LALBA_CAVPO
ID LALBA_CAVPO Reviewed; 142 AA.
AC P00713;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Alpha-lactalbumin;
DE AltName: Full=Lactose synthase B protein;
DE Flags: Precursor;
GN Name=LALBA;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2845947; DOI=10.1042/bj2540085;
RA Laird J.E., Jack L., Hall L., Boulton A.P., Parker D., Craig R.K.;
RT "Structure and expression of the guinea-pig alpha-lactalbumin gene.";
RL Biochem. J. 254:85-94(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6285305; DOI=10.1093/nar/10.11.3503;
RA Hall L., Craig R.K., Edbrooke M.R., Campbell P.N.;
RT "Comparison of the nucleotide sequence of cloned human and guinea-pig pre-
RT alpha-lactalbumin cDNA with that of chick pre-lysozyme cDNA suggests
RT evolution from a common ancestral gene.";
RL Nucleic Acids Res. 10:3503-3515(1982).
RN [3]
RP PROTEIN SEQUENCE OF 20-142.
RX PubMed=5065784; DOI=10.1111/j.1432-1033.1972.tb01844.x;
RA Brew K.;
RT "The complete amino-acid sequence of guinea-pig alpha-lactalbumin.";
RL Eur. J. Biochem. 27:341-353(1972).
RN [4] {ECO:0007744|PDB:1HFX}
RP X-RAY CRYSTALLOGRAPHY (1.9 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).
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; J00051; AAA60337.1; -; mRNA.
DR EMBL; Y00726; CAA68710.1; -; Genomic_DNA.
DR PIR; S01144; LAGP.
DR RefSeq; NP_001166360.1; NM_001172889.1.
DR PDB; 1HFX; X-ray; 1.90 A; A=20-142.
DR PDBsum; 1HFX; -.
DR AlphaFoldDB; P00713; -.
DR SMR; P00713; -.
DR STRING; 10141.ENSCPOP00000019835; -.
DR Ensembl; ENSCPOT00000019635; ENSCPOP00000019835; ENSCPOG00000027342.
DR GeneID; 100379577; -.
DR KEGG; cpoc:100379577; -.
DR CTD; 3906; -.
DR eggNOG; ENOG502T8BJ; Eukaryota.
DR GeneTree; ENSGT00940000161726; -.
DR HOGENOM; CLU_111620_0_1_1; -.
DR InParanoid; P00713; -.
DR OMA; KCELSQV; -.
DR OrthoDB; 1551203at2759; -.
DR TreeFam; TF324882; -.
DR EvolutionaryTrace; P00713; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
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 Lactose biosynthesis; Metal-binding; Milk protein; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:5065784"
FT CHAIN 20..142
FT /note="Alpha-lactalbumin"
FT /id="PRO_0000018443"
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:1HFX"
FT BINDING 101
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8805552,
FT ECO:0007744|PDB:1HFX"
FT BINDING 103
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8805552,
FT ECO:0007744|PDB:1HFX"
FT BINDING 106
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8805552,
FT ECO:0007744|PDB:1HFX"
FT BINDING 107
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8805552,
FT ECO:0007744|PDB:1HFX"
FT DISULFID 25..139
FT DISULFID 47..130
FT DISULFID 80..96
FT DISULFID 92..110
FT CONFLICT 81
FT /note="E -> D (in Ref. 2; AAA60337)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="L -> F (in Ref. 2; AAA60337)"
FT /evidence="ECO:0000305"
FT HELIX 24..30
FT /evidence="ECO:0007829|PDB:1HFX"
FT TURN 31..36
FT /evidence="ECO:0007829|PDB:1HFX"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:1HFX"
FT HELIX 42..53
FT /evidence="ECO:0007829|PDB:1HFX"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:1HFX"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:1HFX"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:1HFX"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:1HFX"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:1HFX"
FT HELIX 96..99
FT /evidence="ECO:0007829|PDB:1HFX"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:1HFX"
FT HELIX 105..117
FT /evidence="ECO:0007829|PDB:1HFX"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:1HFX"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:1HFX"
SQ SEQUENCE 142 AA; 16300 MW; E13FA2ACA8F1029E CRC64;
MMSFFPLLLV GILFPAVQAK QLTKCALSHE LNDLAGYRDI TLPEWLCIIF HISGYDTQAI
VKNSDHKEYG LFQINDKDFC ESSTTVQSRN ICDISCDKLL DDDLTDDIMC VKKILDIKGI
DYWLAHKPLC SDKLEQWYCE AQ
