LALBA_PAPCY
ID LALBA_PAPCY Reviewed; 123 AA.
AC P12065;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Alpha-lactalbumin;
DE AltName: Full=Lactose synthase B protein;
GN Name=LALBA;
OS Papio cynocephalus (Yellow baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9556;
RN [1]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=2769757; DOI=10.1016/0022-2836(89)90091-0;
RA Acharya K.R., Stuart D.I., Walker N.P.C., Lewis M., Phillips D.C.;
RT "Refined structure of baboon alpha-lactalbumin at 1.7-A resolution.
RT Comparison with C-type lysozyme.";
RL J. Mol. Biol. 208:99-127(1989).
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}.
CC -!- CAUTION: This is a tentative sequence based on X-ray data.
CC {ECO:0000305}.
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DR PIR; A58671; A58671.
DR PDB; 1ALC; X-ray; 1.70 A; A=1-123.
DR PDBsum; 1ALC; -.
DR AlphaFoldDB; P12065; -.
DR SMR; P12065; -.
DR EvolutionaryTrace; P12065; -.
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 3D-structure; Calcium; Disulfide bond; Glycoprotein; Lactose biosynthesis;
KW Metal-binding; Milk protein; Secreted.
FT CHAIN 1..123
FT /note="Alpha-lactalbumin"
FT /id="PRO_0000208841"
FT DOMAIN 1..123
FT /note="C-type lysozyme"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00711"
FT BINDING 82
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00711"
FT BINDING 84
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00711"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00711"
FT BINDING 88
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00711"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 6..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680,
FT ECO:0000269|PubMed:2769757"
FT DISULFID 28..111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680,
FT ECO:0000269|PubMed:2769757"
FT DISULFID 61..77
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680,
FT ECO:0000269|PubMed:2769757"
FT DISULFID 73..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680,
FT ECO:0000269|PubMed:2769757"
FT HELIX 5..11
FT /evidence="ECO:0007829|PDB:1ALC"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:1ALC"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:1ALC"
FT HELIX 23..34
FT /evidence="ECO:0007829|PDB:1ALC"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:1ALC"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:1ALC"
FT TURN 51..54
FT /evidence="ECO:0007829|PDB:1ALC"
FT TURN 57..60
FT /evidence="ECO:0007829|PDB:1ALC"
FT HELIX 77..81
FT /evidence="ECO:0007829|PDB:1ALC"
FT HELIX 86..98
FT /evidence="ECO:0007829|PDB:1ALC"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:1ALC"
FT HELIX 106..110
FT /evidence="ECO:0007829|PDB:1ALC"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:1ALC"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:1ALC"
SQ SEQUENCE 123 AA; 14174 MW; 7DAE9AD909B095D9 CRC64;
KQFTKCELSQ NLYDIDGYGR IALPELICTM FHTSGYDTQA IVENNESTEY GLFQISNALW
CKSSQSPQSR NICDITCDKF LDDDITDDIM CAKKILDIKG IDYWIAHKAL CTEKLEQWLC
EKE
