ID LALBA_HUMAN Reviewed; 142 AA. AC P00709; Q6FGX0; Q9UDK4; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 13-FEB-2019, entry version 178. DE RecName: Full=Alpha-lactalbumin; DE AltName: Full=Lactose synthase B protein; DE AltName: Full=Lysozyme-like protein 7; DE Flags: Precursor; GN Name=LALBA; Synonyms=LYZL7; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=6285305; DOI=10.1093/nar/10.11.3503; RA Hall L., Craig R.K., Edbrooke M.R., Campbell P.N.; RT "Comparison of the nucleotide sequence of cloned human and guinea-pig RT pre-alpha-lactalbumin cDNA with that of chick pre-lysozyme cDNA RT suggests evolution from a common ancestral gene."; RL Nucleic Acids Res. 10:3503-3515(1982). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2954544; DOI=10.1042/bj2420735; RA Hall L., Emery D.C., Davies M.S., Parker D., Craig R.K.; RT "Organization and sequence of the human alpha-lactalbumin gene."; RL Biochem. J. 242:735-742(1987). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Fujiwara Y., Takahashi R., Hirabayashi M., Ueda M., Muramatsu T., RA Yamanaka H., Sekikawa K.; RT "Analysis of flanking sequence of human alpha-lactalbumin containing a RT putative locus control region."; RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., RA Korn B., Zuo D., Hu Y., LaBaer J.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP PROTEIN SEQUENCE OF 20-142. RX PubMed=5049057; DOI=10.1111/j.1432-1033.1972.tb01812.x; RA Findlay J.B.C., Brew K.; RT "The complete amino-acid sequence of human alpha-lactalbumin."; RL Eur. J. Biochem. 27:65-86(1972). RN [8] RP PROTEIN SEQUENCE OF 78-81 AND 90-112. RC TISSUE=Milk; RX PubMed=1401360; RA Maynard F.; RT "Identification of a new molecular form of human alpha-lactalbumin."; RL J. Dairy Res. 59:425-429(1992). RN [9] RP GLYCOSYLATION AT ASN-90. RA Cavaletto M., Giuffrida M.G., Giunta C., Conti A.; RT "An unusual glycosylation site in alpha-lactalbumin from human milk."; RL Protein Sci. 4 Suppl. 1:119-119(1995). RN [10] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-64. RC TISSUE=Milk; RX PubMed=18780401; DOI=10.1002/pmic.200701057; RA Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.; RT "Identification of N-linked glycoproteins in human milk by hydrophilic RT interaction liquid chromatography and mass spectrometry."; RL Proteomics 8:3833-3847(2008). RN [11] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS). RX PubMed=1920433; DOI=10.1016/0022-2836(91)80073-4; RA Acharya K.R., Ren J.S., Stuart D.I., Phillips D.C., Fenna R.E.; RT "Crystal structure of human alpha-lactalbumin at 1.7-A resolution."; RL J. Mol. Biol. 221:571-581(1991). RN [12] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS). RX PubMed=8366079; RA Ren J.S., Stuart D.I., Acharya K.R.; RT "Alpha-lactalbumin possesses a distinct zinc binding site."; RL J. Biol. Chem. 268:19292-19298(1993). RN [13] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). RX PubMed=9537992; DOI=10.1021/bi973000t; RA Chandra N., Brew K., Acharya K.R.; RT "Structural evidence for the presence of a secondary calcium binding RT site in human alpha-lactalbumin."; RL Biochemistry 37:4767-4772(1998). RN [14] RP X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS). RX