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Protein

Cubilin

Gene

Cubn

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

Cotransporter which plays a role in lipoprotein, vitamin and iron metabolism, by facilitating their uptake. Binds to ALB, MB, Kappa and lambda-light chains, TF, hemoglobin, GC, SCGB1A1, APOA1, high density lipoprotein, and the GIF-cobalamin complex. The binding of all ligands requires calcium. Serves as important transporter in several absorptive epithelia, including intestine, renal proximal tubules and embryonic yolk sac. Interaction with LRP2 mediates its trafficking throughout vesicles and facilitates the uptake of specific ligands like GC, hemoglobin, ALB, TF and SCGB1A1. Interaction with AMN controls its trafficking to the plasma membrane and facilitates endocytosis of ligands. May play an important role in the development of the peri-implantation embryo through internalization of APOA1 and cholesterol. Binds to LGALS3 at the maternal-fetal interface.6 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi980Calcium 1By similarity1
Metal bindingi988Calcium 1By similarity1
Metal bindingi1027Calcium 1By similarity1
Metal bindingi1030Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi1096Calcium 2By similarity1
Metal bindingi1105Calcium 2By similarity1
Metal bindingi1146Calcium 2By similarity1
Metal bindingi1213Calcium 3By similarity1
Metal bindingi1221Calcium 3By similarity1
Metal bindingi1262Calcium 3By similarity1
Metal bindingi1264Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi1265Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi1328Calcium 4By similarity1
Metal bindingi1336Calcium 4By similarity1
Metal bindingi1373Calcium 4By similarity1
Metal bindingi1375Calcium 4; via carbonyl oxygenBy similarity1

<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

  • calcium ion binding Source: InterPro
  • cargo receptor activity Source: UniProtKB
  • channel regulator activity Source: GO_Central
  • cobalamin binding Source: UniProtKB-KW
  • drug binding Source: UniProtKB
  • hemoglobin binding Source: RGD
  • identical protein binding Source: RGD
  • protein homodimerization activity Source: GO_Central
  • signaling receptor activity Source: RGD

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

Biological processCholesterol metabolism, Lipid metabolism, Protein transport, Steroid metabolism, Sterol metabolism, Transport
LigandCalcium, Cobalamin, Cobalt, Metal-binding

<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:
Cubilin
Alternative name(s):
460 kDa receptor
Glycoprotein 280
Short name:
gp280
Intrinsic factor-cobalamin receptor
Intrinsic factor-vitamin B12 receptor
<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:Cubn
Synonyms:Ifcr
<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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
68355 Cubn

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

Endosome, Lysosome, 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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 20Sequence analysisAdd BLAST20
<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_000004607621 – 32Removed in mature formBy similarityAdd BLAST12
<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_000004607733 – 3623CubilinAdd BLAST3591

