PSNA_DICDI
ID PSNA_DICDI Reviewed; 622 AA.
AC Q54ET2;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Presenilin-A;
DE Short=PS-A;
DE EC=3.4.23.-;
GN Name=psenA; ORFNames=DDB_G0291352;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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. Requires the other
CC members of the gamma-secretase complex to have a protease activity (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Component of the gamma-secretase complex, a complex
CC composed of a presenilin homodimer, nicastrin, aph1 and pen2 (By
CC similarity). {ECO:0000250}.
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 -!- 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; AAFI02000177; EAL61660.1; -; Genomic_DNA.
DR RefSeq; XP_635158.1; XM_630066.1.
DR AlphaFoldDB; Q54ET2; -.
DR SMR; Q54ET2; -.
DR STRING; 44689.DDB0231427; -.
DR MEROPS; A22.A09; -.
DR PaxDb; Q54ET2; -.
DR EnsemblProtists; EAL61660; EAL61660; DDB_G0291352.
DR GeneID; 8628104; -.
DR KEGG; ddi:DDB_G0291352; -.
DR dictyBase; DDB_G0291352; psenA.
DR eggNOG; KOG2736; Eukaryota.
DR HOGENOM; CLU_022975_1_1_1; -.
DR InParanoid; Q54ET2; -.
DR OMA; HEITINN; -.
DR PhylomeDB; Q54ET2; -.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR PRO; PR:Q54ET2; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070765; C:gamma-secretase complex; IMP:dictyBase.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; 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:0006914; P:autophagy; IGI:dictyBase.
DR GO; GO:0055074; P:calcium ion homeostasis; IMP:dictyBase.
DR GO; GO:0044351; P:macropinocytosis; IGI:dictyBase.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006909; P:phagocytosis; IGI:dictyBase.
DR GO; GO:0016485; P:protein processing; IMP:dictyBase.
DR GO; GO:0106070; P:regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; IGI:dictyBase.
DR GO; GO:0030587; P:sorocarp development; IGI:dictyBase.
DR GO; GO:0044671; P:sorocarp spore cell differentiation; IMP:dictyBase.
DR GO; GO:0031149; P:sorocarp stalk cell differentiation; IGI:dictyBase.
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 3: Inferred from homology;
KW Endoplasmic reticulum; Golgi apparatus; Hydrolase; Membrane;
KW Notch signaling pathway; Protease; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..622
FT /note="Presenilin-A"
FT /id="PRO_0000331267"
FT TOPO_DOM 1..168
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..227
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..289
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..341
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 363..538
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 539..559
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 560..562
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 563..583
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 584..588
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 589..609
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 610..622
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 588..590
FT /note="PAL"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..160
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 351
FT /evidence="ECO:0000250"
FT ACT_SITE 543
FT /evidence="ECO:0000250"
SQ SEQUENCE 622 AA; 69503 MW; CEBA16E5212967E6 CRC64;
MKENEDEINK TDEKYKIKNP SNNGNNKNKN NNNNNNNNNN NNNNNNNNNN NNNNNNNNGN
SNLENIEGLN KYNIYKKKKG KNESNTSLNN IYISSPNLSE RSDNSIGSYC TNKTMKSENS
IINIETLFRD SVSEQNSDEC GSKVDKDLDE DDDDDDDETE VPELVDYSEM IVSILYPVCI
TMVIVVLAIR AISSSTSKNS QIVEISNDNS GGNGDSSSGA DKMVFDSVVN SLIFLAVIIL
STTIMVVLYK FKLMKALYAW LMGTSILLLG VFGGFLFLIL LAYLNLGLDY VTFVIVVWNF
SVGGIVCIFW YSPKLLNQGY LISISVLMAL FFSRLPDWTT WGILSIVSIY DIFAVLCPGG
PLRILIETAQ KRNENIPAMI YNASIYIGMI YNEDNLENNN NNNNNNNIEL NINEVDIENN
NNNEDENKNN TEDGNNNNNK NKNNNNNNNN RIENENGAEN SSENGSITPP PTIPNFIKDE
KEINRSSGSN GFPNFKKCAN DNILIGDAET NDEIVSNAES SIDSTISESY VKPKQSIRLG
LGDFVFYSVL IGKAASYQIT TVFTVFIAII TGLFLTLILL AVFRRALPAL PMSIIFGIIV
FFLTFKILIQ YIYFLGENQI FV