PubMed=10080897; DOI=10.1006/jmbi.1999.2598; RA Harata K., Abe Y., Muraki M.; RT "Crystallographic evaluation of internal motion of human alpha- RT lactalbumin refined by full-matrix least-squares method."; RL J. Mol. Biol. 287:347-358(1999). RN [15] RP VARIANT VAL-46, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=15866226; DOI=10.1016/j.jnutbio.2004.12.010; RA Chowanadisai W., Kelleher S.L., Nemeth J.F., Yachetti S., RA Kuhlman C.F., Jackson J.G., Davis A.M., Lien E.L., Loennerdal B.; RT "Detection of a single nucleotide polymorphism in the human alpha- RT lactalbumin gene: implications for human milk proteins."; RL J. Nutr. Biochem. 16:272-278(2005). CC -!- FUNCTION: Regulatory subunit of lactose synthase, changes the CC substrate specificity of galactosyltransferase in the mammary CC gland making glucose a good acceptor substrate for this enzyme. CC This enables LS to synthesize lactose, the major carbohydrate CC component of milk. In other tissues, galactosyltransferase CC transfers galactose onto the N-acetylglucosamine of the CC oligosaccharide chains in glycoproteins. CC -!- SUBUNIT: Lactose synthase (LS) is a heterodimer of a catalytic CC component, beta1,4-galactosyltransferase (beta4Gal-T1) and a CC regulatory 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}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; J00270; AAA60345.1; -; mRNA. DR EMBL; X05153; CAA28799.1; -; Genomic_DNA. DR EMBL; X05153; CAA28800.1; -; Genomic_DNA. DR EMBL; AB049976; BAC06860.1; -; Genomic_DNA. DR EMBL; CR541987; CAG46784.1; -; mRNA. DR EMBL; CR542017; CAG46814.1; -; mRNA. DR EMBL; CH471111; EAW57990.1; -; Genomic_DNA. DR EMBL; BC069103; AAH69103.1; -; mRNA. DR EMBL; BC112316; AAI12317.1; -; mRNA. DR EMBL; BC112318; AAI12319.1; -; mRNA. DR CCDS; CCDS8765.1; -. DR PIR; A27880; LAHU. DR RefSeq; NP_002280.1; NM_002289.2. DR UniGene; Hs.72938; -. DR PDB; 1A4V; X-ray; 1.80 A; A=20-142. DR PDB; 1B9O; X-ray; 1.15 A; A=20-142. DR PDB; 1CB3; NMR; -; A=120-130. DR PDB; 1HML; X-ray; 1.70 A; A=1-142. DR PDB; 3B0I; X-ray; 1.80 A; A=20-142. DR PDB; 3B0O; X-ray; 1.61 A; A/B=21-142. DR PDB; 4L41; X-ray; 2.70 A; A/B=19-142. DR PDBsum; 1A4V; -. DR PDBsum; 1B9O; -. DR PDBsum; 1CB3; -. DR PDBsum; 1HML; -. DR PDBsum; 3B0I; -. DR PDBsum; 3B0O; -. DR PDBsum; 4L41; -. DR ProteinModelPortal; P00709; -. DR SMR; P00709; -. DR BioGrid; 110101; 5. DR STRING; 9606.ENSP00000301046; -. DR DrugBank; DB03796; Palmitic Acid. DR Allergome; 1289; Hom s ALA. DR iPTMnet; P00709; -. DR PhosphoSitePlus; P00709; -. DR BioMuta; LALBA; -. DR DMDM; 126001; -. DR PaxDb; P00709; -. DR PeptideAtlas; P00709; -. DR PRIDE; P00709; -. DR ProteomicsDB; 12680; -. DR ProteomicsDB; 51268; -. DR DNASU; 3906; -. DR Ensembl; ENST00000301046; ENSP00000301046; ENSG00000167531. DR GeneID; 3906; -. DR KEGG; hsa:3906; -. DR UCSC; uc001rrt.3; human. DR CTD; 3906; -. DR DisGeNET; 3906; -. DR EuPathDB; HostDB:ENSG00000167531.6; -. DR GeneCards; LALBA; -. DR HGNC; HGNC:6480; LALBA. DR HPA; CAB026343; -. DR HPA; HPA029855; -. DR HPA; HPA029856; -. DR MIM; 149750; gene. DR neXtProt; NX_P00709; -. DR OpenTargets; ENSG00000167531; -. DR PharmGKB; PA30269; -. DR