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Entry version 155 (02 Dec 2020)
Sequence version 1 (01 May 2000)
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Protein

Cerebellin-1

Gene

Cbln1

Organism
Mus musculus (Mouse)
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

Required for synapse integrity and synaptic plasticity. During cerebellar synapse formation, essential for the matching and maintenance of pre- and post-synaptic elements at parallel fiber-Purkinje cell synapses, the establishment of the proper pattern of climbing fiber-Purkinje cell innervation, and induction of long-term depression at parallel fiber-Purkinje cell synapses (PubMed:16234806). Plays a role as a synaptic organizer that acts bidirectionally on both pre- and post-synaptic components (PubMed:20395510). On the one hand induces accumulation of synaptic vesicles in the pre-synaptic part by binding with NRXN1 and in other hand induces clustering of GRID2 and its associated proteins at the post-synaptic site through association of GRID2 (PubMed:21410790). NRXN1-CBLN1-GRID2 complex directly induces parallel fiber protrusions that encapsulate spines of Purkinje cells leading to accumulation of GRID2 and synaptic vesicles (PubMed:23141067). Required for CBLN3 export from the endoplasmic reticulum and secretion (PubMed:17030622, PubMed:17331201). NRXN1-CBLN1-GRID2 complex mediates the D-Serine-dependent long term depression signals and AMPA receptor endocytosis (By similarity). Essential for long-term maintenance but not establishment of excitatory synapses (PubMed:29691328). Inhibits the formation and function of inhibitory GABAergic synapses in cerebellar Purkinje cells (PubMed:24467251).By similarity8 Publications
The cerebellin peptide exerts neuromodulatory functions. Directly stimulates norepinephrine release via the adenylate cyclase/PKA-dependent signaling pathway; and indirectly enhances adrenocortical secretion in vivo, through a paracrine mechanism involving medullary catecholamine release (By similarity).By similarity

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

  • identical protein binding Source: MGI

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

LigandSialic acid

<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:
Cerebellin-1
Alternative name(s):
Brain protein D3
Precerebellin
Cleaved into the following 2 chains:
Cerebellin
Short name:
CER
[des-Ser1]-cerebellin
Short name:
des-Ser1-cerebellin
<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:Cbln1
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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: Chromosome 8

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:88281, Cbln1

<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 junction, Cell membrane, Membrane, Postsynaptic cell membrane, Secreted, Synapse

<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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mice (reeler, weaver and staggerer) show defects in granule cell migration and parallel fiber formation, synaptogenesis, Purkinje cell dendritic maturation and establishment of adult cytoarchitecture show a correlation between the formation and number of parallel fiber-Purkinje cell synapses and cerebellin levels (PubMed:3199194). CBLN1 single knockout mice show a major impairment in motor behaviors (PubMed:3420533). Double CBLN1 and CBLN2 knockout mice exhibit gait abnormalities, impairments in balance and coordination and develop seizures (PubMed:3420533). Synapse density in the hippocampus is normal in 1-2 months old mice, but severely decreased in 6 month old mice (PubMed:3420533). Triple CBLN1, CBLN2 and CBLN4 knockout mice exhibit impairments in sensory processing and sensorimotor gating, in addition to severe motor deficits, seizures and reduced synapse density in the hippocampus of aging mice (PubMed:3420533).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi23N → Q: No effect on its ability to form homohexameric or heteromeric complexes with other CBLN family members. Increased interaction with GRID2, NRXN1 and NRXN3. Loss of N-glycosylation; when associated with Q-79. 2 Publications1
Mutagenesisi34C → A: Abolishes homohexamer formation from homotrimers; when associated with A-38. 1 Publication1
Mutagenesisi38C → A: Abolishes homohexamer formation from homotrimers; when associated with A-34. 1 Publication1
Mutagenesisi79N → Q: No effect on its ability to form homohexameric or heteromeric complexes with other CBLN family members. Increased interaction with GRID2, NRXN1 and NRXN3. Loss of N-glycosylation; when associated with Q-23. 2 Publications1
Mutagenesisi110G → E: Retention in the endoplasmic reticulum/cis-Golgi; when associated with H-112. 1 Publication1
Mutagenesisi112Y → H: Retention in the endoplasmic reticulum/cis-Golgi; when associated with E-110. 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 – 21Sequence analysisAdd BLAST21
<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_000027421122 – 193Cerebellin-1Add BLAST172
<p>This subsection of the 'PTM / Processing' section describes the position and length of an active peptide in the mature protein.<p><a href='/help/peptide' target='_top'>More...</a></p>PeptideiPRO_000000354957 – 72CerebellinAdd BLAST16
PeptideiPRO_000027421258 – 72[des-Ser1]-cerebellinAdd BLAST15

