LALBA_SHEEP
ID LALBA_SHEEP Reviewed; 142 AA.
AC P09462; Q9GKS5;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 27-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Alpha-lactalbumin;
DE AltName: Full=Lactose synthase B protein;
DE Flags: Precursor;
GN Name=LALBA;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=3120794; DOI=10.1016/0300-9084(87)90179-9;
RA Gaye P., Hue-Delahaie D., Mercier J.-C., Soulier S., Vilotte J.-L.,
RA Furet J.-P.;
RT "Complete nucleotide sequence of ovine alpha-lactalbumin mRNA.";
RL Biochimie 69:601-608(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Corriedale; TISSUE=Blood;
RA Yamamoto N.;
RT "Ovis aries alpha lactalbumin.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PARTIAL PROTEIN SEQUENCE OF 1-35.
RX PubMed=736925; DOI=10.1016/0006-291x(78)91213-5;
RA Mercier J.-C., Haze G., Gaye P., Petrissant G., Hue D., Boisnard M.;
RT "Amino terminal sequence of the precursor of ovine alpha-lactalbumin.";
RL Biochem. Biophys. Res. Commun. 85:662-670(1978).
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; X06367; CAA29665.1; -; mRNA.
DR EMBL; AB052168; BAB18926.1; -; Genomic_DNA.
DR PIR; S01178; S01178.
DR RefSeq; NP_001009797.1; NM_001009797.1.
DR AlphaFoldDB; P09462; -.
DR SMR; P09462; -.
DR STRING; 9940.ENSOARP00000020650; -.
DR PRIDE; P09462; -.
DR GeneID; 443386; -.
DR KEGG; oas:443386; -.
DR CTD; 3906; -.
DR eggNOG; ENOG502T8BJ; Eukaryota.
DR OrthoDB; 1551203at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004461; F:lactose synthase activity; IEA:InterPro.
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 Calcium; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Lactose biosynthesis; Metal-binding; Milk protein; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:3120794"
FT CHAIN 20..142
FT /note="Alpha-lactalbumin"
FT /evidence="ECO:0000269|PubMed:3120794"
FT /id="PRO_0000018450"
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:0000250|UniProtKB:P00711"
FT BINDING 101
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00711"
FT BINDING 103
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00711"
FT BINDING 106
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00711"
FT BINDING 107
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00711"
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 47..130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 80..96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 92..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT CONFLICT 27
FT /note="V -> A (in Ref. 1; CAA29665)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="E -> K (in Ref. 1; CAA29665)"
FT /evidence="ECO:0000305"
FT CONFLICT 109..111
FT /note="MCV -> VCA (in Ref. 1; CAA29665)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 142 AA; 16316 MW; 0FF36C6CD21BEE2F CRC64;
MMSFVSLLLV GILFHATQAE QLTKCEVFQE LKDLKDYGGV SLPEWVCTAF HTSGYDTQAI
VQNNDSTEYG LFQINNKIWC KDDQNPHSRN ICNISCDKFL DDDLTDDIMC VKKILDKVGI
NYWLAHKALC SEKLDQWLCE KL
