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(Top) 1 Interactions 2 Role in pathology 3 References 4 Further reading

Laminin subunit alpha-1

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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; OMA:LAMA1 - orthologs

Gene location (Human)

Chr.	Chromosome 18 (human)^[1]

Band	18p11.31	Start	6,941,742 bp^[1]
Band	18p11.31	End	7,117,797 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 17 (mouse)^[2]

Band	17 E1.1\|17 38.8 cM	Start	68,004,254 bp^[2]
Band	17 E1.1\|17 38.8 cM	End	68,129,642 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

ventricular zone

right testis

left testis

mucosa of ileum

gonad

stromal cell of endometrium

testicle

ganglionic eminence

mucosa of colon

mucosa of sigmoid colon

Top expressed in

Bowman's capsule

tail of embryo

ovary

epithelium of lens

cumulus cell

inner renal medulla

Gonadal ridge

efferent ductule

yolk sac

cortical collecting duct

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	signaling receptor binding extracellular matrix structural constituent protein binding protein C-terminus binding glycosphingolipid binding
Cellular component	extracellular matrix extracellular region basement membrane laminin-1 complex laminin-3 complex extracellular space membrane cell-cell 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 tissue development 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: 68 – 68.13 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

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

Interactions[edit]

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

Role in pathology[edit]

Mutations of the LAMA1 gene cause the Poretti–Boltshauser syndrome.

References[edit]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000101680 – Ensembl, May 2017

^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000032796 – Ensembl, May 2017

^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

^ 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. 272 (5): 2814–20. doi:10.1074/jbc.272.5.2814. ISSN 0021-9258. PMID 9006922. S2CID 24800195.

^ Talts JF, 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. S2CID 36521395.

Further reading[edit]

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. doi:10.1016/S0021-9258(19)38338-3. 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. S2CID 17529055.

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. doi:10.1016/S0021-9258(17)46714-7. 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. doi:10.1016/S0021-9258(18)53103-3. 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. S2CID 37912337.

Zahedi K (1997). "Characterization of the binding of serum amyloid P to laminin". J. Biol. Chem. 272 (4): 2143–8. doi:10.1074/S0021-9258(19)78482-8. 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. S2CID 24800195.

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. S2CID 43911847.

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. S2CID 7310763.

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. S2CID 84569969.

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.