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Glycosylationi95N-linked (GlcNAc...) asparagineSequence analysis1
<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 bondi133 ↔ 144By similarity
Disulfide bondi138 ↔ 153By similarity
Disulfide bondi155 ↔ 164By similarity
Disulfide bondi171 ↔ 187By similarity
Disulfide bondi181 ↔ 196By similarity
Disulfide bondi198 ↔ 207By similarity
Disulfide bondi264 ↔ 277By similarity
Disulfide bondi271 ↔ 286By similarity
Disulfide bondi289 ↔ 300By similarity
Disulfide bondi350 ↔ 363By similarity
Disulfide bondi357 ↔ 376By similarity
Disulfide bondi399 ↔ 409By similarity
Disulfide bondi404 ↔ 418By similarity
Disulfide bondi420 ↔ 429By similarity
Glycosylationi428N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi436 ↔ 447By similarity
Disulfide bondi441 ↔ 456By similarity
Disulfide bondi458 ↔ 467By similarity
Disulfide bondi474 ↔ 500By similarity
Glycosylationi491N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi527 ↔ 549By similarity
Disulfide bondi590 ↔ 616By similarity
Disulfide bondi643 ↔ 665By similarity
Disulfide bondi708 ↔ 734By similarity
Glycosylationi711N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi749N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi761 ↔ 779By similarity
Glycosylationi781N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi817 ↔ 842By similarity
Glycosylationi857N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi869 ↔ 891By similarity
Disulfide bondi932 ↔ 958By similarity
Glycosylationi957N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi984N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi985 ↔ 1005By similarity
Disulfide bondi1048 ↔ 1074By similarity
Disulfide bondi1165 ↔ 1191By similarity
Glycosylationi1168N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1218 ↔ 1240By similarity
Disulfide bondi1278 ↔ 1306By similarity
Glycosylationi1285N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1307N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1319N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1332N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1333 ↔ 1351By similarity
Disulfide bondi1391 ↔ 1417By similarity
Disulfide bondi1444 ↔ 1466By similarity
Glycosylationi1500N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1510 ↔ 1536By similarity
Glycosylationi1551N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1620 ↔ 1647By similarity
Glycosylationi1646N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1671N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1675 ↔ 1697By similarity
Disulfide bondi1738 ↔ 1764By similarity
Disulfide bondi1791 ↔ 1812By similarity
Glycosylationi1802N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1819N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1905 ↔ 1927By similarity
Disulfide bondi1978 ↔ 2006By similarity
Disulfide bondi2032 ↔ 2054By similarity
Glycosylationi2085N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2092 ↔ 2118By similarity
Glycosylationi2117N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2217 ↔ 2247By similarity
Glycosylationi2274N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2275 ↔ 2297By similarity
Disulfide bondi2336 ↔ 2363By similarity
Disulfide bondi2390 ↔ 2411By similarity
Glycosylationi2400N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2452 ↔ 2478By similarity
Disulfide bondi2505 ↔ 2527By similarity
Glycosylationi2531N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2570 ↔ 2599By similarity
Glycosylationi2581N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2610N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2628 ↔ 2649By similarity
Disulfide bondi2689 ↔ 2715By similarity
Disulfide bondi2742 ↔ 2764By similarity
Disulfide bondi2805 ↔ 2831By similarity
Glycosylationi2813N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2860 ↔ 2883By similarity
Glycosylationi2875N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2920 ↔ 2946By similarity
Glycosylationi2945N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2977 ↔ 2999By similarity
Glycosylationi2989N-linked (GlcNAc...) asparagineSequence analysis1
<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 residuei3008PhosphothreonineCombined sources1
Disulfide bondi3037 ↔ 3064By similarity
Glycosylationi3042N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3091 ↔ 3113By similarity
Glycosylationi3106N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi3125N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3157 ↔ 3185By similarity
Glycosylationi3165N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3215 ↔ 3237By similarity
Glycosylationi3268N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3278 ↔ 3306By similarity
Glycosylationi3283N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi3290N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3332 ↔ 3354By similarity
Glycosylationi3357N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3395 ↔ 3421By similarity
Glycosylationi3400N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi3430N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3448 ↔ 3470By similarity
Disulfide bondi3511 ↔ 3537By similarity
Glycosylationi3533N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3564 ↔ 3586By 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 precursor is cleaved by a trans-Golgi proteinase furin. The result is a propeptide cleaved off (By similarity).By similarity
N-glycosylated.1 Publication

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>Sitei32 – 33Cleavage; by furinSequence analysis2

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

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

More...
PaxDbi
O70244

PRoteomics IDEntifications database

More...
PRIDEi
O70244

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O70244

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

More...
PhosphoSitePlusi
O70244

<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

Expressed to intestinal, renal and yalk sac apical membranes. In kidney, expressed in the proximal tubule.1 Publication

