Human Gene LAMC2 (ENST00000264144.5) from GENCODE V44
Description: Homo sapiens laminin subunit gamma 2 (LAMC2), transcript variant 1, mRNA. (from RefSeq NM_005562) RefSeq Summary (NM_005562): Laminins, a family of extracellular matrix glycoproteins, are the major noncollagenous constituent of basement membranes. They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis. Laminins, composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively), have a cruciform structure consisting of 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains. Each laminin chain is a multidomain protein encoded by a distinct gene. Several isoforms of each chain have been described. Different alpha, beta and gamma chain isomers combine to give rise to different heterotrimeric laminin isoforms which are designated by Arabic numerals in the order of their discovery, i.e. alpha1beta1gamma1 heterotrimer is laminin 1. The biological functions of the different chains and trimer molecules are largely unknown, but some of the chains have been shown to differ with respect to their tissue distribution, presumably reflecting diverse functions in vivo. This gene encodes the gamma chain isoform laminin, gamma 2. The gamma 2 chain, formerly thought to be a truncated version of beta chain (B2t), is highly homologous to the gamma 1 chain; however, it lacks domain VI, and domains V, IV and III are shorter. It is expressed in several fetal tissues but differently from gamma 1, and is specifically localized to epithelial cells in skin, lung and kidney. The gamma 2 chain together with alpha 3 and beta 3 chains constitute laminin 5 (earlier known as kalinin), which is an integral part of the anchoring filaments that connect epithelial cells to the underlying basement membrane. The epithelium-specific expression of the gamma 2 chain implied its role as an epithelium attachment molecule, and mutations in this gene have been associated with junctional epidermolysis bullosa, a skin disease characterized by blisters due to disruption of the epidermal-dermal junction. Two transcript variants resulting from alternative splicing of the 3' terminal exon, and encoding different isoforms of gamma 2 chain, have been described. The two variants are differentially expressed in embryonic tissues, however, the biological significance of the two forms is not known. Transcript variants utilizing alternative polyA_signal have also been noted in literature. [provided by RefSeq, Aug 2011]. Gencode Transcript: ENST00000264144.5 Gencode Gene: ENSG00000058085.15 Transcript (Including UTRs) Position: hg38 chr1:183,186,264-183,245,127 Size: 58,864 Total Exon Count: 23 Strand: + Coding Region Position: hg38 chr1:183,186,353-183,243,400 Size: 57,048 Coding Exon Count: 23
ID:LAMC2_HUMAN DESCRIPTION: RecName: Full=Laminin subunit gamma-2; AltName: Full=Cell-scattering factor 140 kDa subunit; Short=CSF 140 kDa subunit; AltName: Full=Epiligrin subunit gamma; AltName: Full=Kalinin subunit gamma; AltName: Full=Kalinin/nicein/epiligrin 100 kDa subunit; AltName: Full=Ladsin 140 kDa subunit; AltName: Full=Laminin B2t chain; AltName: Full=Laminin-5 subunit gamma; AltName: Full=Large adhesive scatter factor 140 kDa subunit; AltName: Full=Nicein subunit gamma; Flags: Precursor; FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Ladsin exerts cell- scattering activity toward a wide variety of cells, including epithelial, endothelial, and fibroblastic cells. SUBUNIT: Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Gamma-2 is a subunit of laminin-5 (laminin-332 or epiligrin/kalinin/nicein). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. Note=Major component. TISSUE SPECIFICITY: The large variant is expressed only in specific epithelial cells of embryonic and neonatal tissues. In 17-week old embryo the small variant is found in cerebral cortex, lung, and distal tubes of kidney, but not in epithelia except for distal tubuli. DOMAIN: The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure. DOMAIN: Domain IV is globular. DISEASE: Defects in LAMC2 are a cause of epidermolysis bullosa junctional Herlitz type (H-JEB) [MIM:226700]; also known as junctional epidermolysis bullosa Herlitz-Pearson type. JEB defines a group of blistering skin diseases characterized by tissue separation which occurs within the dermo-epidermal basement membrane. H-JEB is a severe, infantile and lethal form. Death occurs usually within the first six months of life. Occasionally, children survive to teens. H-JEB is marked by bullous lesions at birth and extensive denudation of skin and mucous membranes that may be hemorrhagic. MISCELLANEOUS: Binds heparin (By similarity). SIMILARITY: Contains 8 laminin EGF-like domains. SIMILARITY: Contains 1 laminin IV type A domain. WEB RESOURCE: Name=GeneReviews; URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/LAMC2";
