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Entry version 120 (07 Oct 2020)
Sequence version 1 (01 May 2000)
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Protein

Cubilin

Gene

CUBN

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
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

Endocytic receptor which plays a role in lipoprotein, vitamin and iron metabolism by facilitating their uptake. Acts together with LRP2 to mediate endocytosis of high-density lipoproteins, GC, hemoglobin, ALB, TF and SCGB1A1. Acts together with AMN to mediate endocytosis of the CBLIF-cobalamin complex. Binds to ALB, MB, Kappa and lambda-light chains, TF, hemoglobin, GC, SCGB1A1, APOA1, high density lipoprotein, and the CBLIF-cobalamin complex. Ligand binding requires calcium. Serves as important transporter in several absorptive epithelia, including intestine, renal proximal tubules and embryonic yolk sac. 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.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi976Calcium 1By similarity1
Metal bindingi984Calcium 1By similarity1
Metal bindingi1023Calcium 1By similarity1
Metal bindingi1025Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi1026Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi1092Calcium 2By similarity1
Metal bindingi1102Calcium 2By similarity1
Metal bindingi1143Calcium 2By similarity1
Metal bindingi1210Calcium 3By similarity1
Metal bindingi1218Calcium 3By similarity1
Metal bindingi1259Calcium 3By similarity1
Metal bindingi1262Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi1325Calcium 4By similarity1
Metal bindingi1333Calcium 4By similarity1
Metal bindingi1370Calcium 4By similarity1
Metal bindingi1372Calcium 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

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%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:
Cubilin
<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:CUBN
<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>OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
<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 identifieri9615 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
<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
  • UP000002254 <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

<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

Keywords - Cellular componenti

Cell membrane, Coated pit, 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%5Fprocessing%5Fsection">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_000004607021 – 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000004607133 – 3620CubilinAdd BLAST3588

