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Entry version 143 (08 May 2019)
Sequence version 2 (02 May 2002)
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Protein

Amyloid-beta-like protein

Gene

apl-1

Organism
Caenorhabditis elegans
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 normal developmental progression throughout all life stages (PubMed:18262516, PubMed:22466039). Specifically required for the molt stage during all larval transitions and morphogenesis (PubMed:18262516, PubMed:17267616, PubMed:22466039). Acts with heterochronic genes, including members of the let-7 family, to regulate larval stage to adult transition (PubMed:18262516, PubMed:28933985). Acts synergistically with acn-1 in let-7 regulated postembryonic cell division of hypodermal seam cells (PubMed:28933985). Acts in multiple pathways to influence daf-12 and daf-16 activity to in turn regulate physiological and reproductive processes such as body size and egg-laying (PubMed:22466039). May play a role in neurotransmission (PubMed:20862215).5 Publications

Miscellaneous

Lacks conserved metal-binding sites and has only weak affinity for copper in vitro.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei382Heparin1 Publication1

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

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDevelopmental protein
Biological processDifferentiation, Neurogenesis

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-CEL-114608 Platelet degranulation
R-CEL-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-CEL-416476 G alpha (q) signalling events
R-CEL-418594 G alpha (i) signalling events
R-CEL-8957275 Post-translational protein phosphorylation
R-CEL-9609523 Insertion of tail-anchored proteins into the endoplasmic reticulum membrane

<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:
Amyloid-beta-like proteinCurated
<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:apl-1Imported
ORF Names:C42D8.8Imported
<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>OrganismiCaenorhabditis elegans
<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 identifieri6239 [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 lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditinaRhabditomorphaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
<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
  • UP000001940 <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: Chromosome X

Organism-specific databases

WormBase

More...
WormBasei
C42D8.8a ; CE04209 ; WBGene00000149 ; apl-1
C42D8.8b ; CE27845 ; WBGene00000149 ; apl-1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini22 – 621ExtracellularSequence analysisAdd BLAST600
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei622 – 642HelicalSequence analysisAdd BLAST21
Topological domaini643 – 686CytoplasmicSequence analysisAdd BLAST44

Keywords - Cellular componenti

Amyloid, Endosome, Membrane

<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

Larval lethality during the L1 stage, with the formation of vacuoles in syncytial hypoderm, organ morphology defects, and molting defects (PubMed:17267616, PubMed:20862215). RNAi-mediated knockdown results in a reduced body size, transparent appearance, sluggish movement and insensitivity to touch (PubMed:18262516, PubMed:20862215). Delayed development and a molting defect that begins at the L3 to L4 larval stage transition and continues through to transition from the L4 larval stage to the young adult stage (PubMed:20862215). Increased sensitivity to acetylcholine inhibition (PubMed:20862215). Increased pharyngeal pumping (PubMed:11896189). In a let-7 mutant background, partial suppression of the let-7 bursting vulva phenotype (PubMed:28933985). Double RNAi-mediated knockdown with acn-1 in a let-7 mutant background leads to complete suppression of the heterochronic seam cell defects (PubMed:28933985).5 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi252N → A: Reduced heparin binding. 1 Publication1
Mutagenesisi254H → A: Reduced heparin binding. 1 Publication1
Mutagenesisi254H → P: Reduced heparin binding. 1 Publication1
Mutagenesisi348D → C: Results in destabilized protein structure; when associated with C-368 and K-377. 1 Publication1
Mutagenesisi368S → C: Results in destabilized protein structure; when associated with C-348 and K-377. 1 Publication1
Mutagenesisi374R → A: Reduced heparin binding; when associated with A-378. 1 Publication1
Mutagenesisi377E → K in yn32: Results in lethality and destabilized protein structure. 2 Publications1
Mutagenesisi378K → A: Reduced heparin binding; when associated with A-374. 1 Publication1
Mutagenesisi382H → A: Moderately reduced heparin binding. 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000020122 – 686Amyloid-beta-like proteinCuratedAdd BLAST665

