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Presenilin homolog (DmPS) (EC 3.4.23.-) (dPS)

 PSN_DROME               Reviewed;         541 AA.
O02194; O02395; O76802; O96340; Q9TY80; Q9V3L9; Q9V3S1;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
15-JUL-1999, sequence version 2.
25-OCT-2017, entry version 159.
RecName: Full=Presenilin homolog;
Short=DmPS;
EC=3.4.23.-;
AltName: Full=dPS;
Name=Psn; Synonyms=PS; ORFNames=CG18803;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, AND DEVELOPMENTAL
STAGE.
TISSUE=Embryo;
PubMed=9141085; DOI=10.1097/00001756-199703030-00041;
Boulianne G.L., Livne-Bar I., Humphreys J.M., Liang Y., Lin C.,
Rogaev E., St George-Hyslop P.H.;
"Cloning and characterization of the Drosophila presenilin
homologue.";
NeuroReport 8:1025-1029(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND DEVELOPMENTAL STAGE.
STRAIN=Canton-S; TISSUE=Embryo, and Head;
PubMed=9106743; DOI=10.1097/00001756-199702100-00017;
Hong C.-S., Koo E.H.;
"Isolation and characterization of Drosophila presenilin homolog.";
NeuroReport 8:665-668(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), TISSUE
SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, AND
ALTERNATIVE SPLICING.
PubMed=10349633; DOI=10.1016/S0925-4773(98)00169-5;
Ye Y., Fortini M.E.;
"Characterization of Drosophila Presenilin and its colocalization with
Notch during development.";
Mech. Dev. 79:199-211(1998).
[4]
NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2), AND FUNCTION IN S3 CLEAVAGE OF
NOTCH.
PubMed=10206647; DOI=10.1038/19096;
Ye Y., Lukinova N., Fortini M.E.;
"Neurogenic phenotypes and altered Notch processing in Drosophila
Presenilin mutants.";
Nature 398:525-529(1999).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ALTERNATIVE SPLICING, AND
DEVELOPMENTAL STAGE.
STRAIN=Canton-S;
PubMed=9666900; DOI=10.3109/01677069809108554;
Marfany G., Del-Favero J., Valero R., De Jonghe C., Woodrow S.,
Hendriks L., Van Broeckhoven C., Gonzalez-Duarte R.;
"Identification of a Drosophila presenilin homologue: evidence of
alternatively spliced forms.";
J. Neurogenet. 12:41-54(1998).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
PubMed=10493744;
Guo Y., Livne-Bar I., Zhou L., Boulianne G.L.;
"Drosophila presenilin is required for neuronal differentiation and
affects notch subcellular localization and signaling.";
J. Neurosci. 19:8435-8442(1999).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[8]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[10]
ALTERNATIVE SPLICING (ISOFORM 3), AND CLEAVAGE.
PubMed=10662508; DOI=10.1006/mcne.1999.0805;
Nowotny P., Gorski S.M., Han S.W., Philips K., Ray W.J., Nowotny V.,
Jones C.J., Clark R.F., Cagan R.L., Goate A.M.;
"Posttranslational modification and plasma membrane localization of
the Drosophila melanogaster presenilin.";
Mol. Cell. Neurosci. 15:88-98(2000).
[11]
FUNCTION IN S3 CLEAVAGE OF NOTCH.
PubMed=10206646; DOI=10.1038/19091;
Struhl G., Greenwald I.;
"Presenilin is required for activity and nuclear access of Notch in
Drosophila.";
Nature 398:522-525(1999).
[12]
INTERACTION WITH METL.
PubMed=11738826; DOI=10.1016/S0378-1119(01)00770-3;
Zhang S.X., Guo Y., Boulianne G.L.;
"Identification of a novel family of putative methyltransferases that
interact with human and Drosophila presenilins.";
Gene 280:135-144(2001).
[13]
FUNCTION IN THE GAMMA-SECRETASE COMPLEX, AND INTERACTION WITH PEN-2;
APH-1 AND NCT.
PubMed=12660785; DOI=10.1038/nature01506;
Takasugi N., Tomita T., Hayashi I., Tsuruoka M., Niimura M.,
Takahashi Y., Thinakaran G., Iwatsubo T.;
"The role of presenilin cofactors in the gamma-secretase complex.";
Nature 422:438-441(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 receptor.