<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

Expressed at 6 dpc in primitive endoderm cells, in apical membrane invaginations, in endocytic vesicles, endoplasmic reticulum and Golgi apparatus. At the egg cylinder stage (7-8 dpc), expressed in visceral and parietal endoderm. From the early headfold stage (8.9 dpc), expressed in ectodermal cells lining the proamniotic cavity. At 10 dpc, detected in the newly forming neuroepithelium.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

Component of the cubam complex composed of CUBN and AMN (By similarity). The cubam complex can oligomerize and form cubam trimers. Interacts with LRP2 in a dual-receptor complex in a calcium-dependent manner. Found in a complex with PID1/PCLI1, LRP1 and CUBNI (By similarity). Interacts with LRP1 and PID1/PCLI1 (By similarity).By similarity

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-3954161,EBI-3954161

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
249486, 1 interactor

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
O70244

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000048477

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
O70244

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

More...
SMRi
O70244

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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>Domaini129 – 165EGF-like 1PROSITE-ProRule annotationAdd BLAST37
Domaini167 – 208EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini260 – 301EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini302 – 345EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd BLAST44
Domaini346 – 385EGF-like 5PROSITE-ProRule annotationAdd BLAST40
Domaini395 – 430EGF-like 6PROSITE-ProRule annotationAdd BLAST36
Domaini432 – 468EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini474 – 586CUB 1PROSITE-ProRule annotationAdd BLAST113
Domaini590 – 702CUB 2PROSITE-ProRule annotationAdd BLAST113
Domaini708 – 816CUB 3PROSITE-ProRule annotationAdd BLAST109
Domaini817 – 928CUB 4PROSITE-ProRule annotationAdd BLAST112
Domaini932 – 1042CUB 5PROSITE-ProRule annotationAdd BLAST111
Domaini1048 – 1161CUB 6PROSITE-ProRule annotationAdd BLAST114
Domaini1165 – 1277CUB 7PROSITE-ProRule annotationAdd BLAST113
Domaini1278 – 1389CUB 8PROSITE-ProRule annotationAdd BLAST112
Domaini1391 – 1506CUB 9PROSITE-ProRule annotationAdd BLAST116
Domaini1510 – 1619CUB 10PROSITE-ProRule annotationAdd BLAST110
Domaini1620 – 1734CUB 11PROSITE-ProRule annotationAdd BLAST115
Domaini1738 – 1850CUB 12PROSITE-ProRule annotationAdd BLAST113
Domaini1852 – 1963CUB 13PROSITE-ProRule annotationAdd BLAST112
Domaini1978 – 2091CUB 14PROSITE-ProRule annotationAdd BLAST114
Domaini2092 – 2213CUB 15PROSITE-ProRule annotationAdd BLAST122
Domaini2217 – 2334CUB 16PROSITE-ProRule annotationAdd BLAST118
Domaini2336 – 2448CUB 17PROSITE-ProRule annotationAdd BLAST113
Domaini2452 – 2565CUB 18PROSITE-ProRule annotationAdd BLAST114
Domaini2570 – 2687CUB 19PROSITE-ProRule annotationAdd BLAST118
Domaini2689 – 2801CUB 20PROSITE-ProRule annotationAdd BLAST113
Domaini2805 – 2919CUB 21PROSITE-ProRule annotationAdd BLAST115
Domaini2920 – 3035CUB 22PROSITE-ProRule annotationAdd BLAST116
Domaini3037 – 3150CUB 23PROSITE-ProRule annotationAdd BLAST114
Domaini3157 – 3274CUB 24PROSITE-ProRule annotationAdd BLAST118
Domaini3278 – 3393CUB 25PROSITE-ProRule annotationAdd BLAST116
Domaini3395 – 3507CUB 26PROSITE-ProRule annotationAdd BLAST113
Domaini3511 – 3623CUB 27PROSITE-ProRule annotationAdd BLAST113

<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 CUB domains 5 to 8 mediate binding to GIF and ALB. CUB domains 1 and 2 mediate interaction with LRP2.1 Publication

