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Alpha-lactalbumin (Lactose synthase B protein) (allergen Bos d 4)

 LALBA_BOVIN             Reviewed;         142 AA.
P00711; Q3T111; Q95NE4;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 2.
05-DEC-2018, entry version 159.
RecName: Full=Alpha-lactalbumin;
AltName: Full=Lactose synthase B protein;
AltName: Allergen=Bos d 4;
Flags: Precursor;
Name=LALBA; Synonyms=ALACTA;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3120795; DOI=10.1016/0300-9084(87)90180-5;
Vilotte J.-L., Soulier S., Mercier J.-C., Gaye P., Hue-Delahaie D.,
Furet J.-P.;
"Complete nucleotide sequence of bovine alpha-lactalbumin gene:
comparison with its rat counterpart.";
Biochimie 69:609-620(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3443304; DOI=10.1016/0378-1119(87)90371-4;
Hurley W.L., Schuler L.A.;
"Molecular cloning and nucleotide sequence of a bovine alpha-
lactalbumin cDNA.";
Gene 61:119-122(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2687274;
Wang M., Scott W.A., Rao K.R., Udey J., Conner G.E., Brew K.;
"Recombinant bovine alpha-lactalbumin obtained by limited proteolysis
of a fusion protein expressed at high levels in Escherichia coli.";
J. Biol. Chem. 264:21116-21121(1989).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Angus, Hereford, Holstein, Japanese black, and Jersey;
TISSUE=Blood;
Yamamoto N.;
"Bos taurus alpha lactalbumin gene.";
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Dhinakar Raj G., Kumanan K.;
"Bovine gene for alpha lactalbumin.";
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=16305752; DOI=10.1186/1471-2164-6-166;
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
"Characterization of 954 bovine full-CDS cDNA sequences.";
BMC Genomics 6:166-166(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Mammary gland;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[8]
PROTEIN SEQUENCE OF 20-142.
PubMed=5532231;
Brew K., Castellino F.J., Vanaman T.C., Hill R.L.;
"The complete amino acid sequence of bovine alpha-lactalbumin.";
J. Biol. Chem. 245:4570-4582(1970).
[9]
SEQUENCE REVISION.
PubMed=6715332;
Shewale J.G., Sinha S.K., Brew K.;
"Evolution of alpha-lactalbumins. The complete amino acid sequence of
the alpha-lactalbumin from a marsupial (Macropus rufogriseus) and
corrections to regions of sequence in bovine and goat alpha-
lactalbumins.";
J. Biol. Chem. 259:4947-4956(1984).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
PubMed=8482536; DOI=10.1016/0378-1119(93)90369-E;
Bleck G.T., Bremel R.D.;
"Sequence and single-base polymorphisms of the bovine alpha-
lactalbumin 5'-flanking region.";
Gene 126:213-218(1993).
[11]
DISULFIDE BONDS.
PubMed=5532232;
Vanaman T.C., Brew K., Hill R.L.;
"The disulfide bonds of bovine alpha-lactalbumin.";
J. Biol. Chem. 245:4583-4590(1970).
[12]
PRELIMINARY PROTEIN SEQUENCE (VARIANTS ALLELIC).
STRAIN=Droughtmaster;
PubMed=5534301;
Bell K., Hopper K.E., McKenzie H.A., Murphy W.H., Shaw D.C.;
"A comparison of bovine alpha-lactalbumin A and B of Droughtmaster.";
Biochim. Biophys. Acta 214:437-444(1970).
[13]
PRELIMINARY PROTEIN SEQUENCE OF 20-142 (VARIANT A).
STRAIN=Zebu cattle;
Gordon W.G., Aschaffenburg R., Sen A., Ghosh S.K.;
"Amino acid composition of several alpha-lactalbumins.";
J. Dairy Sci. 51:947-947(1968).
[14]
CALCIUM-BINDING DATA.
PubMed=6774718; DOI=10.1016/0006-291X(80)91585-5;
Hiraoka Y., Segawa T., Kuwajima K., Sugai S., Murai N.;
"Alpha-lactalbumin: a calcium metalloprotein.";
Biochem. Biophys. Res. Commun. 95:1098-1104(1980).
[15]
CALCIUM-BINDING DATA.
