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UniProtKB - P31977 (EZRI_RAT)

Entry version 184 (25 May 2022)
Sequence version 3 (23 Jan 2007)
Previous versions | rss
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Protein

Ezrin

Gene

Ezr

Organism
Rattus norvegicus (Rat)
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

Probably involved in connections of major cytoskeletal structures to the plasma membrane. In epithelial cells, required for the formation of microvilli and membrane ruffles on the apical pole. Along with PLEKHG6, required for normal macropinocytosis (By similarity).

By similarity

<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

A head-to-tail association, of the N-terminal and C-terminal halves results in a closed conformation (inactive form) which is incapable of actin or membrane-binding.By similarity

<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

Biological processCell shape

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-RNO-373752, Netrin-1 signaling
R-RNO-437239, Recycling pathway of L1

<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:
Ezrin
Alternative name(s):
Cytovillin
Villin-2
p81
<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:Ezr
Synonyms:Vil2
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 › Rattus
<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
  • UP000002494 <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 1

Organism-specific databases

Rat genome database

More...RGDi		621161, Ezr

<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, Cell projection, Cytoplasm, Cytoskeleton, Membrane

<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 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_00002194111 – 586EzrinAdd BLAST586

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei60N6-acetyllysineBy similarity1
Modified residuei146Phosphotyrosine; by PDGFRBy similarity1
Modified residuei366PhosphoserineBy similarity1
Modified residuei478PhosphotyrosineBy similarity1
Modified residuei535PhosphoserineCombined sources1
Modified residuei567Phosphothreonine; by ROCK2 and PKC/PRKCIBy similarity1

<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

Phosphorylated by tyrosine-protein kinases. Phosphorylation by ROCK2 suppresses the head-to-tail association of the N-terminal and C-terminal halves resulting in an opened conformation which is capable of actin and membrane-binding (By similarity).By similarity
S-nitrosylation is induced by interferon-gamma and oxidatively-modified low-densitity lipoprotein (LDL(ox)) possibly implicating the iNOS-S100A8/9 transnitrosylase complex.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, S-nitrosylation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P31977

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

More...PaxDbi		P31977

PRoteomics IDEntifications database

More...PRIDEi		P31977

2D gel databases

The World-2DPAGE database

More...World-2DPAGEi		0004:P31977

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P31977

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

More...PhosphoSitePlusi		P31977

<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 provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Glomerular epithelium cell (podocyte). Expressed in cerebrum, cerebellum and hippocampus (at protein level). Expressed in the small intestine, lung, kidney and ovaries.3 Publications

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Levels increase in the fetal gut epithelium between day 15 and day 20 of gestation and during the first week after birth.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSRNOG00000018524, Expressed in stomach and 20 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P31977, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P31977, RN

<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

Interacts with PODXL and SLC9A3R2.

Found in a complex with EZR, PODXL and SLC9A3R2 (PubMed:11457882).

Interacts with PALS1.

Interacts with MCC, PLEKHG6, SCYL3/PACE1, SLC9A3R1 and TMEM8B.

Interacts (when phosphorylated) with FES/FPS.

Interacts with dimeric S100P, the interaction may be activating through unmasking of F-actin binding sites. Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin. Detected in a complex composed of at least EZR, AHNAK, PPL and PRX.

Interacts with PDPN (via cytoplasmic domain); activates RHOA and promotes epithelial-mesenchymal transition.

Interacts with SPN/CD43 cytoplasmic tail, CD44 and ICAM2 (By similarity).

By similarity1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		248535, 2 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P31977

Protein interaction database and analysis system

More...IntActi		P31977, 3 interactors

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000046593

<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

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P31977

Biological Magnetic Resonance Data Bank

More...BMRBi		P31977

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

More...SMRi		P31977

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>Domaini2 – 295FERMPROSITE-ProRule annotationAdd BLAST294

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>Regioni244 – 586Interaction with SCYL3By similarityAdd BLAST343
Regioni306 – 338DisorderedSequence analysisAdd BLAST33

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili302 – 462Sequence analysisAdd BLAST161

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi115 – 120[IL]-x-C-x-x-[DE] motifBy similarity6