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG3714 Eukaryota
ENOG410ZPX7 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000173840

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG080357

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O70244

KEGG Orthology (KO)

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KOi
K14616

Database for complete collections of gene phylogenies

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PhylomeDBi
O70244

Family and domain databases

Conserved Domains Database

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CDDi
cd00041 CUB, 27 hits

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.120.290, 27 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR000859 CUB_dom
IPR001881 EGF-like_Ca-bd_dom
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR000152 EGF-type_Asp/Asn_hydroxyl_site
IPR018097 EGF_Ca-bd_CS
IPR024731 EGF_dom
IPR035914 Sperma_CUB_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00431 CUB, 27 hits
PF00008 EGF, 3 hits
PF12947 EGF_3, 1 hit
PF07645 EGF_CA, 3 hits

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00042 CUB, 27 hits
SM00181 EGF, 8 hits
SM00179 EGF_CA, 7 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF49854 SSF49854, 27 hits

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00010 ASX_HYDROXYL, 3 hits
PS01180 CUB, 27 hits
PS00022 EGF_1, 4 hits
PS01186 EGF_2, 2 hits
PS50026 EGF_3, 6 hits
PS01187 EGF_CA, 4 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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

O70244-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSSQFLWGFV TLLMIAELDG KTGKPEQRGQ KRIADLHQPR MTTEEGNLVF
60 70 80 90 100
LTSSTQNIEF RTGSLGKIKL NDEDLGECLH QIQRNKDDII DLRKNTTGLP
110 120 130 140 150
QNILSQVHQL NSKLVDLERD FQNLQQNVER KVCSSNPCLN GGTCVNLHDS
160 170 180 190 200
FVCICPSQWK GLFCSEDVNE CVVYSGTPFG CQSGSTCVNT VGSFRCDCTP
210 220 230 240 250
DTYGPQCASK YNDCEQGSKQ LCKHGICEDL QRVHHGQPNF HCICDAGWTT
260 270 280 290 300
PPNGISCTED KDECSLQPSP CSEHAQCFNT QGSFYCGACP KGWQGNGYEC
310 320 330 340 350
QDINECEINN GGCSQAPLVP CLNTPGSFSC GNCPAGFSGD GRVCTPVDIC
360 370 380 390 400
SIHNGGCHPE ATCSSSPVLG SFLPVCTCPP GYTGNGYGSN GCVRLSNICS
410 420 430 440 450
RHPCVNGQCI ETVSSYFCKC DSGWSGQNCT ENINDCSSNP CLNGGTCIDG
460 470 480 490 500
INGFTCDCTS SWTGYYCQTP QAACGGILSG TQGTFAYHSP NDTYIHNVNC
510 520 530 540 550
FWIVRTDEEK VLHVTFTFFD LESASNCPRE YLQIHDGDSS ADFPLGRYCG
560 570 580 590 600
SRPPQGIHSS ANALYFHLYS EYIRSGRGFT ARWEAKLPEC GGILTDNYGS
610 620 630 640 650
