LALBA_BUBBU
ID LALBA_BUBBU Reviewed; 142 AA.
AC Q9TSN6; A3FMK7; Q0PNI0; Q645J4; Q645J5; Q645J6; Q645J7; Q645J8;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Alpha-lactalbumin;
DE AltName: Full=Lactose synthase B protein;
DE Flags: Precursor;
GN Name=LALBA;
OS Bubalus bubalis (Domestic water buffalo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bubalus.
OX NCBI_TaxID=89462;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Fan B., Li N., Wu C.;
RT "Research on the sequences of milk protein genes in ruminants.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS SER-12 AND ARG-32.
RC TISSUE=Mammary gland;
RA Bhattacharya T.K., Kumar P., Sharma A.;
RT "Cloning and characterization of buffalo alpha-lactalbumin gene.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-97 (ALLELES A; B; C; D AND E), AND
RP VARIANTS SER-12; ARG-32; ALA-35; CYS-39; ASP-68; MET-85; LYS-85; LYS-93 AND
RP GLY-96.
RC STRAIN=Bhadawari, Mehsana, Murrah, and Surti; TISSUE=Blood;
RX PubMed=16147872; DOI=10.1080/10425170500088205;
RA Dayal S., Bhattacharya T.K., Vohra V., Kumar P., Sharma A.;
RT "Genetic polymorphism of alpha-lactalbumin gene in riverine buffalo.";
RL DNA Seq. 16:173-179(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44 (ALLELE E), AND VARIANT SER-43.
RC TISSUE=Blood;
RA Nautiyal B., Saxena P., Singh K.B., Sharma D., Mohapatra J.K., Rasool T.J.;
RT "A new variant of alpha-lactalbumin gene in water buffalo.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 19-142, AND MASS SPECTROMETRY.
RA Meignanalakshmi S.;
RT "Antibacterial activity analysis of buffalo milk whey protein.";
RL Submitted (OCT-2010) to UniProtKB.
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=14227; Method=MALDI;
CC Evidence={ECO:0000269|Ref.5};
CC -!- MISCELLANEOUS: In vitro digestion with trypsin produces a peptide
CC comprising residues Ile-78 to Lys-98 which has antibacterial activity.
CC It is active against Gram-negative bacterium E.coli (MIC=150 ug/ml) and
CC against Gram-positive bacterium S.aureus (MIC=250 ug/ml).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00680}.
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DR EMBL; AF194373; AAF06794.1; -; Genomic_DNA.
DR EMBL; DQ785796; ABG78269.1; -; mRNA.
DR EMBL; AH014129; AAU13909.1; -; Genomic_DNA.
DR EMBL; AH014130; AAU13910.1; -; Genomic_DNA.
DR EMBL; AH014131; AAU13911.1; -; Genomic_DNA.
DR EMBL; AH014132; AAU13912.1; -; Genomic_DNA.
DR EMBL; AY726617; AAU13913.1; -; Genomic_DNA.
DR EMBL; EF408824; ABN54437.1; -; Genomic_DNA.
DR PIR; S74175; S74175.
DR RefSeq; NP_001277865.1; NM_001290936.1.
DR AlphaFoldDB; Q9TSN6; -.
DR BMRB; Q9TSN6; -.
DR SMR; Q9TSN6; -.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR GeneID; 102410146; -.
DR KEGG; bbub:102410146; -.
DR CTD; 3906; -.
DR OrthoDB; 1551203at2759; -.
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:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
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 Antibiotic; Antimicrobial; Calcium; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Lactose biosynthesis; Metal-binding;
KW Milk protein; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|Ref.5"
FT CHAIN 19..142
FT /note="Alpha-lactalbumin"
FT /id="PRO_0000018440"
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 CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 VARIANT 12
FT /note="I -> S (in allele D)"
FT /evidence="ECO:0000269|PubMed:16147872, ECO:0000269|Ref.2"
FT VARIANT 32
FT /note="K -> R (in allele B and allele D)"
FT /evidence="ECO:0000269|PubMed:16147872, ECO:0000269|Ref.2"
FT VARIANT 35
FT /note="K -> A (in allele B)"
FT /evidence="ECO:0000269|PubMed:16147872"
FT VARIANT 39
FT /note="G -> C (in allele C)"
FT /evidence="ECO:0000269|PubMed:16147872"
FT VARIANT 43
FT /note="P -> S (in allele E)"
FT /evidence="ECO:0000269|Ref.4"
FT VARIANT 68
FT /note="E -> D (in allele C)"
FT /evidence="ECO:0000269|PubMed:16147872"
FT VARIANT 85
FT /note="N -> K (in allele E)"
FT /evidence="ECO:0000269|PubMed:16147872"
FT VARIANT 85
FT /note="N -> M (in allele C)"
FT /evidence="ECO:0000269|PubMed:16147872"
FT VARIANT 93
FT /note="N -> K (in allele C)"
FT /evidence="ECO:0000269|PubMed:16147872"
FT VARIANT 96
FT /note="C -> G (in allele C, allele D and allele E)"
FT /evidence="ECO:0000269|PubMed:16147872"
FT CONFLICT 19
FT /note="A -> M (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="D -> K (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="A -> T (in Ref. 1; AAF06794 and 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="I -> T (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="D -> T (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="Y -> V (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="M -> V (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 142 AA; 16275 MW; 6EF3254A09779E2D CRC64;
MMSFVSLLLV GILFHATQAE QLTKCEVFRE LKDLKDYGGV SLPEWVCTAF HTSGYDTQAI
VQNNDSTEYG LFQINNKIWC KDDQNPHSSN ICNISCDKFL DDDLTDDIMC VKKILDKVGI
NYWLAHKALC SEKLDQWLCE KL