<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 three main structural domains: an N-terminal FERM domain, a central alpha-helical domain and a C-terminal actin-binding domain.By similarity
The FERM domain is organized in a clover-shaped structure that comprises three subdomains identified as F1 (residues 2-82), F2 (residues 96-198), and F3 (residues 204-296). In the active form, the subdomain F3 adopts two mutually exclusive conformational isomers where a row of four phenylalanine side chains (Phe250, Phe255, Phe267 and Phe269) must point in the same direction. In the autoinhibited form, the F3 subdomain interacts with the C-terminal domain (residues 516-586) and stabilizes the structure, selecting only one possible arrangement of phenylalanine side chains. The FERM domain mediates binding to membrane lipids and signaling molecules.By similarity
The central alpha-helical domain is composed of two alpha helices (residues 326-406 and 417-466) connected by a linker. It protrudes from the FERM domain forming a coiled coil structure where the linker can have either a loop or a helix conformation. The monomer is predicted to form an intra-molecular helix-loop-helix coiled coil structure. Whereas the dimer adopts an elongated dumbbell-shaped configuration where continuous alpha helices from each protomer are organized in a antiparallel coiled coil structure that connect FERM:C-terminal domain swapped complex at each end. The dimer is predicted to link actin filaments parallel to the plasma membrane.By similarity
The [IL]-x-C-x-x-[DE] motif is a proposed target motif for cysteine S-nitrosylation mediated by the iNOS-S100A8/A9 transnitrosylase complex.By similarity

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3529, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00960000186596

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_003623_6_2_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P31977

Identification of Orthologs from Complete Genome Data

More...OMAi		HSGMLRE

Database of Orthologous Groups

More...OrthoDBi		627741at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P31977

TreeFam database of animal gene trees

More...TreeFami		TF313935

Family and domain databases

Conserved Domains Database

More...CDDi		cd14473, FERM_B-lobe, 1 hit
cd13194, FERM_C_ERM, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.20.80.10, 1 hit
2.30.29.30, 1 hit
6.10.360.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR019749, Band_41_domain
IPR011174, ERM
IPR041789, ERM_FERM_C
IPR000798, Ez/rad/moesin-like
IPR014352, FERM/acyl-CoA-bd_prot_sf
IPR035963, FERM_2
IPR019748, FERM_central
IPR019747, FERM_CS
IPR000299, FERM_domain
IPR018979, FERM_N
IPR018980, FERM_PH-like_C
IPR008954, Moesin_tail_sf
IPR011993, PH-like_dom_sf
IPR029071, Ubiquitin-like_domsf

The PANTHER Classification System

More...PANTHERi		PTHR23281, PTHR23281, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF09380, FERM_C, 1 hit
PF00373, FERM_M, 1 hit
PF09379, FERM_N, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF002305, ERM, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00935, BAND41
PR00661, ERMFAMILY

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00295, B41, 1 hit
SM01196, FERM_C, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47031, SSF47031, 1 hit
SSF48678, SSF48678, 1 hit
SSF54236, SSF54236, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00660, FERM_1, 1 hit
PS00661, FERM_2, 1 hit
PS50057, FERM_3, 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>Sequence (1+)i

<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.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

P31977-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPKPINVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWYFGLQYV 
        60         70         80         90        100
DNKGFPTWLK LDKKVSAQEV RKENPVQFKF RAKFYPEDVA DELIQDITQK 
       110        120        130        140        150
LFFLQVKEGI LSDEIYCPPE TAVLLGSYAV QAKFGDYNKE MHKSGYLSSE 
       160        170        180        190        200
RLIPQRVMDQ HKLSRDQWED RIQVWHAEHR GMLKDSAMLE YLKIAQDLEM 
       210        220        230        240        250
YGINYFEIKN KKGTDLWLGV DALGLNIYEK DDKLTPKIGF PWSEIRNISF 
       260        270        280        290        300
NDKKFVIKPI DKKAPDFVFY APRLRINKRI LQLCMGNHEL YMRRRKPDTI 
       310        320        330        340        350
EVQQMKAQAR EEKHQKQLER QQLETEKKRR ETVEREKEQM LREKEELMLR 
       360        370        380        390        400
LQDFEQKTKR AEKELSEQIE KALQLEEERR RAQEEAERLE ADRMAALRAK 
       410        420        430        440        450
EELERQAQDQ IKSQEQLAAE LAEYTAKIAL LEEARRRKED EVEEWQHRAK 
       460        470        480        490        500
EAQDDLVKTK EELHLVMTAP PPPPPPVYEP VNYHVQEGLQ DEGAEPMGYS 
       510        520        530        540        550
AELSSEGILD DRNEEKRITE AEKNERVQRQ LLTLSNELSQ ARDENKRTHN 
       560        570        580 
DIIHNENMRQ GRDKYKTLRQ IRQGNTKQRI DEFEAM
Length:586
Mass (Da):69,391
Last modified:January 23, 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:i3A5287052E74CCC9
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0G2K890A0A0G2K890_RAT
Ezrin
Ezr
590Annotation score:

