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UniProtKB - P35444 (COMP_RAT)

Entry version 154 (23 Feb 2022)
Sequence version 1 (01 Jun 1994)
Previous versions | rss
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Protein

Cartilage oligomeric matrix protein

Gene

Comp

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

Plays a role in the structural integrity of cartilage via its interaction with other extracellular matrix proteins such as the collagens and fibronectin. Can mediate the interaction of chondrocytes with the cartilage extracellular matrix through interaction with cell surface integrin receptors. Could play a role in the pathogenesis of osteoarthritis. Potent suppressor of apoptosis in both primary chondrocytes and transformed cells. Suppresses apoptosis by blocking the activation of caspase-3 and by inducing the IAP family of survival proteins (BIRC3, BIRC2, BIRC5 and XIAP) (By similarity).

Essential for maintaining a vascular smooth muscle cells (VSMCs) contractile/differentiated phenotype under physiological and pathological stimuli. Maintains this phenotype of VSMCs by interacting with ITGA7 (PubMed:20019333).

By similarity1 Publication

<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+By similarityNote: Binds 11-14 calcium ions per subunit.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

Molecular functionHeparin-binding
Biological processApoptosis, Cell adhesion
LigandCalcium

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-RNO-216083, Integrin cell surface interactions
R-RNO-3000178, ECM proteoglycans

<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:
Cartilage oligomeric matrix proteinCurated
Short name:
COMP
<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:CompImported
<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: Unplaced

Organism-specific databases

Rat genome database

More...RGDi		2378, Comp

<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

Extracellular matrix, 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 – 19Sequence analysisAdd BLAST19
<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_000003585920 – 755Cartilage oligomeric matrix proteinAdd BLAST736

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 bondi68Interchain (with C-71)Combined sources1 Publication
Disulfide bondi71Interchain (with C-68)Combined sources1 Publication
Disulfide bondi89 ↔ 100PROSITE-ProRule annotation
Disulfide bondi94 ↔ 109PROSITE-ProRule annotation
Disulfide bondi112 ↔ 123PROSITE-ProRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi119N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi129 ↔ 140PROSITE-ProRule annotation
Disulfide bondi134 ↔ 149PROSITE-ProRule annotation
Disulfide bondi152 ↔ 176PROSITE-ProRule annotation
Disulfide bondi182 ↔ 195PROSITE-ProRule annotation
Disulfide bondi189 ↔ 204PROSITE-ProRule annotation
Disulfide bondi207 ↔ 219PROSITE-ProRule annotation
Disulfide bondi227 ↔ 241PROSITE-ProRule annotation
Disulfide bondi235 ↔ 251PROSITE-ProRule annotation
Disulfide bondi253 ↔ 264PROSITE-ProRule annotation
Disulfide bondi280 ↔ 285PROSITE-ProRule annotation
Disulfide bondi290 ↔ 310PROSITE-ProRule annotation
Disulfide bondi326 ↔ 346PROSITE-ProRule annotation
Disulfide bondi349 ↔ 369PROSITE-ProRule annotation
Disulfide bondi385 ↔ 405PROSITE-ProRule annotation
<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 residuei394PhosphoserineBy similarity1
Disulfide bondi408 ↔ 428PROSITE-ProRule annotation
Disulfide bondi446 ↔ 466PROSITE-ProRule annotation
Disulfide bondi482 ↔ 502PROSITE-ProRule annotation
Disulfide bondi518 ↔ 739PROSITE-ProRule annotation
Glycosylationi740N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

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

More...PaxDbi		P35444

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		P35444, 2 sites

<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

Pentamer; disulfide-linked. Exists in a more compact conformation in the presence of calcium and shows a more extended conformation in the absence of calcium.

Interacts with ITGB3, ITGA5 and FN1. Binding to FN1 requires the presence of divalent cations (Ca2+, Mg2+ or Mn2+). The greatest amount of binding is seen in the presence of Mn2+.

Interacts with MATN1, MATN3, MATN4 and ACAN. Binds heparin, heparan sulfate and chondroitin sulfate. EDTA dimishes significantly its binding to ACAN and abolishes its binding to MATN3, MATN4 and chondroitin sulfate.

Interacts with collagen I, II and IX, and interaction with these collagens is dependent on the presence of zinc ions.

Interacts with ADAMTS12 (By similarity).

Interacts with ITGA7 (PubMed:20019333).

