Laminin, alpha 1

Laminin subunit alpha-1 is a protein that in humans is encoded by the LAMA1 gene.[5][6]

LAMA1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2JD4
Identifiers
Aliases	LAMA1, LAMA, S-LAM-alpha, PTBHS, Laminin, alpha 1, laminin subunit alpha 1
External IDs	OMIM: 150320 MGI: 99892 HomoloGene: 21146 GeneCards: LAMA1
Gene location (Human) Chr. Chromosome 18 (human)[1] Band 18p11.31 Start 6,941,742 bp[1] End 7,117,797 bp[1]
Gene location (Mouse) Chr. Chromosome 17 (mouse)[2] Band 17 E1.1|17 38.8 cM Start 67,697,259 bp[2] End 67,822,647 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • receptor binding • extracellular matrix structural constituent • GO:0001948 protein binding • protein C-terminus binding • glycosphingolipid binding Cellular component • extracellular matrix • proteinaceous extracellular matrix • extracellular region • basement membrane • laminin-1 complex • laminin-3 complex • extracellular • membrane • intercellular junction • laminin complex • collagen-containing extracellular matrix Biological process • cell surface receptor signaling pathway • regulation of cell adhesion • cell adhesion • extracellular matrix organization • regulation of cell migration • regulation of embryonic development • morphogenesis of an epithelial sheet • protein phosphorylation • histogenesis • neuron projection development • establishment of epithelial cell apical/basal polarity • retina development in camera-type eye • epithelial tube branching involved in lung morphogenesis • branching involved in salivary gland morphogenesis • retinal blood vessel morphogenesis • axon guidance • animal organ morphogenesis • camera-type eye development • blood vessel morphogenesis Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	284217	16772
Ensembl	ENSG00000101680	ENSMUSG00000032796
UniProt	P25391	P19137
RefSeq (mRNA)	NM_005559	NM_008480
RefSeq (protein)	NP_005550	NP_032506
Location (UCSC)	Chr 18: 6.94 – 7.12 Mb	Chr 17: 67.7 – 67.82 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Interactions

Laminin, alpha 1 has been shown to interact with FBLN2.[7][8]

References

1. GRCh38: Ensembl release 89: ENSG00000101680 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000032796 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Nagayoshi T, Mattei MG, Passage E, Knowlton R, Chu ML, Uitto J (January 1990). "Human laminin A chain (LAMA) gene: chromosomal mapping to locus 18p11.3". Genomics. 5 (4): 932–5. doi:10.1016/0888-7543(89)90136-5. PMID 2591971.
6. "Entrez Gene: LAMA1 laminin, alpha 1".
7. Utani, A; Nomizu M; Yamada Y (January 1997). "Fibulin-2 binds to the short arms of laminin-5 and laminin-1 via conserved amino acid sequences". J. Biol. Chem. 272 (5): 2814–20. doi:10.1074/jbc.272.5.2814. ISSN 0021-9258. PMID 9006922.
8. Talts, J F; Sasaki T; Miosge N; Göhring W; Mann K; Mayne R; Timpl R (November 2000). "Structural and functional analysis of the recombinant G domain of the laminin alpha4 chain and its proteolytic processing in tissues". J. Biol. Chem. 275 (45): 35192–9. doi:10.1074/jbc.M003261200. ISSN 0021-9258. PMID 10934193.

