Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 117 (11 Dec 2019)
Sequence version 1 (01 Feb 1996)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Secretory phospholipase A2 receptor

Gene

PLA2R1

Organism
Oryctolagus cuniculus (Rabbit)
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

Receptor for secretory phospholipase A2 (sPLA2). Also able to bind to snake PA2-like toxins. Although its precise function remains unclear, binding of sPLA2 to its receptor participates in both positive and negative regulation of sPLA2 functions as well as clearance of sPLA2. Binding of sPLA2-IB/PLA2G1B induces various effects depending on the cell type, such as activation of the mitogen-activated protein kinase (MAPK) cascade to induce cell proliferation, the production of lipid mediators, selective release of arachidonic acid in bone marrow-derived mast cells. In neutrophils, binding of sPLA2-IB/PLA2G1B can activate p38 MAPK to stimulate elastase release and cell adhesion. May be involved in responses in proinflammatory cytokine productions during endotoxic shock. Also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. The soluble secretory phospholipase A2 receptor form is circulating and acts as a negative regulator of sPLA2 functions by blocking the biological functions of sPLA2-IB/PLA2G1B and sPLA2-X/PLA2G10.2 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - 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 functionReceptor
Biological processEndocytosis
LigandLectin

<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:
Secretory phospholipase A2 receptor
Short name:
PLA2-R
Short name:
PLA2R
Alternative name(s):
180 kDa secretory phospholipase A2 receptor
M-type receptor
Cleaved into the following chain:
Soluble secretory phospholipase A2 receptor
Short name:
Soluble PLA2-R
Short name:
Soluble PLA2R
<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:PLA2R1
<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>OrganismiOryctolagus cuniculus (Rabbit)
<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 identifieri9986 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
<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
  • UP000001811 <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

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini24 – 1393ExtracellularSequence analysisAdd BLAST1370
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei1394 – 1416HelicalSequence analysisAdd BLAST23
Topological domaini1417 – 1458CytoplasmicSequence analysisAdd BLAST42

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi1432 – 1438Missing : Abolishes receptor internalization. 1 Publication7
Mutagenesisi1433S → P: Increases receptor internalization. 1 Publication1
Mutagenesisi1434 – 1435YY → AA: Reduces receptor internalization. 1 Publication2
Mutagenesisi1436P → A: Does not affect receptor internalization. 1 Publication1
Mutagenesisi1452S → A: Does not affect receptor internalization. 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 – 23Sequence analysisAdd BLAST23
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001755124 – 1458Secretory phospholipase A2 receptorAdd BLAST1435
ChainiPRO_000031125424 – ?Soluble secretory phospholipase A2 receptorBy similarity

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 bondi49 ↔ 62By similarity
Disulfide bondi87 ↔ 104By similarity
<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>Glycosylationi91N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi176 ↔ 202By similarity
Disulfide bondi190 ↔ 217By similarity
Disulfide bondi258 ↔ 352By similarity
Disulfide bondi328 ↔ 344By similarity
Disulfide bondi404 ↔ 499By similarity
Glycosylationi408N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi431N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi452N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi476 ↔ 491By similarity
Disulfide bondi615 ↔ 632By similarity
Disulfide bondi697 ↔ 794By similarity
Disulfide bondi772 ↔ 786By similarity
Disulfide bondi838 ↔ 935By similarity
Disulfide bondi912 ↔ 927By similarity
Disulfide bondi1065 ↔ 1085By similarity
Disulfide bondi1207 ↔ 1221By similarity
Disulfide bondi1278 ↔ 1373By similarity
Disulfide bondi1350 ↔ 1365By similarity

<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

The secretory phospholipase A2 receptor form may be produced by the action of metalloproteinases. It contains all extracellular domains and only lacks transmembrane and cytosolic regions. It is however unclear whether this form is produced by proteolytic cleavage as suggested by some experiments, or by alternative splicing (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

<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

Lung, skeletal muscle, brain, kidney and heart.

