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0LEPR_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionLeptin receptor precursor (lep-r) (ob receptor) (ob-r) (hub219).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0004888 transmembrane receptor activity (TAS)
0007166 cell surface receptor linked signal transdu... (TAS)
0007275 development (TAS)
0006112 energy reserve metabolism (TAS)

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Domain Architecture (Details)
InterPro domains unassigned to SynO:
This entry represents a ligand-binding domain that displays similarity to C2-set immunoglobulin domains (antibody constant domain 2) . The two cysteine residues form a disulphide bridge.
  IPR010457:Immunoglobulin C2-set-like, ligand-binding
Fibronectins are multi-domain glycoproteins found in a soluble form in plasma.nd in an insoluble form in loose connective tissue and basement membranes . They contain multiple copies of 3 repeat regions (types I.I and III).hich bind to a variety of substances including heparin.ollagen.NA.ctin.ibrin and fibronectin receptors on cell surfaces. The wide variety of these substances means that fibronectins are involved in a number of important functions: e.g..ound healing; cell adhesion; blood coagulation; cell differentiation and migration; maintenance of the cellular cytoskeleton; and tumour metastasis . The role of fibronectin in cell differentiation is demonstrated by the marked reduction in the expression of its gene when neoplastic transformation occurs. Cell attachment has been found to be mediated by the binding of the tetrapeptide RGDS to integrins on the cell surface .lthough related sequences can also display cell adhesion activity.Plasma fibronectin occurs as a dimer of 2 different subunits.inked together by 2 disulphide bonds near the C-terminus. The difference in the 2 chains occurs in the type III repeat region and is caused by alternative splicing of the mRNA from one gene . The observation that.n a given protein.n individual repeat of one of the 3 types (e.g..he first FnIII repeat) shows much less similarity to its subsequent tandem repeats within that protein than to its equivalent repeat between fibronectins from other suggested that the repeating structure of fibronectin arose at an early stage of evolution. It also seems to suggest that the structure is subject to high selective pressure .The fibronectin type III repeat region is an approximately 100 amino acid domain.ifferent tandem repeats of which contain binding sites for DNA.eparin and the cell surface . The superfamily of sequences believed to contain FnIII repeats represents 45 different families.he majority of which are involved in cell surface binding in some manner.r are receptor protein tyrosine kinases.r cytokine receptors.
  IPR003961:Fibronectin, type III
Fibronectin is composed of three repeating structural motifs.f which one is the FnIII module. The three modules form a linear sequence of multiple tandem copies connected by short linker peptides. The secondary structure of the FnIII10 module.hich is the only fibronectin module to possess an integrin binding RGD motif.onsists of two beta-sheets containing the antiparallel beta-strands ABE and DCFG.espectively.hich fold up to form a beta-sandwich. The RGD sequence is located in the loop connecting the beta-strands .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008957:Fibronectin, type III-like fold
This entry represents domains with an immunoglobulin-like (Ig-like) fold.hich consists of a beta-sandwich of seven or more strands in two sheets with a Greek-key topology. Ig-like domains are one of the most common protein modules found in animals.ccurring in a variety of different proteins. These domains are often involved in interactions.ommonly with other Ig-like domains via their beta-sheets . Domains within this fold-family share the same structure.ut can diverge with respect to their sequence. Based on sequence.g-like domains can be classified as V-set domains (antibody variable domain-like).1-set domains (antibody constant domain-like).2-set domains.nd I-set domains (antibody intermediate domain-like). Proteins can contain more than one of these types of Ig-like domains. For example.n the human T-cell receptor antigen CD2.omain 1 (D1) is a V-set domain.hile domain 2 (D2) is a C2-set domain.oth domains having the same Ig-like fold .Domains with an Ig-like fold can be found in many.iverse proteins in addition to immunoglobulin molecules. For example.g-like domains occur in several different types of receptors (such as various T-cell antigen receptors).everal cell adhesion molecules.HC class I and II antigens.s well as the hemolymph protein hemolin.nd the muscle proteins titin.elokin and twitchin.
  IPR013783:Immunoglobulin-like fold
SequencesProtein: LEPR_HUMAN (1165 aa)
mRNA: NM_002303
Local Annotation
Synapse Ontology
transport of vesicles in the presynaptic neuron
sdb:0017 Mobilization: synapsins, CAM kinase I  (Evidence:keywords)
sdb:0265 cAMP mediated STP  (Evidence:keywords)
KO assignmentK05062
  Level 3 annotation:
    leptin receptor
  Level 2 annotation:
    Adipocytokine signaling pathway
    Neuroactive ligand-receptor interaction
    Cytokine receptors
    Cytokine-cytokine receptor interaction
    CD molecules
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 36 residues, 65658905-65659011Exon2: 27 residues, 65663573-65663649Exon3: 22 residues, 65803816-65803876Exon4: 112 residues, 65808743-65809073Exon5: 43 residues, 65810596-65810720Exon6: 71 residues, 65830927-65831136Exon7: 50 residues, 65834718-65834864Exon8: 50 residues, 65836930-65837075Exon9: 99 residues, 65839662-65839953Exon10: 41 residues, 65840113-65840231Exon11: 68 residues, 65843308-65843508Exon12: 51 residues, 65847023-65847172Exon13: 55 residues, 65848217-65848377Exon14: 29 residues, 65848484-65848567Exon15: 74 residues, 65854278-65854495Exon16: 63 residues, 65856234-65856417Exon17: 34 residues, 65858198-65858294Exon18: 37 residues, 65859623-65859729Exon19: 27 residues, 65861176-65861252Exon20: 317 residues, 65874461-65875408Exon21: 2 residues, -Jump to LEPR_HUMAN  
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