ITSPGYPGNY PPGRDCVWQV LVNPNSLITF TFGTLSLESH NDCSKDYLEI
660 670 680 690 700
RDGPFHQDPV LGKFCTSLST PPLKTTGPAA RIHFHSDSET SDKGFHITYL
710 720 730 740 750
TTQSDLDCGG NYTDTDGELL LPPLSGPFSH SRQCVYLITQ AQGEQIVINF
760 770 780 790 800
THVELESQMG CSHTYIEVGD HDSLLRKICG NETLFPIRSV SNKVWIRLRI
810 820 830 840 850
DALVQKASFR ADYQVACGGM LRGEGFFRSP FYPNAYPGRR TCRWTISQPQ
860 870 880 890 900
RQVVLLNFTD FQIGSSASCD TDYIEIGPSS VLGSPGNEKF CSSNIPSFIT
910 920 930 940 950
SVYNILYVTF VKSSSMENRG FTAKFSSDKL ECGEVLTAST GIIESPGHPN
960 970 980 990 1000
VYPRGVNCTW HVVVQRGQLI RLEFSSFYLE FHYNCTNDYL EIYDTAAQTF
1010 1020 1030 1040 1050
LGRYCGKSIP PSLTSNSNSI KLIFVSDSAL AHEGFSINYE AIDASSVCLY
1060 1070 1080 1090 1100
DYTDNFGMLS SPNFPNNYPS NWECIYRITV GLNQQIALHF TDFTLEDYFG
1110 1120 1130 1140 1150
SQCVDFVEIR DGGYETSPLV GIYCGSVLPP TIISHSNKLW LKFKSDAALT
1160 1170 1180 1190 1200
AKGFSAYWDG SSTGCGGNLT TPTGVLTSPN YPMPYYHSSE CYWRLEASHG
1210 1220 1230 1240 1250
SPFELEFQDF HLEHHPSCSL DYLAVFDGPT TNSRLIDKLC GDTTPAPIRS
1260 1270 1280 1290 1300
NKDVVLLKLR TDAGQQGRGF EINFRQRCDN VVIVNKTSGI LESINYPNPY
1310 1320 1330 1340 1350
DKNQRCNWTI QATTGNTVNY TFLGFDVESY MNCSTDYVEL YDGPQWMGRY
1360 1370 1380 1390 1400
CGNNMPPPGA TTGSQLHVLF HTDGINSGEK GFKMQWFTHG CGGEMSGTAG
1410 1420 1430 1440 1450
SFSSPGYPNS YPHNKECIWN IRVAPGSSIQ LTIHDFDVEY HTSCNYDSLE
1460 1470 1480 1490 1500
IYAGLDFNSP RIAQLCSQSP SANPMQVSST GNELAIRFKT DSTLNGRGFN
1510 1520 1530 1540 1550
ASWRAVPGGC GGIIQLSRGE IHSPNYPNNY RANTECSWII QVERHHRVLL
1560 1570 1580 1590 1600
NITDFDLEAP DSCLRLMDGS SSTNARVASV CGRQQPPNSI IASGNSLFVR
1610 1620 1630 1640 1650
FRSGSSSQNR GFRAEFREEC GGRIMTDSSD TIFSPLYPHN YLHNQNCSWI
1660 1670 1680 1690 1700
IEAQPPFNHI TLSFTHFQLQ NSTDCTRDFV EILDGNDYDA PVQGRYCGFS
1710 1720 1730 1740 1750
LPHPIISFGN ALTVRFVTDS TRSFEGFRAI YSASTSSCGG SFYTLDGIFN
1760 1770 1780 1790 1800
SPDYPADYHP NAECVWNIAS SPGNRLQLSF LSFNLENSLN CNKDFVEIRE
1810 1820 1830 1840 1850
GNATGHLIGR YCGNSLPGNY SSAEGHSLWV RFVSDGSGTG MGFQARFKNI
1860 1870 1880 1890 1900
FGNNNIVGTH GKIASPFWPG KYPYNSNYKW VVNVDAYHII HGRILEMDIE
1910 1920 1930 1940 1950
PTTNCFYDSL KIYDGFDTHS RLIGTYCGTQ TESFSSSRNS LTFQFSSDSS
1960 1970 1980 1990 2000
VSGRGFLLEW FAVDVSDSTP PTIAPGACGG FMVTGDTPVH IFSPGWPREY
2010 2020 2030 2040 2050
ANGADCIWII YAPDSTVELN ILSLDIEPQQ SCNYDKLIVK DGDSDLSPEL
2060 2070 2080 2090 2100
AVLCGVSPPG PIRSTGEYMY IRFTSDTSVA GTGFNASFHK SCGGYLHADR
2110 2120 2130 2140 2150
GVITSPKYPD TYLPNLNCSW HVLVQTGLTI AVHFEQPFQI QNRDSFCSQG
2160 2170 2180 2190 2200
DYLVLRNGPD NHSPPLGPSG RNGRFCGMYA PSTLFTSGNE MFVQFISDSS