Required for S3 cleavage of Notch, which releases activated Notch
protein from the cell membrane. Involved in the patterning of the
optic lobes. {ECO:0000269|PubMed:10206646,
ECO:0000269|PubMed:10206647, ECO:0000269|PubMed:12660785}.
-!- SUBUNIT: Homodimer (By similarity). Component of the gamma-
secretase complex, a complex composed of a presenilin (Psn)
homodimer, nicastrin (Nct), Aph-1 and Pen-2. Interacts with Metl.
Isoform 2 shows a better interaction with Metl than isoform 1.
{ECO:0000250, ECO:0000269|PubMed:11738826,
ECO:0000269|PubMed:12660785}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi
apparatus membrane {ECO:0000250}; Multi-pass membrane protein
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=A2, A, DLA-b;
IsoId=O02194-1; Sequence=Displayed;
Name=2; Synonyms=A1, B, PS-d, DLA-a;
IsoId=O02194-2; Sequence=VSP_005195;
Name=3;
IsoId=O02194-3; Sequence=VSP_007988;
-!- TISSUE SPECIFICITY: Maternally expressed in nurse and follicle
cells. In early embryos, expressed in all or most cells and later
increases in CNS and epidermal tissues. In larvae, expression is
seen in all imaginal disks, brain and optic lobes. In pupae,
expression is seen in eye disk and brain.
{ECO:0000269|PubMed:10349633}.
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
throughout development. {ECO:0000269|PubMed:10349633,
ECO:0000269|PubMed:9106743, ECO:0000269|PubMed:9141085,
ECO:0000269|PubMed:9666900}.
-!- DOMAIN: The PAL motif is required for normal active site
conformation. {ECO:0000250}.
-!- PTM: Cleaved. The cleavage, which probably takes place between the
6th and the 7th transmembrane regions, may be required for
activation of the gamma-secretase activity.
{ECO:0000269|PubMed:10662508}.
-!- SIMILARITY: Belongs to the peptidase A22A family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U77934; AAB61139.1; -; mRNA.
EMBL; U78084; AAB53369.1; -; mRNA.
EMBL; AF084184; AAC33129.1; -; Genomic_DNA.
EMBL; AF084184; AAC33128.1; -; Genomic_DNA.
EMBL; AF017024; AAD01610.1; -; mRNA.
EMBL; AF017025; AAD01611.1; -; mRNA.
EMBL; AF017026; AAD01612.1; -; Genomic_DNA.
EMBL; AF093402; AAD52707.1; -; Genomic_DNA.
EMBL; AF093402; AAD52708.1; -; Genomic_DNA.
EMBL; AE014296; AAN12132.1; -; Genomic_DNA.
EMBL; AE014296; AAF51598.1; -; Genomic_DNA.
EMBL; AY061316; AAL28864.1; -; mRNA.
RefSeq; NP_001262110.1; NM_001275181.1. [O02194-2]
RefSeq; NP_001262111.1; NM_001275182.1. [O02194-1]
RefSeq; NP_524184.1; NM_079460.2. [O02194-1]
RefSeq; NP_730535.1; NM_168856.3. [O02194-2]
UniGene; Dm.3254; -.
ProteinModelPortal; O02194; -.
BioGrid; 65518; 39.
DIP; DIP-1139N; -.
STRING; 7227.FBpp0077850; -.
MEROPS; A22.014; -.
PaxDb; O02194; -.
PRIDE; O02194; -.
EnsemblMetazoa; FBtr0078192; FBpp0077850; FBgn0019947. [O02194-1]
EnsemblMetazoa; FBtr0078193; FBpp0077851; FBgn0019947. [O02194-2]
EnsemblMetazoa; FBtr0114517; FBpp0113009; FBgn0019947. [O02194-3]
EnsemblMetazoa; FBtr0333478; FBpp0305665; FBgn0019947. [O02194-2]
EnsemblMetazoa; FBtr0333479; FBpp0305666; FBgn0019947. [O02194-1]
GeneID; 40260; -.
KEGG; dme:Dmel_CG18803; -.
UCSC; CG18803-RA; d. melanogaster. [O02194-1]
CTD; 40260; -.
FlyBase; FBgn0284421; Psn.
eggNOG; KOG2736; Eukaryota.
eggNOG; ENOG410XPZD; LUCA.
GeneTree; ENSGT00390000016593; -.
InParanoid; O02194; -.
KO; K04505; -.
OMA; VCDERTS; -.
OrthoDB; EOG091G0C72; -.
