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Entry version 19 (02 Jun 2021)
Sequence version 1 (13 Feb 2019)
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Protein

Internalin B

Gene

inlB

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

Mediates the entry of L.monocytogenes into normally non-phagocytic mammalian host cells (Probable) (PubMed:9282740, PubMed:11081636).

Its host receptor is hepatocyte growth factor receptor (HGF receptor, a tyrosine kinase, MET) which is tyrosine-phosphorylated in response to InlB in human, green monkey, mouse and dog cell lines (PubMed:11081636, PubMed:15049825).

Downstream adapter proteins GAB1 and CBL are phosphorylated in response to InlB, which also causes cell colony scattering (PubMed:11081636).

InlB binding to mammalian cells is saturable and inhibited by EDTA; InlB-coated beads can be taken up by host cells (PubMed:10747014).

Complement component 1 Q subcomponent-binding protein (gC1q-R, C1QBP) might act as an InlB receptor, leading to activation of PI3-kinase in green monkey cells (PubMed:10747014).

Stimulation of Tyr-phosphorylation by InlB is antagonized by C1QBP, showing that potentiation of MET signaling via the GW domains is not mediated by C1QBP; the exact role of C1QBP remains to be determined (PubMed:15049825).

Stimulation of Tyr-phosphorylation of MET by InlB is potentiated by the InlB GW domains and glycosaminoglycans such as heparin; exogenously added InlB, or hepatocyte growth factor (HGF) will also substitute for bacterial InlB, suggesting InlB promotes bacterial invasion by mimicking the hormone HGF (PubMed:15049825).

May stimulate phosphatidylinositol 4,5-bisphosphate 3-kinase (PI3-kinase) in green monkey cells, has less effect in humans as PI3-kinase is constitutively and highly expressed in Caco cells (Probable). Binds heparin; C1QBP and heparin seem to bind to the GW domains (PubMed:12411480).

3 Publications5 Publications

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Ca2+2 PublicationsNote: Binds 2 Ca2+ ions; binding site 1 has a 10-fold higher affinity binding site 2 (PubMed:10635330, PubMed:15020228). Loss of Ca2+-binding has no measurable effect on host receptor activation or invasion by Listeria, suggesting ion-binding is fortuitous (PubMed:15020228).2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi49Calcium 1; via carbonyl oxygenCombined sources2 Publications1
Metal bindingi51Calcium 1Combined sources2 Publications1
Metal bindingi55Calcium 2Combined sources2 Publications1
Metal bindingi59Calcium 2Combined sources2 Publications1

<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

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

Molecular functionHeparin-binding
Biological processVirulence
LigandCalcium, Lipid-binding, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-8875360, InlB-mediated entry of Listeria monocytogenes into host cell

<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:
Internalin B1 Publication
Short name:
InlB
Alternative name(s):
Invasion protein InlB
<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:inlB
<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>OrganismiListeria monocytogenes serotype 1/2a (strain EGD / Mackaness)
<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 identifieri1334565 [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 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

Keywords - Cellular componenti

Cell membrane, Membrane, 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

Deletion of both inlA and inlB prevents uptake of Listeria by human enterocyte-like cell line Caco-2 (PubMed:1905979). Single inlB deletion no longer invades various cell lines (PubMed:9282740, PubMed:15049825, PubMed:8864117). Decreased synthesis of phosphatidylinositol 3,4,5-trisphosphate (PIP3) in green monkey cells, decreased infection of host cells, decreased association of host PI3-kinase catalytic subunit with tyrosine-phosphorylated proteins (PubMed:8864117). Deletion no longer Tyr-phosphorylates mammalian MET (PubMed:11081636, PubMed:15049825).5 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi51 – 59DAFAETIKD → AAFAETIKA: No Ca(2+) binding, no change in Tyr-phosphorylation of host MET, wild-type invasion of host Vero cells. 1 Publication9
Mutagenesisi51D → A: Only binds 1 Ca(2+), no change in Tyr-phosphorylation of host MET, wild-type invasion of host Vero cells. 1 Publication1
Mutagenesisi59D → A: No Ca(2+) binding, no change in Tyr-phosphorylation of host MET, wild-type invasion of host Vero cells. 1 Publication1

<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 – 30Sequence analysisAdd BLAST30
<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_000044628931 – 630Internalin BAdd BLAST600

<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

Monomer (PubMed:15049825).