Further reading

• Haaparanta T, Uitto J, Ruoslahti E, Engvall E (1991). "Molecular cloning of the cDNA encoding human laminin A chain". Matrix. 11 (3): 151–60. doi:10.1016/s0934-8832(11)80153-8. PMID 1714537.
• Nissinen M, Vuolteenaho R, Boot-Handford R, et al. (1991). "Primary structure of the human laminin A chain. Limited expression in human tissues". Biochem. J. 276 ( Pt 2) (Pt 2): 369–79. doi:10.1042/bj2760369. PMC 1151101. PMID 2049067.
• Taraboletti G, Rao CN, Krutzsch HC, et al. (1990). "Sulfatide-binding domain of the laminin A chain". J. Biol. Chem. 265 (21): 12253–8. PMID 2373692.
• Olsen D, Nagayoshi T, Fazio M, et al. (1989). "Human laminin: cloning and sequence analysis of cDNAs encoding A, B1 and B2 chains, and expression of the corresponding genes in human skin and cultured cells". Lab. Invest. 60 (6): 772–82. PMID 2733383.
• Leivo I, Engvall E (1986). "C3d fragment of complement interacts with laminin and binds to basement membranes of glomerulus and trophoblast". J. Cell Biol. 103 (3): 1091–100. doi:10.1083/jcb.103.3.1091. PMC 2114300. PMID 3488995.
• Wewer UM, Gerecke DR, Durkin ME, et al. (1995). "Human beta 2 chain of laminin (formerly S chain): cDNA cloning, chromosomal localization, and expression in carcinomas". Genomics. 24 (2): 243–52. doi:10.1006/geno.1994.1612. PMID 7698745.
• Yamada H, Shimizu T, Tanaka T, et al. (1994). "Dystroglycan is a binding protein of laminin and merosin in peripheral nerve". FEBS Lett. 352 (1): 49–53. doi:10.1016/0014-5793(94)00917-1. PMID 7925941.
• Moser TL, Enghild JJ, Pizzo SV, Stack MS (1993). "The extracellular matrix proteins laminin and fibronectin contain binding domains for human plasminogen and tissue plasminogen activator". J. Biol. Chem. 268 (25): 18917–23. PMID 8360181.
• Yurchenco PD, Sung U, Ward MD, et al. (1993). "Recombinant laminin G domain mediates myoblast adhesion and heparin binding". J. Biol. Chem. 268 (11): 8356–65. PMID 8463343.
• Ancsin JB, Kisilevsky R (1997). "Characterization of high affinity binding between laminin and the acute-phase protein, serum amyloid A". J. Biol. Chem. 272 (1): 406–13. doi:10.1074/jbc.272.1.406. PMID 8995276.
• Zahedi K (1997). "Characterization of the binding of serum amyloid P to laminin". J. Biol. Chem. 272 (4): 2143–8. doi:10.1074/jbc.272.4.2143 (inactive 2020-01-22). PMID 8999915.
• Utani A, Nomizu M, Yamada Y (1997). "Fibulin-2 binds to the short arms of laminin-5 and laminin-1 via conserved amino acid sequences". J. Biol. Chem. 272 (5): 2814–20. doi:10.1074/jbc.272.5.2814. PMID 9006922.
• Cáceres J, Brandan E (1997). "Interaction between Alzheimer's disease beta A4 precursor protein (APP) and the extracellular matrix: evidence for the participation of heparan sulfate proteoglycans". J. Cell. Biochem. 65 (2): 145–58. doi:10.1002/(SICI)1097-4644(199705)65:2<145::AID-JCB2>3.0.CO;2-U. PMID 9136074.
• Chen M, Marinkovich MP, Veis A, et al. (1997). "Interactions of the amino-terminal noncollagenous (NC1) domain of type VII collagen with extracellular matrix components. A potential role in epidermal-dermal adherence in human skin". J. Biol. Chem. 272 (23): 14516–22. doi:10.1074/jbc.272.23.14516. PMID 9169408.
• Schuger L, Skubitz AP, Zhang J, et al. (1997). "Laminin α1 Chain Synthesis in the Mouse Developing Lung: Requirement for Epithelial–Mesenchymal Contact and Possible Role in Bronchial Smooth muscle Development". J. Cell Biol. 139 (2): 553–62. doi:10.1083/jcb.139.2.553. PMC 2139794. PMID 9334356.
• Mrowiec T, Melchar C, Górski A (1998). "HIV-protein-mediated alterations in T cell interactions with the extracellular matrix proteins and endothelium". Arch. Immunol. Ther. Exp. (Warsz.). 45 (2–3): 255–9. PMID 9597096.
• O'Grady P, Thai TC, Saito H (1998). "The Laminin–Nidogen Complex is a Ligand for a Specific Splice Isoform of the Transmembrane Protein Tyrosine Phosphatase LAR". J. Cell Biol. 141 (7): 1675–84. doi:10.1083/jcb.141.7.1675. PMC 2133008. PMID 9647658.
• Ettner N, Göhring W, Sasaki T, et al. (1998). "The N-terminal globular domain of the laminin alpha1 chain binds to alpha1beta1 and alpha2beta1 integrins and to the heparan sulfate-containing domains of perlecan". FEBS Lett. 430 (3): 217–21. doi:10.1016/S0014-5793(98)00601-2. PMID 9688542.
• Ludwig HC, Rausch S, Schallock K, Markakis E (1999). "Expression of CD 73 (ecto-5'-nucleotidase) in 165 glioblastomas by immunohistochemistry and electronmicroscopic histochemistry". Anticancer Res. 19 (3A): 1747–52. PMID 10470109.