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Protein

Presenilin sel-12

Gene

sel-12

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors (lin-12 or glp-1). Provides the major presenilin function compared to hop-1 and spe-4. Required cell-autonomously for correct neurite connectivity of the AIY cholinergic interneurons and their correct functioning in thermotaxis. Required for mesodermal patterning of muscle function.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei226 – 2261By similarity
Active sitei364 – 3641By similarity

GO - Molecular functioni

GO - Biological processi

  • apical protein localization Source: WormBase
  • cell fate specification Source: WormBase
  • detection of temperature stimulus Source: UniProtKB
  • nervous system development Source: UniProtKB
  • Notch signaling pathway Source: UniProtKB
  • oviposition Source: WormBase
  • positive regulation of Notch signaling pathway Source: WormBase
  • post-embryonic organ morphogenesis Source: WormBase
  • protein processing Source: InterPro
  • regulation of transforming growth factor beta receptor signaling pathway Source: WormBase
Complete GO annotation...

Keywords - Biological processi

Notch signaling pathway

Enzyme and pathway databases

ReactomeiR-CEL-3928665. EPH-ephrin mediated repulsion of cells.
SignaLinkiP52166.

Protein family/group databases

MEROPSiA22.009.

Names & Taxonomyi

Protein namesi
Recommended name:
Presenilin sel-12
Alternative name(s):
Suppressor/enhancer of lin-12 protein 12
Gene namesi
Name:sel-12
ORF Names:F35H12.3
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome X

Organism-specific databases

WormBaseiF35H12.3; CE24946; WBGene00004769; sel-12.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4545CytoplasmicSequence analysisAdd
BLAST
Transmembranei46 – 6621HelicalSequence analysisAdd
BLAST
Topological domaini67 – 10135LumenalSequence analysisAdd
BLAST
Transmembranei102 – 12221HelicalSequence analysisAdd
BLAST
Topological domaini123 – 1308CytoplasmicSequence analysis
Transmembranei131 – 15121HelicalSequence analysisAdd
BLAST
Topological domaini152 – 16312LumenalSequence analysisAdd
BLAST
Transmembranei164 – 18421HelicalSequence analysisAdd
BLAST
Topological domaini185 – 1895CytoplasmicSequence analysis
Transmembranei190 – 21021HelicalSequence analysisAdd
BLAST
Topological domaini211 – 2122LumenalSequence analysis
Transmembranei213 – 23321HelicalSequence analysisAdd
BLAST
Topological domaini234 – 359126CytoplasmicSequence analysisAdd
BLAST
Transmembranei360 – 38021HelicalSequence analysisAdd
BLAST
Topological domaini381 – 3844LumenalSequence analysis
Transmembranei385 – 40521HelicalSequence analysisAdd
BLAST
Topological domaini406 – 4138CytoplasmicSequence analysis
Intramembranei414 – 43421HelicalSequence analysisAdd
BLAST
Topological domaini435 – 44410CytoplasmicSequence analysis

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • gamma-secretase complex Source: WormBase
  • Golgi membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • perinuclear region of cytoplasm Source: WormBase
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi60 – 601C → S in ar131; egg-laying-defective. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 444444Presenilin sel-12PRO_0000073903Add
BLAST

Proteomic databases

EPDiP52166.
PaxDbiP52166.
PRIDEiP52166.

Expressioni

Tissue specificityi

Expressed in most neurons.1 Publication

Developmental stagei

Expressed both maternally and zygotically. Ubiquitously expressed throughout the development and in the adult.1 Publication

Interactioni

Subunit structurei

Homodimer. Component of the gamma-secretase complex, a complex probably composed of the presenilin homodimer (sel-12, hop-1 or spe-4), nicastrin (aph-2), aph-1 and pen-2 (Probable). Interacts with sel-10 (PubMed:9861048).Curated1 Publication

Protein-protein interaction databases

BioGridi45394. 56 interactions.
STRINGi6239.F35H12.3.

Structurei

3D structure databases

ProteinModelPortaliP52166.
SMRiP52166. Positions 46-231, 326-438.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi410 – 4123PAL

Domaini

The PAL motif is required for normal active site conformation.By similarity

Sequence similaritiesi

Belongs to the peptidase A22A family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2736. Eukaryota.
ENOG410XPZD. LUCA.
GeneTreeiENSGT00390000016593.
HOGENOMiHOG000240228.
InParanoidiP52166.
KOiK04505.
OMAiERQENIP.
OrthoDBiEOG7NGQBG.
PhylomeDBiP52166.