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>Glycosylationi23N-linked (GlcNAc...) asparagine2 Publications1
<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 bondi34Interchain1 Publication
Disulfide bondi38Interchain1 Publication
Glycosylationi79N-linked (GlcNAc...) asparagine2 Publications1

<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 proteolytic processing to yield cerebellin seems to occur either prior to the secretion by presynaptic neurons and subsequent oligomerization or in some other location after release of the mature protein. In the cerebellum, cerebellin is much more abundant than [des-Ser1]-cerebellin.1 Publication
Sialoglycoprotein.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q9R171

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

More...
PaxDbi
Q9R171

PRoteomics IDEntifications database

More...
PRIDEi
Q9R171

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...
GlyGeni
Q9R171, 2 sites

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9R171

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

More...
PhosphoSitePlusi
Q9R171

<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 and secreted by presynaptic neurons, such as cerebellar granule cells. Following secretion, the protein binds to GRID2 on the postsynaptic Purkinje cell membranes. Expressed at the highest level in the cerebellar cortex. High levels are also seen in the olfactory bulb, posterior part of the cerebral cortex, certain thalamic nuclei, and deep cerebellar nuclei. Low to moderate levels are detected in some hypothalamic and brainstem nuclei. In the thalamus, expressed in parafascicular nucleus neurons and other regions (at protein level).6 Publications

<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

In the developing brain, expressed as early as embryonic day 10-13, and transiently up-regulated during the late embryonic and neonatal periods. Cerebellin and [des-Ser1]-cerebellin are expressed as easly as postnatal day 3-4. The levels of both peptides rise rapidly to a maximum at approximately day 25-30 after birth, whereafter they fall to stable adult values.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000031654, Expressed in cerebellum and 178 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q9R171, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9R171, MM

<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

Homohexamer; disulfide-linked homotrimers. The trimers are assembled via the globular C1q domains. The trimers associate via N-terminal cysteine residues to form disulfide-linked hexamers (PubMed:16135095). May form oligomers with CBLN2, CBLN3 AND CBLN4 prior to secretion (PubMed:29782851). Once secreted, does not interact with other CBLN family members (PubMed:17030622, PubMed:17331201, PubMed:10964938).

Interacts with GRID1 (PubMed:22220752).

Interacts with NRXN1 and NRXN2 long (alpha) and short (beta) isoforms produced by alternative promoter usage (PubMed:21410790, PubMed:22220752, PubMed:29782851). Competes with NLGN1 for NRXN1-binding. Weakly interacts with NRXN3 short isoform and not at all with NRXN3 long isoform (PubMed:21410790, PubMed:22220752, PubMed:29782851).

Interacts (via C1q domain) with GRID2; GRID2-binding is calcium-independent; CBLN1 hexamers anchor GRID2 N-terminal domain dimers to monomeric NRXN1 isoform beta; promotes synaptogenesis and mediates the D-Serine-dependent long term depression signals and AMPA receptor endocytosis (PubMed:20395510, PubMed:21410790, PubMed:22220752, PubMed:29782851).

Interacts with OTOL1 (PubMed:20856818).

9 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
198528, 2 interactors

Protein interaction database and analysis system

More...
IntActi
Q9R171, 3 interactors

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000034076

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q9R171, protein

<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

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SMRi
Q9R171

Database of comparative protein structure models

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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>Domaini57 – 193C1qPROSITE-ProRule annotationAdd BLAST137

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>Regioni34 – 38Essential for interaction with NRXN1 and linker of two C1q trimers into disulfide-linked hexamersBy similarity5
Regioni62 – 193Necessary for interaction with CBLN3, and homotrimerization1 PublicationAdd BLAST132
Regioni122 – 147Essential for interaction with GRID2By similarityAdd BLAST26

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG502QVN9, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00940000159811

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_001074_8_2_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9R171

Identification of Orthologs from Complete Genome Data

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OMAi
PARAQNE

Database of Orthologous Groups

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OrthoDBi
1398761at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9R171

TreeFam database of animal gene trees

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TreeFami
TF329591

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.120.40, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR001073, C1q_dom
IPR008983, Tumour_necrosis_fac-like_dom

Pfam protein domain database

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Pfami
View protein in Pfam
PF00386, C1q, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00007, COMPLEMNTC1Q

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00110, C1Q, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF49842, SSF49842, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50871, C1Q, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>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.