<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

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9986.ENSOCUP00000012759

<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
P49260

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>Domaini49 – 113Ricin B-type lectinPROSITE-ProRule annotationAdd BLAST65
Domaini171 – 219Fibronectin type-IIPROSITE-ProRule annotationAdd BLAST49
Domaini227 – 356C-type lectin 1PROSITE-ProRule annotationAdd BLAST130
Domaini374 – 502C-type lectin 2PROSITE-ProRule annotationAdd BLAST129
Domaini511 – 645C-type lectin 3PROSITE-ProRule annotationAdd BLAST135
Domaini660 – 798C-type lectin 4PROSITE-ProRule annotationAdd BLAST139
Domaini815 – 939C-type lectin 5PROSITE-ProRule annotationAdd BLAST125
Domaini954 – 1098C-type lectin 6PROSITE-ProRule annotationAdd BLAST145
Domaini1117 – 1231C-type lectin 7PROSITE-ProRule annotationAdd BLAST115
Domaini1243 – 1376C-type lectin 8PROSITE-ProRule annotationAdd BLAST134

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>Motifi1432 – 1438Endocytosis signal7

<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

C-type lectin domains 3-5 mediate the interaction with phospholipase PLA2G1B.By similarity
The endocytosis signal probably mediates endocytosis via clathrin-coated pits.

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410KDES Eukaryota
ENOG4111FAE LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000231191

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P49260

KEGG Orthology (KO)

More...
KOi
K06560

Database of Orthologous Groups

More...
OrthoDBi
29241at2759

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00062 FN2, 1 hit
cd00161 RICIN, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.10.10.10, 1 hit
3.10.100.10, 8 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001304 C-type_lectin-like
IPR016186 C-type_lectin-like/link_sf
IPR018378 C-type_lectin_CS
IPR016187 CTDL_fold
IPR000562 FN_type2_dom
IPR036943 FN_type2_sf
IPR035992 Ricin_B-like_lectins
IPR000772 Ricin_B_lectin

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00040 fn2, 1 hit
PF00059 Lectin_C, 8 hits

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00034 CLECT, 8 hits
SM00059 FN2, 1 hit
SM00458 RICIN, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50370 SSF50370, 1 hit
SSF56436 SSF56436, 8 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00615 C_TYPE_LECTIN_1, 3 hits
PS50041 C_TYPE_LECTIN_2, 8 hits
PS00023 FN2_1, 1 hit
PS51092 FN2_2, 1 hit
PS50231 RICIN_B_LECTIN, 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>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P49260-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLLSLLLLLL LGAPRRCTEG AAAALSPERV LKWQEKGIFI IQSESLKSCI
60 70 80 90 100
QAGKSVLTLE SCKQPNKNML WKWVSNQHLF NIGGSGCLGL NLSNPEQPLG
110 120 130 140 150
LYECDSTHVS LRWRCNRKMI TGPLQHTVQV KQDNIIVASG KRLHKWISYM
160 170 180 190 200
SDSGDICQHV HKDLYTRKGN AHGTPCMFPF QYNHQWHHEC TREGRQDDSL
210 220 230 240 250
WCATTSRYER DEKWGFCPDP TSAEVGCDAV WEKDLNSHIC YQFNLLSSLS
260 270 280 290 300
WSEAHSSCQM HGGALLSIVD EAEENFIRKQ VSGEAVEVWT GLNQLDVNAG
310 320 330 340 350
WQWSDGTPLS YLNWSPEISF EPFVEYHCGT FNSFMPRAWR SRNCESTLPY
360 370 380 390 400
ICKKYLNHVD DEIVEKDAWK YYATDCEPGW APYHRNCYKL QKEEKTWNEA
410 420 430 440 450
LHSCLSSNST LIDIGSLAEV EFLVTLLGNE NASETWIGLS SNTFPVSFEW
460 470 480 490 500
SNGSSVIFTN WHTLEPQIFP NRSQLCVSAE QSEGHWKVTD CEETHFYVCK
510 520 530 540 550
KPGHVLSDAE SGCQEGWERH GGFCYKIDTV LRSFDHASSG YYCPPALVTI
560 570 580 590 600
ADRFEQAFIT SLISSVVNMK DSYFWIALQD QNDTGEYTWK TAGQKSEPVQ
610 620 630 640 650
YTHWNAHQPR SSGGCVAIRG RNPIGRWEVK DCVHFKAMSL CKQPVETREK
660 670 680 690 700
MEHEERWPFH PCYLDWESQP GLASCFKVFH SEKVLMKRTW REAEAFCEEF
710 720 730 740 750
GAHLASFAHI EEENFVNELL HPKFNRSEER QFWIGFNKRN PLNAGSWEWS
760 770 780 790 800
DGTPVISSFL DNNYFGEDTR NCAVYKANKT LLPLHCGSKR EWICKIPRDV
810 820 830 840 850
RPKIPSWYQY DAPWLFHQDA EYLFYPHSSE WSSFEFVCGW LRSDILTIHS
860 870 880 890 900
AHEQEFILSK IKALSKYGAN WWIGLQEETA NDELRWRDGT PVIYQNWDKE
910 920 930 940 950
RDRSMNNQSQ RCAFISSITG LWDREECSVS MPSICKRKTF WVIEKEKDTP
960 970 980 990 1000
KQHGTCPKGW LYFDYKCLLV NVPKDPSNWK NWTQARDFCF DEGGTLVAIE
1010 1020 1030 1040 1050
SEVEQAFITM NLFGQTTNVW IGLQNDDYEK WLNGNPVAYS NWSPSDIINI
1060 1070 1080 1090 1100
PSYNTTADQK PIPLCALLSS NPNFHFTGKW YFEDCGKEGY GFVCEKIQDS
1110 1120 1130 1140 1150
AGHEVNTSIM DPIPNTLEYG NRTYKIINAN MTWYAAIKSC QLHGAELVSI
1160 1170 1180 1190 1200
TDQYHQSFLT VILSRLGHAH WIGLFTADNG LHFDWSDGTK SSFTFWKDED
1210 1220 1230 1240 1250
SSFLGDCVFA DTSGRWHSTA CESFLQGAIC HVPTETRPFE HPELCSETSI
1260 1270 1280 1290 1300
PWIKFKSNCY SFSTVLHSAS FEAAHEFCKK EGSNLLTIKD EAENSFLLEE
1310 1320 1330 1340 1350
PFAFGASVQM VWLNAQFDNE TVKWLDGTPA DQSNWGIRKP DMAHFEPHQC
1360 1370 1380 1390 1400
LALRIPEGVW QLSPCQKNMG FICKMKADIH TVKEHPGKGP SHSIVPLAVA
1410 1420 1430 1440 1450
LTLVVILAII TLSFYIYKQN KGFFRRLAGV GNSYYPTTNF STIHLEENIL