PubMed=7263672;
Kronman M.J., Sinha S.K., Brew K.;
"Characteristics of the binding of Ca2+ and other divalent metal ions
to bovine alpha-lactalbumin.";
J. Biol. Chem. 256:8582-8587(1981).
[16]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
PubMed=8805552; DOI=10.1016/S0969-2126(96)00075-5;
Pike A.C.W., Brew K., Acharya K.R.;
"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.";
Structure 4:691-703(1996).
-!- 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: Lactose synthase (LS) is a heterodimer of a catalytic
component, beta1,4-galactosyltransferase (beta4Gal-T1) and a
regulatory component, alpha-lactalbumin (LA).
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-7080486, EBI-7080486;
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Mammary gland specific. Secreted in milk.
-!- ALLERGEN: Causes an allergic reaction in human. Is one of the
causes of cow's milk allergy.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
{ECO:0000255|PROSITE-ProRule:PRU00680}.
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EMBL; X06366; CAA29664.1; -; Genomic_DNA.
EMBL; M18780; AAA30615.1; -; mRNA.
EMBL; J05147; AAA30367.1; -; mRNA.
EMBL; AB052163; BAB18921.1; -; Genomic_DNA.
EMBL; AB052164; BAB18922.1; -; Genomic_DNA.
EMBL; AB052165; BAB18923.1; -; Genomic_DNA.
EMBL; AB052166; BAB18924.1; -; Genomic_DNA.
EMBL; AB052167; BAB18925.1; -; Genomic_DNA.
EMBL; AF249896; AAF63624.1; -; Genomic_DNA.
EMBL; BT025469; ABF57425.1; -; mRNA.
EMBL; BC102173; AAI02174.1; -; mRNA.
EMBL; M90645; AAA30614.1; -; Genomic_DNA.
PIR; A27360; LABO.
RefSeq; NP_776803.1; NM_174378.2.
UniGene; Bt.87412; -.
PDB; 1F6R; X-ray; 2.20 A; A/B/C/D/E/F=20-142.
PDB; 1F6S; X-ray; 2.20 A; A/B/C/D/E/F=20-142.
PDB; 1HFZ; X-ray; 2.30 A; A/B/C/D=20-142.
PDB; 2G4N; X-ray; 2.30 A; A/B/C/D/E/F=20-142.
PDB; 5X84; X-ray; 1.75 A; A=20-142.
PDBsum; 1F6R; -.
PDBsum; 1F6S; -.
PDBsum; 1HFZ; -.
PDBsum; 2G4N; -.
PDBsum; 5X84; -.
ProteinModelPortal; P00711; -.
SMR; P00711; -.
BioGrid; 159201; 1.
IntAct; P00711; 3.
MINT; P00711; -.
STRING; 9913.ENSBTAP00000007701; -.
Allergome; 163; Bos d 4.
Allergome; 3165; Bos d 4.0101.
CarbonylDB; P00711; -.
PaxDb; P00711; -.
PeptideAtlas; P00711; -.
PRIDE; P00711; -.
Ensembl; ENSBTAT00000007701; ENSBTAP00000007701; ENSBTAG00000005859.
GeneID; 281894; -.
KEGG; bta:281894; -.
CTD; 3906; -.
VGNC; VGNC:30768; LALBA.
eggNOG; ENOG410IX41; Eukaryota.
eggNOG; ENOG410ZQK6; LUCA.
GeneTree; ENSGT00940000161726; -.
HOGENOM; HOG000037357; -.
HOVERGEN; HBG052297; -.
InParanoid; P00711; -.
KO; K00704; -.
OMA; LAHKPLC; -.
OrthoDB; EOG091G0R9V; -.
TreeFam; TF324882; -.
Reactome; R-BTA-5653890; Lactose synthesis.
EvolutionaryTrace; P00711; -.
Proteomes; UP000009136; Chromosome 5.
Bgee; ENSBTAG00000005859; Expressed in 1 organ(s), highest expression level in prefrontal cortex.
ExpressionAtlas; P00711; differential.
GO; GO:0005615; C:extracellular space; IDA:AgBase.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004461; F:lactose synthase activity; IEA:InterPro.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IBA:GO_Central.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central.
