ID   Q9GLA4_9CETA            Unreviewed;       108 AA.
AC   Q9GLA4;
DT   01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2001, sequence version 1.
DT   22-FEB-2023, entry version 64.
DE   RecName: Full=Alpha-lactalbumin {ECO:0000256|ARBA:ARBA00017299};
DE   AltName: Full=Lactose synthase B protein {ECO:0000256|ARBA:ARBA00031746};
DE   Flags: Fragment;
OS   Globicephala sp. IIC2000.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Delphinidae; Globicephala.
OX   NCBI_TaxID=139690 {ECO:0000313|EMBL:AAG27445.1};
RN   [1] {ECO:0000313|EMBL:AAG27445.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=11027333; DOI=10.1073/pnas.97.21.11343;
RA   Cassens I., Vicario S., Waddell V.G., Balchowsky H., Van Belle D., Ding W.,
RA   Fan C., Mohan L., Simoes-Lopes P.C., Bastida R., Meyer A., Stanhope M.J.,
RA   Milinkovitch M.C.;
RT   "Independent adaptation to riverine habitats allowed survival of ancient
RT   cetacean lineages.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:11343-11347(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       {ECO:0000256|ARBA:ARBA00002592}.
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). {ECO:0000256|ARBA:ARBA00011582}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC       {ECO:0000256|RuleBase:RU004440}.
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DR   EMBL; AF304090; AAG27445.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9GLA4; -.
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   Gene3D; 1.10.530.10; -; 1.
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:SF32; ALPHA-LACTALBUMIN; 1.
DR   PANTHER; PTHR11407; LYSOZYME C; 1.
DR   Pfam; PF00062; Lys; 1.
DR   PRINTS; PR00136; LACTALBUMIN.
DR   PRINTS; PR00135; LYZLACT.
DR   SMART; SM00263; LYZ1; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   PROSITE; PS00128; GLYCOSYL_HYDROL_F22_1; 1.
DR   PROSITE; PS51348; GLYCOSYL_HYDROL_F22_2; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Lactose biosynthesis {ECO:0000256|ARBA:ARBA00023091};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Milk protein {ECO:0000256|ARBA:ARBA00022743}.
FT   DOMAIN          86..104
FT                   /note="Glycosyl hydrolases family 22 (GH22)"
FT                   /evidence="ECO:0000259|PROSITE:PS00128"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAG27445.1"
FT   NON_TER         108
FT                   /evidence="ECO:0000313|EMBL:AAG27445.1"
SQ   SEQUENCE   108 AA;  12269 MW;  84623FF81A47DF13 CRC64;
     LLLVGILFHA VQAEQLTKCE LFQRLKDLDG YGGVTLPEWV CTVFHTSGCD TQTIVNNNDS
     TEYGLFQINN KIWCRDNQIP HSRDICGISC DKFLDDDLTD DIMCVKKI
//