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0MAMC1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameMAMDC1
DescriptionMam domain containing protein 1 precursor (mam domain-containing glycosylphosphatidylinositol anchor protein 2).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
Domain Architecture (Details)
InterPro domains unassigned to SynO:
A 170 amino acid domain.he so-called MAM domain.as been recognised in the extracellular region of functionally diverse proteins . These proteins have a modular.eceptor-like architecture comprising a signal peptide.n N-terminal extracellular domain. single transmembrane domain and an intracellular domain. Such proteins include meprin (a cell surface glycoprotein) ; A5 antigen (a developmentally-regulated cell surface protein) ; and receptor-like tyrosine protein phosphatase . The MAM domain is thought to have an adhesive function. It contains 4 conserved cysteine residues.hich probably form disulphide bridges.
  IPR000998:MAM
The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda.ach composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains: alpha.elta.psilon.amma and mu.ll consisting of a variable domain (VH) and three (in alpha.elta and gamma) or four (in epsilon and mu) constant domains (CH1 to CH4). Ig molecules are highly modular proteins.n which the variable and constant domains have clear.onserved sequence patterns. The domains in Ig and Ig-like molecules are grouped into four types: V-set (variable; ).1-set (constant-1; ).2-set (constant-2; ) and I-set (intermediate; ) . Structural studies have shown that these domains share a common core Greek-key beta-sandwich structure.ith the types differing in the number of strands in the beta-sheets as well as in their sequence patterns .Immunoglobulin-like domains that are related in both sequence and structure can be found in several diverse protein families. Ig-like domains are involved in a variety of functions.ncluding cell-cell recognition.ell-surface receptors.uscle structure and the immune system . This entry represents a subtype of the immunoglobulin domain.nd is found in a diverse range of protein families that includes glycoproteins.ibroblast growth factor receptors.ascular endothelial growth factor receptors.nterleukin-6 receptor.nd neural cell adhesion molecules. It also includes proteins that are classified as unassigned proteinase inhibitors belonging to MEROPS inhibitor families I2.17 and I43 .
  IPR003598:Immunoglobulin subtype 2
This entry is for immunoglobulin-like domains. Studies indicate that the interactions essential for defining the structure of these beta sandwich proteins are also important in nucleation of folding.nd that proteins containing this fold may share similar folding pathways even though the proteins may have low sequence homology. The fold consists of a beta-sandwich formed of 7 strands in 2 sheets with a Greek-key topology. Some members of the fold have additional strands. The Pfam alignments do not include the first and last strand of the immunoglobulin-like domain.
  IPR013151:Immunoglobulin
The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda.ach composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains: alpha.elta.psilon.amma and mu.ll consisting of a variable domain (VH) and three (in alpha.elta and gamma) or four (in epsilon and mu) constant domains (CH1 to CH4). Ig molecules are highly modular proteins.n which the variable and constant domains have clear.onserved sequence patterns. The domains in Ig and Ig-like molecules are grouped into four types: V-set (variable; ).1-set (constant-1; ).2-set (constant-2; ) and I-set (intermediate; ) . Structural studies have shown that these domains share a common core Greek-key beta-sandwich structure.ith the types differing in the number of strands in the beta-sheets as well as in their sequence patterns .Immunoglobulin-like domains that are related in both sequence and structure can be found in several diverse protein families. Ig-like domains are involved in a variety of functions.ncluding cell-cell recognition.ell-surface receptors.uscle structure and the immune system . This entry represents I-set domains.hich are found in several cell adhesion molecules.ncluding vascular (VCAM).ntercellular (ICAM).eural (NCAM) and mucosal addressin (MADCAM) cell adhesion molecules.s well as junction adhesion molecules (JAM). I-set domains are also present in several other diverse protein families.ncluding several tyrosine-protein kinase receptors.he hemolymph protein hemolin.he muscle proteins titin.elokin.nd twitchin.he neuronal adhesion molecule axonin-1 .nd the signalling molecule semaphorin 4D that is involved in axonal guidance.mmune function and angiogenesis .
  IPR013098:Immunoglobulin I-set
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
The basic structure of immunoglobulin (Ig) molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda.ach composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains: alpha.elta.psilon.amma and mu.ll consisting of a variable domain (VH) and three (in alpha.elta and gamma) or four (in epsilon and mu) constant domains (CH1 to CH4). Ig molecules are highly modular proteins.n which the variable and constant domains have clear.onserved sequence patterns. The domains in Ig and Ig-like molecules are grouped into four types: V-set (variable; ).1-set (constant-1; ).2-set (constant-2; ) and I-set (intermediate; ) . Structural studies have shown that these domains share a common core Greek-key beta-sandwich structure.ith the types differing in the number of strands in the beta-sheets as well as in their sequence patterns .Immunoglobulin-like domains that are related in both sequence and structure can be found in several diverse protein families. Ig-like domains are involved in a variety of functions.ncluding cell-cell recognition.ell-surface receptors.uscle structure and the immune system . This subfamily includes:Cell surface receptors containing an immunoglobin domain.Killer cell inhibitory receptors.Oprin a snake venom metalloproteinase inhibitor from Didelphis marsupialis (Southern opossum) .hich belongs to MEROPS inhibitor family I43.lan I- .Oprin homologues.
  IPR003599:Immunoglobulin subtype
IPR000998:MAM 
Evalue:-72.3279037475586 
Location:748-921IPR003598:IGc2 
Evalue:-14.8860566476932 
Location:53-117IPR003598:IGc2 
Evalue:-13.9208187539524 
Location:255-317IPR003598:IGc2 
Evalue:-10.7958800173441 
Location:456-522IPR013151:ig 
Evalue:-7.88605642318726 
Location:352-419IPR013151:ig 
Evalue:-4.85387182235718 
Location:152-218IPR008957:FN_III-like 
Evalue:0 
Location:641-741IPR013783:Ig-like_fold 
Evalue:0 
Location:540-627IPR000998:MAM_1 
Evalue:0 
Location:0-0
SequencesProtein: MAMC1_HUMAN (956 aa)
mRNA: AY369208
Local Annotation
Synapse Ontology
Typical ecretory organelles, some 50 nm in diameter, of presynaptic nerve terminals; accumulate high concentrations of nonpeptide neurotransmitters and secrete these into the synaptic cleft by fusion with the 'active zone' of the presynaptic plasma membrane.
sdb:0094 typical synaptic vesicle  (Evidence:keywords)
Various stages of the synaptic vesicle cycle, including attachment, prefusion, triggering, recycling and reloading of the vesicles with transmitter.
sdb:0098 synaptic vesicle cycling  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 236 residues, 46380267-46380972Exon2: 37 residues, 46384718-46384824Exon3: 45 residues, 46393976-46394107Exon4: 55 residues, 46412385-46412544Exon5: 54 residues, 46412997-46413153Exon6: 9 residues, 46416441-46416462Exon7: 61 residues, 46420996-46421174Exon8: 51 residues, 46458964-46459113Exon9: 92 residues, 46496326-46496596Exon10: 100 residues, 46573963-46574257Exon11: 112 residues, 46600201-46600531Exon12: 92 residues, 46635806-46636076Exon13: 46 residues, 46670666-46670799Exon14: 67 residues, 46683030-46683227Exon15: 60 residues, 46756973-46757148Exon16: 48 residues, 46840363-46840503Exon17: 80 residues, 47213469-47213703Exon18: 2 residues, -Jump to MAMC1_HUMAN