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi42 ↔ 65PROSITE-ProRule annotation
Disulfide bondi76 ↔ 119PROSITE-ProRule annotation
<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>Glycosylationi84N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi101 ↔ 108PROSITE-ProRule annotation
Disulfide bondi135 ↔ 195PROSITE-ProRule annotation2 Publications
Disulfide bondi146 ↔ 182PROSITE-ProRule annotation2 Publications
Disulfide bondi160 ↔ 194PROSITE-ProRule annotation2 Publications
Glycosylationi201N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi249N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi417N-linked (GlcNAc...) asparagineSequence analysis1

<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

Extracellular region is proteolytically cleaved.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q10651

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

More...
PaxDbi
Q10651

PeptideAtlas

More...
PeptideAtlasi
Q10651

PRoteomics IDEntifications database

More...
PRIDEi
Q10651

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q10651

<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 in the head, pharynx, spermatheca, uterus, vulva, tail and ventral neurons (PubMed:18262516). Specifically expressed in nerve ring interneurons, the ventral cord, socket and amphids in the head, with strong expression in junctional cells, including the pharyngeal intestinal valve and uterine seam junction, and the excretory cell and weak expression in epidermal epithelial cells, including hyp7 cells, vulval cells, rectal valve cells, pharyngeal arcade cells and the tail hypodermis (PubMed:20862215).2 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

Similar expression pattern in larval and adult cells with expression in neuronal, muscle, hypodermal and supporting cells (PubMed:17267616). Temporally expressed in seam cells from the middle of larval stage L4 and throughout adult stages (PubMed:18262516, PubMed:28933985).3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
WBGene00000149 Expressed in 4 organ(s), highest expression level in pharyngeal muscle cell (C elegans)

<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

Interacts (via cytoplasmic domain) with feh-1 (via PID 2 domain).1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
45718, 1 interactor

Database of interacting proteins

More...
DIPi
DIP-25431N

STRING: functional protein association networks

More...
STRINGi
6239.C42D8.8a

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1686
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2M05NMR-A135-197[»]
3K66X-ray2.70A240-478[»]
3K6BX-ray2.80A240-478[»]

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

More...
SMRi
Q10651

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q10651

<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>Domaini32 – 197E1PROSITE-ProRule annotationAdd BLAST166
Domaini240 – 440E2PROSITE-ProRule annotationAdd BLAST201

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>Regioni32 – 125GFLD subdomainPROSITE-ProRule annotationAdd BLAST94
Regioni133 – 197CuBD subdomainPROSITE-ProRule annotationAdd BLAST65
Regioni252 – 255Heparin-binding1 Publication4

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi676 – 679Clathrin-bindingSequence analysis4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi205 – 228Asp-richAdd BLAST24

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

Belongs to the APP family.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3540 Eukaryota
ENOG410ZW2A LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00530000063252

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000272569

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q10651

KEGG Orthology (KO)

More...
KOi
K04520

Identification of Orthologs from Complete Genome Data

More...
OMAi
KQCKTHA

Database of Orthologous Groups

More...
OrthoDBi
953529at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q10651

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.20.120.770, 1 hit
2.30.29.30, 1 hit
3.30.1490.140, 1 hit
3.90.570.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR036669 Amyloid_Cu-bd_sf
IPR008155 Amyloid_glyco
IPR011178 Amyloid_glyco_Cu-bd
IPR024329 Amyloid_glyco_E2_domain
IPR008154 Amyloid_glyco_extra
IPR015849 Amyloid_glyco_heparin-bd
IPR036454 Amyloid_glyco_heparin-bd_sf
IPR019745 Amyloid_glyco_intracell_CS
IPR019543 APP_amyloid_C
IPR019744 APP_CUBD_CS
IPR036176 E2_sf
IPR011993 PH-like_dom_sf

