LALBA_TRIVU
ID LALBA_TRIVU Reviewed; 140 AA.
AC Q29145;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Alpha-lactalbumin;
DE AltName: Full=Lactose synthase B protein;
DE Flags: Precursor;
GN Name=LALBA;
OS Trichosurus vulpecula (Brush-tailed possum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Diprotodontia; Phalangeridae; Trichosurus.
OX NCBI_TaxID=9337;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND MASS
RP SPECTROMETRY.
RC TISSUE=Mammary gland;
RX PubMed=9305795; DOI=10.1016/s0304-4165(97)00033-0;
RA Piotte C.P., Marshall C.J., Hubbard M.J., Collet C., Grigor M.R.;
RT "Lysozyme and alpha-lactalbumin from the milk of a marsupial, the common
RT brush-tailed possum (Trichosurus vulpecula).";
RL Biochim. Biophys. Acta 1336:235-242(1997).
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 -!- MASS SPECTROMETRY: Mass=13985; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9305795};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00680}.
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DR EMBL; U34288; AAB97108.1; -; mRNA.
DR AlphaFoldDB; Q29145; -.
DR SMR; Q29145; -.
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; Lactose biosynthesis;
KW Metal-binding; Milk protein; Secreted; Signal.
FT SIGNAL 1..19
FT CHAIN 20..140
FT /note="Alpha-lactalbumin"
FT /id="PRO_0000018451"
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 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"
SQ SEQUENCE 140 AA; 15957 MW; AAE8405D043BE6B0 CRC64;
MMSLLPLLLI GIVLPATQAK DYGKCELNQI LRERGVDKVI SLPELICTMF HSSGFSTETE
VDNNNHKEYG IFQISSNGWC AEKQEDVERS VCGILCSKLL DDDITDDIVC AKKILQLPER
LDHWKAHNTF CRENLDQWNC