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Alpha-lactalbumin (Lactose synthase B protein)

 LALBA_CAPHI             Reviewed;         142 AA.
P00712;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-NOV-1988, sequence version 1.
25-OCT-2017, entry version 106.
RecName: Full=Alpha-lactalbumin;
AltName: Full=Lactose synthase B protein;
Flags: Precursor;
Name=LALBA;
Capra hircus (Goat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Caprinae; Capra.
NCBI_TaxID=9925;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2884215; DOI=10.1093/oxfordjournals.jbchem.a121938;
Kumagai I., Tamaki E., Kakinuma S., Miura K.;
"Molecular cloning and sequencing of cDNA encoding goat pre alpha-
lactalbumin.";
J. Biochem. 101:511-517(1987).
[2]
NUCLEOTIDE SEQUENCE.
PubMed=2016067; DOI=10.1016/0378-1119(91)90185-E;
Vilotte J.-L., Soulier S., Printz C., Mercier J.-C.;
"Sequence of the goat alpha-lactalbumin-encoding gene: comparison with
the bovine gene and evidence of related sequences in the goat
genome.";
Gene 98:271-276(1991).
[3]
PROTEIN SEQUENCE OF 20-142.
PubMed=507821; DOI=10.1016/0003-9861(79)90262-5;
McGillivray R.T.A., Brew K., Barnes K.;
"The amino acid sequence of goat alpha-lactalbumin.";
Arch. Biochem. Biophys. 197:404-414(1979).
[4]
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).
[5]
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).
[6]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=9887272; DOI=10.1006/jmbi.1998.2362;
Chaudhuri T.K., Horii K., Yoda T., Arai M., Nagata S., Terada T.P.,
Uchiyama H., Ikura T., Tsumoto K., Kataoka H., Matsushima M.,
Kuwajima K., Kumagai I.;
"Effect of the extra N-terminal methionine residue on the stability
and folding of recombinant alpha-lactalbumin expressed in Escherichia
coli.";
J. Mol. Biol. 285:1179-1194(1999).
-!- 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).
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Mammary gland specific. Secreted in milk.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
{ECO:0000255|PROSITE-ProRule:PRU00680}.
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EMBL; X05149; CAA28797.1; -; mRNA.
EMBL; M63868; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; JU0455; LAGT.
RefSeq; NP_001272564.1; NM_001285635.1.
UniGene; Chi.599; -.
PDB; 1FKQ; X-ray; 1.80 A; A=20-142.
PDB; 1FKV; X-ray; 2.00 A; A=20-142.
PDB; 1HFY; X-ray; 2.30 A; A/B=20-142.
PDB; 1HMK; X-ray; 2.00 A; A=19-142.
PDB; 3B0K; X-ray; 1.60 A; A/B=21-142.
PDBsum; 1FKQ; -.
PDBsum; 1FKV; -.
PDBsum; 1HFY; -.
PDBsum; 1HMK; -.
PDBsum; 3B0K; -.
ProteinModelPortal; P00712; -.
SMR; P00712; -.
GeneID; 100860779; -.
KEGG; chx:100860779; -.
CTD; 3906; -.
HOVERGEN; HBG052297; -.
KO; K00704; -.
OrthoDB; EOG091G0R9V; -.
EvolutionaryTrace; P00712; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0004461; F:lactose synthase activity; IEA:InterPro.
GO; GO:0005989; P:lactose biosynthetic process; IEA:UniProtKB-KW.
CDD; cd00119; LYZ1; 1.
InterPro; IPR001916; Glyco_hydro_22.
InterPro; IPR019799; Glyco_hydro_22_CS.
InterPro; IPR000545; Lactalbumin.
InterPro; IPR023346; Lysozyme-like_dom.
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; Calcium; Direct protein sequencing; Disulfide bond;
Glycoprotein; Lactose biosynthesis; Metal-binding; Milk protein;
Secreted; Signal.
SIGNAL 1 19 {ECO:0000269|PubMed:507821}.
CHAIN 20 142 Alpha-lactalbumin.
/FTId=PRO_0000018442.
CA_BIND 97 108
CARBOHYD 64 64 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 93 93 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 25 139
DISULFID 47 130
DISULFID 80 96
DISULFID 92 110
HELIX 24 30 {ECO:0000244|PDB:3B0K}.
HELIX 32 34 {ECO:0000244|PDB:3B0K}.
HELIX 37 39 {ECO:0000244|PDB:3B0K}.
HELIX 42 53 {ECO:0000244|PDB:3B0K}.
STRAND 60 62 {ECO:0000244|PDB:3B0K}.
STRAND 67 69 {ECO:0000244|PDB:3B0K}.
TURN 70 73 {ECO:0000244|PDB:3B0K}.
TURN 76 79 {ECO:0000244|PDB:3B0K}.
HELIX 96 100 {ECO:0000244|PDB:3B0K}.
HELIX 105 118 {ECO:0000244|PDB:3B0K}.
HELIX 120 122 {ECO:0000244|PDB:3B0K}.
HELIX 127 130 {ECO:0000244|PDB:3B0K}.
STRAND 131 133 {ECO:0000244|PDB:1FKV}.
HELIX 134 137 {ECO:0000244|PDB:3B0K}.
SEQUENCE 142 AA; 16255 MW; ABA2C83D821BE493 CRC64;
MMSFVSLLLV GILFHATQAE QLTKCEVFQK LKDLKDYGGV SLPEWVCTAF HTSGYDTQAI
VQNNDSTEYG LFQINNKIWC KDDQNPHSRN ICNISCDKFL DDDLTDDIVC AKKILDKVGI
NYWLAHKALC SEKLDQWLCE KL


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