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UniProtKB - P27590 (UROM_RAT)

Entry version 153 (29 Sep 2021)
Sequence version 1 (01 Aug 1992)
Previous versions | rss
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Protein

Uromodulin

Gene

Umod

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 transcript 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

Functions in biogenesis and organization of the apical membrane of epithelial cells of the thick ascending limb of Henle's loop (TALH), where it promotes formation of complex filamentous gel-like structure that may play a role in the water barrier permeability. May serve as a receptor for binding and endocytosis of cytokines (IL-1, IL-2) and TNF. Facilitates neutrophil migration across renal epithelia.

By similarity

In the urine, may contribute to colloid osmotic pressure, retards passage of positively charged electrolytes, prevents urinary tract infection and inhibits formation of liquid containing supersaturated salts and subsequent formation of salt crystals.

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>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:
Uromodulin
Alternative name(s):
Tamm-Horsfall urinary glycoprotein
Short name:
THP
Cleaved into the following chain:
Uromodulin, secreted form
<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:Umod
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 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_and_taxonomy_section">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_manual">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: Unplaced

Organism-specific databases

Rat genome database

More...RGDi		3940, Umod

<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

<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>Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane, Secreted

<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 – 26By similarityAdd BLAST26
<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_000004167527 – 615UromodulinAdd BLAST589
ChainiPRO_000040791227 – 590Uromodulin, secreted formAdd BLAST564
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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_0000041676616 – 644Removed in mature formSequence analysisAdd BLAST29

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 bondi34 ↔ 43PROSITE-ProRule annotation
Disulfide bondi37 ↔ 52PROSITE-ProRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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>Glycosylationi40N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi54 ↔ 65PROSITE-ProRule annotation
Disulfide bondi71 ↔ 84PROSITE-ProRule annotation
Glycosylationi78N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi79 ↔ 93PROSITE-ProRule annotation
Disulfide bondi95 ↔ 107PROSITE-ProRule annotation
Disulfide bondi113 ↔ 127PROSITE-ProRule annotation
Disulfide bondi121 ↔ 136PROSITE-ProRule annotation
Disulfide bondi138 ↔ 149PROSITE-ProRule annotation
Glycosylationi235N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi278N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi300 ↔ 309By similarity
Disulfide bondi303 ↔ 318By similarity
Disulfide bondi320 ↔ 350By similarity
Glycosylationi325N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi338 ↔ 428By similarity
Disulfide bondi369 ↔ 392By similarity
Glycosylationi399N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi450N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi509 ↔ 569PROSITE-ProRule annotation
Glycosylationi516N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi530 ↔ 585By similarity
Disulfide bondi574 ↔ 581By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi615GPI-anchor amidated serineSequence analysis1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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

N-glycosylated.By similarity
Proteolytically cleaved at a conserved C-terminal proteolytic cleavage site to generate the secreted form found in urine. This cleavage is catalyzed by HPN.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>Sitei590 – 591CleavageBy similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

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

More...PaxDbi		P27590

PRoteomics IDEntifications database

More...PRIDEi		P27590

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		P27590, 8 sites

<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

Expression restricted to the thick ascending limb of the loop of Henle (TALH).1 Publication

<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

Homodimer that then polymerizes into long filaments. The filaments can additionally assemble laterally to form a sheet.

By similarity

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000021027

<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		P27590

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_and_domains_section">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>Domaini30 – 66EGF-like 1PROSITE-ProRule annotationAdd BLAST37
Domaini67 – 108EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini109 – 150EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini337 – 592ZPPROSITE-ProRule annotationAdd BLAST256

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>Regioni337 – 432ZP-NSequence analysisAdd BLAST96
Regioni433 – 456Flexible linker; important for secretion and polymerization into filamentsBy similarityAdd BLAST24
Regioni457 – 467Internal hydrophobic patch (IHP)Sequence analysisAdd BLAST11
Regioni468 – 592ZP-CSequence analysisAdd BLAST125
Regioni589 – 592Essential for cleavage by HPNBy similarity4
Regioni601 – 610Regulates polymerization into filamentsBy similarity10

<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

The ZP domain mediates polymerization, leading to the formation of long filaments. The core of the filament consists of stacked ZP domains which assemble into a helical structure. Each ZP domain consists of an N-terminal (ZP-N) and C-terminal (ZP-C) region connected by a flexible linker; the linker allows the ZP domain to wrap around the ZP-C subdomain of the preceding subunit. The heavily glycosylated N-terminal part of the protein (containing several EGF-like domains) forms branches which protrude from the core and may be involved in pathogen capture.By similarity

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG502QT6B, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P27590

Database of Orthologous Groups

More...OrthoDBi		665331at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P27590

TreeFam database of animal gene trees

More...TreeFami		TF330284

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.60.40.4100, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001881, EGF-like_Ca-bd_dom
IPR000742, EGF-like_dom
IPR000152, EGF-type_Asp/Asn_hydroxyl_site
IPR018097, EGF_Ca-bd_CS
IPR024731, EGF_dom
IPR009030, Growth_fac_rcpt_cys_sf
IPR042235, ZP-C
IPR001507, ZP_dom
IPR017977, ZP_dom_CS

Pfam protein domain database

More...Pfami		View protein in Pfam
PF12947, EGF_3, 1 hit
PF07645, EGF_CA, 1 hit
PF00100, Zona_pellucida, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00023, ZPELLUCIDA

