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UniProtKB - P11214 (TPA_MOUSE)

Entry version 201 (23 Feb 2022)
Sequence version 3 (02 Oct 2007)
Previous versions | rss
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Protein

Tissue-type plasminogen activator

Gene

Plat

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Converts the abundant, but inactive, zymogen plasminogen to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By controlling plasmin-mediated proteolysis, it plays an important role in tissue remodeling and degradation, in cell migration and many other physiopathological events. During oocyte activation, plays a role in cortical granule reaction in the zona reaction, which contributes to the block to polyspermy (By similarity).

By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Specific cleavage of Arg-|-Val bond in plasminogen to form plasmin. EC:3.4.21.68

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by SERPINA5.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei99Important for binding to LRP1By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei355Charge relay system1
Active sitei404Charge relay system1
Sitei462Important for single-chain activityBy similarity1
Sitei509Important for single-chain activityBy similarity1
Active sitei510Charge relay system1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Protease, Serine protease
Biological processPlasminogen activation

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.4.21.68, 3474

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-186797, Signaling by PDGF
R-MMU-75205, Dissolution of Fibrin Clot

Protein family/group databases

MEROPS protease database

More...MEROPSi		S01.232

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Tissue-type plasminogen activator (EC:3.4.21.68)
Short name:
t-PA
Short name:
t-plasminogen activator
Short name:
tPA
Cleaved into the following 2 chains:
Tissue-type plasminogen activator chain A
Tissue-type plasminogen activator chain B
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Plat
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 8

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:97610, Plat

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSMUSG00000031538

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3259492

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 17Sequence analysisAdd BLAST17
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000002835318 – 29By similarityAdd BLAST12
PropeptideiPRO_000028590630 – 32Removed by plasmin1 Publication3
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000002835433 – 559Tissue-type plasminogen activatorAdd BLAST527
ChainiPRO_000002835533 – 308Tissue-type plasminogen activator chain AAdd BLAST276
ChainiPRO_0000028356309 – 559Tissue-type plasminogen activator chain BAdd BLAST251

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi38 ↔ 68By similarity
Disulfide bondi66 ↔ 75By similarity
Disulfide bondi83 ↔ 94By similarity
Disulfide bondi88 ↔ 105By similarity
Disulfide bondi107 ↔ 116By similarity
Disulfide bondi124 ↔ 205By similarity
Disulfide bondi145 ↔ 187By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi149N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi176 ↔ 200By similarity
Disulfide bondi213 ↔ 294By similarity
Disulfide bondi234 ↔ 276By similarity
Disulfide bondi265 ↔ 289By similarity
Disulfide bondi297 ↔ 428Interchain (between A and B chains)PROSITE-ProRule annotation
Disulfide bondi340 ↔ 356By similarity
Disulfide bondi348 ↔ 417By similarity
Disulfide bondi442 ↔ 516By similarity
Disulfide bondi474 ↔ 490By similarity
Glycosylationi481N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi506 ↔ 534By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The single chain, almost fully active enzyme, can be further processed into a two-chain fully active form by a cleavage after Arg-308 catalyzed by plasmin, tissue kallikrein or factor Xa.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P11214

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P11214

PeptideAtlas

More...PeptideAtlasi		P11214

PRoteomics IDEntifications database

More...PRIDEi		P11214

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		258819

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		P11214, 2 sites

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P11214

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P11214

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000031538, Expressed in primary oocyte and 307 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P11214, MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Heterodimer of chain A and chain B held by a disulfide bond. Binds to fibrin with high affinity. This interaction leads to an increase in the catalytic efficiency of the enzyme due to an increase in affinity for plasminogen. Similarly, binding to heparin increases the activation of plasminogen. Binds to annexin A2, cytokeratin-8, fibronectin and laminin. Binds to mannose receptor and the low-density lipoprotein receptor-related protein (LRP1); these proteins are involved in TPA clearance. Binds LRP1B; binding is followed by internalization and degradation. Forms heterodimer with SERPINA5 (By similarity). In complex with SERPINE1, interacts with SORL1 (By similarity).

By similarity

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		202229, 4 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-518, tPA-PAI-1 complex

Protein interaction database and analysis system

More...IntActi		P11214, 2 interactors

Molecular INTeraction database

More...MINTi		P11214

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000033941

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P11214

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P11214, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P11214

Database of comparative protein structure models

More...ModBasei		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini36 – 78Fibronectin type-IPROSITE-ProRule annotationAdd BLAST43
Domaini79 – 117EGF-likePROSITE-ProRule annotationAdd BLAST39
Domaini124 – 205Kringle 1PROSITE-ProRule annotationAdd BLAST82
Domaini213 – 294Kringle 2PROSITE-ProRule annotationAdd BLAST82
Domaini309 – 558Peptidase S1PROSITE-ProRule annotationAdd BLAST250