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q13753
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Z15009 - H.sapiens mRNA for laminin. Z15008 - H.sapiens mRNA for laminin. AK296944 - Homo sapiens cDNA FLJ57342 complete cds, highly similar to Laminin gamma-2 chain precursor. X73902 - H.sapiens mRNA for nicein B2 chain. BC113378 - Homo sapiens laminin, gamma 2, mRNA (cDNA clone MGC:141938 IMAGE:8322430), complete cds. BC112286 - Homo sapiens laminin, gamma 2, mRNA (cDNA clone MGC:138491 IMAGE:8327754), complete cds. BC143653 - Homo sapiens cDNA clone IMAGE:9052167. AK307945 - Homo sapiens cDNA, FLJ97893. JD083722 - Sequence 64746 from Patent EP1572962. JD493039 - Sequence 474063 from Patent EP1572962. JD090348 - Sequence 71372 from Patent EP1572962. JD207355 - Sequence 188379 from Patent EP1572962. JD528546 - Sequence 509570 from Patent EP1572962. JD179003 - Sequence 160027 from Patent EP1572962. JD369310 - Sequence 350334 from Patent EP1572962. JD182094 - Sequence 163118 from Patent EP1572962. JD349034 - Sequence 330058 from Patent EP1572962. JD171292 - Sequence 152316 from Patent EP1572962. JD273325 - Sequence 254349 from Patent EP1572962. JD311460 - Sequence 292484 from Patent EP1572962. JD347705 - Sequence 328729 from Patent EP1572962. JD177940 - Sequence 158964 from Patent EP1572962. JD089426 - Sequence 70450 from Patent EP1572962. JD382894 - Sequence 363918 from Patent EP1572962. JD363164 - Sequence 344188 from Patent EP1572962. JD563872 - Sequence 544896 from Patent EP1572962. JD086824 - Sequence 67848 from Patent EP1572962. JD314480 - Sequence 295504 from Patent EP1572962. JD052342 - Sequence 33366 from Patent EP1572962. JD385974 - Sequence 366998 from Patent EP1572962. JD554326 - Sequence 535350 from Patent EP1572962. JD455953 - Sequence 436977 from Patent EP1572962. JD455582 - Sequence 436606 from Patent EP1572962. JD102444 - Sequence 83468 from Patent EP1572962. JD052182 - Sequence 33206 from Patent EP1572962. JD126999 - Sequence 108023 from Patent EP1572962. JD274487 - Sequence 255511 from Patent EP1572962. JD479387 - Sequence 460411 from Patent EP1572962. JD292894 - Sequence 273918 from Patent EP1572962. JD258201 - Sequence 239225 from Patent EP1572962. JD504353 - Sequence 485377 from Patent EP1572962. JD158077 - Sequence 139101 from Patent EP1572962. JD444981 - Sequence 426005 from Patent EP1572962. JD516503 - Sequence 497527 from Patent EP1572962. JD116423 - Sequence 97447 from Patent EP1572962. JD222374 - Sequence 203398 from Patent EP1572962. JD231218 - Sequence 212242 from Patent EP1572962.
Biochemical and Signaling Pathways
KEGG - Kyoto Encyclopedia of Genes and Genomes hsa04510 - Focal adhesion hsa04512 - ECM-receptor interaction hsa05200 - Pathways in cancer hsa05222 - Small cell lung cancer
Reactome (by CSHL, EBI, and GO)
Protein Q13753 (Reactome details) participates in the following event(s):
R-HSA-349626 Integrin alpha2beta1 binds laminin-332 R-HSA-446089 BP180 interacts extracellularly with Laminin 332 R-HSA-1566979 Laminin-332 degradation by laminin-322 degrading extracellular proteinases R-HSA-2396234 Collagen type VII binds laminin-322 and collagen IV R-HSA-3787997 Laminin-332 binds collagen type VII R-HSA-3791155 Laminin-322 degradation by MMP14 R-HSA-432956 BP230 is recruited to the hemidesmosome R-HSA-2213192 Hemidesmosome formation R-HSA-216048 Integrins alpha3beta1, alpha6beta4 bind laminin-332, 511, 521, (211, 221) R-HSA-3907292 Integrin alpha6beta1 binds laminin-322, 512, 521, 211, 221, 411 R-HSA-2328129 Dystroglycan binds Laminins and Dystrophin R-HSA-2396083 Laminins bind galactosyl sulfatide and related sulfated glycolipids R-HSA-4084505 Laminins bind HSPG2 R-HSA-446083 CD151 interacts with BP180 and the integrin alpha 6 subunit R-HSA-446077 BP230 interacts with keretin K5/K14 R-HSA-3000157 Laminin interactions R-HSA-446107 Type I hemidesmosome assembly R-HSA-1474228 Degradation of the extracellular matrix R-HSA-2214320 Anchoring fibril formation R-HSA-2022090 Assembly of collagen fibrils and other multimeric structures R-HSA-3000171 Non-integrin membrane-ECM interactions R-HSA-1474244 Extracellular matrix organization R-HSA-446728 Cell junction organization R-HSA-1474290 Collagen formation R-HSA-1500931 Cell-Cell communication
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