Family and domain databases

InterProiIPR001686. Pept_A22A_Ceel.
IPR001108. Peptidase_A22A.
IPR006639. Preselin/SPP.
[Graphical view]
PANTHERiPTHR10202. PTHR10202. 1 hit.
PfamiPF01080. Presenilin. 1 hit.
[Graphical view]
PRINTSiPR01072. PRESENILIN.
PR01075. PRESENILNSEL.
SMARTiSM00730. PSN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P52166-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSTRRQQEG GGADAETHTV YGTNLITNRN SQEDENVVEE AELKYGASHV
60 70 80 90 100
IHLFVPVSLC MALVVFTMNT ITFYSQNNGR HLLYTPFVRE TDSIVEKGLM
110 120 130 140 150
SLGNALVMLC VVVLMTVLLI VFYKYKFYKL IHGWLIVSSF LLLFLFTTIY
160 170 180 190 200
VQEVLKSFDV SPSALLVLFG LGNYGVLGMM CIHWKGPLRL QQFYLITMSA
210 220 230 240 250
LMALVFIKYL PEWTVWFVLF VISVWDLVAV LTPKGPLRYL VETAQERNEP
260 270 280 290 300
IFPALIYSSG VIYPYVLVTA VENTTDPREP TSSDSNTSTA FPGEASCSSE
310 320 330 340 350
TPKRPKVKRI PQKVQIESNT TASTTQNSGV RVERELAAER PTVQDANFHR
360 370 380 390 400
HEEEERGVKL GLGDFIFYSV LLGKASSYFD WNTTIACYVA ILIGLCFTLV
410 420 430 440
LLAVFKRALP ALPISIFSGL IFYFCTRWII TPFVTQVSQK CLLY
Length:444
Mass (Da):50,034
Last modified:May 27, 2002 - v2
Checksum:i37ADBC124E16429C
GO

Sequence cautioni

The sequence AAA85511.1 differs from that shown. Reason: Frameshift at position 413. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35660 mRNA. Translation: AAA85511.1. Frameshift.
AF171064 mRNA. Translation: AAD50991.1.
FO081301 Genomic DNA. Translation: CCD70617.1.
RefSeqiNP_508175.1. NM_075774.5.
UniGeneiCel.19557.

Genome annotation databases

EnsemblMetazoaiF35H12.3; F35H12.3; WBGene00004769.
GeneIDi180441.
KEGGicel:CELE_F35H12.3.
UCSCiF35H12.3. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35660 mRNA. Translation: AAA85511.1. Frameshift.
AF171064 mRNA. Translation: AAD50991.1.
FO081301 Genomic DNA. Translation: CCD70617.1.
RefSeqiNP_508175.1. NM_075774.5.
UniGeneiCel.19557.

3D structure databases

ProteinModelPortaliP52166.
SMRiP52166. Positions 46-231, 326-438.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi45394. 56 interactions.
STRINGi6239.F35H12.3.

Protein family/group databases

MEROPSiA22.009.

Proteomic databases

EPDiP52166.
PaxDbiP52166.
PRIDEiP52166.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiF35H12.3; F35H12.3; WBGene00004769.
GeneIDi180441.
KEGGicel:CELE_F35H12.3.
UCSCiF35H12.3. c. elegans.

Organism-specific databases

CTDi180441.
WormBaseiF35H12.3; CE24946; WBGene00004769; sel-12.

Phylogenomic databases

eggNOGiKOG2736. Eukaryota.
ENOG410XPZD. LUCA.
GeneTreeiENSGT00390000016593.
HOGENOMiHOG000240228.
InParanoidiP52166.
KOiK04505.
OMAiERQENIP.
OrthoDBiEOG7NGQBG.
PhylomeDBiP52166.

Enzyme and pathway databases

ReactomeiR-CEL-3928665. EPH-ephrin mediated repulsion of cells.
SignaLinkiP52166.

Miscellaneous databases

NextBioi909386.
PROiP52166.

Family and domain databases

InterProiIPR001686. Pept_A22A_Ceel.
IPR001108. Peptidase_A22A.
IPR006639. Preselin/SPP.
[Graphical view]
PANTHERiPTHR10202. PTHR10202. 1 hit.
PfamiPF01080. Presenilin. 1 hit.
[Graphical view]
PRINTSiPR01072. PRESENILIN.
PR01075. PRESENILNSEL.
SMARTiSM00730. PSN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Facilitation of lin-12-mediated signalling by sel-12, a Caenorhabditis elegans S182 Alzheimer's disease gene."
    Levitan D., Greenwald I.
    Nature 377:351-354(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF CYS-60.
    Strain: Bristol N2.
  2. Levitan D.
    Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 84-85.
  3. "Presenilin is required for proper morphology and function of neurons in C. elegans."
    Wittenburg N., Eimer S., Lakowski B., Roehrig S., Rudolph C., Baumeister R.
    Nature 406:306-309(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Strain: Bristol N2.
  4. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.
  5. "Evidence for functional and physical association between Caenorhabditis elegans SEL-10, a Cdc4p-related protein, and SEL-12 presenilin."
    Wu G., Hubbard E.J.A., Kitajewski J.K., Greenwald I.
    Proc. Natl. Acad. Sci. U.S.A. 95:15787-15791(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SEL-10.
  6. "The Caenorhabditis elegans presenilin sel-12 is required for mesodermal patterning and muscle function."
    Eimer S., Donhauser R., Baumeister R.
    Dev. Biol. 251:178-192(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLY-60.
  7. "Two suppressors of sel-12 encode C2H2 zinc-finger proteins that regulate presenilin transcription in Caenorhabditis elegans."
    Lakowski B., Eimer S., Goebel C., Boettcher A., Wagler B., Baumeister R.
    Development 130:2117-2128(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiPSN_CAEEL
AccessioniPrimary (citable) accession number: P52166
Secondary accession number(s): Q20076, Q9U9C7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 27, 2002
Last modified: May 11, 2016
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.