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Entry version 124 (18 Sep 2019)
Sequence version 1 (01 Feb 1997)
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Protein

Internalin C

Gene

inlC

Organism
Listeria monocytogenes serotype 1/2a (strain EGD / Mackaness)
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

A virulence enhancer that has at least 2 dissociable functions in infection; it impairs translocation of host transcription factor NF-kappa-B to the nucleus and antagonizes the function of the Tuba dynamin-binding protein, promoting bacterial spreading (PubMed:20855622, PubMed:19767742, PubMed:24332715). Perturbs the morphology of host cell junctions by impairing host DNMBP (Tuba) and WASL interaction, altering cortical tension at the cell junctions and allowing bacteria to more efficiently form bacteria-filled cell protrusions which promote bacterial spreading within infected host tissue (PubMed:19767742, PubMed:24332715). Down-regulates the host inflammation response usually induced by Listeria infection. Interacts with host I-kappa-B kinase alpha (IKKA, CHUK), which prevents IKKA from phosphorylating NF-kappa-B inhibitor alpha (IKBA, NFKBIA) and thus delays degradation of phospho-IKBA. Translocation of host transcription factor p65 (a subunit of NF-kappa-B, RELA) into the nucleus is impaired, which prevents activation of NF-KB-regulated genes (PubMed:20855622). Recognized by serum from healthy humans exposed to L.monocytogenes as well from patients who have recovered from listeriosis (PubMed:9284184).4 Publications

Miscellaneous

In infected host cells Listeria surface protein ActA induces formation of F-actin 'comet tails' that propel bacteria. Motile bacteria ultimately encounter the host plasma membrane, deforming it into protrusions. Finally, pathogen-containing protrusions are engulfed by adjacent mammalian cells.1 Publication

Caution

Conflicting results are seen for mutagenesis of Lys-173. It is seen to reduce binding to the SH3 6 domain of human DNMBP (Tuba) by surface plasmon resonance (PubMed:19767742). In the crystal structure with Tuba this reside is seen not to be in the protein-protein interface, and pull-down assays show it interacts normally with Tuba (PubMed:24332715). Two studies show this residue is important for virulence in the mouse model (PubMed:19767742, PubMed:23403554).3 Publications

<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 - Biological processi

<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

Biological processVirulence

<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_and_taxonomy_section">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:
Internalin C1 Publication
Short name:
InlC1 Publication
Alternative name(s):
Internalin-related protein A1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:inlC1 Publication
Synonyms:irpA1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiListeria monocytogenes serotype 1/2a (strain EGD / Mackaness)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri1334565 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria

<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

GO - Cellular componenti

Keywords - Cellular componenti

Host cytoplasm, 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

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Significant reduction in virulence when injected intravenously into C57BL/6 mice; no effect on intracellular growth of bacteria in infected cell lines (PubMed:8878044, PubMed:20855622, PubMed:23403554). Slightly reduced virulence when injected intravenously into BALB/c mice; no effect on intracellular growth of bacteria in infected cell lines (PubMed:8975898). Decreased bacterial spreading in polarized epithelial cells (human Caco-2 BBE1 cell line), decreased formation of host cell plasma membrane protusions, host cell junctions are not perturbed by bacteria (PubMed:19767742). Significantly increased production of cytokines, significantly increased recruitment of neutrophils to the peritoneum, after intraperitoneal injection into BALB/c mice (PubMed:20855622).5 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi146F → A: Reduced binding to the SH3 6 domain of human DNMBP (Tuba), decreased bacterial spreading in an infected polarized enterocyte cell line, host cell junctions are no longer perturbed. 1 Publication1
Mutagenesisi173K → A: Reduced binding to the SH3 6 domain of human DNMBP (Tuba); conflicting results are also found. Host NF-kappa-B is still not translocated into the nucleus, decreased virulence in C57BL/6 mice, bacteria replicate less well in mouse liver. 3 Publications1
Mutagenesisi246 – 247YY → AA: Prevents InlC-only crystals. 1 Publication2

<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 – 342 PublicationsAdd BLAST34
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_501509684635 – 297Internalin CSequence analysisAdd BLAST263

<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

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Expression induced by PrfA; expressed in bacterial growth medium at very low levels in the absence of extra copies of prfA (at protein level) (PubMed:8878044, PubMed:8641748, PubMed:8975898). Transcription induced upon a shift to growth in minimal medium and also in infected mouse cells; expression is low 1 hour post-infection and reaches its maximum 5 hour post-infection (PubMed:8878044). Detected by 5 hours post infection in human Caco-2 cells (at protein level) (PubMed:19767742). In infected HeLa cells expression increases gradually over time (at protein level) (PubMed:20855622).5 Publications

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts in vitro with human intestinal mucin-2 (MUC2) but not with mucin-1; binding is slightly better at pH 5.5, (the pH of the intestine) than at pH 7.4 (PubMed:18327567).

