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Presenilin spe-4

 SPE4_CAEEL              Reviewed;         465 AA.
Q01608;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
28-FEB-2018, entry version 131.
RecName: Full=Presenilin spe-4;
Name=spe-4; ORFNames=ZK524.1;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
STRAIN=Bristol N2;
PubMed=1527173; DOI=10.1083/jcb.119.1.55;
L'Hernault S.W., Arduengo P.M.;
"Mutation of a putative sperm membrane protein in Caenorhabditis
elegans prevents sperm differentiation but not its associated meiotic
divisions.";
J. Cell Biol. 119:55-68(1992).
[2]
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).
[3]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
SER-177 AND PRO-440.
PubMed=9819355;
Arduengo P.M., Appleberry O.K., Chuang P., L'Hernault S.W.;
"The presenilin protein family member SPE-4 localizes to an ER/Golgi
derived organelle and is required for proper cytoplasmic partitioning
during Caenorhabditis elegans spermatogenesis.";
J. Cell Sci. 111:3645-3654(1998).
-!- FUNCTION: Potential catalytic subunit of the gamma-secretase
complex during spermatogenesis, an endoprotease complex that
catalyzes the intramembrane cleavage of integral membrane proteins
such as Notch receptors (lin-12 or glp-1). Involved in spermatid
formation during meiosis II. May be required for proper
localization of macromolecules that are subject to asymmetric
partitioning during spermatogenesis. {ECO:0000269|PubMed:9819355}.
-!- SUBUNIT: Homodimer. Potential 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). {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:9819355}; Multi-pass membrane protein
{ECO:0000269|PubMed:9819355}. Golgi apparatus, cis-Golgi network
membrane {ECO:0000269|PubMed:9819355}; Multi-pass membrane protein
{ECO:0000269|PubMed:9819355}. Note=Predominantly located in the
endoplasmic reticulum and in the cis-Golgi.
-!- DEVELOPMENTAL STAGE: Expressed during L4 stage, during
spermatogenesis, when hermaphrodites produces sperm.
-!- DOMAIN: The PAL motif is required for normal active site
conformation. {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase A22A family. {ECO:0000305}.
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EMBL; Z14066; CAA78449.1; -; mRNA.
EMBL; Z14067; CAA78450.1; -; Genomic_DNA.
EMBL; Z73912; CAA98145.1; -; Genomic_DNA.
PIR; T27885; T27885.
RefSeq; NP_492095.1; NM_059694.5.
UniGene; Cel.18295; -.
ProteinModelPortal; Q01608; -.
STRING; 6239.ZK524.1; -.
MEROPS; A22.012; -.
PaxDb; Q01608; -.
PeptideAtlas; Q01608; -.
EnsemblMetazoa; ZK524.1; ZK524.1; WBGene00004958.
GeneID; 172498; -.
KEGG; cel:CELE_ZK524.1; -.
UCSC; ZK524.1; c. elegans.
CTD; 172498; -.
WormBase; ZK524.1; CE06618; WBGene00004958; spe-4.
eggNOG; KOG2736; Eukaryota.
eggNOG; ENOG410XPZD; LUCA.
GeneTree; ENSGT00390000016593; -.
InParanoid; Q01608; -.
KO; K06060; -.
OMA; CGTFCYF; -.
OrthoDB; EOG091G0AV5; -.
PhylomeDB; Q01608; -.
Reactome; R-CEL-1251985; Nuclear signaling by ERBB4.
Reactome; R-CEL-6798695; Neutrophil degranulation.
PRO; PR:Q01608; -.
Proteomes; UP000001940; Chromosome I.
Bgee; WBGene00004958; -.
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:0005794; C:Golgi apparatus; 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:0043231; C:intracellular membrane-bounded organelle; IDA:WormBase.
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; IBA:GO_Central.
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:0006816; P:calcium ion transport; IBA:GO_Central.
GO; GO:0061024; P:membrane organization; IMP:WormBase.
