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0TMPS5_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameTMPRSS5
DescriptionTransmembrane protease, serine 5 (ec 3.4.21.-) (spinesin).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Proteolytic enzymes that exploit serine in their catalytic activity areubiquitous.eing found in viruses.acteria and eukaryotes . Theyinclude a wide range of peptidase activity.ncluding exopeptidase.ndopeptidase.ligopeptidase and omega-peptidase activity. Over 20 families(denoted S1 - S27) of serine protease have been identified.hese beinggrouped into 6 clans (SA.B.C.E.F and SG) on the basis of structuralsimilarity and other functional evidence . Structures are known for fourof the clans (SA.B.C and SE): these appear to be totally unrelated.uggesting at least four evolutionary origins of serine peptidases andpossibly many more .Notwithstanding their different evolutionary origins.here are similaritiesin the reaction mechanisms of several peptidases. Chymotrypsin.ubtilisinand carboxypeptidase C clans have a catalytic triad of serine.spartate andhistidine in common: serine acts as a nucleophile.spartate as anelectrophile.nd histidine as a base . The geometric orientations ofthe catalytic residues are similar between families.espite differentprotein folds . The linear arrangements of the catalytic residuescommonly reflect clan relationships. For example the catalytic triad inthe chymotrypsin clan (SA) is ordered HDS.ut is ordered DHS in thesubtilisin clan (SB) and SDH in the carboxypeptidase clan (SC) .Peptidases are grouped into clans and families. Clans are groups of families for which there is evidence of common ancestry. Families are grouped by their catalytic type.he first character representing the catalytic type: A.spartic; C.ysteine; G.lutamic acid; M.etallo; S.erine; T.hreonine; and U.nknown. A clan that contains families of more than one type is described as being of type P. The serine.hreonine and cysteine peptidases utilise the catalytic part of an amino acid as a nucleophile and form an acyl intermediate - these peptidases can also readily act as transferases. In the case of aspartic.lutamic and metallopeptidases.he nucleophile is an activated water molecule. This group of serine proteases belong to the MEROPS peptidase family S1 (chymotrypsin family.lan PA(S))and to peptidase family S6 (Hap serine peptidases).The chymotrypsin family is almost totally confined to animals.lthough trypsin-like enzymes are found in actinomycetes of the genera Streptomyces and Saccharopolyspora.nd in the fungus Fusarium oxysporum . The enzymes are inherently secreted.eing synthesised with a signal peptide thattargets them to the secretory pathway. Animal enzymes are either secreteddirectly.ackaged into vesicles for regulated secretion.r are retainedin leukocyte granules .The Hap family.aemophilus adhesion and penetration.re proteins that play a role in the interaction with human epithelial cells. The serine protease activity is localized at the N-terminal domain.hereas the binding domain is in the C-terminal region.
  IPR001254:Peptidase S1 and S6, chymotrypsin/Hap
The egg peptide speract receptor is a transmembrane glycoprotein . Other members of this family include the macrophagescavenger receptor type I (a membrane glycoprotein implicated in the pathologicdeposition of cholesterol in arterial walls during artherogenesis).n enteropeptidaseand T-cell surface glycoprotein CD5 (may act as a receptor in regulating T-cellproliferation).
  IPR001190:Speract/scavenger receptor
Proteolytic enzymes that exploit serine in their catalytic activity areubiquitous.eing found in viruses.acteria and eukaryotes . Theyinclude a wide range of peptidase activity.ncluding exopeptidase.ndopeptidase.ligopeptidase and omega-peptidase activity. Over 20 families(denoted S1 - S27) of serine protease have been identified.hese beinggrouped into 6 clans (SA.B.C.E.F and SG) on the basis of structuralsimilarity and other functional evidence . Structures are known for fourof the clans (SA.B.C and SE): these appear to be totally unrelated.uggesting at least four evolutionary origins of serine peptidases andpossibly many more .Notwithstanding their different evolutionary origins.here are similaritiesin the reaction mechanisms of several peptidases. Chymotrypsin.ubtilisinand carboxypeptidase C clans have a catalytic triad of serine.spartate andhistidine in common: serine acts as a nucleophile.spartate as anelectrophile.nd histidine as a base . The geometric orientations ofthe catalytic residues are similar between families.espite differentprotein folds . The linear arrangements of the catalytic residuescommonly reflect clan relationships. For example the catalytic triad inthe chymotrypsin clan (SA) is ordered HDS.ut is ordered DHS in thesubtilisin clan (SB) and SDH in the carboxypeptidase clan (SC) .Peptidases are grouped into clans and families. Clans are groups of families for which there is evidence of common ancestry. Families are grouped by their catalytic type.he first character representing the catalytic type: A.spartic; C.ysteine; G.lutamic acid; M.etallo; S.erine; T.hreonine; and U.nknown. A clan that contains families of more than one type is described as being of type P. The serine.hreonine and cysteine peptidases utilise the catalytic part of an amino acid as a nucleophile and form an acyl intermediate - these peptidases can also readily act as transferases. In the case of aspartic.lutamic and metallopeptidases.he nucleophile is an activated water molecule. This group of serine peptidases and non-peptidase homologs belong to the MEROPS peptidase family S1.ubfamily S1A (chymotrypsin subfamily.lan PA(S)). The type example being chymotrypsin A from Bos taurus. Members of the chymotrypsin family may occasionally function intracellularly (for example.he intracellular digestion of bacteria in neutrophils).ut most function extracellularly.or example in roles such as food digestion.ibrinolysis and complement activation . The essential catalytic unit of the chymotrypsin family is around 220 amino acids in length.lthough the protein may be extended at the N-terminus with unrelated sequences.ften containing modules. They are rarely extended at the C-terminus: exceptions include acrosin.omplement component C2.nd coagulation factor X.hich has a 16 residue extension that is removed upon activation .
