ID   LALBA_NOTRU             Reviewed;         121 AA.
AC   P07458;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Alpha-lactalbumin;
DE   AltName: Full=Lactose synthase B protein;
GN   Name=LALBA;
OS   Notamacropus rufogriseus (Red-necked wallaby) (Macropus rufogriseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Diprotodontia; Macropodidae; Notamacropus.
OX   NCBI_TaxID=1960652;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=6715332; DOI=10.1016/s0021-9258(17)42938-3;
RA   Shewale J.G., Sinha S.K., Brew K.;
RT   "Evolution of alpha-lactalbumins. The complete amino acid sequence of the
RT   alpha-lactalbumin from a marsupial (Macropus rufogriseus) and corrections
RT   to regions of sequence in bovine and goat alpha-lactalbumins.";
RL   J. Biol. Chem. 259:4947-4956(1984).
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   PIR; A25251; LAKGAW.
DR   AlphaFoldDB; P07458; -.
DR   SMR; P07458; -.
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   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Lactose biosynthesis; Metal-binding; Milk protein; Secreted.
FT   CHAIN           1..121
FT                   /note="Alpha-lactalbumin"
FT                   /id="PRO_0000208839"
FT   DOMAIN          1..121
FT                   /note="C-type lysozyme"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   BINDING         79
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P00711"
FT   BINDING         82
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P00711"
FT   BINDING         84
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P00711"
FT   BINDING         87
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P00711"
FT   BINDING         88
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P00711"
FT   CARBOHYD        44
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        6..121
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        28..112
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        61..77
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        73..91
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
SQ   SEQUENCE   121 AA;  13785 MW;  1FCD233F4321F347 CRC64;
     IDYRKCQASQ ILKEHGMDKV IPLPELVCTM FHISGLSTQA EVNNHSNKEY GIFQISNDGW
     CAEKQEDVAN SVCGILCSKF LDDDITDDIE CAKKILQLPE GLGYWKAHET FCLEDLDQWR
     C