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Glycosylationi102N-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
Glycosylationi253N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi264 ↔ 277By similarity
Disulfide bondi271 ↔ 286By similarity
Disulfide bondi289 ↔ 300By similarity
Disulfide bondi306 ↔ 321By similarity
Disulfide bondi313 ↔ 330By similarity
Disulfide bondi333 ↔ 344By similarity
Disulfide bondi350 ↔ 363By similarity
Disulfide bondi357 ↔ 373By similarity
Disulfide bondi396 ↔ 406By similarity
Disulfide bondi401 ↔ 415By similarity
Disulfide bondi417 ↔ 426By similarity
Glycosylationi425N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi433 ↔ 444By similarity
Disulfide bondi438 ↔ 453By similarity
Disulfide bondi455 ↔ 464By similarity
Disulfide bondi471 ↔ 497By similarity
Disulfide bondi524 ↔ 546By similarity
Disulfide bondi587 ↔ 613By similarity
Disulfide bondi640 ↔ 662By similarity
Disulfide bondi705 ↔ 730By similarity
Glycosylationi708N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi745N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi757 ↔ 775By similarity
Glycosylationi777N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi813 ↔ 838By similarity
Glycosylationi853N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi865 ↔ 887By similarity
Disulfide bondi928 ↔ 954By similarity
Glycosylationi953N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi980N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi981 ↔ 1001By similarity
Disulfide bondi1044 ↔ 1070By similarity
Disulfide bondi1099 ↔ 1121By similarity
Disulfide bondi1162 ↔ 1188By similarity
Glycosylationi1165N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1214N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1215 ↔ 1237By similarity
Disulfide bondi1275 ↔ 1303By similarity
Glycosylationi1304N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1316N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1329N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1330 ↔ 1348By similarity
Disulfide bondi1388 ↔ 1414By similarity
Disulfide bondi1441 ↔ 1463By similarity
Glycosylationi1497N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1507 ↔ 1533By similarity
Glycosylationi1548N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1560 ↔ 1578By similarity
Disulfide bondi1617 ↔ 1644By similarity
Glycosylationi1643N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1672 ↔ 1694By similarity
Disulfide bondi1735 ↔ 1761By similarity
Disulfide bondi1788 ↔ 1809By similarity
Glycosylationi1799N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1816N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1882N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1902 ↔ 1924By similarity
Glycosylationi1961N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1975 ↔ 2003By similarity
Disulfide bondi2029 ↔ 2051By similarity
Glycosylationi2082N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2089 ↔ 2115By similarity
Glycosylationi2114N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2214 ↔ 2244By similarity
Disulfide bondi2272 ↔ 2294By similarity
Glycosylationi2317N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2333 ↔ 2360By similarity
Glycosylationi2383N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2387 ↔ 2408By similarity
Glycosylationi2397N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2449 ↔ 2475By similarity
Disulfide bondi2502 ↔ 2524By similarity
Glycosylationi2528N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2567 ↔ 2596By similarity
Glycosylationi2578N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2589N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2607N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2625 ↔ 2646By similarity
Disulfide bondi2686 ↔ 2712By similarity
Disulfide bondi2739 ↔ 2761By similarity
Disulfide bondi2802 ↔ 2828By similarity
Glycosylationi2810N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2857 ↔ 2880By similarity
Disulfide bondi2917 ↔ 2943By similarity
Glycosylationi2920N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2942N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2974 ↔ 2996By similarity
Glycosylationi2986N-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 residuei3005PhosphothreonineBy similarity1
Disulfide bondi3034 ↔ 3061By similarity
Glycosylationi3039N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3088 ↔ 3110By similarity
Glycosylationi3100N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi3122N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3154 ↔ 3182By similarity
Disulfide bondi3212 ↔ 3234By similarity
Glycosylationi3265N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3275 ↔ 3303By similarity
Glycosylationi3280N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi3292N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3329 ↔ 3351By similarity
Glycosylationi3354N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3392 ↔ 3418By similarity
Glycosylationi3427N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3445 ↔ 3467By similarity
Glycosylationi3454N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3508 ↔ 3534By similarity
Glycosylationi3530N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3561 ↔ 3583By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The precursor is cleaved by a trans-Golgi proteinase furin, removing a propeptide.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
Q9TU53

PRoteomics IDEntifications database

More...
PRIDEi
Q9TU53

<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

Detected in kidney cortex (at protein level). Detected in kidney, duodenum and jejunum.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%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with AMN (PubMed:15845892).

Component of the cubam complex composed of one CUBN trimer and one AMN chain (By similarity). The cubam complex can dimerize (By similarity).

Interacts with LRP2 in a dual-receptor complex in a calcium-dependent manner.

Found in a complex with PID1/PCLI1, LRP1 and CUBNI.

Interacts with LRP1 and PID1/PCLI1 (By similarity).

By similarity1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9612.ENSCAFP00000006833

