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(-) Description

Title :  SOLUTION STRUCTURE OF THE PDZ DOMAIN FROM HUMAN SHROOM FAMILY MEMBER 4
 
Authors :  H. Endo, M. Yoshida, F. Hayashi, S. Yokoyama, Riken Structural Genomics/Proteomics Initiative (Rsgi)
Date :  14 Feb 07  (Deposition) - 14 Aug 07  (Release) - 24 Feb 09  (Revision)
Method :  SOLUTION NMR
Resolution :  NOT APPLICABLE
Chains :  NMR Structure  :  A  (20x)
Keywords :  Apx/Shroom Family Member, Kiaa1202 Protein, Structural Genomics, Nppsfa, National Project On Protein Structural And Functional Analyses, Riken Structural Genomics/Proteomics Initiative, Rsgi, Structural Protein (Keyword Search: [Gene Ontology, PubMed, Web (Google))
 
Reference :  H. Endo, M. Yoshida, F. Hayashi, S. Yokoyama
Solution Structure Of The Pdz Domain From Human Shroom Family Member 4
To Be Published
PubMed: search
(for further references see the PDB file header)

(-) Compounds

Molecule 1 - SHROOM FAMILY MEMBER 4
    ChainsA
    EngineeredYES
    Expression System PlasmidP050627-31
    Expression System Vector TypePLASMID
    FragmentPDZ DOMAIN
    GeneKIAA1202
    Organism CommonHUMAN
    Organism ScientificHOMO SAPIENS
    Organism Taxid9606
    Other DetailsCELL FREE PROTEIN SYNTHESIS
    SynonymFRAGMENT

 Structural Features

(-) Chains, Units

  
NMR Structure (20x)

Summary Information (see also Sequences/Alignments below)

(-) Ligands, Modified Residues, Ions  (0, 0)

(no "Ligand,Modified Residues,Ions" information available for 2EDP)

(-) Sites  (0, 0)

(no "Site" information available for 2EDP)

(-) SS Bonds  (0, 0)

(no "SS Bond" information available for 2EDP)

(-) Cis Peptide Bonds  (1, 20)

NMR Structure
No.ModelResidues
11, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20Ala A:21 -Pro A:22

 Sequence-Structure Mapping

(-) SAPs(SNPs)/Variants  (0, 0)

(no "SAP(SNP)/Variant" information available for 2EDP)

(-) PROSITE Motifs  (1, 1)

NMR Structure (1, 1)
 PROSITEUniProtKBPDB
No.IDACDescriptionIDLocationCountLocation
1PDZPS50106 PDZ domain profile.SHRM4_HUMAN10-92  1A:12-94

(-) Exons   (3, 3)

NMR Structure (3, 3)
 ENSEMBLUniProtKBPDB
No.Transcript IDExonExon IDGenome LocationLengthIDLocationLengthCountLocationLength
1.1bENST000003760201bENSE00002042413X:50557044-50556902143SHRM4_HUMAN1-39391A:3-4139
1.2ENST000003760202ENSE00001038490X:50438937-50438786152SHRM4_HUMAN40-90511A:42-9251
1.5ENST000003760205ENSE00001750094X:50381308-50381174135SHRM4_HUMAN90-135461A:92-100 (gaps)42
1.6ENST000003760206ENSE00001038494X:50378668-503761782491SHRM4_HUMAN135-9658310--
1.7ENST000003760207ENSE00001325221X:50370675-5037061462SHRM4_HUMAN966-986210--
1.8ENST000003760208ENSE00001302283X:50351184-50350381804SHRM4_HUMAN986-12542690--
1.9ENST000003760209ENSE00001038487X:50345813-50345633181SHRM4_HUMAN1254-1314610--
1.10ENST0000037602010ENSE00001038485X:50341535-50341266270SHRM4_HUMAN1315-1404900--
1.11cENST0000037602011cENSE00001525342X:50339964-503346475318SHRM4_HUMAN1405-1493890--

(-) Sequences/Alignments

NMR Structure
   Reformat: Number of residues per line =  ('0' or empty: single-line sequence representation)
  Number of residues per labelling interval =   
  UniProt sequence: complete  aligned part    
   Show mapping: SCOP domains CATH domains Pfam domains Secondary structure (by author)
SAPs(SNPs) PROSITE motifs Exons
(details for a mapped element are shown in a popup box when the mouse pointer rests over it)
Chain A from PDB  Type:PROTEIN  Length:100
 aligned with SHRM4_HUMAN | Q9ULL8 from UniProtKB/Swiss-Prot  Length:1493