The PANTHER Classification System

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PANTHERi
PTHR23103 PTHR23103, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF10515 APP_amyloid, 1 hit
PF12924 APP_Cu_bd, 1 hit
PF12925 APP_E2, 1 hit
PF02177 APP_N, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00203 AMYLOIDA4

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00006 A4_EXTRA, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF109843 SSF109843, 1 hit
SSF56491 SSF56491, 1 hit
SSF89811 SSF89811, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00319 APP_CUBD, 1 hit
PS51869 APP_E1, 1 hit
PS51870 APP_E2, 1 hit
PS00320 APP_INTRA, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)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 describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform a (identifier: Q10651-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MTVGKLMIGL LIPILVATVY AEGSPAGSKR HEKFIPMVAF SCGYRNQYMT
60 70 80 90 100
EEGSWKTDDE RYATCFSGKL DILKYCRKAY PSMNITNIVE YSHEVSISDW
110 120 130 140 150
CREEGSPCKW THSVRPYHCI DGEFHSEALQ VPHDCQFSHV NSRDQCNDYQ
160 170 180 190 200
HWKDEAGKQC KTKKSKGNKD MIVRSFAVLE PCALDMFTGV EFVCCPNDQT
210 220 230 240 250
NKTDVQKTKE DEDDDDDEDD AYEDDYSEES DEKDEEEPSS QDPYFKIANW
260 270 280 290 300
TNEHDDFKKA EMRMDEKHRK KVDKVMKEWG DLETRYNEQK AKDPKGAEKF
310 320 330 340 350
KSQMNARFQK TVSSLEEEHK RMRKEIEAVH EERVQAMLNE KKRDATHDYR
360 370 380 390 400
QALATHVNKP NKHSVLQSLK AYIRAEEKDR MHTLNRYRHL LKADSKEAAA
410 420 430 440 450
YKPTVIHRLR YIDLRINGTL AMLRDFPDLE KYVRPIAVTY WKDYRDEVSP
460 470 480 490 500
DISVEDSELT PIIHDDEFSK NAKLDVKAPT TTAKPVKETD NAKVLPTEAS
510 520 530 540 550
DSEEEADEYY EDEDDEQVKK TPDMKKKVKV VDIKPKEIKV TIEEEKKAPK
560 570 580 590 600
LVETSVQTDD EDDDEDSSSS TSSESDEDED KNIKELRVDI EPIIDEPASF
610 620 630 640 650
YRHDKLIQSP EVERSASSVF QPYVLASAMF ITAICIIAFA ITNARRRRAM
660 670 680
RGFIEVDVYT PEERHVAGMQ VNGYENPTYS FFDSKA
Length:686
Mass (Da):79,435
Last modified:May 2, 2002 - 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:iA0816858FDD48608
GO
Isoform b (identifier: Q10651-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     538-539: Missing.

Note: No experimental confirmation available.
Show »
Length:684
Mass (Da):79,193
Checksum:i2E86C4ABD2CD0C59
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 AAC46470 differs from that shown. Reason: Erroneous initiation.Curated

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_000017538 – 539Missing in isoform b. Curated2

Sequence databases

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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

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DDBJi
Links Updated
FO080659 Genomic DNA Translation: CCD65568.1
FO080659 Genomic DNA Translation: CCD65569.1
U00240 mRNA Translation: AAC46470.1 Different initiation.

Protein sequence database of the Protein Information Resource

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PIRi
T15795

NCBI Reference Sequences

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RefSeqi
NP_508870.3, NM_076469.5 [Q10651-1]
NP_508871.1, NM_076470.4 [Q10651-2]

Genome annotation databases

Ensembl metazoan genome annotation project

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EnsemblMetazoai
C42D8.8a; C42D8.8a; WBGene00000149 [Q10651-1]
C42D8.8b; C42D8.8b; WBGene00000149 [Q10651-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
180783

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
cel:CELE_C42D8.8

UCSC genome browser

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UCSCi
C42D8.8a c. elegans [Q10651-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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
FO080659 Genomic DNA Translation: CCD65568.1
FO080659 Genomic DNA Translation: CCD65569.1
U00240 mRNA Translation: AAC46470.1 Different initiation.
PIRiT15795
RefSeqiNP_508870.3, NM_076469.5 [Q10651-1]
NP_508871.1, NM_076470.4 [Q10651-2]

