PSN2_DANRE
ID PSN2_DANRE Reviewed; 441 AA.
AC Q90ZE4; Q9I991;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2003, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Presenilin-2;
DE Short=PS-2;
DE Short=Zf-PS2;
DE EC=3.4.23.-;
DE AltName: Full=Pre2;
GN Name=psen2;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=12424519; DOI=10.1007/s00427-002-0269-5;
RA Groth C., Nornes S., McCarty R., Tamme R., Lardelli M.;
RT "Identification of a second presenilin gene in zebrafish with similarity to
RT the human Alzheimer's disease gene presenilin2.";
RL Dev. Genes Evol. 212:486-490(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Jiang Y.-J., Davies A., Lewis J.;
RT "The cloning and function of ps2 in zebrafish.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable catalytic subunit of the gamma-secretase complex, an
CC endoprotease complex that catalyzes the intramembrane cleavage of
CC integral membrane proteins such as Notch receptors. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Component of the gamma-secretase complex, a complex
CC composed of a presenilin homodimer (PSEN1 or PSEN2), nicastrin, APH1
CC and PEN2 (Probable). {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}. Golgi apparatus membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Protein expression is initiated from 6 and 12
CC hours of embryonic development.
CC -!- DOMAIN: The PAL motif is required for normal active site conformation.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: While the protein appears only from 6 hours of
CC development, the transcript is maternally derived and ubiquitously
CC expressed during early embryonic development, suggesting that its
CC translation is strictly regulated.
CC -!- SIMILARITY: Belongs to the peptidase A22A family. {ECO:0000305}.
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DR EMBL; AJ271795; CAB71930.1; -; mRNA.
DR EMBL; AF178539; AAK61828.1; -; mRNA.
DR RefSeq; NP_571589.2; NM_131514.2.
DR AlphaFoldDB; Q90ZE4; -.
DR SMR; Q90ZE4; -.
DR STRING; 7955.ENSDARP00000011791; -.
DR MEROPS; A22.002; -.
DR PaxDb; Q90ZE4; -.
DR Ensembl; ENSDART00000006381; ENSDARP00000011791; ENSDARG00000015540.
DR GeneID; 58026; -.
DR KEGG; dre:58026; -.
DR CTD; 5664; -.
DR ZFIN; ZDB-GENE-000330-9; psen2.
DR eggNOG; KOG2736; Eukaryota.
DR GeneTree; ENSGT00940000157923; -.
DR HOGENOM; CLU_022975_3_1_1; -.
DR InParanoid; Q90ZE4; -.
DR OMA; GVLIWNF; -.
DR OrthoDB; 797738at2759; -.
DR PhylomeDB; Q90ZE4; -.
DR TreeFam; TF315040; -.
DR Reactome; R-DRE-1251985; Nuclear signaling by ERBB4.
DR Reactome; R-DRE-193692; Regulated proteolysis of p75NTR.
DR Reactome; R-DRE-205043; NRIF signals cell death from the nucleus.
DR Reactome; R-DRE-3928665; EPH-ephrin mediated repulsion of cells.
DR PRO; PR:Q90ZE4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 1.
DR Bgee; ENSDARG00000015540; Expressed in intestine and 29 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0035253; C:ciliary rootlet; IBA:GO_Central.
DR GO; GO:0043198; C:dendritic shaft; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030426; C:growth cone; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0042987; P:amyloid precursor protein catabolic process; IBA:GO_Central.
DR GO; GO:0034205; P:amyloid-beta formation; IMP:ZFIN.
DR GO; GO:0050435; P:amyloid-beta metabolic process; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IMP:ZFIN.
DR GO; GO:0006816; P:calcium ion transport; IBA:GO_Central.
DR GO; GO:0030318; P:melanocyte differentiation; IMP:ZFIN.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0022008; P:neurogenesis; IMP:ZFIN.
DR GO; GO:0007220; P:Notch receptor processing; IBA:GO_Central.
DR GO; GO:0007219; P:Notch signaling pathway; IMP:ZFIN.
DR GO; GO:0016485; P:protein processing; IEA:InterPro.
DR GO; GO:0061053; P:somite development; IMP:ZFIN.
DR Gene3D; 1.10.472.100; -; 1.
DR InterPro; IPR001108; Peptidase_A22A.
DR InterPro; IPR006639; Preselin/SPP.
DR InterPro; IPR042524; Presenilin_C.
DR PANTHER; PTHR10202; PTHR10202; 1.
DR Pfam; PF01080; Presenilin; 2.
DR PRINTS; PR01072; PRESENILIN.
DR SMART; SM00730; PSN; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Golgi apparatus; Hydrolase; Membrane;
KW Notch signaling pathway; Protease; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..441
FT /note="Presenilin-2"
FT /id="PRO_0000073899"
FT TOPO_DOM 1..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..137
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..165
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..199
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..225
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..248
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..355
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 377..381
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 403..406
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 407..409
FT /note="PAL"
FT COMPBIAS 15..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 262
FT /evidence="ECO:0000250"
FT ACT_SITE 360
FT /evidence="ECO:0000250"
FT CONFLICT 204
FT /note="L -> V (in Ref. 2; AAK61828)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="H -> D (in Ref. 2; AAK61828)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 441 AA; 49169 MW; BC720F2398E5F82A CRC64;
MNTSDSEEDS YNERSALVQS ESPTVPSYNQ DNAMSLPQDT DSKRSGAVRS RSASGSGDAG
PVDRERADTP DGEEEELTLK YGAKHVIMLF IPVTLCMVVV VATIKSVSFY TEKSGQRLIY
TPFEEDPNSV GQRLLNSVLN TLVMISVIVF MTIILVLLYK YRCYKFIHGW LILSSLMLLF
WFSFMYLGEV FKTYNVAMDY PTLLMIIWNF GVVGMICIHW KGPLRLQQAY LIVISALMAL
IFIKYLPEWS AWVILGAISI YDLIAVLCPK GPLRMLVETA QERNEPIFPA LIYSSAMVWM
VGMADSNNPD SAGERRRSGG GVRTQEGVES EHDAPQAGRR QYSAEEDLEE DRGVKLGLGD
FIFYSVLVGK AAATGGDWNT TLACFVAILI GLCLTLLLLA IFKKALPALP ISITFGLVFY
FSTDNLVRPF MDSLAAHQYY I