2210 2220 2230 2240 2250
NGGQGFKIRY EAKSLACGGT VYIHDADSDG YLTSPNYPAN YPQHAECIWI
2260 2270 2280 2290 2300
LEAPPGRSIQ LQFEDQFNIE DTPNCSVSYL ELRDGANSNA RLVSKLCGHT
2310 2320 2330 2340 2350
LPHSWVSSRE RIYLKFHTDG GSSYMGFKAK YSIASCGGTV SGDSGVIESI
2360 2370 2380 2390 2400
GYPTLPYANN VFCQWFIRGL PGHYLTLSFE DFNLQSSPGC TKDFVEIWEN
2410 2420 2430 2440 2450
HTSGRVLGRY CGNSTPSSVD TSSNVASVKF VTDGSVTASG FRLQFKSSRQ
2460 2470 2480 2490 2500
VCGGDLHGPT GTFTSPNYPN PNPHARICEW TITVQEGRRI VLTFTNLRLS
2510 2520 2530 2540 2550
TQPSCNSEHL IVFNGIRSNS PLLQKLCSRV NVTNEFKSSG NTMKVVFFTD
2560 2570 2580 2590 2600
GSRPYGGFTA SYTSTEDAVC GGFLPSVSGG NFSSPGYNGI RDYARNLDCE
2610 2620 2630 2640 2650
WTLSNPNREN SSISIYFLEL SIESHQDCTF DVLEFRVGDA DGPLIEKFCS
2660 2670 2680 2690 2700
LSAPTAPLVI PYPQVWIHFV SNERVEYTGF YIEYSFTDCG GIRTGDNGVI
2710 2720 2730 2740 2750
SSPNYPNLYS AWTHCSWLLK APEGHTITLT FSDFLLEAHP TCTSDSVTVR
2760 2770 2780 2790 2800
NGDSPGSPVI GRYCGQSVPR PIQSGSNQLI VTFNTNNQGQ TRGFYATWTT
2810 2820 2830 2840 2850
NALGCGGTFH SANGTIKSPH WPQTFPENSR CSWTVITHES KHWEISFDSN
2860 2870 2880 2890 2900
FRIPSSDSQC QNSFVKVWEG RLMINKTLLA TSCGDVAPSP IVTSGNIFTA
2910 2920 2930 2940 2950
VFQSEEMAAQ GFSASFISRC GRTFNTSPGD IISPNFPKQY DNNMNCTYLI
2960 2970 2980 2990 3000
DADPQSLVIL TFVSFHLEDR SAITGTCDHD GLHIIKGRNL SSTPLVTICG
3010 3020 3030 3040 3050
SETLRPLTVD GPVLLNFYSD AYTTDFGFKI SYRAITCGGI YNESSGILRS
3060 3070 3080 3090 3100
PSYSYSNYPN NLYCVYSLHV RSSRVIIIRF NDFDVAPSNL CAHDFLEVFD
3110 3120 3130 3140 3150
GPSIGNRSLG KFCGSTRPQT VKSTNSSLTL LFKTDSSQTA RGWKIFFRET
3160 3170 3180 3190 3200
IGPQQGCGGY LTEDNQSFVS PDSDSNGRYD KGLSCIWYIV APENKLVKLT
3210 3220 3230 3240 3250
FNVFTLEGPS SAGSCVYDYV QIADGASINS YLGGKFCGSR MPAPFISSGN
3260 3270 3280 3290 3300
FLTFQFVSDV TVEMRGFNAT YTFVDMPCGG TYNATSTPQN ASSPHLSNIG
3310 3320 3330 3340 3350
RPYSTCTWVI AAPPQQQVQI TVWDLQLPSQ DCSQSYLELQ DSVQTGGNRV
3360 3370 3380 3390 3400
TQFCGANYTT LPVFYSSMST AVVVFKSGVL NRNSQVQFSY QIADCNREYN
3410 3420 3430 3440 3450
QTFGNLKSPG WPQNYDNNLD CTIILRAPQN HSISLFFYWF QLEDSRQCMN
3460 3470 3480 3490 3500
DFLEVRNGGS STSPLLDKYC SNLLPNPVFS QSNELYLHFH SDHSVTNNGY
3510 3520 3530 3540 3550
EIIWTSSAAG CGGTLLGDEG IFTNPGFPDS YPNNTHCEWT IVAPSGRPVS
3560 3570 3580 3590 3600
VGFPFLSIDS SGGCDQNYLI VFNGPDANSP PFGPLCGINT GIAPFYASSN
3610 3620
RVFIRFHAEY TTRLSGFEIM WSS
Length:3,623
Mass (Da):398,987
Last modified:January 1, 1999 - v2
<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:i39FB792AC6545240
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
F1LNU2F1LNU2_RAT
Cubilin
Cubn
3,623Annotation score:

