ID   LALBA_CANLF             Reviewed;         142 AA.
AC   Q9N2G9;
DT   27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Alpha-lactalbumin;
DE   AltName: Full=Lactose synthase B protein;
DE   Flags: Precursor;
GN   Name=LALBA;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11129870; DOI=10.1292/jvms.62.1217;
RA   Watanabe M., Tateyama S., Togashi T., Uchida K., Yamaguchi R., Shimizu T.,
RA   Sugano S.;
RT   "Identification of canine alpha-lactalbumin.";
RL   J. Vet. Med. Sci. 62:1217-1219(2000).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB035079; BAA95930.1; -; mRNA.
DR   RefSeq; NP_001003129.1; NM_001003129.1.
DR   AlphaFoldDB; Q9N2G9; -.
DR   SMR; Q9N2G9; -.
DR   STRING; 9615.ENSCAFP00000013149; -.
DR   PaxDb; Q9N2G9; -.
DR   PRIDE; Q9N2G9; -.
DR   GeneID; 403730; -.
DR   KEGG; cfa:403730; -.
DR   CTD; 3906; -.
DR   eggNOG; ENOG502T8BJ; Eukaryota.
DR   InParanoid; Q9N2G9; -.
DR   OrthoDB; 1551203at2759; -.
DR   Proteomes; UP000002254; 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: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; Lactose biosynthesis; Metal-binding; Milk protein;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250"
FT   CHAIN           20..142
FT                   /note="Alpha-lactalbumin"
FT                   /id="PRO_0000018441"
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         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   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"
SQ   SEQUENCE   142 AA;  16285 MW;  8BBD1ECCD5DF5A46 CRC64;
     MMSFVSLLLV SILFPAIQAK QFTKCELPQV LKDMDGFGGI ALPEWICTIF HTSGYDTQTI
     VNNNGGTDYG LFQISNKFWC KDDQNLQSRN ICDISCDKFL DDDLTDDMIC AKKILDKEGI
     DYWLAHKPLC SEKLEQWRCE KL