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2M05NMR-A135-197[»]
3K66X-ray2.70A240-478[»]
3K6BX-ray2.80A240-478[»]
SMRiQ10651
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi45718, 1 interactor
DIPiDIP-25431N
STRINGi6239.C42D8.8a

PTM databases

iPTMnetiQ10651

Proteomic databases

EPDiQ10651
PaxDbiQ10651
PeptideAtlasiQ10651
PRIDEiQ10651

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiC42D8.8a; C42D8.8a; WBGene00000149 [Q10651-1]
C42D8.8b; C42D8.8b; WBGene00000149 [Q10651-2]
GeneIDi180783
KEGGicel:CELE_C42D8.8
UCSCiC42D8.8a c. elegans [Q10651-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
180783
WormBaseiC42D8.8a ; CE04209 ; WBGene00000149 ; apl-1
C42D8.8b ; CE27845 ; WBGene00000149 ; apl-1

Phylogenomic databases

eggNOGiKOG3540 Eukaryota
ENOG410ZW2A LUCA
GeneTreeiENSGT00530000063252
HOGENOMiHOG000272569
InParanoidiQ10651
KOiK04520
OMAiKQCKTHA
OrthoDBi953529at2759
PhylomeDBiQ10651

Enzyme and pathway databases

ReactomeiR-CEL-114608 Platelet degranulation
R-CEL-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-CEL-416476 G alpha (q) signalling events
R-CEL-418594 G alpha (i) signalling events
R-CEL-8957275 Post-translational protein phosphorylation
R-CEL-9609523 Insertion of tail-anchored proteins into the endoplasmic reticulum membrane

Miscellaneous databases

EvolutionaryTraceiQ10651

Protein Ontology

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PROi
PR:Q10651

Gene expression databases

BgeeiWBGene00000149 Expressed in 4 organ(s), highest expression level in pharyngeal muscle cell (C elegans)

Family and domain databases

Gene3Di1.20.120.770, 1 hit
2.30.29.30, 1 hit
3.30.1490.140, 1 hit
3.90.570.10, 1 hit
InterProiView protein in InterPro
IPR036669 Amyloid_Cu-bd_sf
IPR008155 Amyloid_glyco
IPR011178 Amyloid_glyco_Cu-bd
IPR024329 Amyloid_glyco_E2_domain
IPR008154 Amyloid_glyco_extra
IPR015849 Amyloid_glyco_heparin-bd
IPR036454 Amyloid_glyco_heparin-bd_sf
IPR019745 Amyloid_glyco_intracell_CS
IPR019543 APP_amyloid_C
IPR019744 APP_CUBD_CS
IPR036176 E2_sf
IPR011993 PH-like_dom_sf
PANTHERiPTHR23103 PTHR23103, 1 hit
PfamiView protein in Pfam
PF10515 APP_amyloid, 1 hit
PF12924 APP_Cu_bd, 1 hit
PF12925 APP_E2, 1 hit
PF02177 APP_N, 1 hit
PRINTSiPR00203 AMYLOIDA4
SMARTiView protein in SMART
SM00006 A4_EXTRA, 1 hit
SUPFAMiSSF109843 SSF109843, 1 hit
SSF56491 SSF56491, 1 hit
SSF89811 SSF89811, 1 hit
PROSITEiView protein in PROSITE
PS00319 APP_CUBD, 1 hit
PS51869 APP_E1, 1 hit
PS51870 APP_E2, 1 hit
PS00320 APP_INTRA, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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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 nameiA4_CAEEL
<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: Q10651
Secondary accession number(s): Q18583, Q95ZX1
<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: May 2, 2002
Last sequence update: May 2, 2002
Last modified: May 8, 2019
This is version 143 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 programCaenorhabditis annotation project

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
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