Annotation score:3 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
AF022247 mRNA Translation: AAC71661.1

Protein sequence database of the Protein Information Resource

More...
PIRi
T08618

NCBI Reference Sequences

More...
RefSeqi
NP_445784.1, NM_053332.2

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Rn.3236

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
80848

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:80848

UCSC genome browser

More...
UCSCi
RGD:68355 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
AF022247 mRNA Translation: AAC71661.1
PIRiT08618
RefSeqiNP_445784.1, NM_053332.2
UniGeneiRn.3236

3D structure databases

ProteinModelPortaliO70244
SMRiO70244
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249486, 1 interactor
CORUMiO70244
STRINGi10116.ENSRNOP00000048477

PTM databases

iPTMnetiO70244
PhosphoSitePlusiO70244

Proteomic databases

PaxDbiO70244
PRIDEiO70244

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi80848
KEGGirno:80848
UCSCiRGD:68355 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
8029
RGDi68355 Cubn

Phylogenomic databases

eggNOGiKOG3714 Eukaryota
ENOG410ZPX7 LUCA
HOGENOMiHOG000173840
HOVERGENiHBG080357
InParanoidiO70244
KOiK14616
PhylomeDBiO70244

Miscellaneous databases

Protein Ontology

More...
PROi
PR:O70244

Family and domain databases

CDDicd00041 CUB, 27 hits
Gene3Di2.60.120.290, 27 hits
InterProiView protein in InterPro
IPR000859 CUB_dom
IPR001881 EGF-like_Ca-bd_dom
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR000152 EGF-type_Asp/Asn_hydroxyl_site
IPR018097 EGF_Ca-bd_CS
IPR024731 EGF_dom
IPR035914 Sperma_CUB_dom_sf
PfamiView protein in Pfam
PF00431 CUB, 27 hits
PF00008 EGF, 3 hits
PF12947 EGF_3, 1 hit
PF07645 EGF_CA, 3 hits
SMARTiView protein in SMART
SM00042 CUB, 27 hits
SM00181 EGF, 8 hits
SM00179 EGF_CA, 7 hits
SUPFAMiSSF49854 SSF49854, 27 hits
PROSITEiView protein in PROSITE
PS00010 ASX_HYDROXYL, 3 hits
PS01180 CUB, 27 hits
PS00022 EGF_1, 4 hits
PS01186 EGF_2, 2 hits
PS50026 EGF_3, 6 hits
PS01187 EGF_CA, 4 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiCUBN_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: O70244
<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 7, 2006
Last sequence update: January 1, 1999
Last modified: November 7, 2018
This is version 131 of the entry and version 2 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

Complete proteome, Direct protein sequencing, Reference proteome
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