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni39 – 49Important for binding to annexin A2By similarityAdd BLAST11

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Both FN1 and one of the kringle domains are required for binding to fibrin.By similarity
Both FN1 and EGF-like domains are important for binding to LRP1.By similarity
The FN1 domain mediates binding to annexin A2.By similarity
The second kringle domain is implicated in binding to cytokeratin-8 and to the endothelial cell surface binding site.By similarity

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Kringle, Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3627, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000158930

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_006842_18_4_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P11214

Identification of Orthologs from Complete Genome Data

More...OMAi		TWEYCDI

Database of Orthologous Groups

More...OrthoDBi		1314811at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P11214

TreeFam database of animal gene trees

More...TreeFami		TF329901

Family and domain databases

Conserved Domains Database

More...CDDi		cd00061, FN1, 1 hit
cd00108, KR, 2 hits
cd00190, Tryp_SPc, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.40.10.10, 2 hits
2.40.20.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR000742, EGF-like_dom
IPR000083, Fibronectin_type1
IPR000001, Kringle
IPR013806, Kringle-like
IPR018056, Kringle_CS
IPR038178, Kringle_sf
IPR009003, Peptidase_S1_PA
IPR043504, Peptidase_S1_PA_chymotrypsin
IPR001314, Peptidase_S1A
IPR026280, Tissue_plasm_act
IPR034811, tPA
IPR001254, Trypsin_dom
IPR018114, TRYPSIN_HIS
IPR033116, TRYPSIN_SER

The PANTHER Classification System

More...PANTHERi		PTHR24264:SF42, PTHR24264:SF42, 3 hits

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00008, EGF, 1 hit
PF00039, fn1, 1 hit
PF00051, Kringle, 2 hits
PF00089, Trypsin, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF001145, Tissue_plasm_act, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00722, CHYMOTRYPSIN

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00181, EGF, 1 hit
SM00058, FN1, 1 hit
SM00130, KR, 2 hits
SM00020, Tryp_SPc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50494, SSF50494, 1 hit
SSF57440, SSF57440, 2 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00022, EGF_1, 1 hit
PS01186, EGF_2, 1 hit
PS50026, EGF_3, 1 hit
PS01253, FN1_1, 1 hit
PS51091, FN1_2, 1 hit
PS00021, KRINGLE_1, 2 hits
PS50070, KRINGLE_2, 2 hits
PS50240, TRYPSIN_DOM, 1 hit
PS00134, TRYPSIN_HIS, 1 hit
PS00135, TRYPSIN_SER, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P11214-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKRELLCVLL LCGLAFPLPD QGIHGRFRRG ARSYRATCRD EPTQTTYQQH 
        60         70         80         90        100
QSWLRPMLRS SRVEYCRCNS GLVQCHSVPV RSCSEPRCFN GGTCQQALYF 
       110        120        130        140        150
SDFVCQCPDG FVGKRCDIDT RATCFEEQGI TYRGTWSTAE SGAECINWNS 
       160        170        180        190        200
SVLSLKPYNA RRPNAIKLGL GNHNYCRNPD RDLKPWCYVF KAGKYTTEFC 
       210        220        230        240        250
STPACPKGKS EDCYVGKGVT YRGTHSLTTS QASCLPWNSI VLMGKSYTAW 
       260        270        280        290        300
RTNSQALGLG RHNYCRNPDG DARPWCHVMK DRKLTWEYCD MSPCSTCGLR 
       310        320        330        340        350
QYKRPQFRIK GGLYTDITSH PWQAAIFVKN KRSPGERFLC GGVLISSCWV 
       360        370        380        390        400
LSAAHCFLER FPPNHLKVVL GRTYRVVPGE EEQTFEIEKY IVHEEFDDDT 
       410        420        430        440        450
YDNDIALLQL RSQSKQCAQE SSSVGTACLP DPNLQLPDWT ECELSGYGKH 
       460        470        480        490        500
EASSPFFSDR LKEAHVRLYP SSRCTSQHLF NKTVTNNMLC AGDTRSGGNQ 
       510        520        530        540        550
DLHDACQGDS GGPLVCMINK QMTLTGIISW GLGCGQKDVP GVYTKVTNYL 

DWIHDNMKQ
Length:559
Mass (Da):63,097
Last modified:October 2, 2007 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i0A158A5A273CFAA0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti260G → A in AAA40470 (PubMed:2826484).Curated1
Sequence conflicti325A → P in AAH11256 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
J03520 mRNA Translation: AAA40470.1
AK135857 mRNA Translation: BAE22698.1
AK135965 mRNA Translation: BAE22749.1
BC011256 mRNA Translation: AAH11256.1
BC057967 mRNA Translation: AAH57967.1
BC061508 mRNA Translation: AAH61508.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS22183.1

Protein sequence database of the Protein Information Resource

More...PIRi		A29941

NCBI Reference Sequences

More...RefSeqi		NP_032898.2, NM_008872.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000033941; ENSMUSP00000033941; ENSMUSG00000031538