By similarity1 Publication

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		247343, 2 interactors

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000067037

<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

1755
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		P35444

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		P35444

<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>Domaini85 – 124EGF-like 1PROSITE-ProRule annotationAdd BLAST40
Domaini125 – 177EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd BLAST53
Domaini178 – 220EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd BLAST43
Domaini223 – 265EGF-like 4PROSITE-ProRule annotationAdd BLAST43
<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>Repeati266 – 298TSP type-3 1Add BLAST33
Repeati299 – 334TSP type-3 2Add BLAST36
Repeati335 – 357TSP type-3 3Add BLAST23
Repeati358 – 393TSP type-3 4Add BLAST36
Repeati394 – 416TSP type-3 5Add BLAST23
Repeati417 – 454TSP type-3 6Add BLAST38
Repeati455 – 490TSP type-3 7Add BLAST36
Repeati491 – 526TSP type-3 8Add BLAST36
Domaini530 – 744TSP C-terminalPROSITE-ProRule annotationAdd BLAST215

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>Regioni21 – 84COMP N-terminalAdd BLAST64
Regioni295 – 501DisorderedSequence analysisAdd BLAST207
Regioni525 – 755Mediates cell survival and induction of the IAP family of survival proteinsBy similarityAdd BLAST231

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi298 – 312Basic and acidic residuesSequence analysisAdd BLAST15
Compositional biasi333 – 381Basic and acidic residuesSequence analysisAdd BLAST49
Compositional biasi410 – 442Basic and acidic residuesSequence analysisAdd BLAST33

<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 cell attachment motif mediates the attachment to chondrocytes. It mediates the induction of both the IAP family of survival proteins and the antiapoptotic response.By similarity
The TSP C-terminal domain mediates interaction with FN1 and ACAN.By similarity
Each of the eight TSP type-3 repeats binds two calcium ions. The TSP C-terminal domain binds three calcium ions.By similarity

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

Belongs to the thrombospondin family.Curated

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG502QRK8, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P35444

Database of Orthologous Groups

More...OrthoDBi		120983at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P35444

Family and domain databases

Conserved Domains Database

More...CDDi		cd16077, TSP-5cc, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		4.10.1080.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR013320, ConA-like_dom_sf
IPR001881, EGF-like_Ca-bd_dom
IPR000742, EGF-like_dom
IPR018097, EGF_Ca-bd_CS
IPR009030, Growth_fac_rcpt_cys_sf
IPR024665, Thbs/COMP_coiled-coil
IPR003367, Thrombospondin_3-like_rpt
IPR017897, Thrombospondin_3_rpt
IPR008859, Thrombospondin_C
IPR028492, TSP-5
IPR039081, TSP-5_cc
IPR028974, TSP_type-3_rpt

The PANTHER Classification System

More...PANTHERi		PTHR10199:SF88, PTHR10199:SF88, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF11598, COMP, 1 hit
PF07645, EGF_CA, 2 hits
PF02412, TSP_3, 6 hits
PF05735, TSP_C, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00181, EGF, 4 hits
SM00179, EGF_CA, 2 hits

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF103647, SSF103647, 3 hits
SSF49899, SSF49899, 1 hit
SSF57184, SSF57184, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS01186, EGF_2, 1 hit
PS50026, EGF_3, 3 hits
PS01187, EGF_CA, 2 hits
PS51234, TSP3, 8 hits
PS51236, TSP_CTER, 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.

<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.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

P35444-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSPTACVLVL ALAALRATGQ GQIPLGGDLA PQMLRELQET NAALQDVREL 
        60         70         80         90        100
LRHRVKEITF LKNTVMECDA CGMQPARTPG LSVRPVALCA PGSCFPGVVC 
       110        120        130        140        150
TETATGARCG PCPPGYTGNG SHCTDVNECN AHPCFPRVRC INTSPGFHCE 
       160        170        180        190        200
ACPPGFSGPT HEGVGLTFAK TNKQVCTDIN ECETGQHNCV PNSVCVNTRG 
       210        220        230        240        250
SFQCGPCQPG FVGDQRSGCQ RRGQHFCPDG SPSPCHEKAD CILERDGSRS 
       260        270        280        290        300
CVCAVGWAGN GLLCGRDTDL DGFPDEKLRC SERQCRKDNC VTVPNSGQED 
       310        320        330        340        350
VDRDRIGDAC DPDADGDGVP NEQDNCPLVR NPDQRNSDKD KWGDACDNCR 
       360        370        380        390        400
SQKNDDQKDT DRDGQGDACD DDIDGDRIRN VADNCPRVPN FDQSDSDGDG 
       410        420        430        440        450
VGDACDNCPQ KDNPDQRDVD HDFVGDACDS DQDQDGDGHQ DSRDNCPTVP 
       460        470        480        490        500
NSAQQDSDHD GKGDACDDDD DNDGVPDSRD NCRLVPNPGQ EDNDRDGVGD 
       510        520        530        540        550
ACQGDFDADK VIDKIDVCPE NAEVTLTDFR AFQTVVLDPE GDAQIDPNWV 
       560        570        580        590        600
VLNQGMEIVQ TMNSDPGLAV GYTAFNGVDF EGTFHVNTAT DDDYAGFIFG 
       610        620        630        640        650
YQDSSSFYVV MWKQMEQTYW QANPFRAVAE PGIQLKAVKS STGPGEQLRN 
       660        670        680        690        700
ALWHTGDTAS QVRLLWKDPR NVGWKDKTSY RWFLQHRPQV GYIRVRFYEG 
       710        720        730        740        750
PELVADSNVV LDTAMRGGRL GVFCFSQENI IWANLRYRCN DTIPEDYERH 