Interacts via its LRR repeats with the extracellular portion of mammalian host MET; MET can bind HGF, its endogenous ligand, and InlB simultaneously (PubMed:11081636). Probably forms a dimer upon interaction with host MET, which subsequently allows dimerization of the host MET and subsequent host signaling; dimerization probably occurs via the convex surface of InlB (By similarity).

Interacts with host complement component 1 Q subcomponent-binding protein (C1QBP) (PubMed:10747014, PubMed:12411480).

Interacts in vitro with human intestinal mucin-2 (MUC2) but not with mucin-1 (PubMed:18327567).

By similarity5 Publications

<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

Secondary structure

1630
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
P0DQD3

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P25147

<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>Domaini31 – 76LRRNTAdd BLAST46
<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>Repeati75 – 97LRR 1Sequence analysisAdd BLAST23
Repeati98 – 121LRR 2Sequence analysisAdd BLAST24
Repeati123 – 141LRR 3Sequence analysisAdd BLAST19
Repeati142 – 163LRR 4Sequence analysisAdd BLAST22
Repeati164 – 187LRR 5Sequence analysisAdd BLAST24
Repeati189 – 207LRR 6Sequence analysisAdd BLAST19
Repeati208 – 231LRR 7Sequence analysisAdd BLAST24
Domaini241 – 330LRRCTAdd BLAST90
Domaini393 – 467GW 1PROSITE-ProRule annotationAdd BLAST75
Domaini472 – 550GW 2PROSITE-ProRule annotationAdd BLAST79
Domaini553 – 630GW 3PROSITE-ProRule annotationAdd BLAST78

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>Regioni241 – 319Ig-like region2 PublicationsAdd BLAST79
Regioni320 – 392B repeat region2 PublicationsAdd BLAST73
Regioni399 – 630GW repeat region, necessary and sufficient for cell surface attachment, interacts with host C1QBP and with heparin1 Publication3 PublicationsAdd BLAST232

<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

Has an N-terminal region with 8 leucine-rich repeats (LRR) and has 3 GW repeats in the C-terminus (Probable). Residues 241-319 form an Ig-like region, followed by a 72 residue-long flexible B repeat region (PubMed:12411480) (Probable). The GW repeats mediate non-covalent binding of the protein to lipoteichoic acid (LTA) on the bacterial membrane (PubMed:10594817). The GW domain mediates binding to host complement component 1 Q subcomponent-binding protein (gC1q-R, C1QBP) and to heparin; heprin binding dissociates InlB from the bacterial surface (PubMed:12411480). The LRR domain forms a curved tube, the N-terminus of which has a cap that binds 2 Ca2+ ions (PubMed:10635330, PubMed:15020228). The LRR domain alone (31-241) binds mammalian MET and stimulates its Tyr-phosphorylation; the LRR plus Ig-like region (31-321) are required for receptor dimerization, and the GW domains, especially GW2 and GW3, potentiate MET activation (PubMed:11081636, PubMed:15049825).3 Publications6 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

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.30.30.170, 3 hits
3.10.20.660, 1 hit
3.80.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR025987, GW_dom
IPR038200, GW_dom_sf
IPR014756, Ig_E-set
IPR024634, Internalin_N
IPR001611, Leu-rich_rpt
IPR025875, Leu-rich_rpt_4
IPR003591, Leu-rich_rpt_typical-subtyp
IPR013378, Listeria/Bacterioides_rpt
IPR042229, Listeria/Bacterioides_rpt_sf
IPR012569, LRR-contain_adjacent_dom
IPR032675, LRR_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF09479, Flg_new, 1 hit
PF13457, GW, 3 hits
PF12354, Internalin_N, 1 hit
PF12799, LRR_4, 1 hit
PF13855, LRR_8, 1 hit
PF08191, LRR_adjacent, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00369, LRR_TYP, 5 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF81296, SSF81296, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR02543, List_Bact_rpt, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51780, GW, 3 hits
PS51450, LRR, 6 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%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.

