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    LAM4 Lam4p [ Saccharomyces cerevisiae S288C ]

    Gene ID: 856480, updated on 9-Dec-2024

    Summary

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    Official Symbol
    LAM4
    Official Full Name
    Lam4p
    Primary source
    SGD:S000001122
    Locus tag
    YHR080C
    See related
    AllianceGenome:SGD:S000001122; FungiDB:YHR080C; VEuPathDB:YHR080C
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Saccharomyces cerevisiae S288C (strain: S288C)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
    Also known as
    LTC3
    Summary
    Enables sterol binding activity and sterol transfer activity. Acts upstream of or within sterol transport. Located in cortical endoplasmic reticulum. Orthologous to human GRAMD1A (GRAM domain containing 1A) and GRAMD1C (GRAM domain containing 1C). [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See LAM4 in Genome Data Viewer
    Location:
    chromosome: VIII
    Exon count:
    1
    Sequence:
    Chromosome: VIII; NC_001140.6 (262801..266838, complement)

    Chromosome VIII - NC_001140.6Genomic Context describing neighboring genes Neighboring gene bifunctional endoribonuclease/protein kinase IRE1 Neighboring gene Sae3p Neighboring gene Lrp1p Neighboring gene putative serine/threonine protein kinase KSP1

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001140.6

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Exchange of water for sterol underlies sterol egress from a StARkin domain. Khelashvili G, et al. Elife, 2019 Dec 4. PMID 31799930, Free PMC Article
    2. Structural basis of sterol binding and transport by a yeast StARkin domain. Jentsch JA, et al. J Biol Chem, 2018 Apr 13. PMID 29463678, Free PMC Article
    3. Structural insights into a StART-like domain in Lam4 and its interaction with sterol ligands. Gatta AT, et al. Biochem Biophys Res Commun, 2018 Jan 15. PMID 29274338
    4. Structural basis of sterol recognition and nonvesicular transport by lipid transfer proteins anchored at membrane contact sites. Tong J, et al. Proc Natl Acad Sci U S A, 2018 Jan 30. PMID 29339490, Free PMC Article
    5. LAM Genes Contribute to Environmental Stress Tolerance but Sensibilize Yeast Cells to Azoles. Sokolov SS, et al. Front Microbiol, 2020. PMID 32047490, Free PMC Article

    See all (33) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Large-scale atomistic molecular dynamics simulations reveal that sterol egress involves widening of the fracture, penetration of water into the cavity, and consequent destabilization of the bound sterol. The simulations identify polar residues along the fracture that are important for sterol release.
      Title: Exchange of water for sterol underlies sterol egress from a StARkin domain.
    2. results suggest that Lam4S2 engages anionic membranes via a basic surface patch, enabling "head-first" entry of sterol into the binding pocket followed by partial closure of the entryway. Reversal of these steps enables sterol egress.
      Title: Structural basis of sterol binding and transport by a yeast StARkin domain.
    3. Ltc1 and Ltc3/4 function at the vacuole and plasma membrane, respectively, to create membrane domains that partition upstream regulators of the TORC1 and TORC2 signaling pathways to coordinate cellular stress responses with sterol homeostasis.
      Title: Sterol transporters at membrane contact sites regulate TORC1 and TORC2 signaling.
    Submit: New GeneRIF Correction

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    Gene Ontology Provided by SGD

    Function Evidence Code Pubs
    enables sterol binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables sterol binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables sterol transfer activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables sterol transfer activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in intracellular sterol transport IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within sterol transport IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    is_active_in cortical endoplasmic reticulum IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cortical endoplasmic reticulum IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in endoplasmic reticulum IEA
    Inferred from Electronic Annotation
    more info
    		  
    is_active_in endoplasmic reticulum membrane IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in endoplasmic reticulum membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    is_active_in endoplasmic reticulum-plasma membrane contact site IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in mitochondrion HDA PubMed 
    is_active_in mitochondrion IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in organelle IEA
    Inferred from Electronic Annotation
    more info
    		  
    is_active_in plasma membrane IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  

    General protein information

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    Preferred Names
    Lam4p
    NP_011948.1
    • Sterol-binding protein that localizes to puncta in the cortical ER; sterol binding occurs via two StART-like domains; one of six StART-like domain-containing proteins in yeast that may be involved in intracellular sterol transfer between membranes; conserved across eukaryotes; has both GRAM and StART-like (VASt) domains; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies

    NCBI Reference Sequences (RefSeq)

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    Genome Annotation

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference assembly

    Genomic

    1. NC_001140.6 Reference assembly

      Range
      262801..266838 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001179210.1 → NP_011948.1  TPA: Lam4p [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_011948.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D3DL31, P38800
      UniProtKB/TrEMBL
      A6ZSY9, B3LSJ7, N1P2P0
      Conserved Domains (2) summary
      cd13220
      Location:561 → 654
      PH-GRAM_GRAMDC; GRAM domain-containing protein (GRAMDC) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain
      pfam16016
      Location:761 → 910
      DUF4782; Domain of unknown function (DUF4782)
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P38800.1

    Gene LinkOut

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