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Presenilin sel-12 (Suppressor/enhancer of lin-12 protein 12)

 PSN_CAEEL               Reviewed;         444 AA.
P52166; Q20076; Q9U9C7;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
27-MAY-2002, sequence version 2.
22-NOV-2017, entry version 142.
RecName: Full=Presenilin sel-12;
AltName: Full=Suppressor/enhancer of lin-12 protein 12;
Name=sel-12; ORFNames=F35H12.3;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS OF CYS-60.
STRAIN=Bristol N2;
PubMed=7566091; DOI=10.1038/377351a0;
Levitan D., Greenwald I.;
"Facilitation of lin-12-mediated signalling by sel-12, a
Caenorhabditis elegans S182 Alzheimer's disease gene.";
Nature 377:351-354(1995).
[2]
SEQUENCE REVISION TO 84-85.
Levitan D.;
Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
STRAIN=Bristol N2;
PubMed=10917532; DOI=10.1038/35018575;
Wittenburg N., Eimer S., Lakowski B., Roehrig S., Rudolph C.,
Baumeister R.;
"Presenilin is required for proper morphology and function of neurons
in C. elegans.";
Nature 406:306-309(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[5]
INTERACTION WITH SEL-10.
PubMed=9861048; DOI=10.1073/pnas.95.26.15787;
Wu G., Hubbard E.J.A., Kitajewski J.K., Greenwald I.;
"Evidence for functional and physical association between
Caenorhabditis elegans SEL-10, a Cdc4p-related protein, and SEL-12
presenilin.";
Proc. Natl. Acad. Sci. U.S.A. 95:15787-15791(1998).
[6]
FUNCTION, AND MUTAGENESIS OF GLY-60.
PubMed=12413907; DOI=10.1006/dbio.2002.0782;
Eimer S., Donhauser R., Baumeister R.;
"The Caenorhabditis elegans presenilin sel-12 is required for
mesodermal patterning and muscle function.";
Dev. Biol. 251:178-192(2002).
[7]
DEVELOPMENTAL STAGE.
PubMed=12668626; DOI=10.1242/dev.00429;
Lakowski B., Eimer S., Goebel C., Boettcher A., Wagler B.,
Baumeister R.;
"Two suppressors of sel-12 encode C2H2 zinc-finger proteins that
regulate presenilin transcription in Caenorhabditis elegans.";
Development 130:2117-2128(2003).
-!- FUNCTION: 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. {ECO:0000269|PubMed:10917532,
ECO:0000269|PubMed:12413907}.
-!- SUBUNIT: 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).
{ECO:0000269|PubMed:9861048, ECO:0000305}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi
apparatus membrane {ECO:0000250}; Multi-pass membrane protein
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in most neurons.
{ECO:0000269|PubMed:10917532}.
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
Ubiquitously expressed throughout the development and in the
adult. {ECO:0000269|PubMed:12668626}.
-!- DOMAIN: The PAL motif is required for normal active site
conformation. {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase A22A family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA85511.1; Type=Frameshift; Positions=413; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; U35660; AAA85511.1; ALT_FRAME; mRNA.
EMBL; AF171064; AAD50991.1; -; mRNA.
EMBL; FO081301; CCD70617.1; -; Genomic_DNA.
RefSeq; NP_508175.1; NM_075774.5.
UniGene; Cel.19557; -.
ProteinModelPortal; P52166; -.
BioGrid; 45394; 56.
STRING; 6239.F35H12.3; -.
MEROPS; A22.009; -.
EPD; P52166; -.
PaxDb; P52166; -.
EnsemblMetazoa; F35H12.3; F35H12.3; WBGene00004769.
GeneID; 180441; -.
KEGG; cel:CELE_F35H12.3; -.
UCSC; F35H12.3; c. elegans.
CTD; 180441; -.
WormBase; F35H12.3; CE24946; WBGene00004769; sel-12.
eggNOG; KOG2736; Eukaryota.
eggNOG; ENOG410XPZD; LUCA.
GeneTree; ENSGT00390000016593; -.
HOGENOM; HOG000240228; -.
InParanoid; P52166; -.
KO; K04505; -.
OMA; VCDERTS; -.
OrthoDB; EOG091G0C72; -.
PhylomeDB; P52166; -.
Reactome; R-CEL-3928665; EPH-ephrin mediated repulsion of cells.
Reactome; R-CEL-6798695; Neutrophil degranulation.
SignaLink; P52166; -.
PRO; PR:P52166; -.
Proteomes; UP000001940; Chromosome X.
Bgee; WBGene00004769; -.
GO; GO:0030424; C:axon; IBA:GO_Central.
GO; GO:0005938; C:cell cortex; IBA:GO_Central.
GO; GO:0009986; C:cell surface; IBA:GO_Central.
GO; GO:0035253; C:ciliary rootlet; IBA:GO_Central.
GO; GO:0043198; C:dendritic shaft; IBA:GO_Central.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0070765; C:gamma-secretase complex; ISS:WormBase.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0030426; C:growth cone; IBA:GO_Central.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005765; C:lysosomal membrane; IBA:GO_Central.
