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Protein

Myeloblastin

Gene

Prtn3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Serine protease that degrades elastin, fibronectin, laminin, vitronectin, and collagen types I, III, and IV (in vitro). By cleaving and activating receptor F2RL1/PAR-2, enhances endothelial cell barrier function and thus vascular integrity during neutrophil transendothelial migration. May play a role in neutrophil transendothelial migration, probably when associated with CD177.By similarity

Catalytic activityi

Hydrolysis of proteins, including elastin, by preferential cleavage: -Ala-|-Xaa- > -Val-|-Xaa-.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei73Charge relay systemPROSITE-ProRule annotation1
Active sitei120Charge relay systemPROSITE-ProRule annotation1
Active sitei205Charge relay systemPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Protease, Serine protease
Biological processCollagen degradation

Enzyme and pathway databases

BRENDAi3.4.21.76 3474

Protein family/group databases

MEROPSiS01.134

Names & Taxonomyi

Protein namesi
Recommended name:
Myeloblastin (EC:3.4.21.76)
Alternative name(s):
Proteinase 3
Short name:
PR-3
Gene namesi
Name:Prtn3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:893580 Prtn3

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Lysosome, Membrane, Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL5384

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27By similarityAdd BLAST27
PropeptideiPRO_000002771028 – 29By similarity2
ChainiPRO_000002771130 – 250MyeloblastinAdd BLAST221
PropeptideiPRO_0000027712251 – 254By similarity4

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi58 ↔ 74PROSITE-ProRule annotation
Glycosylationi127N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi154 ↔ 211PROSITE-ProRule annotation
Glycosylationi176N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi184 ↔ 190PROSITE-ProRule annotation
Disulfide bondi201 ↔ 226PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiQ61096
PaxDbiQ61096
PeptideAtlasiQ61096
PRIDEiQ61096

Expressioni

Gene expression databases

CleanExiMM_PRTN3

Interactioni

Subunit structurei

May form dimers. Interacts with CD177; the interaction tethers PRTN3 to the cell surface; the interaction is direct.By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ61096, 1 interactor
MINTiQ61096
STRINGi10090.ENSMUSP00000006679

Chemistry databases

BindingDBiQ61096

Structurei

3D structure databases

ProteinModelPortaliQ61096
SMRiQ61096
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini30 – 250Peptidase S1PROSITE-ProRule annotationAdd BLAST221

Sequence similaritiesi

Belongs to the peptidase S1 family. Elastase subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3627 Eukaryota
COG5640 LUCA
HOGENOMiHOG000251820
HOVERGENiHBG013304
InParanoidiQ61096
KOiK01350
PhylomeDBiQ61096
TreeFamiTF335284

Family and domain databases

CDDicd00190 Tryp_SPc, 1 hit
InterProiView protein in InterPro
IPR009003 Peptidase_S1_PA
IPR001314 Peptidase_S1A
IPR001254 Trypsin_dom
IPR018114 TRYPSIN_HIS
IPR033116 TRYPSIN_SER
PfamiView protein in Pfam
PF00089 Trypsin, 1 hit
PRINTSiPR00722 CHYMOTRYPSIN
SMARTiView protein in SMART
SM00020 Tryp_SPc, 1 hit
SUPFAMiSSF50494 SSF50494, 1 hit
PROSITEiView protein in PROSITE
PS50240 TRYPSIN_DOM, 1 hit
PS00134 TRYPSIN_HIS, 1 hit
PS00135 TRYPSIN_SER, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q61096-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGSYPSPKG IHPFLLLALV VGGAVQASKI VGGHEARPHS RPYVASLQLS
60 70 80 90 100
RFPGSHFCGG TLIHPRFVLT AAHCLQDISW QLVTVVLGAH DLLSSEPEQQ
110 120 130 140 150
KFTISQVFQN NYNPEENLND VLLLQLNRTA SLGKEVAVAS LPQQDQTLSQ
160 170 180 190 200
GTQCLAMGWG RLGTQAPTPR VLQELNVTVV TFLCREHNVC TLVPRRAAGI
210 220 230 240 250
CFGDSGGPLI CNGILHGVDS FVIRECASLQ FPDFFARVSM YVDWIQNVLR

GAEP
Length:254
Mass (Da):27,626
Last modified:August 1, 1999 - v2
Checksum:i00CEB989A3CB79CA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti2S → A in AAB58055 (PubMed:9187364).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF082186 Genomic DNA Translation: AAC79701.1
U97073 mRNA Translation: AAB58055.1
U43525 mRNA Translation: AAB67271.1
CCDSiCCDS23993.1
RefSeqiNP_035308.2, NM_011178.2
UniGeneiMm.2364

Genome annotation databases

GeneIDi19152
KEGGimmu:19152
UCSCiuc007gah.1 mouse

Similar proteinsi

Entry informationi

Entry nameiPRTN3_MOUSE
AccessioniPrimary (citable) accession number: Q61096
Secondary accession number(s): O08809
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: August 1, 1999
Last modified: February 28, 2018
This is version 131 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health