Annotation score:1 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>
A0A8I5Y4R7A0A8I5Y4R7_RAT
Ezrin
Ezr
592Annotation score:

Annotation score:1 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>
A0A8I6A8I6A0A8I6A8I6_RAT
Ezrin
Ezr
575Annotation score:

Annotation score:1 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 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 conflicti455D → E in AAL47844 (Ref. 3) Curated1
Sequence conflicti531L → P in CAA48004 (PubMed:7640303).Curated1
Sequence conflicti532L → Q in AAR91694 (Ref. 1) 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
AY428869 mRNA Translation: AAR91694.1
BC081958 mRNA Translation: AAH81958.1
AF450298 mRNA Translation: AAL47844.1
X67788 mRNA Translation: CAA48004.1

Protein sequence database of the Protein Information Resource

More...PIRi		S58759

NCBI Reference Sequences

More...RefSeqi		NP_062230.1, NM_019357.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSRNOT00000046746; ENSRNOP00000046593; ENSRNOG00000018524

Database of genes from NCBI RefSeq genomes

More...GeneIDi		54319

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:54319

<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
AY428869 mRNA Translation: AAR91694.1
BC081958 mRNA Translation: AAH81958.1
AF450298 mRNA Translation: AAL47844.1
X67788 mRNA Translation: CAA48004.1
PIRiS58759
RefSeqiNP_062230.1, NM_019357.1

3D structure databases

AlphaFoldDBiP31977
BMRBiP31977
SMRiP31977
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi248535, 2 interactors
CORUMiP31977
IntActiP31977, 3 interactors
STRINGi10116.ENSRNOP00000046593

PTM databases

iPTMnetiP31977
PhosphoSitePlusiP31977

2D gel databases

World-2DPAGEi0004:P31977

Proteomic databases

jPOSTiP31977
PaxDbiP31977
PRIDEiP31977

Genome annotation databases

EnsembliENSRNOT00000046746; ENSRNOP00000046593; ENSRNOG00000018524
GeneIDi54319
KEGGirno:54319

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		7430
RGDi621161, Ezr

Phylogenomic databases

eggNOGiKOG3529, Eukaryota
GeneTreeiENSGT00960000186596
HOGENOMiCLU_003623_6_2_1
InParanoidiP31977
OMAiHSGMLRE
OrthoDBi627741at2759
PhylomeDBiP31977
TreeFamiTF313935

Enzyme and pathway databases

ReactomeiR-RNO-373752, Netrin-1 signaling
R-RNO-437239, Recycling pathway of L1

Miscellaneous databases

Protein Ontology

More...PROi		PR:P31977

Gene expression databases

BgeeiENSRNOG00000018524, Expressed in stomach and 20 other tissues
ExpressionAtlasiP31977, baseline and differential
GenevisibleiP31977, RN

Family and domain databases

CDDicd14473, FERM_B-lobe, 1 hit
cd13194, FERM_C_ERM, 1 hit
Gene3Di1.20.80.10, 1 hit
2.30.29.30, 1 hit
6.10.360.10, 1 hit
InterProiView protein in InterPro
IPR019749, Band_41_domain
IPR011174, ERM
IPR041789, ERM_FERM_C
IPR000798, Ez/rad/moesin-like
IPR014352, FERM/acyl-CoA-bd_prot_sf
IPR035963, FERM_2
IPR019748, FERM_central
IPR019747, FERM_CS
IPR000299, FERM_domain
IPR018979, FERM_N
IPR018980, FERM_PH-like_C
IPR008954, Moesin_tail_sf
IPR011993, PH-like_dom_sf
IPR029071, Ubiquitin-like_domsf
PANTHERiPTHR23281, PTHR23281, 1 hit
PfamiView protein in Pfam
PF09380, FERM_C, 1 hit
PF00373, FERM_M, 1 hit
PF09379, FERM_N, 1 hit
PIRSFiPIRSF002305, ERM, 1 hit
PRINTSiPR00935, BAND41
PR00661, ERMFAMILY
SMARTiView protein in SMART
SM00295, B41, 1 hit
SM01196, FERM_C, 1 hit
SUPFAMiSSF47031, SSF47031, 1 hit
SSF48678, SSF48678, 1 hit
SSF54236, SSF54236, 1 hit
PROSITEiView protein in PROSITE
PS00660, FERM_1, 1 hit
PS00661, FERM_2, 1 hit
PS50057, FERM_3, 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 nameiEZRI_RAT
<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: P31977
Secondary accession number(s): Q5WQV4, Q66H97, Q8VHK3
<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, 1993
Last sequence update: January 23, 2007
Last modified: May 25, 2022
This is version 184 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
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