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P27435

- TRYB1_RAT

UniProt

P27435 - TRYB1_RAT

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Protein
Tryptase
Gene
Tpsab1, Mcp7, Mcpt7, Tpsb1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type.

Catalytic activityi

Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa, but with more restricted specificity than trypsin.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei72 – 721Charge relay system By similarity
Active sitei119 – 1191Charge relay system By similarity
Active sitei222 – 2221Charge relay system By similarity

GO - Molecular functioni

  1. serine-type endopeptidase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Protein family/group databases

MEROPSiS01.026.

Names & Taxonomyi

Protein namesi
Recommended name:
Tryptase (EC:3.4.21.59)
Alternative name(s):
Mast cell protease 7
Short name:
rMCP-7
Tryptase alpha/beta-1
Tryptase, skin
Gene namesi
Name:Tpsab1
Synonyms:Mcp7, Mcpt7, Tpsb1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi3066. Tpsab1.

Subcellular locationi

Secreted
Note: Released from the secretory granules upon mast cell activation.

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818 Reviewed prediction
Add
BLAST
Propeptidei19 – 2810Activation peptide
PRO_0000027496
Chaini29 – 273245Tryptase
PRO_0000027497Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi49 – 491N-linked (GlcNAc...) Inferred
Disulfide bondi57 ↔ 73 By similarity
Disulfide bondi153 ↔ 228 By similarity
Disulfide bondi186 ↔ 209 By similarity
Disulfide bondi218 ↔ 246 By similarity

Post-translational modificationi

Glycosylated Inferred.

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP27435.
PRIDEiP27435.

Expressioni

Tissue specificityi

Mast cells.

Gene expression databases

GenevestigatoriP27435.

Interactioni

Subunit structurei

Homotetramer.

Structurei

3D structure databases

ProteinModelPortaliP27435.
SMRiP27435. Positions 29-271.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 270242Peptidase S1
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5640.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiP27435.
KOiK01340.
PhylomeDBiP27435.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P27435-1 [UniParc]FASTAAdd to Basket

« Hide

MLKLLLLTLP LLSSLVHAAP SLAMPREGIV GGQEASGNKW PWQVSLRVND    50
TYWMHFCGGS LIHPQWVLTA AHCVGPNKAD PNKLRVQLRK QYLYYHDHLL 100
TVSQIISHPD FYIAQDGADI ALLKLTNPVN ITSNVHTVSL PPASETFPSG 150
TLCWVTGWGN INNDVSLPPP FPLEEVQVPI VENRLCDLKY HKGLNTGDNV 200
HIVRDDMLCA GNEGHDSCQG DSGGPLVCKV EDTWLQAGVV SWGEGCAQPN 250
RPGIYTRVTY YLDWIYRYVP KYF 273
Length:273
Mass (Da):30,400
Last modified:November 1, 1997 - v2
Checksum:i65A5ED4D279FB284
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti42 – 421W → V AA sequence 1 Publication
Sequence conflicti49 – 513NDT → WLP AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U67910 mRNA. Translation: AAB48263.1.
PIRiA23698.
S21275.
RefSeqiNP_062195.2. NM_019322.2.
UniGeneiRn.10699.

Genome annotation databases

GeneIDi54271.
KEGGirno:54271.
UCSCiRGD:3066. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U67910 mRNA. Translation: AAB48263.1 .
PIRi A23698.
S21275.
RefSeqi NP_062195.2. NM_019322.2.
UniGenei Rn.10699.

3D structure databases

ProteinModelPortali P27435.
SMRi P27435. Positions 29-271.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P27435.
ChEMBLi CHEMBL3320.

Protein family/group databases

MEROPSi S01.026.

Proteomic databases

PaxDbi P27435.
PRIDEi P27435.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 54271.
KEGGi rno:54271.
UCSCi RGD:3066. rat.

Organism-specific databases

CTDi 7177.
RGDi 3066. Tpsab1.

Phylogenomic databases

eggNOGi COG5640.
HOGENOMi HOG000251820.
HOVERGENi HBG013304.
InParanoidi P27435.
KOi K01340.
PhylomeDBi P27435.

Miscellaneous databases

NextBioi 610832.

Gene expression databases

Genevestigatori P27435.

Family and domain databases

InterProi IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF00089. Trypsin. 1 hit.
[Graphical view ]
PRINTSi PR00722. CHYMOTRYPSIN.
SMARTi SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
PROSITEi PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Secretory granule proteases in rat mast cells. Cloning of 10 different serine proteases and a carboxypeptidase A from various rat mast cell populations."
    Lutzelschwab C., Pejler G., Aveskogh M., Hellman L.
    J. Exp. Med. 185:13-29(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
  2. "Tryptase from rat skin: purification and properties."
    Braganza V.J., Simmons W.H.
    Biochemistry 30:4997-5007(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 29-53.
    Strain: Sprague-Dawley.
    Tissue: Skin.
  3. "Separation, purification and N-terminal sequence analysis of a novel leupeptin-sensitive serine endopeptidase present in chemically induced rat mammary tumour."
    Eto I., Grubbs C.J.
    Biochem. J. 283:209-216(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 29-51.
    Tissue: Mammary carcinoma.

Entry informationi

Entry nameiTRYB1_RAT
AccessioniPrimary (citable) accession number: P27435
Secondary accession number(s): P27436
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: November 1, 1997
Last modified: May 14, 2014
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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