PSN2_XENLA
ID PSN2_XENLA Reviewed; 449 AA.
AC O12977; Q6GQ85;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Presenilin-2;
DE Short=PS-2;
DE EC=3.4.23.-;
DE AltName: Full=Presenilin beta;
DE Short=PS-beta;
GN Name=psen2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=9070286; DOI=10.1006/bbrc.1996.6043;
RA Tsujimura A., Yasojima K., Hashimoto-Gotoh T.;
RT "Cloning of Xenopus presenilin-alpha and -beta cDNAs and their differential
RT expression in oogenesis and embryogenesis.";
RL Biochem. Biophys. Res. Commun. 231:392-396(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) 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 (By similarity). May
CC play a role in negative regulation of apoptotic cascades during
CC oogenesis and embryogenesis, and in developmentally matured tissues
CC such as brain tissue. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Probable component of the gamma-secretase complex,
CC a complex composed of a presenilin homodimer (PS-alpha or PS-beta),
CC nicastrin (NCSTN), APH1 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 -!- TISSUE SPECIFICITY: Highest expression in ovaries and to a lesser
CC extent in kidney, brain, eye and lung. Weak expression in testis,
CC intestine, liver and heart. Present in trace amounts in skeletal
CC muscle.
CC -!- DEVELOPMENTAL STAGE: Abundant in early stages of oogenesis after which
CC it is nearly constant.
CC -!- DOMAIN: The PAL motif is required for normal active site conformation.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase A22A family. {ECO:0000305}.
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DR EMBL; D84428; BAA19571.1; -; mRNA.
DR EMBL; BC072862; AAH72862.1; -; mRNA.
DR PIR; JC5391; JC5391.
DR RefSeq; NP_001081211.1; NM_001087742.1.
DR RefSeq; XP_018119744.1; XM_018264255.1.
DR AlphaFoldDB; O12977; -.
DR SMR; O12977; -.
DR MEROPS; A22.002; -.
DR DNASU; 397713; -.
DR GeneID; 397713; -.
DR KEGG; xla:397713; -.
DR CTD; 397713; -.
DR Xenbase; XB-GENE-6252626; psen2.S.
DR OMA; GVLIWNF; -.
DR OrthoDB; 797738at2759; -.
DR Proteomes; UP000186698; Chromosome 5S.
DR Bgee; 397713; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0016485; P:protein processing; IEA:InterPro.
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; 1.
DR PRINTS; PR01072; PRESENILIN.
DR SMART; SM00730; PSN; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Hydrolase; Membrane;
KW Notch signaling pathway; Protease; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..449
FT /note="Presenilin-2"
FT /id="PRO_0000073900"
FT TOPO_DOM 1..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..141
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..203
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..226
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..252
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..362
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 384..389
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 411..414
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 436..449
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 415..417
FT /note="PAL"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 266
FT /evidence="ECO:0000250"
FT ACT_SITE 367
FT /evidence="ECO:0000250"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 449 AA; 50274 MW; 2C2C105F5C723F2B CRC64;
MIKLSDSEDE ECNERTSLIT SESPPLPSYQ DGVQASEGLE TSYHRERQPD STQNNEDVPN
GRTSGADAYN SETTVENEEE ELTLKYGARH VIMLFVPVTL CMVVVVATIK SVSFYTEKDG
QLIYTPFSED TTSVGERLLN SVLNTLIMIS VILVMTIFLV LLYKYRCYKF IHGWLILSSL
MLLFMFTYIY LSEVFKTYNI AMDYPTLFMV IWNFGAVGMI CIHWKGPLQL QQAYLIMISA
LMALVFIKYL PEWSAWVILG AISVYDLLAV LCPKGPLRML VETAQERNEP IFPALIYSSA
MMWTVGMADS ATADGRMNQQ VQHIDRNTPE GANSTVEDAA ETRIQTQSNL SSEDPDEERG
VKLGLGDFIF YSVLVGKAAA TASGDWNTTL ACFVAILIGL CLTLLLLAVF KKALPALPIS
ITFGLIFYFS TDNIVRPFMD TLASHQMYI