Interacts with the SH3 6 domain of human DNMBP (Tuba) (PubMed:19767742, PubMed:24332715).

Interacts with I-kappa-B kinase alpha (IKKA, CHUK) (PubMed:20855622).

4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P71451, 3 interactors

<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

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SMRi
P71451

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 ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati74 – 96LRR 1Sequence analysisAdd BLAST23
Repeati97 – 120LRR 2Sequence analysisAdd BLAST24
Repeati122 – 139LRR 3Sequence analysisAdd BLAST18
Repeati140 – 161LRR 4Sequence analysisAdd BLAST22
Repeati162 – 184LRR 5Sequence analysisAdd BLAST23
Repeati186 – 207LRR 6Sequence analysisAdd BLAST22

<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

Consists of the cap domain (residues 35-76) and LRR repeat region (77-213) and an Ig-like region (207-297), where the latter 2 overlap slightly (PubMed:17057330). The LRR repear region interacts via its concave face with host DNMBP (Tuba) (PubMed:24332715).2 Publications

<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 internalin family.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG4886 LUCA

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.80.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR014756 Ig_E-set
IPR024634 Internalin_N
IPR001611 Leu-rich_rpt
IPR025875 Leu-rich_rpt_4
IPR003591 Leu-rich_rpt_typical-subtyp
IPR012569 LRR-contain_adjacent_dom
IPR032675 LRR_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF12354 Internalin_N, 1 hit
PF12799 LRR_4, 2 hits
PF08191 LRR_adjacent, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00369 LRR_TYP, 4 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF81296 SSF81296, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51450 LRR, 5 hits

<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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

P71451-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLKKNNWLQN AVIAMLVLIV GLCINMGSGT KVQAESIQRP TPINQVFPDP
60 70 80 90 100
GLANAVKQNL GKQSVTDLVS QKELSGVQNF NGDNSNIQSL AGMQFFTNLK
110 120 130 140 150
ELHLSHNQIS DLSPLKDLTK LEELSVNRNR LKNLNGIPSA CLSRLFLDNN
160 170 180 190 200
ELRDTDSLIH LKNLEILSIR NNKLKSIVML GFLSKLEVLD LHGNEITNTG
210 220 230 240 250
GLTRLKKVNW IDLTGQKCVN EPVKYQPELY ITNTVKDPDG RWISPYYISN
260 270 280 290
GGSYVDGCVL WELPVYTDEV SYKFSEYINV GETEAIFDGT VTQPIKN
Length:297
Mass (Da):33,192
Last modified:February 1, 1997 - v1
<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:i85B35FF31CEBB9F5
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 conflicti56V → A in CAA67098 (PubMed:8975898).Curated1
Sequence conflicti232 – 234TNT → ANA in CAA67098 (PubMed:8975898).Curated3

<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 29.763 Da from positions 35 - 297. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X95822 Genomic DNA Translation: CAA65088.1
X98458 Genomic DNA Translation: CAA67098.1
Y07640 Genomic DNA Translation: CAA68919.1

Genome annotation databases

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1234141.3.peg.2214

<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
X95822 Genomic DNA Translation: CAA65088.1
X98458 Genomic DNA Translation: CAA67098.1
Y07640 Genomic DNA Translation: CAA68919.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XEUX-ray2.05A35-297[»]
4CC4X-ray2.60A/C/E35-297[»]
SMRiP71451
ModBaseiSearch...

Protein-protein interaction databases

IntActiP71451, 3 interactors

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

PATRICifig|1234141.3.peg.2214

Phylogenomic databases

eggNOGiCOG4886 LUCA

Family and domain databases

Gene3Di3.80.10.10, 1 hit
InterProiView protein in InterPro
IPR014756 Ig_E-set
IPR024634 Internalin_N
IPR001611 Leu-rich_rpt
IPR025875 Leu-rich_rpt_4
IPR003591 Leu-rich_rpt_typical-subtyp
IPR012569 LRR-contain_adjacent_dom
IPR032675 LRR_dom_sf
PfamiView protein in Pfam
PF12354 Internalin_N, 1 hit
PF12799 LRR_4, 2 hits
PF08191 LRR_adjacent, 1 hit
SMARTiView protein in SMART
SM00369 LRR_TYP, 4 hits
SUPFAMiSSF81296 SSF81296, 1 hit
PROSITEiView protein in PROSITE
PS51450 LRR, 5 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

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 nameiINLC_LISMG
<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: P71451
Secondary accession number(s): Q48787, Q799Z7
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 10, 2019
Last sequence update: February 1, 1997
Last modified: September 18, 2019
This is version 124 of the entry and version 1 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 programProkaryotic 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

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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