LALBA_CAPHI
ID LALBA_CAPHI Reviewed; 142 AA.
AC P00712;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Alpha-lactalbumin;
DE AltName: Full=Lactose synthase B protein;
DE Flags: Precursor;
GN Name=LALBA;
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2884215; DOI=10.1093/oxfordjournals.jbchem.a121938;
RA Kumagai I., Tamaki E., Kakinuma S., Miura K.;
RT "Molecular cloning and sequencing of cDNA encoding goat pre alpha-
RT lactalbumin.";
RL J. Biochem. 101:511-517(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=2016067; DOI=10.1016/0378-1119(91)90185-e;
RA Vilotte J.-L., Soulier S., Printz C., Mercier J.-C.;
RT "Sequence of the goat alpha-lactalbumin-encoding gene: comparison with the
RT bovine gene and evidence of related sequences in the goat genome.";
RL Gene 98:271-276(1991).
RN [3]
RP PROTEIN SEQUENCE OF 20-142.
RX PubMed=507821; DOI=10.1016/0003-9861(79)90262-5;
RA McGillivray R.T.A., Brew K., Barnes K.;
RT "The amino acid sequence of goat alpha-lactalbumin.";
RL Arch. Biochem. Biophys. 197:404-414(1979).
RN [4]
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 [5] {ECO:0007744|PDB:1HFY}
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).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=9887272; DOI=10.1006/jmbi.1998.2362;
RA Chaudhuri T.K., Horii K., Yoda T., Arai M., Nagata S., Terada T.P.,
RA Uchiyama H., Ikura T., Tsumoto K., Kataoka H., Matsushima M., Kuwajima K.,
RA Kumagai I.;
RT "Effect of the extra N-terminal methionine residue on the stability and
RT folding of recombinant alpha-lactalbumin expressed in Escherichia coli.";
RL J. Mol. Biol. 285:1179-1194(1999).
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 -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Mammary gland specific. Secreted in milk.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00680}.
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DR EMBL; X05149; CAA28797.1; -; mRNA.
DR EMBL; M63868; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; JU0455; LAGT.
DR RefSeq; NP_001272564.1; NM_001285635.1.
DR PDB; 1FKQ; X-ray; 1.80 A; A=20-142.
DR PDB; 1FKV; X-ray; 2.00 A; A=20-142.
DR PDB; 1HFY; X-ray; 2.30 A; A/B=20-142.
DR PDB; 1HMK; X-ray; 2.00 A; A=19-142.
DR PDB; 3B0K; X-ray; 1.60 A; A/B=21-142.
DR PDBsum; 1FKQ; -.
DR PDBsum; 1FKV; -.
DR PDBsum; 1HFY; -.
DR PDBsum; 1HMK; -.
DR PDBsum; 3B0K; -.
DR AlphaFoldDB; P00712; -.
DR SMR; P00712; -.
DR STRING; 9925.ENSCHIP00000024154; -.
DR PRIDE; P00712; -.
DR Ensembl; ENSCHIT00000032014; ENSCHIP00000024154; ENSCHIG00000021449.
DR GeneID; 100860779; -.
DR KEGG; chx:100860779; -.
DR CTD; 3906; -.
DR GeneTree; ENSGT00940000161726; -.
DR OMA; KCELSQV; -.
DR OrthoDB; 1551203at2759; -.
DR EvolutionaryTrace; P00712; -.
DR Proteomes; UP000291000; Chromosome 5.
DR Bgee; ENSCHIG00000021449; Expressed in testis.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004461; F:lactose synthase activity; IEA:Ensembl.
DR GO; GO:0005989; P:lactose biosynthetic process; IEA:UniProtKB-KW.
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; 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:507821"
FT CHAIN 20..142
FT /note="Alpha-lactalbumin"
FT /id="PRO_0000018442"
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:1HFY"
FT BINDING 101
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8805552,
FT ECO:0007744|PDB:1HFY"
FT BINDING 103
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8805552,
FT ECO:0007744|PDB:1HFY"
FT BINDING 106
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8805552,
FT ECO:0007744|PDB:1HFY"
FT BINDING 107
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8805552,
FT ECO:0007744|PDB:1HFY"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 25..139
FT DISULFID 47..130
FT DISULFID 80..96
FT DISULFID 92..110
FT HELIX 24..30
FT /evidence="ECO:0007829|PDB:3B0K"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:3B0K"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:3B0K"
FT HELIX 42..53
FT /evidence="ECO:0007829|PDB:3B0K"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:3B0K"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:3B0K"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:3B0K"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:3B0K"
FT HELIX 96..100
FT /evidence="ECO:0007829|PDB:3B0K"
FT HELIX 105..118
FT /evidence="ECO:0007829|PDB:3B0K"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:3B0K"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:3B0K"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:1FKV"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:3B0K"
SQ SEQUENCE 142 AA; 16255 MW; ABA2C83D821BE493 CRC64;
MMSFVSLLLV GILFHATQAE QLTKCEVFQK LKDLKDYGGV SLPEWVCTAF HTSGYDTQAI
VQNNDSTEYG LFQINNKIWC KDDQNPHSRN ICNISCDKFL DDDLTDDIVC AKKILDKVGI
NYWLAHKALC SEKLDQWLCE KL