PhylomeDB; O02194; -.
Reactome; R-DME-1251985; Nuclear signaling by ERBB4.
Reactome; R-DME-1980148; Signaling by NOTCH3.
Reactome; R-DME-1980150; Signaling by NOTCH4.
Reactome; R-DME-3928665; EPH-ephrin mediated repulsion of cells.
Reactome; R-DME-6798695; Neutrophil degranulation.
SignaLink; O02194; -.
GenomeRNAi; 40260; -.
PRO; PR:O02194; -.
Proteomes; UP000000803; Chromosome 3L.
Bgee; FBgn0019947; -.
ExpressionAtlas; O02194; differential.
Genevisible; O02194; DM.
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: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; 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:0006915; P:apoptotic process; IMP:CACAO.
GO; GO:0006816; P:calcium ion transport; IBA:GO_Central.
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:0016485; P:protein processing; IEA:InterPro.
InterPro; IPR001108; Peptidase_A22A.
InterPro; IPR006639; Preselin/SPP.
PANTHER; PTHR10202; PTHR10202; 1.
Pfam; PF01080; Presenilin; 1.
PRINTS; PR01072; PRESENILIN.
SMART; SM00730; PSN; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Endoplasmic reticulum;
Glycoprotein; Golgi apparatus; Hydrolase; Membrane;
Notch signaling pathway; Protease; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 541 Presenilin homolog.
/FTId=PRO_0000073901.
TOPO_DOM 1 106 Cytoplasmic. {ECO:0000255}.
TRANSMEM 107 127 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 128 154 Lumenal. {ECO:0000255}.
TRANSMEM 155 175 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 176 182 Cytoplasmic. {ECO:0000255}.
TRANSMEM 183 203 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 204 216 Lumenal. {ECO:0000255}.
TRANSMEM 217 237 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 238 242 Cytoplasmic. {ECO:0000255}.
TRANSMEM 243 263 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 264 265 Lumenal. {ECO:0000255}.
TRANSMEM 266 286 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 287 453 Cytoplasmic. {ECO:0000255}.
TRANSMEM 454 474 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 475 481 Lumenal. {ECO:0000255}.
TRANSMEM 482 502 Helical; Name=8. {ECO:0000255}.
TOPO_DOM 503 506 Cytoplasmic. {ECO:0000255}.
INTRAMEM 507 527 Helical; Name=9. {ECO:0000255}.
TOPO_DOM 528 541 Cytoplasmic. {ECO:0000255}.
REGION 320 481 Interaction with metl.
MOTIF 507 509 PAL.
ACT_SITE 279 279 {ECO:0000250}.
ACT_SITE 461 461 {ECO:0000250}.
CARBOHYD 129 129 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 365 397 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_007988.
VAR_SEQ 384 397 Missing (in isoform 2).
{ECO:0000303|PubMed:9106743}.
/FTId=VSP_005195.
CONFLICT 80 81 GG -> RS (in Ref. 2; AAB53369).
{ECO:0000305}.
SEQUENCE 541 AA; 59304 MW; A3B3D54348A2C03F CRC64;
MAAVNLQASC SSGLASEDDA NVGSQIGAAE RLERPPRRQQ QRNNYGSSNQ DQPDAAILAV
PNVVMREPCG SRPSRLTGGG GGSGGPPTNE MEEEQGLKYG AQHVIKLFVP VSLCMLVVVA
TINSISFYNS TDVYLLYTPF HEQSPEPSVK FWSALANSLI LMSVVVVMTF LLIVLYKKRC
YRIIHGWLIL SSFMLLFIFT YLYLEELLRA YNIPMDYPTA LLIMWNFGVV GMMSIHWQGP
LRLQQGYLIF VAALMALVFI KYLPEWTAWA VLAAISIWDL IAVLSPRGPL RILVETAQER
NEQIFPALIY SSTVVYALVN TVTPQQSQAT ASSSPSSSNS TTTTRATQNS LASPEAAAAS
GQRTGNSHPR QNQRDDGSVL ATEGMPLVTF KSNLRGNAEA AGFTQEWSAN LSERVARRQI
EVQSTQSGNA QRSNEYRTVT APDQNHPDGQ EERGIKLGLG DFIFYSVLVG KASSYGDWTT
TIACFVAILI GLCLTLLLLA IWRKALPALP ISITFGLIFC FATSAVVKPF MEDLSAKQVF
I


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