Laminin, alpha 1

LAMA1

Available structures

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

MGI: 99892 HomoloGene: 21146 GeneCards: LAMA1

Genetically Related Diseases

type 2 diabetes mellitus^[1]

Gene ontology
Molecular function	• receptor binding • extracellular matrix structural constituent • protein binding
Cellular component	• extracellular matrix • extracellular space • proteinaceous extracellular matrix • extracellular region • basement membrane • laminin-1 complex • laminin-3 complex
Biological process	• cell surface receptor signaling pathway • regulation of cell adhesion • cell adhesion • extracellular matrix organization • regulation of cell migration • regulation of embryonic development
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


284217


16772

Ensembl


ENSG00000101680


ENSMUSG00000032796

UniProt


P25391


P19137

RefSeq (mRNA)


NM_005559


NM_008480

RefSeq (protein)


NP_005550.2


NP_032506.2

Location (UCSC)

Chr 18: 6.94 – 7.12 Mb

Chr 17: 67.7 – 67.82 Mb

PubMed search

^[2]

^[3]

Wikidata

View/Edit Human

View/Edit Mouse

Laminin subunit alpha-1 is a protein that in humans is encoded by the LAMA1 gene.^[4]^[5]

Interactions

Laminin, alpha 1 has been shown to interact with FBLN2.^[6]^[7]

References

↑ "Diseases that are genetically associated with LAMA1 view/edit references on wikidata".
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ 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.
↑ "Entrez Gene: LAMA1 laminin, alpha 1".
↑ 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. UNITED STATES. 272 (5): 2814–20. doi:10.1074/jbc.272.5.2814. ISSN 0021-9258. PMID 9006922.
↑ 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. UNITED STATES. 275 (45): 35192–9. doi:10.1074/jbc.M003261200. ISSN 0021-9258. PMID 10934193.

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. 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. 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.

Protein: scleroproteins

Extracellular matrix

Collagen

Fibril forming	type I COL1A1 COL1A2 type II (COL2A1) type III type V COL5A1 COL5A2 COL5A3 COL24A1 COL26A1

Other	FACIT: type IX COL9A1 COL9A2 COL9A3 type XII (COL12A1) COL14A1 COL16A1 COL19A1 COL20A1 COL21A1 COL22A1 basement membrane: type IV COL4A1 COL4A2 COL4A3 COL4A4 COL4A5 COL4A6 multiplexin: COL15A1 type XVIII COL18A1 Endostatin transmembrane: COL13A1 COL17A1 COL23A1 COL25A1 other: type VI COL6A1 COL6A2 COL6A3 COL6A5 type VII (COL7A1) type VIII COL8A1 COL8A2 type X (COL10A1) type XI COL11A1 COL11A2 COL27A1 COL28A1

Enzymes	Prolyl hydroxylase/Lysyl hydroxylase Cartilage associated protein/Leprecan ADAMTS2 Procollagen peptidase Lysyl oxidase

Laminin

alpha
- LAMA1
- LAMA2
- LAMA3
- LAMA4
- LAMA5
beta
- LAMB1
- LAMB2
- LAMB3
- LAMB4
gamma
- LAMC1
- LAMC2
- LAMC3

Other

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Laminin, alpha 1

Interactions

References

Further reading