<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
Q9TU53

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>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 – 382EGF-like 5PROSITE-ProRule annotationAdd BLAST37
Domaini392 – 427EGF-like 6PROSITE-ProRule annotationAdd BLAST36
Domaini429 – 465EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini471 – 583CUB 1PROSITE-ProRule annotationAdd BLAST113
Domaini587 – 699CUB 2PROSITE-ProRule annotationAdd BLAST113
Domaini705 – 812CUB 3PROSITE-ProRule annotationAdd BLAST108
Domaini813 – 924CUB 4PROSITE-ProRule annotationAdd BLAST112
Domaini928 – 1038CUB 5PROSITE-ProRule annotationAdd BLAST111
Domaini1044 – 1158CUB 6PROSITE-ProRule annotationAdd BLAST115
Domaini1162 – 1274CUB 7PROSITE-ProRule annotationAdd BLAST113
Domaini1275 – 1386CUB 8PROSITE-ProRule annotationAdd BLAST112
Domaini1388 – 1503CUB 9PROSITE-ProRule annotationAdd BLAST116
Domaini1507 – 1616CUB 10PROSITE-ProRule annotationAdd BLAST110
Domaini1617 – 1731CUB 11PROSITE-ProRule annotationAdd BLAST115
Domaini1735 – 1847CUB 12PROSITE-ProRule annotationAdd BLAST113
Domaini1849 – 1960CUB 13PROSITE-ProRule annotationAdd BLAST112
Domaini1975 – 2088CUB 14PROSITE-ProRule annotationAdd BLAST114
Domaini2089 – 2210CUB 15PROSITE-ProRule annotationAdd BLAST122
Domaini2214 – 2331CUB 16PROSITE-ProRule annotationAdd BLAST118
Domaini2333 – 2445CUB 17PROSITE-ProRule annotationAdd BLAST113
Domaini2449 – 2562CUB 18PROSITE-ProRule annotationAdd BLAST114
Domaini2567 – 2684CUB 19PROSITE-ProRule annotationAdd BLAST118
Domaini2686 – 2798CUB 20PROSITE-ProRule annotationAdd BLAST113
Domaini2802 – 2916CUB 21PROSITE-ProRule annotationAdd BLAST115
Domaini2917 – 3032CUB 22PROSITE-ProRule annotationAdd BLAST116
Domaini3034 – 3147CUB 23PROSITE-ProRule annotationAdd BLAST114
Domaini3154 – 3271CUB 24PROSITE-ProRule annotationAdd BLAST118
Domaini3275 – 3392CUB 25PROSITE-ProRule annotationAdd BLAST118
Domaini3392 – 3504CUB 26PROSITE-ProRule annotationAdd BLAST113
Domaini3508 – 3620CUB 27PROSITE-ProRule annotationAdd BLAST113

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>Regioni39 – 46Interaction with AMNBy similarity8

<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 CBLIF and ALB. CUB domains 1 and 2 mediate interaction with LRP2.By similarity
The cubam complex is composed of a 400 Angstrom long stem and a globular crown region. The stem region is probably formed by AMN and the CUBN N-terminal region, including the EGF-like domains. The crown is probably formed by the CUBN CUB domains.By similarity

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG4292, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9TU53

KEGG Orthology (KO)

More...
KOi
K14616

Database of Orthologous Groups

More...
OrthoDBi
4105at2759

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00041, CUB, 27 hits

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.120.290, 27 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000859, CUB_dom
IPR001881, EGF-like_Ca-bd_dom
IPR000742, EGF-like_dom
IPR000152, EGF-type_Asp/Asn_hydroxyl_site
IPR018097, EGF_Ca-bd_CS
IPR024731, EGF_dom
IPR009030, Growth_fac_rcpt_cys_sf
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

More...
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

More...
SUPFAMi
SSF49854, SSF49854, 27 hits
SSF57184, SSF57184, 1 hit

PROSITE; a protein domain and family database

More...
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, 7 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%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>Sequencei

<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.