Q9R171-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLGVVELLLL GTAWLAGPAR GQNETEPIVL EGKCLVVCDS NPTSDPTGTA
60 70 80 90 100
LGISVRSGSA KVAFSAIRST NHEPSEMSNR TMIIYFDQVL VNIGNNFDSE
110 120 130 140 150
RSTFIAPRKG IYSFNFHVVK VYNRQTIQVS LMLNGWPVIS AFAGDQDVTR
160 170 180 190
EAASNGVLIQ MEKGDRAYLK LERGNLMGGW KYSTFSGFLV FPL
Length:193
Mass (Da):21,113
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:iA23C796C7D11BE5F
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence CAA43688 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti5V → L no nucleotide entry (PubMed:7877445).Curated1

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
AF164680 Genomic DNA Translation: AAD47280.1
X61448 mRNA Translation: CAA43688.1 Sequence problems.

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS22506.1

Protein sequence database of the Protein Information Resource

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PIRi
S16862

NCBI Reference Sequences

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RefSeqi
NP_062600.2, NM_019626.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000034076; ENSMUSP00000034076; ENSMUSG00000031654
ENSMUST00000169693; ENSMUSP00000126575; ENSMUSG00000031654

Database of genes from NCBI RefSeq genomes

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GeneIDi
12404

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:12404

UCSC genome browser

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UCSCi
uc009mqr.1, mouse

<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
AF164680 Genomic DNA Translation: AAD47280.1
X61448 mRNA Translation: CAA43688.1 Sequence problems.
CCDSiCCDS22506.1
PIRiS16862
RefSeqiNP_062600.2, NM_019626.3

3D structure databases

SMRiQ9R171
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi198528, 2 interactors
IntActiQ9R171, 3 interactors
STRINGi10090.ENSMUSP00000034076

PTM databases

GlyGeniQ9R171, 2 sites
iPTMnetiQ9R171
PhosphoSitePlusiQ9R171

Proteomic databases

MaxQBiQ9R171
PaxDbiQ9R171
PRIDEiQ9R171

Protocols and materials databases

Antibodypedia a portal for validated antibodies

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Antibodypediai
14491, 212 antibodies

Genome annotation databases

EnsembliENSMUST00000034076; ENSMUSP00000034076; ENSMUSG00000031654
ENSMUST00000169693; ENSMUSP00000126575; ENSMUSG00000031654
GeneIDi12404
KEGGimmu:12404
UCSCiuc009mqr.1, mouse

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
869
MGIiMGI:88281, Cbln1

Phylogenomic databases

eggNOGiENOG502QVN9, Eukaryota
GeneTreeiENSGT00940000159811
HOGENOMiCLU_001074_8_2_1
InParanoidiQ9R171
OMAiPARAQNE
OrthoDBi1398761at2759
PhylomeDBiQ9R171
TreeFamiTF329591

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
12404, 1 hit in 17 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
Cbln1, mouse

Protein Ontology

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PROi
PR:Q9R171
RNActiQ9R171, protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSMUSG00000031654, Expressed in cerebellum and 178 other tissues
ExpressionAtlasiQ9R171, baseline and differential
GenevisibleiQ9R171, MM

Family and domain databases

Gene3Di2.60.120.40, 1 hit
InterProiView protein in InterPro
IPR001073, C1q_dom
IPR008983, Tumour_necrosis_fac-like_dom
PfamiView protein in Pfam
PF00386, C1q, 1 hit
PRINTSiPR00007, COMPLEMNTC1Q
SMARTiView protein in SMART
SM00110, C1Q, 1 hit
SUPFAMiSSF49842, SSF49842, 1 hit
PROSITEiView protein in PROSITE
PS50871, C1Q, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiCBLN1_MOUSE
<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: Q9R171
Secondary accession number(s): P28655, Q9QVT5
<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: December 1, 2000
Last sequence update: May 1, 2000
Last modified: December 2, 2020
This is version 155 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

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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