LALBA_MOUSE
ID LALBA_MOUSE Reviewed; 143 AA.
AC P29752;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Alpha-lactalbumin;
DE AltName: Full=Lactose synthase B protein;
DE Flags: Precursor;
GN Name=Lalba;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=1555774; DOI=10.1016/0378-1119(92)90385-3;
RA Vilotte J.-L., Soulier S., Mercier J.-C.;
RT "Sequence of the murine alpha-lactalbumin-encoding cDNA: interspecies
RT comparison of the coding frame and deduced pre-protein.";
RL Gene 112:251-255(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1398111; DOI=10.1016/0378-1119(92)90285-w;
RA Vilotte J.-L., Soulier S.;
RT "Isolation and characterization of the mouse alpha-lactalbumin-encoding
RT gene: interspecies comparison, tissue- and stage-specific expression.";
RL Gene 119:287-292(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 21-143 IN COMPLEX WITH B4GALT1.
RX PubMed=11419947; DOI=10.1006/jmbi.2001.4757;
RA Ramakrishnan B., Qasba P.K.;
RT "Crystal structure of lactose synthase reveals a large conformational
RT change in its catalytic component, the beta1,4-galactosyltransferase-I.";
RL J. Mol. Biol. 310:205-218(2001).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 21-143 IN COMPLEX WITH B4GALT1.
RX PubMed=12927542; DOI=10.1016/s0022-2836(03)00790-3;
RA Ramasamy V., Ramakrishnan B., Boeggeman E., Qasba P.K.;
RT "The role of tryptophan 314 in the conformational changes of beta1,4-
RT galactosyltransferase-I.";
RL J. Mol. Biol. 331:1065-1076(2003).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) OF 21-143 IN COMPLEX WITH B4GALT1
RP AND UDP-GLC.
RX PubMed=11485999; DOI=10.1074/jbc.m102458200;
RA Ramakrishnan B., Shah P.S., Qasba P.K.;
RT "Alpha-lactalbumin (LA) stimulates milk beta-1,4-galactosyltransferase I
RT (beta 4Gal-T1) to transfer glucose from UDP-glucose to N-acetylglucosamine.
RT Crystal structure of beta 4Gal-T1 x LA complex with UDP-Glc.";
RL J. Biol. Chem. 276:37665-37671(2001).
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 heterodimer of a catalytic component,
CC beta1,4-galactosyltransferase (beta4Gal-T1) and a regulatory component,
CC alpha-lactalbumin (LA). {ECO:0000269|PubMed:11419947,
CC ECO:0000269|PubMed:11485999, ECO:0000269|PubMed:12927542}.
CC -!- INTERACTION:
CC P29752; P08037: B4GALT1; Xeno; NbExp=10; IntAct=EBI-1031454, EBI-1031436;
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; M80909; AAA37208.1; -; mRNA.
DR EMBL; M87863; AAA37209.1; -; Genomic_DNA.
DR EMBL; BC006922; AAH06922.1; -; mRNA.
DR EMBL; BC069916; AAH69916.1; -; mRNA.
DR CCDS; CCDS27795.1; -.
DR PIR; JC1302; JC1302.
DR RefSeq; NP_034809.1; NM_010679.1.
DR RefSeq; XP_006520580.1; XM_006520517.1.
DR PDB; 1NF5; X-ray; 2.00 A; A/C=21-143.
DR PDB; 1NHE; X-ray; 2.50 A; A/C=21-143.
DR PDB; 1NKH; X-ray; 2.00 A; A/C=21-143.
DR PDB; 1NMM; X-ray; 2.00 A; A/C=21-143.
DR PDB; 1NQI; X-ray; 2.00 A; A/C=21-143.
DR PDB; 1NWG; X-ray; 2.32 A; A/C=21-143.
DR PDB; 1O23; X-ray; 2.32 A; A/C=21-143.
DR PDB; 1OQM; X-ray; 2.10 A; A/C=21-143.
DR PDB; 1PZY; X-ray; 2.30 A; A/C=21-143.
DR PDB; 1YRO; X-ray; 1.90 A; A/C=21-143.