P0DQD3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKEKHNPRRK YCLISGLAII FSLWIIIGNG AKVQAETITV STPIKQIFPD
60 70 80 90 100
DAFAETIKDN LKKKSVTDAV TQNELNSIDQ IIANNSDIKS VQGIQYLPNV
110 120 130 140 150
TKLFLNGNKL TDIKPLTNLK NLGWLFLDEN KIKDLSSLKD LKKLKSLSLE
160 170 180 190 200
HNGISDINGL VHLPQLESLY LGNNKITDIT VLSRLTKLDT LSLEDNQISD
210 220 230 240 250
IVPLAGLTKL QNLYLSKNHI SDLRALAGLK NLDVLELFSQ ECLNKPINHQ
260 270 280 290 300
SNLVVPNTVK NTDGSLVTPE IISDDGDYEK PNVKWHLPEF TNEVSFIFYQ
310 320 330 340 350
PVTIGKAKAR FHGRVTQPLK EVYTVSYDVD GTVIKTKVEA GTRITAPKPP
360 370 380 390 400
TKQGYVFKGW YTEKNGGHEW NFNTDYMSGN DFTLYAVFKA ETTEKTVNLT
410 420 430 440 450
RYVKYIRGNA GIYKLPREDN SLKQGTLASH RCKALTVDRE ARNGGKLWYR
460 470 480 490 500
LKNIGWTKAE NLSLDRYDKM EYDKGVTAYA RVRNASGNSV WTKPYNTAGA
510 520 530 540 550
KHVNKLSVYQ GKNMRILREA KTPITTWYQF SIGGKVIGWV DTRALNTFYK
560 570 580 590 600
QSMEKPTRLT RYVSANKAGE SYYKVPVADN PVKRGTLAKY KNQKLIVDCQ
610 620 630
ATIEGQLWYR IRTSSTFIGW TKAANLRAQK
Length:630
Mass (Da):71,221
Last modified:February 13, 2019 - 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:iEFBDCF52DBAF0C45
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 conflicti41S → P in CAC20629 (Ref. 2) 1
Sequence conflicti49P → S in CAC20629 (Ref. 2) 1
Sequence conflicti117T → A in CAC20629 (Ref. 2) 1
Sequence conflicti132I → V in CAC20629 (Ref. 2) 1
Sequence conflicti396T → A in CAC20629 (Ref. 2) 1

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
M67471 Genomic DNA Translation: AAA25290.1
AJ012346 Genomic DNA Translation: CAC20629.1

Protein sequence database of the Protein Information Resource

More...
PIRi
C39930

NCBI Reference Sequences

More...
RefSeqi
WP_014930830.1, NC_022568.1

<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
M67471 Genomic DNA Translation: AAA25290.1
AJ012346 Genomic DNA Translation: CAC20629.1
PIRiC39930
RefSeqiWP_014930830.1, NC_022568.1

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
1D0BX-ray1.86A36-248[»]
1M9SX-ray2.65A36-630[»]
1OTMX-ray1.93A36-248[»]
1OTNX-ray1.97A36-248[»]
1OTOX-ray1.96A36-248[»]
6GCUX-ray6.00B/E36-321[»]
6U12X-ray1.56A36-248[»]
SMRiP0DQD3
ModBaseiSearch...
PDBe-KBiSearch...

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...
ABCDi
P0DQD3, 12 sequenced antibodies

Enzyme and pathway databases

ReactomeiR-HSA-8875360, InlB-mediated entry of Listeria monocytogenes into host cell

Miscellaneous databases

EvolutionaryTraceiP25147

Family and domain databases

Gene3Di2.30.30.170, 3 hits
3.10.20.660, 1 hit
3.80.10.10, 1 hit
InterProiView protein in InterPro
IPR025987, GW_dom
IPR038200, GW_dom_sf
IPR014756, Ig_E-set
IPR024634, Internalin_N
IPR001611, Leu-rich_rpt
IPR025875, Leu-rich_rpt_4
IPR003591, Leu-rich_rpt_typical-subtyp
IPR013378, Listeria/Bacterioides_rpt
IPR042229, Listeria/Bacterioides_rpt_sf
IPR012569, LRR-contain_adjacent_dom
IPR032675, LRR_dom_sf
PfamiView protein in Pfam
PF09479, Flg_new, 1 hit
PF13457, GW, 3 hits
PF12354, Internalin_N, 1 hit
PF12799, LRR_4, 1 hit
PF13855, LRR_8, 1 hit
PF08191, LRR_adjacent, 1 hit
SMARTiView protein in SMART
SM00369, LRR_TYP, 5 hits
SUPFAMiSSF81296, SSF81296, 1 hit
TIGRFAMsiTIGR02543, List_Bact_rpt, 1 hit
PROSITEiView protein in PROSITE
PS51780, GW, 3 hits
PS51450, LRR, 6 hits

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 nameiINLB_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: P0DQD3
Secondary accession number(s): P25147, Q9EXG1
<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: February 13, 2019
Last sequence update: February 13, 2019
Last modified: June 2, 2021
This is version 19 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

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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