Q9TU53-1 [UniParc]FASTAAdd to basket
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MSSPFLWSLI ILLTFAESNG EAGGFELQRQ KRSIDFQQPR MATERGNLVF
60 70 80 90 100
LVGSAQNIEF RTGSLGKIKL NEEDLGECLH QIQKNKEDIT DLKRSAVNVP
110 120 130 140 150
QNISSQIHQL NSKLVDLERK FQSLQQTVDK KVCSSNPCQN GGTCLNLHDS
160 170 180 190 200
FFCICPSQWK GPLCSVDVNE CQIYSGTPLG CQNGATCENT AGSYSCLCSP
210 220 230 240 250
ETHGPQCASK YDDCEGGSKA LCVHGICEDL VRVKADEPKY NCICDAGWTS
260 270 280 290 300
PLNSSACVLD IDECNLQHAP CSPLVQCFNT QGSFYCGACP TGWQGNGYSC
310 320 330 340 350
QDIDECKINN GGCSVVPPVM CVNTLGSYHC QACPPGYQGD GRVCTVIDIC
360 370 380 390 400
SVNNGGCHPE ASCSSVLGSL PLCTCLPGYT GNGYGPNGCA QLSDTCLSHP
410 420 430 440 450
CLNGQCIETV SGYLCKCESG WAGINCTENI NECLSNPCFN GGTCVDGVNA
460 470 480 490 500
FSCECTRFWT GFLCQIPQQV CGGSLSGMDG SFSYMSPDVG YVHDVNCFWV
510 520 530 540 550
IRTEDRKVLR ITFTFFQLES VNNCPHEFLQ IHDGDSSAAL QLGRFCGSVL
560 570 580 590 600
PHELLSSNNA LYFHLYSEHF RSGRGFTIRW ETQQPECGGI LMGTYGSIKS
610 620 630 640 650
PGYPGNYPPG RDCVWQVVTS PDLLITFTFG TLSLEHHDDC SKDYLEIRDG
660 670 680 690 700
PLYQDPSLGK FCTTLSVPPL QTTGPFARVH FHSDNQINDQ GFHITYLTSP
710 720 730 740 750
SDLHCGGNYT DPEGLLSSDL SGPFTHNRQC IYIIKQPLGE QIQVNFTHVE
760 770 780 790 800
LEGQSSCSQS HIEVRDDKIL LGKVCDNETL PHIKSIRNHI WIRLKIDASL
810 820 830 840 850
VRASFRAVYQ VACGGELTGE GVIRSPFYPN VYPGERICRW TIHQPQSQVV
860 870 880 890 900
ILNFTAFGIE SSAHCDTDYI EIGSSSILGS PENKKYCGTD IPLFITSVYN
910 920 930 940 950
FLYVIFVKSS STENHGFMAK FSAADLACGE ILTESTGIIQ SPGHPNIYPH
960 970 980 990 1000
GINCTWHILV QPGHLIHLIF RKFHLEFHYN CTNDYLEVYD TGSNTYLGRY
1010 1020 1030 1040 1050
CGKSIPPSLT SSTNSLKLIF VADSDLAYEG FLINYEATDA SSACMEDYTE
1060 1070 1080 1090 1100
NSGTFTSPNF PNNYPNNWKC IYRITVETSQ QIALHFTNFA LEEAIGGQCV
1110 1120 1130 1140 1150
ADFVEIRDGG YETSPPLGTY CGSIPPPRII SHSNKLWLQF TSDFLGSGPG
1160 1170 1180 1190 1200
FSAYWDGSLT GCGGNITTPT GVFTSPSYPM PYYHSSECYW LLKASHGSPF
1210 1220 1230 1240 1250
ELEFEDFHLE HHPNCTLDYL AVYDGPSTSS HLLSQLCGNE KPPVIRSTGD
1260 1270 1280 1290 1300
SMFLKFRTDE DQQGGGFLAK YQQTCRNVVI VNRNYGILES IHYPNPYSDN
1310 1320 1330 1340 1350
QRCNWTIQAT TGNTVNYTFL AFELENHINC STDYLELYDG PRRMGRYCGA
1360 1370 1380 1390 1400
DMPPTGSTTG SKLQVLFYTD GVGHQEKGFQ MQWFIHGCGG ELSGTTGSFS
1410 1420 1430 1440 1450
SPGYPNTYPP NKECIWYITT APGSSIQLTI HDFDVEYHAR CNFDVLEVYG
1460 1470 1480 1490 1500
GPDFHSPRIT QLCSQRSSEN PMQVSSTGNE LAIRFKTDSS INGRGFNASW
1510 1520 1530 1540 1550
QAVPGGCGGI FQAPNGEIHS PNYPSPYRGN TDCSWVIRVE RNHRILLNFT
1560 1570 1580 1590 1600
DFDLEPQDSC ITAYDGLSST TTRLASVCGR QQLTNPITSS GNSLFLRFQS