DR PDB; 2FYC; X-ray; 2.00 A; A/C=21-143.
DR PDB; 2FYD; X-ray; 2.00 A; A/C=21-143.
DR PDBsum; 1NF5; -.
DR PDBsum; 1NHE; -.
DR PDBsum; 1NKH; -.
DR PDBsum; 1NMM; -.
DR PDBsum; 1NQI; -.
DR PDBsum; 1NWG; -.
DR PDBsum; 1O23; -.
DR PDBsum; 1OQM; -.
DR PDBsum; 1PZY; -.
DR PDBsum; 1YRO; -.
DR PDBsum; 2FYC; -.
DR PDBsum; 2FYD; -.
DR AlphaFoldDB; P29752; -.
DR SMR; P29752; -.
DR IntAct; P29752; 1.
DR STRING; 10090.ENSMUSP00000023726; -.
DR GlyGen; P29752; 1 site.
DR PhosphoSitePlus; P29752; -.
DR PaxDb; P29752; -.
DR PeptideAtlas; P29752; -.
DR PRIDE; P29752; -.
DR Antibodypedia; 13654; 371 antibodies from 30 providers.
DR DNASU; 16770; -.
DR Ensembl; ENSMUST00000023726; ENSMUSP00000023726; ENSMUSG00000022991.
DR GeneID; 16770; -.
DR KEGG; mmu:16770; -.
DR UCSC; uc007xmo.1; mouse.
DR CTD; 3906; -.
DR MGI; MGI:96742; Lalba.
DR VEuPathDB; HostDB:ENSMUSG00000022991; -.
DR eggNOG; ENOG502T8BJ; Eukaryota.
DR GeneTree; ENSGT00940000161726; -.
DR HOGENOM; CLU_111620_0_1_1; -.
DR InParanoid; P29752; -.
DR OMA; KCELSQV; -.
DR OrthoDB; 1551203at2759; -.
DR PhylomeDB; P29752; -.
DR TreeFam; TF324882; -.
DR Reactome; R-MMU-5653890; Lactose synthesis.
DR BioGRID-ORCS; 16770; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Lalba; mouse.
DR EvolutionaryTrace; P29752; -.
DR PRO; PR:P29752; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P29752; protein.
DR Bgee; ENSMUSG00000022991; Expressed in thoracic mammary gland and 58 other tissues.
DR ExpressionAtlas; P29752; baseline and differential.
DR Genevisible; P29752; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004461; F:lactose synthase activity; IDA:MGI.
DR GO; GO:0003796; F:lysozyme activity; IBA:GO_Central.
DR GO; GO:0005989; P:lactose biosynthetic process; IMP:MGI.
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; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT CHAIN 21..143
FT /note="Alpha-lactalbumin"
FT /id="PRO_0000018446"
FT DOMAIN 21..143
FT /note="C-type lysozyme"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT BINDING 99
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00711"
FT BINDING 102
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 BINDING 108
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00711"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..140
FT DISULFID 48..131
FT DISULFID 81..97
FT DISULFID 93..111
FT HELIX 25..31
FT /evidence="ECO:0007829|PDB:1YRO"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:1YRO"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:1YRO"
FT HELIX 43..54
FT /evidence="ECO:0007829|PDB:1YRO"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:1YRO"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:1YRO"
FT TURN 71..74
FT /evidence="ECO:0007829|PDB:1YRO"
FT TURN 77..80
FT /evidence="ECO:0007829|PDB:1YRO"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:2FYC"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:1NMM"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:1YRO"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:1YRO"
FT HELIX 106..118
FT /evidence="ECO:0007829|PDB:1YRO"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:1YRO"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:1YRO"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:1YRO"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:1YRO"
SQ SEQUENCE 143 AA; 16260 MW; 0322892711FF4309 CRC64;
MMHFVPLFLV CILSLPAFQA TELTKCKVSH AIKDIDGYQG ISLLEWACVL FHTSGYDTQA
VVNDNGSTEY GLFQISDRFW CKSSEFPESE NICGISCDKL LDDELDDDIA CAKKILAIKG
IDYWKAYKPM CSEKLEQWRC EKP
