSeq; NP_776803.1; NM_174378.2.
DR PDB; 1F6R; X-ray; 2.20 A; A/B/C/D/E/F=20-142.
DR PDB; 1F6S; X-ray; 2.20 A; A/B/C/D/E/F=20-142.
DR PDB; 1HFZ; X-ray; 2.30 A; A/B/C/D=20-142.
DR PDB; 2G4N; X-ray; 2.30 A; A/B/C/D/E/F=20-142.
DR PDB; 6IP9; X-ray; 1.85 A; A=20-142.
DR PDBsum; 1F6R; -.
DR PDBsum; 1F6S; -.
DR PDBsum; 1HFZ; -.
DR PDBsum; 2G4N; -.
DR PDBsum; 6IP9; -.
DR AlphaFoldDB; P00711; -.
DR BMRB; P00711; -.
DR SMR; P00711; -.
DR BioGRID; 159201; 1.
DR IntAct; P00711; 3.
DR MINT; P00711; -.
DR STRING; 9913.ENSBTAP00000007701; -.
DR Allergome; 163; Bos d 4.
DR Allergome; 3165; Bos d 4.0101.
DR CarbonylDB; P00711; -.
DR PaxDb; P00711; -.
DR PeptideAtlas; P00711; -.
DR PRIDE; P00711; -.
DR GeneID; 281894; -.
DR KEGG; bta:281894; -.
DR CTD; 3906; -.
DR eggNOG; ENOG502T8BJ; Eukaryota.
DR HOGENOM; CLU_111620_0_1_1; -.
DR InParanoid; P00711; -.
DR OrthoDB; 1551203at2759; -.
DR TreeFam; TF324882; -.
DR EvolutionaryTrace; P00711; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004461; F:lactose synthase activity; IEA:InterPro.
DR GO; GO:0003796; F:lysozyme activity; IBA:GO_Central.
DR GO; GO:0005989; P:lactose biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:1903496; P:response to 11-deoxycorticosterone; IDA:AgBase.
DR GO; GO:1903494; P:response to dehydroepiandrosterone; IDA:AgBase.
DR GO; GO:0032355; P:response to estradiol; IDA:AgBase.
DR GO; GO:0032570; P:response to progesterone; IDA:AgBase.
DR InterPro; IPR001916; Glyco_hydro_22.
DR InterPro; IPR019799; Glyco_hydro_22_CS.
DR InterPro; IPR000545; Lactalbumin.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR PANTHER; PTHR11407; PTHR11407; 1.
DR PANTHER; PTHR11407:SF32; PTHR11407:SF32; 1.
DR Pfam; PF00062; Lys; 1.
DR PRINTS; PR00136; LACTALBUMIN.
DR PRINTS; PR00135; LYZLACT.
DR SMART; SM00263; LYZ1; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR PROSITE; PS00128; GLYCOSYL_HYDROL_F22_1; 1.
DR PROSITE; PS51348; GLYCOSYL_HYDROL_F22_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Calcium; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Lactose biosynthesis; Metal-binding; Milk protein;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:5532231"
FT CHAIN 20..142
FT /note="Alpha-lactalbumin"
FT /id="PRO_0000018439"
FT DOMAIN 20..142
FT /note="C-type lysozyme"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8805552,
FT ECO:0007744|PDB:1HFZ"
FT BINDING 101
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8805552,
FT ECO:0007744|PDB:1HFZ"
FT BINDING 103
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8805552,
FT ECO:0007744|PDB:1HFZ"
FT BINDING 106
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8805552,
FT ECO:0007744|PDB:1HFZ"
FT BINDING 107
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8805552,
FT ECO:0007744|PDB:1HFZ"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 25..139
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680,
FT ECO:0000269|PubMed:5532232"
FT DISULFID 47..130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680,
FT ECO:0000269|PubMed:5532232"
FT DISULFID 80..96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680,
FT ECO:0000269|PubMed:5532232"
FT DISULFID 92..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680,
FT ECO:0000269|PubMed:5532232"
FT VARIANT 29
FT /note="R -> Q (in an allele of Droughtmaster cattle; an
FT Australian breed)"
FT CONFLICT 49
FT /note="T -> A (in Ref. 1 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="Q -> E (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 82..85
FT /note="DDQN -> NDQD (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 24..30
FT /evidence="ECO:0007829|PDB:6IP9"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:6IP9"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:6IP9"
FT HELIX 42..53
FT /evidence="ECO:0007829|PDB:6IP9"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:6IP9"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:6IP9"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:6IP9"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:6IP9"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:1HFZ"
FT HELIX 96..99
FT /evidence="ECO:0007829|PDB:6IP9"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:6IP9"
FT HELIX 105..117
FT /evidence="ECO:0007829|PDB:6IP9"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:6IP9"
FT HELIX 125..129
FT /evidence="ECO:0007829|PDB:6IP9"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:6IP9"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:6IP9"
SQ SEQUENCE 142 AA; 16247 MW; 810CDB1145901405 CRC64;
MMSFVSLLLV GILFHATQAE QLTKCEVFRE LKDLKGYGGV SLPEWVCTTF HTSGYDTQAI
VQNNDSTEYG LFQINNKIWC KDDQNPHSSN ICNISCDKFL DDDLTDDIMC VKKILDKVGI
NYWLAHKALC SEKLDQWLCE KL