1610 1620 1630 1640 1650
GPSRQGRGFR AQFNQVCGGH ILTNSFDTIS SPLFPAKYPN NQNCSWVIQA
1660 1670 1680 1690 1700
QPPFNHITLS FDHFGLESST TCTQDFLEIL DGDYDDAPLR GRYCGHSMPH
1710 1720 1730 1740 1750
PITSFSSALT LRFVSDSRVN SDGFHATYAA SSSACGGTFH MAEGIFNSPG
1760 1770 1780 1790 1800
YPEVYPSNVE CVWNIVSSPG NRLQLSFITF QLEDSQDCSR DFVEVREGNA
1810 1820 1830 1840 1850
TGHLVGRYCG NVLPLNYSSI VGHILWIRFV SDGSGSGTGF QATFTKIFGN
1860 1870 1880 1890 1900
DNIVGTHGKI ASPLWPGRYP HNSNYQWIVN VNATQVIHGR ILEIDIEGAQ
1910 1920 1930 1940 1950
SCYYDKLRVY DGLGIHSRLI GTYCGTQTTS FSSSRNSLTF QFSSDSSITG
1960 1970 1980 1990 2000
KGFLLEWFAV NASGGPLPTI ATGACGGFLR TGDAPVFLFS PGWPESYSNS
2010 2020 2030 2040 2050
ADCTWLIQAP DSTVELNILS LDIEAQRTCD YDKLVIRDGD SNLAPQLAVL
2060 2070 2080 2090 2100
CGREIPGPIR STGEYMFIRF TSDFSITGAG FNASFHKSCG GYLHADRGII
2110 2120 2130 2140 2150
TSPQYPETYS PNLNCSWHVL VQSGLTIAVH FEQPFQIPSG DSSCSQGDYL
2160 2170 2180 2190 2200
VLKNGPDIYS PPLGPYGRNG HFCGSRPSST LFTSDNQMFV QFISDGSNGG
2210 2220 2230 2240 2250
QGFKIKYEAK SLACGGNIYI HDVNSAGYVT SPGHPNNYPQ HADCNWLIAA
2260 2270 2280 2290 2300
PPGKLIRVQF EDQFNIEETP NCVSNYLELR DGVDSNAPLL AKLCGRSLPS
2310 2320 2330 2340 2350
SQLSSGEVMY LRFRSDNSST QVGFKIKYAI AQCGGRVTGQ SGIIESSGYP
2360 2370 2380 2390 2400
TLPYRDNSFC EWHLKGPSGH YLTIHFEDFH LQNSSGCEKD FVEIWENHTS
2410 2420 2430 2440 2450
GNLLGRYCGN TIPDSIDTSS NVALVRFVTD GSVTASGFRL RFESSMEACG
2460 2470 2480 2490 2500
GELQGPTGTF TSPNYPNPNP HGRVCEWRIM VQEGRRITLT FNNLRLEAHP
2510 2520 2530 2540 2550
SCYSEHVTIF NGIRNNSPQL EKLCGSVNAS SEIKSSGNTM KVVFFTDGSR
2560 2570 2580 2590 2600
PFGGFSATYT SSEDAVCGGS LTHFPEGNFT SPGYNGVSNY SRNLNCEWTL
2610 2620 2630 2640 2650
SNPNQGNSSI YIHFEDFYLE SHQDCQFDVL EFRVGNADGP LMWRLCGPSK
2660 2670 2680 2690 2700
PIVPLVIPYP EVWIHFVTNE HVEHVGFHAE YSFTDCGGIQ LGESGVIASP
2710 2720 2730 2740 2750
NYPASYDSLT HCSWLLEAPQ GFTITLTFSD FDIEDHATCA WDSVSVRNGG
2760 2770 2780 2790 2800
SPGSPIIGQY CGTSNPRTIQ SGSNQLVVIF NSDHSVQNGG FYATWNTQTL
2810 2820 2830 2840 2850
GCGGILHSDN GTIRSPHWPQ NFPENSRCSW TVITHESKQL EISFDNNFRI
2860 2870 2880 2890 2900
PSGDGQCQNS FVKVWAGTEE VAESLLATGC GNVAPGSILT PRNVFIAVFQ
2910 2920 2930 2940 2950
SQETPAQGFS ASFVSRCGGN FTNPSGYILS PNYPRQYDNN MNCTYIIEAD
2960 2970 2980 2990 3000
PLSVVLLTFE SFHLEARSAI TGSCANDGVH IIRGSNLSST PFATVCGNEI
3010 3020 3030 3040 3050
LSPVTILGPV LLNFYSNAHT TDLGFKFNYK ITSCGGVFNV STGVIKSPAY
3060 3070 3080 3090 3100
SYSDYPNNIY CLYTIVGRDD RVVQLKFSDF DVVPSTFCSQ DYLAIYDGSN
3110 3120 3130 3140 3150
ISDPLLGKFC GSNLPPNIKS SNHSMLLVFK TDSFQTARGW KITFQQTLGP
