ID   LALBA_RABIT             Reviewed;         141 AA.
AC   P00716; Q9TQT7;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Alpha-lactalbumin;
DE   AltName: Full=Lactose synthase B protein;
DE   Flags: Precursor;
GN   Name=LALBA;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=New Zealand white; TISSUE=Mammary gland;
RA   Pak K.-W., Kim S.J., Min W.-K., Park I.-Y., Huang H., Kim S.-W., Lee K.-K.;
RT   "Cloning of the rabbit alpha-lactalbumin gene and characterization of its
RT   promoter in cultured mammary-cells.";
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 20-141.
RX   PubMed=497176; DOI=10.1021/bi00590a024;
RA   Hopp T.P., Woods K.R.;
RT   "Primary structure of rabbit alpha-lactalbumin.";
RL   Biochemistry 18:5182-5191(1979).
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; AF124257; AAD56599.1; -; mRNA.
DR   EMBL; AF123893; AAD56598.1; -; Genomic_DNA.
DR   RefSeq; NP_001075521.1; NM_001082052.1.
DR   RefSeq; XP_008254616.1; XM_008256394.2.
DR   RefSeq; XP_017197107.1; XM_017341618.1.
DR   AlphaFoldDB; P00716; -.
DR   SMR; P00716; -.
DR   STRING; 9986.ENSOCUP00000013596; -.
DR   PRIDE; P00716; -.
DR   Ensembl; ENSOCUT00000023351; ENSOCUP00000024236; ENSOCUG00000015834.
DR   GeneID; 100008717; -.
DR   KEGG; ocu:100008717; -.
DR   CTD; 3906; -.
DR   eggNOG; ENOG502T8BJ; Eukaryota.
DR   GeneTree; ENSGT00940000161726; -.
DR   HOGENOM; CLU_111620_0_1_1; -.
DR   InParanoid; P00716; -.
DR   OMA; KCELSQV; -.
DR   OrthoDB; 1551203at2759; -.
DR   Proteomes; UP000001811; Chromosome 4.
DR   Bgee; ENSOCUG00000015834; Expressed in testis and 3 other tissues.
DR   ExpressionAtlas; P00716; baseline.
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; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:497176"
FT   CHAIN           20..141
FT                   /note="Alpha-lactalbumin"
FT                   /id="PRO_0000018448"
FT   DOMAIN          20..141
FT                   /note="C-type lysozyme"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
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   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        75..76
FT                   /note="SD -> NS (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   141 AA;  16082 MW;  A41C125B3E774544 CRC64;
     MMPLVPLLLV SIVFPGIQAT QLTRCELTEK LKELDGYRDI SMSEWICTLF HTSGLDTKIT
     VNNNGSTEYG IFQISDKLWC VSKQNPQSKN ICDTPCENFL DDNLTDDVKC AMKILDKEGI
     DHWLAHKPLC SENLEQWVCK K