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00181, EGF, 3 hits
SM00179, EGF_CA, 2 hits
SM00241, ZP, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF57184, SSF57184, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00010, ASX_HYDROXYL, 2 hits
PS01186, EGF_2, 4 hits
PS50026, EGF_3, 3 hits
PS01187, EGF_CA, 2 hits
PS00682, ZP_1, 1 hit
PS51034, ZP_2, 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_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>Sequence (1+)i

<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.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P27590-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGQLLSLTWL LLVMVVTPWF TVAGANDSPE ARRCSECHDN ATCVLDGVVT 
        60         70         80         90        100
TCSCQAGFTG DGLVCEDIDE CATPWTHNCS NSICMNTLGS YECSCQDGFR 
       110        120        130        140        150
LTPGLGCIDV NECTEQGLSN CHSLATCVNT EGSYSCVCPK GYRGDGWYCE 
       160        170        180        190        200
CSPGFCEPGL DCLPQGPSGK LVCQDPCNVY ETLTEYWRST DYGAGYSCDS 
       210        220        230        240        250
DMHGWYRFTG QGGVRMAETC VPVLRCNTAA PMWLNGSHPS SREGIVSRTA 
       260        270        280        290        300
CAHWSDHCCL WSTEIQVKAC PGGFYVYNLT EPPECNLAYC TDPSSVEGTC 
       310        320        330        340        350
EECGVDEDCV SDNGRWRCQC KQDFNVTDVS LLEHRLECEA NEIKISLSKC 
       360        370        380        390        400
QLQSLGFMKV FMYLNDRQCS GFSERGERDW MSIVTPARDG PCGTVLRRNE 
       410        420        430        440        450
THATYSNTLY LASEIIIRDI NIRINFECSY PLDMKVSLKT SLQPMVSALN 
       460        470        480        490        500
ISLGGTGKFT VQMALFQNPT YTQPYQGPSV MLSTEAFLYV GTMLDGGDLS 
       510        520        530        540        550
RFVLLMTNCY ATPSSNSTDP VKYFIIQDRC PHTEDTTIQV TENGESSQAR 
       560        570        580        590        600
FSIQMFRFAG NSDLVYLHCE VYLCDTMSEQ CKPTCSGTRY RSGNFIDQTR 
       610        620        630        640 
VLNLGPITRQ GVQASVSKAA SSNLGFLSIW LLLFLSATLT LMVH
Length:644
Mass (Da):71,062
Last modified:August 1, 1992 - 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:iD26DB419C669826A
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0G2JSP1A0A0G2JSP1_RAT
Uromodulin
Umod
644Annotation 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 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 conflicti155F → S in AAH81814 (PubMed:15489334).Curated1
Sequence conflicti326V → I in AAH81814 (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
M63510 mRNA Translation: AAA42319.1
S75960 mRNA Translation: AAB33313.1
BC081814 mRNA Translation: AAH81814.1

Protein sequence database of the Protein Information Resource

More...PIRi		A40212

NCBI Reference Sequences

More...RefSeqi		NP_058778.1, NM_017082.1
XP_006230169.1, XM_006230107.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		25128

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:25128

UCSC genome browser

More...UCSCi		RGD:3940, rat

<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
M63510 mRNA Translation: AAA42319.1
S75960 mRNA Translation: AAB33313.1
BC081814 mRNA Translation: AAH81814.1
PIRiA40212
RefSeqiNP_058778.1, NM_017082.1
XP_006230169.1, XM_006230107.2

3D structure databases

SMRiP27590
ModBaseiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000021027

PTM databases

GlyGeniP27590, 8 sites

Proteomic databases

PaxDbiP27590
PRIDEiP27590

Genome annotation databases

GeneIDi25128
KEGGirno:25128
UCSCiRGD:3940, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		7369
RGDi3940, Umod

Phylogenomic databases

eggNOGiENOG502QT6B, Eukaryota
InParanoidiP27590
OrthoDBi665331at2759
PhylomeDBiP27590
TreeFamiTF330284

Miscellaneous databases

Protein Ontology

More...PROi		PR:P27590

Family and domain databases

Gene3Di2.60.40.4100, 1 hit
InterProiView protein in InterPro
IPR001881, EGF-like_Ca-bd_dom
IPR000742, EGF-like_dom
IPR000152, EGF-type_Asp/Asn_hydroxyl_site
IPR018097, EGF_Ca-bd_CS
IPR024731, EGF_dom
IPR009030, Growth_fac_rcpt_cys_sf
IPR042235, ZP-C
IPR001507, ZP_dom
IPR017977, ZP_dom_CS
PfamiView protein in Pfam
PF12947, EGF_3, 1 hit
PF07645, EGF_CA, 1 hit
PF00100, Zona_pellucida, 1 hit
PRINTSiPR00023, ZPELLUCIDA
SMARTiView protein in SMART
SM00181, EGF, 3 hits
SM00179, EGF_CA, 2 hits
SM00241, ZP, 1 hit
SUPFAMiSSF57184, SSF57184, 1 hit
PROSITEiView protein in PROSITE
PS00010, ASX_HYDROXYL, 2 hits
PS01186, EGF_2, 4 hits
PS50026, EGF_3, 3 hits
PS01187, EGF_CA, 2 hits
PS00682, ZP_1, 1 hit
PS51034, ZP_2, 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 nameiUROM_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: P27590
Secondary accession number(s): Q642D6
<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: August 1, 1992
Last sequence update: August 1, 1992
Last modified: September 29, 2021
This is version 153 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 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

Reference proteome
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