Database of genes from NCBI RefSeq genomes

More...GeneIDi		18791

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:18791

UCSC genome browser

More...UCSCi		uc009ldx.2, mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03520 mRNA Translation: AAA40470.1
AK135857 mRNA Translation: BAE22698.1
AK135965 mRNA Translation: BAE22749.1
BC011256 mRNA Translation: AAH11256.1
BC057967 mRNA Translation: AAH57967.1
BC061508 mRNA Translation: AAH61508.1
CCDSiCCDS22183.1
PIRiA29941
RefSeqiNP_032898.2, NM_008872.3

3D structure databases

SMRiP11214
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi202229, 4 interactors
ComplexPortaliCPX-518, tPA-PAI-1 complex
IntActiP11214, 2 interactors
MINTiP11214
STRINGi10090.ENSMUSP00000033941

Chemistry databases

BindingDBiP11214
ChEMBLiCHEMBL3259492

Protein family/group databases

MEROPSiS01.232

PTM databases

GlyGeniP11214, 2 sites
iPTMnetiP11214
PhosphoSitePlusiP11214

Proteomic databases

MaxQBiP11214
PaxDbiP11214
PeptideAtlasiP11214
PRIDEiP11214
ProteomicsDBi258819

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...ABCDi		P11214, 5 sequenced antibodies

Antibodypedia a portal for validated antibodies

More...Antibodypediai		998, 801 antibodies from 39 providers

The DNASU plasmid repository

More...DNASUi		18791

Genome annotation databases

EnsembliENSMUST00000033941; ENSMUSP00000033941; ENSMUSG00000031538
GeneIDi18791
KEGGimmu:18791
UCSCiuc009ldx.2, mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5327
MGIiMGI:97610, Plat
VEuPathDBiHostDB:ENSMUSG00000031538

Phylogenomic databases

eggNOGiKOG3627, Eukaryota
GeneTreeiENSGT00940000158930
HOGENOMiCLU_006842_18_4_1
InParanoidiP11214
OMAiTWEYCDI
OrthoDBi1314811at2759
PhylomeDBiP11214
TreeFamiTF329901

Enzyme and pathway databases

BRENDAi3.4.21.68, 3474
ReactomeiR-MMU-186797, Signaling by PDGF
R-MMU-75205, Dissolution of Fibrin Clot

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		18791, 1 hit in 64 CRISPR screens

Protein Ontology

More...PROi		PR:P11214
RNActiP11214, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000031538, Expressed in primary oocyte and 307 other tissues
GenevisibleiP11214, MM

Family and domain databases

CDDicd00061, FN1, 1 hit
cd00108, KR, 2 hits
cd00190, Tryp_SPc, 1 hit
Gene3Di2.40.10.10, 2 hits
2.40.20.10, 2 hits
InterProiView protein in InterPro
IPR000742, EGF-like_dom
IPR000083, Fibronectin_type1
IPR000001, Kringle
IPR013806, Kringle-like
IPR018056, Kringle_CS
IPR038178, Kringle_sf
IPR009003, Peptidase_S1_PA
IPR043504, Peptidase_S1_PA_chymotrypsin
IPR001314, Peptidase_S1A
IPR026280, Tissue_plasm_act
IPR034811, tPA
IPR001254, Trypsin_dom
IPR018114, TRYPSIN_HIS
IPR033116, TRYPSIN_SER
PANTHERiPTHR24264:SF42, PTHR24264:SF42, 3 hits
PfamiView protein in Pfam
PF00008, EGF, 1 hit
PF00039, fn1, 1 hit
PF00051, Kringle, 2 hits
PF00089, Trypsin, 1 hit
PIRSFiPIRSF001145, Tissue_plasm_act, 1 hit
PRINTSiPR00722, CHYMOTRYPSIN
SMARTiView protein in SMART
SM00181, EGF, 1 hit
SM00058, FN1, 1 hit
SM00130, KR, 2 hits
SM00020, Tryp_SPc, 1 hit
SUPFAMiSSF50494, SSF50494, 1 hit
SSF57440, SSF57440, 2 hits
PROSITEiView protein in PROSITE
PS00022, EGF_1, 1 hit
PS01186, EGF_2, 1 hit
PS50026, EGF_3, 1 hit
PS01253, FN1_1, 1 hit
PS51091, FN1_2, 1 hit
PS00021, KRINGLE_1, 2 hits
PS50070, KRINGLE_2, 2 hits
PS50240, TRYPSIN_DOM, 1 hit
PS00134, TRYPSIN_HIS, 1 hit
PS00135, TRYPSIN_SER, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTPA_MOUSE
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P11214
Secondary accession number(s): Q6P7U0, Q91VP2
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 2, 2007
Last modified: February 23, 2022
This is version 201 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families
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