    Alignment length:133
                              1                                                                                                                                  
                              |      8        18        28        38        48        58        68        78        88        98       108       118       128   
          SHRM4_HUMAN     - --MENRPGSFQYVPVQLQGGAPWGFTLKGGLEHCEPLTVSKIEDGGKAALSQKMRTGDELVNINGTPLYGSRQEALILIKGSFRILKLIVRRRNAPVSRPHSWHVAKLLEGCPEAATTMHFPSEAFSLSWHSG 131
               SCOP domains d2edpa_ A: automated matches                                                                                                          SCOP domains
               CATH domains ------------------------------------------------------------------------------------------------------------------------------------- CATH domains
               Pfam domains ------------------------------------------------------------------------------------------------------------------------------------- Pfam domains
         Sec.struct. author ..........eeeeee..........eeeehhhheeeee......hhhhhhh......eeeee..ee....hhhhhhhhhh.....eeeeee......---------------------------------.. Sec.struct. author
                 SAPs(SNPs) ------------------------------------------------------------------------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE -----------PDZ  PDB: A:12-94 UniProt: 10-92                                                   --------------------------------------- PROSITE
           Transcript 1 (1) --Exon 1.1b  PDB: A:3-41 UniProt: 1-39   Exon 1.2  PDB: A:42-92 UniProt: 40-90              ----------------------------------------- Transcript 1 (1)
           Transcript 1 (2) -------------------------------------------------------------------------------------------Exon 1.5  PDB: A:92-100 (gaps)             Transcript 1 (2)
                 2edp A   1 GSSGSSGGSFQYVPVQLQGGAPWGFTLKGGLEHCEPLTVSKIEDGGKAALSQKMRTGDELVNINGTPLYGSRQEALILIKGSFRILKLIVRRRNSGPS---------------------------------SG 100
                                    10        20        30        40        50        60        70        80        90       | -         -         -         - | 
                                                                                                                            98                                99 

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  x → Chemical Group (purple background, 'x', labelled with number + name, e.g. ACE or NH2)
  extra numbering lines below/above indicate numbering irregularities and modified residue names etc., number ends below/above '|'

 Classification and Annotation

(-) SCOP Domains  (1, 1)

NMR Structure

(-) CATH Domains  (0, 0)

(no "CATH Domain" information available for 2EDP)

(-) Pfam Domains  (0, 0)

(no "Pfam Domain" information available for 2EDP)

(-) Gene Ontology  (18, 18)

NMR Structure(hide GO term definitions)
Chain A   (SHRM4_HUMAN | Q9ULL8)
molecular function
    GO:0003779    actin binding    Interacting selectively and non-covalently with monomeric or multimeric forms of actin, including actin filaments.
    GO:0051015    actin filament binding    Interacting selectively and non-covalently with an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits.
biological process
    GO:0030036    actin cytoskeleton organization    A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments and their associated proteins.
    GO:0007015    actin filament organization    A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments. Includes processes that control the spatial distribution of actin filaments, such as organizing filaments into meshworks, bundles, or other structures, as by cross-linking.
    GO:0007420    brain development    The process whose specific outcome is the progression of the brain over time, from its formation to the mature structure. Brain development begins with patterning events in the neural tube and ends with the mature structure that is the center of thought and emotion. The brain is responsible for the coordination and control of bodily activities and the interpretation of information from the senses (sight, hearing, smell, etc.).
    GO:0000902    cell morphogenesis    The developmental process in which the size or shape of a cell is generated and organized.
    GO:0050890    cognition    The operation of the mind by which an organism becomes aware of objects of thought or perception; it includes the mental activities associated with thinking, learning, and memory.
    GO:0007275    multicellular organism development    The biological process whose specific outcome is the progression of a multicellular organism over time from an initial condition (e.g. a zygote or a young adult) to a later condition (e.g. a multicellular animal or an aged adult).
cellular component
    GO:0015629    actin cytoskeleton    The part of the cytoskeleton (the internal framework of a cell) composed of actin and associated proteins. Includes actin cytoskeleton-associated complexes.
    GO:0016324    apical plasma membrane    The region of the plasma membrane located at the apical end of the cell.
    GO:0009925    basal plasma membrane    The region of the plasma membrane located at the basal end of the cell. Often used in reference to animal polarized epithelial membranes, where the basal membrane is the part attached to the extracellular matrix, or in plant cells, where the basal membrane is defined with respect to the zygotic axis.
    GO:0030864    cortical actin cytoskeleton    The portion of the actin cytoskeleton, comprising filamentous actin and associated proteins, that lies just beneath the plasma membrane.
    GO:0005737    cytoplasm    All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
    GO:0009898    cytoplasmic side of plasma membrane    The leaflet the plasma membrane that faces the cytoplasm and any proteins embedded or anchored in it or attached to its surface.
    GO:0005856    cytoskeleton    Any of the various filamentous elements that form the internal framework of cells, and typically remain after treatment of the cells with mild detergent to remove membrane constituents and soluble components of the cytoplasm. The term embraces intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles.
    GO:0031941    filamentous actin    A two-stranded helical polymer of the protein actin.
    GO:0016460    myosin II complex    A myosin complex containing two class II myosin heavy chains, two myosin essential light chains and two myosin regulatory light chains. Also known as classical myosin or conventional myosin, the myosin II class includes the major muscle myosin of vertebrate and invertebrate muscle, and is characterized by alpha-helical coiled coil tails that self assemble to form a variety of filament structures.
    GO:0001725    stress fiber    A contractile actin filament bundle that consists of short actin filaments with alternating polarity, cross-linked by alpha-actinin and possibly other actin bundling proteins, and with myosin present in a periodic distribution along the fiber.

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    Ala A:21 - Pro A:22   [ RasMol ]  
 

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