ID   LALBA_NOTEU             Reviewed;         140 AA.
AC   Q06655;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 2.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Alpha-lactalbumin;
DE   AltName: Full=Lactose synthase B protein;
DE   Flags: Precursor;
GN   Name=LALBA;
OS   Notamacropus eugenii (Tammar wallaby) (Macropus eugenii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Diprotodontia; Macropodidae; Notamacropus.
OX   NCBI_TaxID=9315;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Mammary gland;
RX   PubMed=2095590; DOI=10.1071/rd9900693;
RA   Collet C., Joseph R., Nicholas K.R.;
RT   "Cloning, cDNA analysis and prolactin-dependent expression of a marsupial
RT   alpha-lactalbumin.";
RL   Reprod. Fertil. Dev. 2:693-701(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7794241; DOI=10.1007/bf00554559;
RA   Collet C., Joseph R.;
RT   "Exon organization and sequence of the genes encoding alpha-lactalbumin and
RT   beta-lactoglobulin from the tammar wallaby (Macropodidae, Marsupialia).";
RL   Biochem. Genet. 33:61-72(1995).
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; X15211; CAA33281.1; -; mRNA.
DR   EMBL; L15010; AAA31602.1; -; Genomic_DNA.
DR   EMBL; L15007; AAA31602.1; JOINED; Genomic_DNA.
DR   EMBL; L15008; AAA31602.1; JOINED; Genomic_DNA.
DR   EMBL; L15009; AAA31602.1; JOINED; Genomic_DNA.
DR   PIR; A60394; A60394.
DR   AlphaFoldDB; Q06655; -.
DR   SMR; Q06655; -.
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   2: Evidence at transcript level;
KW   Calcium; Disulfide bond; Glycoprotein; Lactose biosynthesis; Metal-binding;
KW   Milk protein; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250"
FT   CHAIN           20..140
FT                   /note="Alpha-lactalbumin"
FT                   /id="PRO_0000018445"
FT   DOMAIN          20..140
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         103
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        63
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        25..140
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        47..131
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        132
FT                   /note="I -> L (in Ref. 2; AAA31602)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   140 AA;  15722 MW;  7B1B4C8E093A7A43 CRC64;
     MMSLLSLLLL GIALPATQAI DYRKCQASQI LKEHGMDKVI PLPELVCTMF HISGLSTQAE
     VNNHSNKEYG IFQISNNGWC AEKQEDVANS VCGILCSKFL DDDITDDIEC AKKILQLPEG
     LGYWKAHETF CIEDLDQWRC