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Protein

Presenilin-1

Gene

psen1

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein). Requires the presence of the other members of the gamma-secretase complex for protease activity. Plays a role in Notch and Wnt signaling cascades and regulation of downstream processes via its role in processing key regulatory proteins.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei223By similarity1
Active sitei351By similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Protease
Biological processNotch signaling pathway

Protein family/group databases

MEROPSiA22.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Presenilin-1 (EC:3.4.23.-)
Short name:
PS-1
Alternative name(s):
Presenilin alpha
Short name:
PS-alpha
Gene namesi
Name:psen1
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-481920. psen1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 48CytoplasmicBy similarityAdd BLAST48
Transmembranei49 – 69HelicalBy similarityAdd BLAST21
Topological domaini70 – 98LumenalBy similarityAdd BLAST29
Transmembranei99 – 119HelicalBy similarityAdd BLAST21
Topological domaini120 – 132CytoplasmicBy similarityAdd BLAST13
Transmembranei133 – 155HelicalBy similarityAdd BLAST23
Topological domaini156 – 160LumenalBy similarity5
Transmembranei161 – 182HelicalBy similarityAdd BLAST22
Topological domaini183 – 186CytoplasmicBy similarity4
Transmembranei187 – 207HelicalBy similarityAdd BLAST21
Topological domaini208 – 214LumenalBy similarity7
Transmembranei215 – 238HelicalBy similarityAdd BLAST24
Topological domaini239 – 346CytoplasmicBy similarityAdd BLAST108
Transmembranei347 – 367HelicalBy similarityAdd BLAST21
Topological domaini368 – 373LumenalBy similarity6
Transmembranei374 – 394HelicalBy similarityAdd BLAST21
Topological domaini395 – 398CytoplasmicBy similarity4
Transmembranei399 – 419HelicalBy similarityAdd BLAST21
Topological domaini420 – 433LumenalBy similarityAdd BLAST14

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Endoplasmic reticulum, Golgi apparatus, Membrane, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000738981 – 433Presenilin-1Add BLAST433

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi371N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

Heterogeneous proteolytic processing generates N-terminal (NTF) and C-terminal (CTF) fragments of approximately 35 and 20 kDa, respectively. During apoptosis, the C-terminal fragment (CTF) is further cleaved by a caspase.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei257 – 258Cleavage; alternateBy similarity2
Sitei258 – 259Cleavage; alternateBy similarity2
Sitei264 – 265CleavageBy similarity2

Keywords - PTMi

Glycoprotein, Phosphoprotein

Expressioni

Tissue specificityi

Highest expression in ovaries and to a lesser extent in testis, intestine, kidney, brain, eye and lung. Weak expression in liver and heart. Present in trace amounts in skeletal muscle.1 Publication

Developmental stagei

Abundant in early stages of oogenesis. The expression is rapidly reduced between meiotic maturation and fertilization stages.1 Publication

Interactioni

Subunit structurei

Homodimer. The functional gamma-secretase complex is composed of at least four polypeptides: a presenilin homodimer (PSEN1 or PSEN2), nicastrin (NCSTN), APH1 (APH1A or APH1B) and PEN2. Such minimal complex is sufficient for secretase activity.By similarity

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi399 – 401PALCurated3

Domaini

The PAL motif is required for normal active site conformation.By similarity

Sequence similaritiesi

Belongs to the peptidase A22A family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG011375.
KOiK04505.

Family and domain databases

InterProiView protein in InterPro
IPR002031. Pept_A22A_PS1.
IPR001108. Peptidase_A22A.
IPR006639. Preselin/SPP.
PANTHERiPTHR10202. PTHR10202. 1 hit.
PTHR10202:SF27. PTHR10202:SF27. 1 hit.
PfamiView protein in Pfam
PF01080. Presenilin. 1 hit.
PRINTSiPR01072. PRESENILIN.
SMARTiView protein in SMART
SM00730. PSN. 1 hit.

Sequencei

Sequence statusi: Complete.

O12976-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNDTSERRSN ENSESQSNGQ TQSSSQQVLE QDEEEDEELT LKYGAKHVIM
60 70 80 90 100
LFVPVTLCMV VVVATIKSVS FYTRFDGQLI YTPFTEDTES VGQRALNSIL
110 120 130 140 150
NATIMISVII VMTILLVVLY KYRCYKVIHG WLIISSLLLL FFFSYIYLGE
160 170 180 190 200
VFKTYNVAVD YITLALLIWN FGVVGMICIH WKGPLLLQQA YLIMISALMA
210 220 230 240 250
LVFIKYLPEW TTWLILAVIS VYDLVAVLSP KGPLRMLVET AQERNETLFP
260 270 280 290 300
ALIYSSTMIW LVNMADGDPG LKQSASTKTY NTQAPTAHPR SDSAASDDNG
310 320 330 340 350
GFDTTWEDHR NAQIGPINST PESRVAVQAL PSNSPPSEDP EERGVKLGLG
360 370 380 390 400
DFIFYSVLVG KASATASGDW NTTLACFVAI LIGLCLTLLL LAIFKKALPA
410 420 430
LPISITFGLV FYFATDYLVQ PFMDQLAFHQ FYI
Length:433
Mass (Da):48,301
Last modified:July 1, 1997 - v1
Checksum:i71CCEE3F6BB9C0AF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D84427 mRNA. Translation: BAA19570.1.
BC077762 mRNA. Translation: AAH77762.1.
PIRiJC5390.
RefSeqiNP_001084023.1. NM_001090554.2.
XP_018084271.1. XM_018228782.1.
XP_018084272.1. XM_018228783.1.
XP_018084273.1. XM_018228784.1.
XP_018084274.1. XM_018228785.1.
UniGeneiXl.55408.

Genome annotation databases

GeneIDi399258.
KEGGixla:399258.

Similar proteinsi

Entry informationi

Entry nameiPSN1_XENLA
AccessioniPrimary (citable) accession number: O12976
Secondary accession number(s): Q6DD65
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 1, 1997
Last modified: September 27, 2017
This is version 90 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families