GO; GO:0045121; C:membrane raft; IBA:GO_Central.
GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:WormBase.
GO; GO:0030018; C:Z disc; IBA:GO_Central.
GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
GO; GO:0042987; P:amyloid precursor protein catabolic process; IBA:GO_Central.
GO; GO:0050435; P:amyloid-beta metabolic process; IBA:GO_Central.
GO; GO:0045176; P:apical protein localization; IDA:WormBase.
GO; GO:0006816; P:calcium ion transport; IBA:GO_Central.
GO; GO:0001708; P:cell fate specification; IMP:WormBase.
GO; GO:0016048; P:detection of temperature stimulus; IMP:UniProtKB.
GO; GO:0006509; P:membrane protein ectodomain proteolysis; IBA:GO_Central.
GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
GO; GO:0007399; P:nervous system development; IMP:UniProtKB.
GO; GO:0007220; P:Notch receptor processing; IBA:GO_Central.
GO; GO:0007219; P:Notch signaling pathway; NAS:UniProtKB.
GO; GO:0018991; P:oviposition; IMP:WormBase.
GO; GO:0045747; P:positive regulation of Notch signaling pathway; IGI:WormBase.
GO; GO:0048563; P:post-embryonic animal organ morphogenesis; IMP:WormBase.
GO; GO:0016485; P:protein processing; IEA:InterPro.
GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IGI:WormBase.
InterPro; IPR001686; Pept_A22A_Ceel.
InterPro; IPR001108; Peptidase_A22A.
InterPro; IPR006639; Preselin/SPP.
PANTHER; PTHR10202; PTHR10202; 1.
Pfam; PF01080; Presenilin; 1.
PRINTS; PR01072; PRESENILIN.
PRINTS; PR01075; PRESENILNSEL.
SMART; SM00730; PSN; 1.
1: Evidence at protein level;
Complete proteome; Endoplasmic reticulum; Golgi apparatus; Membrane;
Notch signaling pathway; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 444 Presenilin sel-12.
/FTId=PRO_0000073903.
TOPO_DOM 1 45 Cytoplasmic. {ECO:0000255}.
TRANSMEM 46 66 Helical. {ECO:0000255}.
TOPO_DOM 67 101 Lumenal. {ECO:0000255}.
TRANSMEM 102 122 Helical. {ECO:0000255}.
TOPO_DOM 123 130 Cytoplasmic. {ECO:0000255}.
TRANSMEM 131 151 Helical. {ECO:0000255}.
TOPO_DOM 152 163 Lumenal. {ECO:0000255}.
TRANSMEM 164 184 Helical. {ECO:0000255}.
TOPO_DOM 185 189 Cytoplasmic. {ECO:0000255}.
TRANSMEM 190 210 Helical. {ECO:0000255}.
TOPO_DOM 211 212 Lumenal. {ECO:0000255}.
TRANSMEM 213 233 Helical. {ECO:0000255}.
TOPO_DOM 234 359 Cytoplasmic. {ECO:0000255}.
TRANSMEM 360 380 Helical. {ECO:0000255}.
TOPO_DOM 381 384 Lumenal. {ECO:0000255}.
TRANSMEM 385 405 Helical. {ECO:0000255}.
TOPO_DOM 406 413 Cytoplasmic. {ECO:0000255}.
INTRAMEM 414 434 Helical. {ECO:0000255}.
TOPO_DOM 435 444 Cytoplasmic. {ECO:0000255}.
MOTIF 410 412 PAL.
ACT_SITE 226 226 {ECO:0000250}.
ACT_SITE 364 364 {ECO:0000250}.
MUTAGEN 60 60 C->S: In ar131; egg-laying-defective.
{ECO:0000269|PubMed:12413907,
ECO:0000269|PubMed:7566091}.
SEQUENCE 444 AA; 50034 MW; 37ADBC124E16429C CRC64;
MPSTRRQQEG GGADAETHTV YGTNLITNRN SQEDENVVEE AELKYGASHV IHLFVPVSLC
MALVVFTMNT ITFYSQNNGR HLLYTPFVRE TDSIVEKGLM SLGNALVMLC VVVLMTVLLI
VFYKYKFYKL IHGWLIVSSF LLLFLFTTIY VQEVLKSFDV SPSALLVLFG LGNYGVLGMM
CIHWKGPLRL QQFYLITMSA LMALVFIKYL PEWTVWFVLF VISVWDLVAV LTPKGPLRYL
VETAQERNEP IFPALIYSSG VIYPYVLVTA VENTTDPREP TSSDSNTSTA FPGEASCSSE
TPKRPKVKRI PQKVQIESNT TASTTQNSGV RVERELAAER PTVQDANFHR HEEEERGVKL
GLGDFIFYSV LLGKASSYFD WNTTIACYVA ILIGLCFTLV LLAVFKRALP ALPISIFSGL
IFYFCTRWII TPFVTQVSQK CLLY


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