eggNOG; ENOG410IX41; Eukaryota. DR eggNOG; ENOG410ZQK6; LUCA. DR GeneTree; ENSGT00940000161726; -. DR HOGENOM; HOG000037357; -. DR HOVERGEN; HBG052297; -. DR InParanoid; P00709; -. DR KO; K00704; -. DR OMA; LAHKPLC; -. DR OrthoDB; 199083at2759; -. DR PhylomeDB; P00709; -. DR TreeFam; TF324882; -. DR BioCyc; MetaCyc:HS09571-MONOMER; -. DR Reactome; R-HSA-5653890; Lactose synthesis. DR EvolutionaryTrace; P00709; -. DR GeneWiki; Alpha-lactalbumin; -. DR GenomeRNAi; 3906; -. DR PRO; PR:P00709; -. DR Proteomes; UP000005640; Chromosome 12. DR Bgee; ENSG00000167531; Expressed in 40 organ(s), highest expression level in epithelium of mammary gland. DR ExpressionAtlas; P00709; baseline and differential. DR Genevisible; P00709; HS. DR GO; GO:0005615; C:extracellular space; TAS:ProtInc. DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0004461; F:lactose synthase activity; IEA:InterPro. DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc. DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc. DR GO; GO:0042742; P:defense response to bacterium; TAS:ProtInc. DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IBA:GO_Central. DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central. DR GO; GO:0005989; P:lactose biosynthetic process; TAS:Reactome. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR CDD; cd00119; LYZ1; 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; 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; LACTALBUMIN_LYSOZYME_1; 1. DR PROSITE; PS51348; LACTALBUMIN_LYSOZYME_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Complete proteome; Direct protein sequencing; KW Disulfide bond; Glycoprotein; Lactose biosynthesis; Metal-binding; KW Milk protein; Polymorphism; Reference proteome; Secreted; Signal. FT SIGNAL 1 19 {ECO:0000269|PubMed:5049057}. FT CHAIN 20 142 Alpha-lactalbumin. FT /FTId=PRO_0000018444. FT CA_BIND 97 108 FT CARBOHYD 64 64 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:18780401}. FT CARBOHYD 90 90 N-linked (GlcNAc...) asparagine; FT atypical; partial. {ECO:0000269|Ref.9}. FT DISULFID 25 139 FT DISULFID 47 130 FT DISULFID 80 96 FT DISULFID 92 110 FT VARIANT 46 46 I -> V (in dbSNP:rs2232565). FT {ECO:0000269|PubMed:15866226}. FT /FTId=VAR_024526. FT CONFLICT 99 99 F -> K (in Ref. 8; AA sequence). FT {ECO:0000305}. FT HELIX 24 30 {ECO:0000244|PDB:1B9O}. FT HELIX 32 34 {ECO:0000244|PDB:1B9O}. FT HELIX 37 39 {ECO:0000244|PDB:1B9O}. FT HELIX 42 53 {ECO:0000244|PDB:1B9O}. FT STRAND 60 62 {ECO:0000244|PDB:1B9O}. FT STRAND 67 69 {ECO:0000244|PDB:1B9O}. FT TURN 70 73 {ECO:0000244|PDB:1B9O}. FT TURN 76 78 {ECO:0000244|PDB:1B9O}. FT STRAND 79 81 {ECO:0000244|PDB:1B9O}. FT STRAND 83 85 {ECO:0000244|PDB:4L41}. FT STRAND 91 95 {ECO:0000244|PDB:4L41}. FT HELIX 96 100 {ECO:0000244|PDB:1B9O}. FT HELIX 105 117 {ECO:0000244|PDB:1B9O}. FT TURN 118 120 {ECO:0000244|PDB:1B9O}. FT HELIX 121 124 {ECO:0000244|PDB:1B9O}. FT HELIX 128 130 {ECO:0000244|PDB:3B0O}. FT HELIX 134 137 {ECO:0000244|PDB:1B9O}. SQ SEQUENCE 142 AA; 16225 MW; 647F448733B06D65 CRC64; MRFFVPLFLV GILFPAILAK QFTKCELSQL LKDIDGYGGI ALPELICTMF HTSGYDTQAI VENNESTEYG LFQISNKLWC KSSQVPQSRN ICDISCDKFL DDDITDDIMC AKKILDIKGI DYWLAHKALC TEKLEQWLCE KL //