RLRRA
Length:755
Mass (Da):82,664
Last modified:June 1, 1994 - 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:iAB48888FE093C598
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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
M0RBU0M0RBU0_RAT
Cartilage oligomeric matrix protein
Comp rCG_38834
755Annotation 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>
A0A0G2JXN9A0A0G2JXN9_RAT
Cartilage oligomeric matrix protein
Comp
109Annotation 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>

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
X72914 mRNA Translation: CAA51419.1

Protein sequence database of the Protein Information Resource

More...PIRi		A44315

NCBI Reference Sequences

More...RefSeqi		NP_036966.1, NM_012834.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		25304

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:25304

<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
X72914 mRNA Translation: CAA51419.1
PIRiA44315
RefSeqiNP_036966.1, NM_012834.1

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
1FBMX-ray2.70A/B/C/D/E28-72[»]
1VDFX-ray2.05A/B/C/D/E28-72[»]
6SF6X-ray1.90C/D232-250[»]
SMRiP35444
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi247343, 2 interactors
STRINGi10116.ENSRNOP00000067037

PTM databases

GlyGeniP35444, 2 sites

Proteomic databases

PaxDbiP35444

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...ABCDi		P35444, 1 sequenced antibody

Genome annotation databases

GeneIDi25304
KEGGirno:25304

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		1311
RGDi2378, Comp

Phylogenomic databases

eggNOGiENOG502QRK8, Eukaryota
InParanoidiP35444
OrthoDBi120983at2759
PhylomeDBiP35444

Enzyme and pathway databases

ReactomeiR-RNO-216083, Integrin cell surface interactions
R-RNO-3000178, ECM proteoglycans

Miscellaneous databases

EvolutionaryTraceiP35444

Protein Ontology

More...PROi		PR:P35444

Family and domain databases

CDDicd16077, TSP-5cc, 1 hit
Gene3Di4.10.1080.10, 2 hits
InterProiView protein in InterPro
IPR013320, ConA-like_dom_sf
IPR001881, EGF-like_Ca-bd_dom
IPR000742, EGF-like_dom
IPR018097, EGF_Ca-bd_CS
IPR009030, Growth_fac_rcpt_cys_sf
IPR024665, Thbs/COMP_coiled-coil
IPR003367, Thrombospondin_3-like_rpt
IPR017897, Thrombospondin_3_rpt
IPR008859, Thrombospondin_C
IPR028492, TSP-5
IPR039081, TSP-5_cc
IPR028974, TSP_type-3_rpt
PANTHERiPTHR10199:SF88, PTHR10199:SF88, 1 hit
PfamiView protein in Pfam
PF11598, COMP, 1 hit
PF07645, EGF_CA, 2 hits
PF02412, TSP_3, 6 hits
PF05735, TSP_C, 1 hit
SMARTiView protein in SMART
SM00181, EGF, 4 hits
SM00179, EGF_CA, 2 hits
SUPFAMiSSF103647, SSF103647, 3 hits
SSF49899, SSF49899, 1 hit
SSF57184, SSF57184, 1 hit
PROSITEiView protein in PROSITE
PS01186, EGF_2, 1 hit
PS50026, EGF_3, 3 hits
PS01187, EGF_CA, 2 hits
PS51234, TSP3, 8 hits
PS51236, TSP_CTER, 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 nameiCOMP_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: P35444
<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: June 1, 1994
Last sequence update: June 1, 1994
Last modified: February 23, 2022
This is version 154 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

3D-structure, Reference proteome

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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