  IPR001314:Peptidase S1A, chymotrypsin
Proteolytic enzymes that exploit serine in their catalytic activity areubiquitous.eing found in viruses.acteria and eukaryotes . Theyinclude a wide range of peptidase activity.ncluding exopeptidase.ndopeptidase.ligopeptidase and omega-peptidase activity. Over 20 families(denoted S1 - S27) of serine protease have been identified.hese beinggrouped into 6 clans (SA.B.C.E.F and SG) on the basis of structuralsimilarity and other functional evidence . Structures are known for fourof the clans (SA.B.C and SE): these appear to be totally unrelated.uggesting at least four evolutionary origins of serine peptidases andpossibly many more .Notwithstanding their different evolutionary origins.here are similaritiesin the reaction mechanisms of several peptidases. Chymotrypsin.ubtilisinand carboxypeptidase C clans have a catalytic triad of serine.spartate andhistidine in common: serine acts as a nucleophile.spartate as anelectrophile.nd histidine as a base . The geometric orientations ofthe catalytic residues are similar between families.espite differentprotein folds . The linear arrangements of the catalytic residuescommonly reflect clan relationships. For example the catalytic triad inthe chymotrypsin clan (SA) is ordered HDS.ut is ordered DHS in thesubtilisin clan (SB) and SDH in the carboxypeptidase clan (SC) .Peptidases are grouped into clans and families. Clans are groups of families for which there is evidence of common ancestry. Families are grouped by their catalytic type.he first character representing the catalytic type: A.spartic; C.ysteine; G.lutamic acid; M.etallo; S.erine; T.hreonine; and U.nknown. A clan that contains families of more than one type is described as being of type P. The serine.hreonine and cysteine peptidases utilise the catalytic part of an amino acid as a nucleophile and form an acyl intermediate - these peptidases can also readily act as transferases. In the case of aspartic.lutamic and metallopeptidases.he nucleophile is an activated water molecule. Cysteine peptidases have characteristic molecular topologies.hich can be seen not only in their three-dimensional structures.ut commonly also in the two-dimensional structures. The peptidase domain is responsible for peptide bond hydrolysis; in Merops this is termed the peptidase unit. These are peptidases in which the nucleophile is the sulphydryl group of a cysteine residue. Cysteine proteases are divided into clans (proteins which are evolutionary related).nd further sub-divided into families.n the basis of the architecture of their catalytic dyad or triad : Clan CA contains the families of papain (C1).alpain (C2).treptopain (C10) and the ubiquitin-specific peptidases (C12.19).s well as many families of viral cysteine endopeptidases. Clan CD contains the families of clostripain (C11).ingipain R (C25).egumain (C13).aspase-1 (C14) and separin (C50). These enzymes have specificities dominated by the interactions of the S1 subsite. Clan CE contains the families of adenain (C5) from adenoviruses.he eukaryotic Ulp1 protease (C48) and the bacterial YopJ proteases (C55). Clan CF contains only pyroglutamyl peptidase I (C15). Clan PA contains the picornains (C3).hich have probably evolved from serine peptidases and which form the majority of enzymes in this clan. Clans PB and CH contain the autolytic cysteine peptidases. This signature recognises a large group of serine and cysteine peptidases which share a common closed beta barrel structure. The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR009003:Peptidase, trypsin-like serine and cysteine
IPR001254:Tryp_SPc 
Evalue:-92 
Location:217-448IPR001190:Srcr_receptor 
Evalue:0 
Location:107-214IPR001190:SRCR_2 
Evalue:0 
Location:0-0
SequencesProtein: TMPS5_HUMAN (457 aa)
mRNA: NM_030770
Local Annotation
Synapse Ontology
introduce the substructure of the synapse and the location where the molecule can be seen. It will contain all the constructive special organelle and molecule we known.
sdb:0001 Structure/Biochemistry of synapse  (Evidence:keywords)
KO assignmentK01362
  Level 3 annotation:
    
  Level 2 annotation:
    Other amino acid metabolism
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 242 residues, 113063482-113064206Exon2: 53 residues, 113065696-113065849Exon3: 49 residues, 113066162-113066305Exon4: 35 residues, 113066772-113066871Exon5: 61 residues, 113069002-113069181Exon6: 56 residues, 113070409-113070572Exon7: 16 residues, 113071331-113071375Exon8: 40 residues, 113072789-113072903Exon9: 47 residues, 113073214-113073350Exon10: 43 residues, 113074836-113074959Exon11: 35 residues, 113075526-113075625Exon12: 36 residues, 113075997-113076100Exon13: 52 residues, 113082153-113082305Exon14: 2 residues, -Jump to TMPS5_HUMAN  
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Loci Cluster (Details)Loci: 3992 113063482-113082305 ~-19K 7767(TMPRSS5)(-)Loci: 3993 113109120-113149635 ~-41K 7769(ZW10)(-)Loci: 2706 113280798-113322492 ~-42K 7774(+)Loci: 2707 113351119-113366242 ~-15K 7775(HTR3A)(+)Loci: 2708 113435640-113626604 ~-191K 7782(ZBTB16)(+)Loci: 3991 112785527-112851091 ~-66K 7762(DRD2)(-)Link out to UCSC