3160 3170 3180 3190 3200
QQGCGGYLTG SDNTFASPDS DSNGRYDKNL NCVWFIIAPV NKLIKLTFNT
3210 3220 3230 3240 3250
FALEAQSAMQ RCIYDYVKLY DGDSENANLA GTFCGSTVPA PFISSGNFLT
3260 3270 3280 3290 3300
VQFVSDVTLE REGFNATYTT VDMPCGGTYN ATWTPQSISS PNSSNPEVPL
3310 3320 3330 3340 3350
SMCMWFLEAP PHQQVKITVW ALELHSQDCD QNYLEFRDSP ESNGSPGPQI
3360 3370 3380 3390 3400
CGRNASATPT FYSSRSTAIV IFKSEVLNRN SRVGFTYQIA GCNREYNKAF
3410 3420 3430 3440 3450
GNLKSPGWPD NYDNNLDCTV ILTAPQNHTI SLFFHSFGIE DSSECTHDFL
3460 3470 3480 3490 3500
EVRNGSDSSS PLFGTYCGTL LPDPIFSRNN KLYLRFKTDS ATSNRGYEIV
3510 3520 3530 3540 3550
WTSSPSGCGG TLYGDSGSFT SPGYPGTYPN NTDCEWAIIA PAGRPVTVTF
3560 3570 3580 3590 3600
YFISIDDPGD CVQNYLILYD GPDANSPSFG PYCGADTNIA PFVASSHRVF
3610 3620
IKFHAEYAVY PSAIRLTWDS
Length:3,620
Mass (Da):397,435
Last modified:May 1, 2000 - 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:i00B041EE6AD07348
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF137068 mRNA Translation: AAF14258.1

NCBI Reference Sequences

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RefSeqi
NP_001003148.1, NM_001003148.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
403767

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
cfa:403767

<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
AF137068 mRNA Translation: AAF14258.1
RefSeqiNP_001003148.1, NM_001003148.1

3D structure databases

SMRiQ9TU53
ModBaseiSearch...

Protein-protein interaction databases

STRINGi9612.ENSCAFP00000006833

Proteomic databases

PaxDbiQ9TU53
PRIDEiQ9TU53

Genome annotation databases

GeneIDi403767
KEGGicfa:403767

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
8029

Phylogenomic databases

eggNOGiKOG4292, Eukaryota
InParanoidiQ9TU53
KOiK14616
OrthoDBi4105at2759

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
IPR000742, EGF-like_dom
IPR000152, EGF-type_Asp/Asn_hydroxyl_site
IPR018097, EGF_Ca-bd_CS
IPR024731, EGF_dom
IPR009030, Growth_fac_rcpt_cys_sf
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
SSF57184, SSF57184, 1 hit
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, 7 hits
PS01187, EGF_CA, 4 hits

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 nameiCUBN_CANLF
<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: Q9TU53
<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: February 7, 2006
Last sequence update: May 1, 2000
Last modified: October 7, 2020
This is version 120 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
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