LALBA_CAMDR
ID LALBA_CAMDR Reviewed; 123 AA.
AC P00710;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Alpha-lactalbumin;
DE AltName: Full=Lactose synthase B protein;
GN Name=LALBA;
OS Camelus dromedarius (Dromedary) (Arabian camel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX NCBI_TaxID=9838;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=3971980; DOI=10.1111/j.1432-1033.1985.tb08741.x;
RA Beg O.U., von Bahr-Lindstroem H., Zaidi Z.H., Joernvall H.;
RT "The primary structure of alpha-lactalbumin from camel milk.";
RL Eur. J. Biochem. 147:233-239(1985).
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; A00865; LACM.
DR AlphaFoldDB; P00710; -.
DR SMR; P00710; -.
DR STRING; 9838.ENSCDRP00005013763; -.
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.
FT CHAIN 1..123
FT /note="Alpha-lactalbumin"
FT /id="PRO_0000208833"
FT DOMAIN 1..123
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 DISULFID 6..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 28..111
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 123 AA; 14430 MW; 69F23608B0DE0188 CRC64;
KQFTKCKLSD ELKDMNGHGG ITLAEWICII FHMSGYDTET VVSNNGNREY GLFQINNKIW
CRDNENLQSR NICDISCDKF LDDDLTDDKM CAKKILDKEG IDYWLAHKPL CSEKLEQWQC
EKW