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:0007220; P:Notch receptor processing; IBA:GO_Central.
GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
GO; GO:0006996; P:organelle organization; IMP:WormBase.
GO; GO:0008104; P:protein localization; IMP:WormBase.
GO; GO:0016485; P:protein processing; IEA:InterPro.
GO; GO:0007286; P:spermatid development; IMP:WormBase.
InterPro; IPR001108; Peptidase_A22A.
InterPro; IPR006639; Preselin/SPP.
InterPro; IPR033153; SPE-4.
PANTHER; PTHR10202; PTHR10202; 1.
PANTHER; PTHR10202:SF17; PTHR10202:SF17; 1.
Pfam; PF01080; Presenilin; 1.
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 1 465 Presenilin spe-4.
/FTId=PRO_0000073904.
TOPO_DOM 1 18 Cytoplasmic. {ECO:0000255}.
TRANSMEM 19 39 Helical. {ECO:0000255}.
TOPO_DOM 40 71 Lumenal. {ECO:0000255}.
TRANSMEM 72 92 Helical. {ECO:0000255}.
TOPO_DOM 93 96 Cytoplasmic. {ECO:0000255}.
TRANSMEM 97 117 Helical. {ECO:0000255}.
TOPO_DOM 118 136 Lumenal. {ECO:0000255}.
TRANSMEM 137 157 Helical. {ECO:0000255}.
TOPO_DOM 158 160 Cytoplasmic. {ECO:0000255}.
TRANSMEM 161 181 Helical. {ECO:0000255}.
TOPO_DOM 182 190 Lumenal. {ECO:0000255}.
TRANSMEM 191 211 Helical. {ECO:0000255}.
TOPO_DOM 212 389 Cytoplasmic. {ECO:0000255}.
TRANSMEM 390 410 Helical. {ECO:0000255}.
TOPO_DOM 411 411 Lumenal. {ECO:0000255}.
TRANSMEM 412 432 Helical. {ECO:0000255}.
TOPO_DOM 433 439 Cytoplasmic. {ECO:0000255}.
INTRAMEM 440 460 Helical. {ECO:0000255}.
TOPO_DOM 461 465 Cytoplasmic. {ECO:0000255}.
MOTIF 440 442 PAL.
ACT_SITE 200 200 {ECO:0000250}.
ACT_SITE 394 394 {ECO:0000250}.
MUTAGEN 177 177 S->F: In HC78; induces an aberrant
localization of tubulin in spermatids.
{ECO:0000269|PubMed:9819355}.
MUTAGEN 440 440 P->L: In HC78; induces an aberrant
localization of tubulin in spermatids.
{ECO:0000269|PubMed:9819355}.
SEQUENCE 465 AA; 51830 MW; 65BE2A4DFDF3C844 CRC64;
MDTLRSISSE LVRSSQLRWT LFSVIANMSL TLSIWIGVYN MEVNSELSKT YFLDPSFEQT
TGNLLLDGFI NGVGTILVLG CVSFIMLAFV LFDFRRIVKA WLTLSCLLIL FGVSAQTLHD
MFSQVFDQDD NNQYYMTIVL IVVPTVVYGF GGIYAFFSNS SLILHQIFVV TNCSLISVFY
LRVFPSKTTW FVLWIVLFWD LFAVLAPMGP LKKVQEKASD YSKCVLNLIM FSANEKRLTA
GSNQEETNEG EESTIRRTVK QTIEYYTKRE AQDDEFYQKI RQRRAAINPD SVPTEHSPLV
EAEPSPIELK EKNSTEELSD DESDTSETSS GSSNLSSSDS STTVSTSDIS TAEECDQKEW
DDLVSNSLPN NDKRPATAAD ALNDGEVLRL GFGDFVFYSL LIGQAAASGC PFAVISAALG
ILFGLVVTLT VFSTEESTTP ALPLPVICGT FCYFSSMFFW EQLYG


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