LALBA_PIG
ID LALBA_PIG Reviewed; 141 AA.
AC P18137;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Alpha-lactalbumin;
DE AltName: Full=Lactose synthase B protein;
DE Flags: Precursor;
GN Name=LALBA;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1537566; DOI=10.1016/0378-1119(92)90660-h;
RA Das Gupta N.A., Alexander L.J., Beattie C.W.;
RT "The sequence of a porcine cDNA encoding alpha-lactalbumin.";
RL Gene 110:265-266(1992).
RN [2]
RP PROTEIN SEQUENCE OF 20-141.
RX PubMed=2222864; DOI=10.1515/bchm3.1990.371.2.649;
RA Godovac-Zimmermann J., Conti A., Napolitano L.;
RT "The complete primary structure of alpha-lactalbumin isolated from pig (Sus
RT scrofa) milk.";
RL Biol. Chem. Hoppe-Seyler 371:649-653(1990).
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 -!- MISCELLANEOUS: The pig alpha-lactalbumin shows complete loss of both
CC lysozyme functional residues.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00680}.
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DR EMBL; M80520; AAA31060.1; -; mRNA.
DR PIR; JH0264; LAPG.
DR RefSeq; NP_999525.1; NM_214360.1.
DR AlphaFoldDB; P18137; -.
DR SMR; P18137; -.
DR STRING; 9823.ENSSSCP00000024183; -.
DR PaxDb; P18137; -.
DR PeptideAtlas; P18137; -.
DR PRIDE; P18137; -.
DR Ensembl; ENSSSCT00000025257; ENSSSCP00000024183; ENSSSCG00000024573.
DR Ensembl; ENSSSCT00005072419; ENSSSCP00005045287; ENSSSCG00005044914.
DR Ensembl; ENSSSCT00015071737; ENSSSCP00015028751; ENSSSCG00015053812.
DR Ensembl; ENSSSCT00025079522; ENSSSCP00025034521; ENSSSCG00025058072.
DR Ensembl; ENSSSCT00030092348; ENSSSCP00030042493; ENSSSCG00030066079.
DR Ensembl; ENSSSCT00035091014; ENSSSCP00035038154; ENSSSCG00035067467.
DR Ensembl; ENSSSCT00040099823; ENSSSCP00040044797; ENSSSCG00040072476.
DR Ensembl; ENSSSCT00050063597; ENSSSCP00050027322; ENSSSCG00050046729.
DR Ensembl; ENSSSCT00055001666; ENSSSCP00055001255; ENSSSCG00055000939.
DR Ensembl; ENSSSCT00060055234; ENSSSCP00060023591; ENSSSCG00060040757.
DR Ensembl; ENSSSCT00065048580; ENSSSCP00065020974; ENSSSCG00065035655.
DR Ensembl; ENSSSCT00070015251; ENSSSCP00070012608; ENSSSCG00070007907.
DR GeneID; 397647; -.
DR KEGG; ssc:397647; -.
DR CTD; 3906; -.
DR VGNC; VGNC:89618; LALBA.
DR eggNOG; ENOG502T8BJ; Eukaryota.
DR GeneTree; ENSGT00940000161726; -.
DR HOGENOM; CLU_111620_0_1_1; -.
DR InParanoid; P18137; -.
DR OMA; KCELSQV; -.
DR OrthoDB; 1551203at2759; -.
DR TreeFam; TF324882; -.
DR Reactome; R-SSC-5653890; Lactose synthesis.
DR Proteomes; UP000008227; Chromosome 5.
DR Proteomes; UP000314985; Chromosome 5.
DR Bgee; ENSSSCG00000024573; Expressed in oocyte and 1 other tissue.
DR Genevisible; P18137; SS.
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:0003796; F:lysozyme activity; IBA:GO_Central.
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; Lactose biosynthesis;
KW Metal-binding; Milk protein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:2222864"
FT CHAIN 20..141
FT /note="Alpha-lactalbumin"
FT /id="PRO_0000018447"
FT DOMAIN 20..141
FT /note="C-type lysozyme"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT BINDING 97
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00711"
FT BINDING 100
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 105
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 DISULFID 25..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 47..129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 80..95
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 91..109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT CONFLICT 62..63
FT /note="HD -> SN (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="M -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="M -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 141 AA; 16174 MW; C1524571466A0D27 CRC64;
MMSFVSLLVV GILFPAIQAK QFTKCELSQV LKDMDGYGDI TLPEWICTIF HISGYDTKTI
VHDNGSTEYG LFQINNKLWC RDNQIQSKNI CGISCDKFLD DDLTDDMMCA KKILDNEGID
YWLAHKALCS EKLDQWLCEK M