GO; GO:0005989; P:lactose biosynthetic process; IEA:UniProtKB-KW.
GO; GO:1903496; P:response to 11-deoxycorticosterone; IDA:AgBase.
GO; GO:1903494; P:response to dehydroepiandrosterone; IDA:AgBase.
GO; GO:0032355; P:response to estradiol; IDA:AgBase.
GO; GO:0032570; P:response to progesterone; IDA:AgBase.
CDD; cd00119; LYZ1; 1.
InterPro; IPR001916; Glyco_hydro_22.
InterPro; IPR019799; Glyco_hydro_22_CS.
InterPro; IPR000545; Lactalbumin.
InterPro; IPR023346; Lysozyme-like_dom_sf.
PANTHER; PTHR11407:SF32; PTHR11407:SF32; 1.
Pfam; PF00062; Lys; 1.
PRINTS; PR00136; LACTALBUMIN.
PRINTS; PR00135; LYZLACT.
SMART; SM00263; LYZ1; 1.
SUPFAM; SSF53955; SSF53955; 1.
PROSITE; PS00128; LACTALBUMIN_LYSOZYME_1; 1.
PROSITE; PS51348; LACTALBUMIN_LYSOZYME_2; 1.
1: Evidence at protein level;
3D-structure; Allergen; Calcium; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Lactose biosynthesis; Metal-binding; Milk protein; Reference proteome;
Secreted; Signal.
SIGNAL 1 19 {ECO:0000269|PubMed:5532231}.
CHAIN 20 142 Alpha-lactalbumin.
/FTId=PRO_0000018439.
CA_BIND 97 108 {ECO:0000255|PROSITE-ProRule:PRU00680}.
CARBOHYD 64 64 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 25 139 {ECO:0000255|PROSITE-ProRule:PRU00680,
ECO:0000269|PubMed:5532232}.
DISULFID 47 130 {ECO:0000255|PROSITE-ProRule:PRU00680,
ECO:0000269|PubMed:5532232}.
DISULFID 80 96 {ECO:0000255|PROSITE-ProRule:PRU00680,
ECO:0000269|PubMed:5532232}.
DISULFID 92 110 {ECO:0000255|PROSITE-ProRule:PRU00680,
ECO:0000269|PubMed:5532232}.
VARIANT 29 29 R -> Q (in an allele of Droughtmaster
cattle; an Australian breed).
CONFLICT 49 49 T -> A (in Ref. 1 and 5). {ECO:0000305}.
CONFLICT 58 58 Q -> E (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 82 85 DDQN -> NDQD (in Ref. 8; AA sequence).
{ECO:0000305}.
HELIX 24 30 {ECO:0000244|PDB:5X84}.
HELIX 32 34 {ECO:0000244|PDB:5X84}.
HELIX 37 39 {ECO:0000244|PDB:5X84}.
HELIX 42 53 {ECO:0000244|PDB:5X84}.
STRAND 60 63 {ECO:0000244|PDB:5X84}.
STRAND 66 69 {ECO:0000244|PDB:5X84}.
TURN 70 73 {ECO:0000244|PDB:5X84}.
TURN 76 79 {ECO:0000244|PDB:5X84}.
STRAND 80 82 {ECO:0000244|PDB:1HFZ}.
HELIX 96 99 {ECO:0000244|PDB:5X84}.
STRAND 100 102 {ECO:0000244|PDB:5X84}.
HELIX 105 117 {ECO:0000244|PDB:5X84}.
HELIX 120 122 {ECO:0000244|PDB:5X84}.
HELIX 125 129 {ECO:0000244|PDB:5X84}.
STRAND 130 132 {ECO:0000244|PDB:5X84}.
HELIX 134 137 {ECO:0000244|PDB:5X84}.
SEQUENCE 142 AA; 16247 MW; 810CDB1145901405 CRC64;
MMSFVSLLLV GILFHATQAE QLTKCEVFRE LKDLKGYGGV SLPEWVCTTF HTSGYDTQAI
VQNNDSTEYG LFQINNKIWC KDDQNPHSSN ICNISCDKFL DDDLTDDIMC VKKILDKVGI
NYWLAHKALC SEKLDQWLCE KL


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