LALBA_RAT
ID LALBA_RAT Reviewed; 159 AA.
AC P00714; P00715;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Alpha-lactalbumin;
DE AltName: Full=Lactose synthase B protein;
DE Flags: Precursor;
GN Name=Lalba;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6709045; DOI=10.1038/308377a0;
RA Qasba P.K., Safaya S.K.;
RT "Similarity of the nucleotide sequences of rat alpha-lactalbumin and
RT chicken lysozyme genes.";
RL Nature 308:377-380(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 44-159.
RX PubMed=6272279; DOI=10.1073/pnas.78.8.4853;
RA Dandekar A.M., Qasba P.K.;
RT "Rat alpha-lactalbumin has a 17-residue-long COOH-terminal hydrophobic
RT extension as judged by sequence analysis of the cDNA clones.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:4853-4857(1981).
RN [3]
RP PROTEIN SEQUENCE OF 20-159.
RX PubMed=7044414; DOI=10.1021/bi00536a002;
RA Prasad R.V., Butkowski R.J., Hamilton J.W., Ebner K.E.;
RT "Amino acid sequence of rat alpha-lactalbumin: a unique alpha-
RT lactalbumin.";
RL Biochemistry 21:1479-1482(1982).
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; X00461; CAA25150.1; -; Genomic_DNA.
DR EMBL; V01251; CAA24564.2; -; mRNA.
DR PIR; A93327; LART.
DR RefSeq; NP_036726.1; NM_012594.1.
DR AlphaFoldDB; P00714; -.
DR SMR; P00714; -.
DR STRING; 10116.ENSRNOP00000014457; -.
DR GlyGen; P00714; 1 site.
DR iPTMnet; P00714; -.
DR PaxDb; P00714; -.
DR GeneID; 24528; -.
DR KEGG; rno:24528; -.
DR UCSC; RGD:2987; rat.
DR CTD; 3906; -.
DR RGD; 2987; Lalba.
DR eggNOG; ENOG502T8BJ; Eukaryota.
DR InParanoid; P00714; -.
DR PhylomeDB; P00714; -.
DR PRO; PR:P00714; -.
DR Proteomes; UP000002494; 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: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; Glycoprotein;
KW Lactose biosynthesis; Metal-binding; Milk protein; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:7044414"
FT CHAIN 20..159
FT /note="Alpha-lactalbumin"
FT /evidence="ECO:0000269|PubMed:7044414"
FT /id="PRO_0000018449"
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 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:0000269|PubMed:7044414"
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 38..40
FT /note="QGI -> EGV (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="L -> P (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 57..60
FT /note="SQAI -> TEAS (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="N -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="N -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 82..86
FT /note="SSEFP -> ENQFV (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="D -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="K -> L (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 153..154
FT /note="NS -> DG (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 159 AA; 17850 MW; D2C097A0548E7BD3 CRC64;
MMRFVPLFLA CISLPAFQAT EFTKCEVSHA IEDMDGYQGI SLLEWTCVLF HTSGYDSQAI
VKNNGSTEYG LFQISNRNWC KSSEFPESEN ICDISCDKFL DDELADDIVC AKKIVAIKGI
DYWKAHKPMC SEKLEQWRCE KPGAPALVVP ALNSETPVP