ISDLEKND
Length:1,458
Mass (Da):167,200
Last modified:February 1, 1996 - 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:i686163066DAB9511
GO

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
U03455 mRNA Translation: AAC48402.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A49707

NCBI Reference Sequences

More...
RefSeqi
NP_001075803.1, NM_001082334.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
100009180

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ocu:100009180

<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
U03455 mRNA Translation: AAC48402.1
PIRiA49707
RefSeqiNP_001075803.1, NM_001082334.1

3D structure databases

SMRiP49260
ModBaseiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000012759

Genome annotation databases

GeneIDi100009180
KEGGiocu:100009180

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
22925

Phylogenomic databases

eggNOGiENOG410KDES Eukaryota
ENOG4111FAE LUCA
HOGENOMiHOG000231191
InParanoidiP49260
KOiK06560
OrthoDBi29241at2759

Family and domain databases

CDDicd00062 FN2, 1 hit
cd00161 RICIN, 1 hit
Gene3Di2.10.10.10, 1 hit
3.10.100.10, 8 hits
InterProiView protein in InterPro
IPR001304 C-type_lectin-like
IPR016186 C-type_lectin-like/link_sf
IPR018378 C-type_lectin_CS
IPR016187 CTDL_fold
IPR000562 FN_type2_dom
IPR036943 FN_type2_sf
IPR035992 Ricin_B-like_lectins
IPR000772 Ricin_B_lectin
PfamiView protein in Pfam
PF00040 fn2, 1 hit
PF00059 Lectin_C, 8 hits
SMARTiView protein in SMART
SM00034 CLECT, 8 hits
SM00059 FN2, 1 hit
SM00458 RICIN, 1 hit
SUPFAMiSSF50370 SSF50370, 1 hit
SSF56436 SSF56436, 8 hits
PROSITEiView protein in PROSITE
PS00615 C_TYPE_LECTIN_1, 3 hits
PS50041 C_TYPE_LECTIN_2, 8 hits
PS00023 FN2_1, 1 hit
PS51092 FN2_2, 1 hit
PS50231 RICIN_B_LECTIN, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPLA2R_RABIT
<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: P49260
<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: February 1, 1996
Last sequence update: February 1, 1996
Last modified: December 11, 2019
This is version 117 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

Direct protein sequencing, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again