PSNB_DICDI
ID PSNB_DICDI Reviewed; 473 AA.
AC Q54DE8;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Presenilin-B;
DE Short=PS-B;
DE EC=3.4.23.-;
GN Name=psenB; ORFNames=DDB_G0292310;
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; AAFI02000189; EAL61279.1; -; Genomic_DNA.
DR RefSeq; XP_629693.1; XM_629691.1.
DR AlphaFoldDB; Q54DE8; -.
DR SMR; Q54DE8; -.
DR STRING; 44689.DDB0231428; -.
DR MEROPS; A22.A10; -.
DR PaxDb; Q54DE8; -.
DR EnsemblProtists; EAL61279; EAL61279; DDB_G0292310.
DR GeneID; 8628609; -.
DR KEGG; ddi:DDB_G0292310; -.
DR dictyBase; DDB_G0292310; psenB.
DR eggNOG; KOG2736; Eukaryota.
DR HOGENOM; CLU_578009_0_0_1; -.
DR InParanoid; Q54DE8; -.
DR OMA; MQPVADP; -.
DR PhylomeDB; Q54DE8; -.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR PRO; PR:Q54DE8; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:dictyBase.
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:0005635; C:nuclear envelope; IDA:dictyBase.
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; IMP: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; 2.
DR Pfam; PF01080; Presenilin; 2.
DR PRINTS; PR01072; PRESENILIN.
DR SMART; SM00730; PSN; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Hydrolase; Membrane;
KW Notch signaling pathway; Protease; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..473
FT /note="Presenilin-B"
FT /id="PRO_0000331268"
FT TOPO_DOM 1..164
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..224
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..286
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 330..334
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..389
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 411..413
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 435..442
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 443..463
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 464..473
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 439..441
FT /note="PAL"
FT COMPBIAS 19..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 348
FT /evidence="ECO:0000250"
FT ACT_SITE 394
FT /evidence="ECO:0000250"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 473 AA; 52559 MW; CA2263FCFDFA2C54 CRC64;
MSSDNNNDPF DLNEDGHDYF NRVSTTTSPN RQSINSSPKQ SSPKSTNNND DKNNIILDLN
DNNNDNNNTN NYNDEDIDVD NKNKFENKDN TYNSNGGSNN KNKNKKKDNK SNNSSDNEEA
DENTSLISDS EPLLNKKEKD DEQIEIENLD GEDYDDEVSL QDFSSMIVSI IIPVSITMMA
VVFFVKYLNN QTLYASTLSY TIAGGSSGGG SGADSITGNS FVDSLIVAGI VLGMIIVTTV
AFVLLYKYRC LKILYGWLFL SVGMMLGSFG TTFFQAMLSA ANLPLDYITF AFLIFNFTVC
GIIGVFWYAH QYVNQLYLVI ISVLMAISLT RLPQWTIFTL LVIVAIYDLF AVLCPRGPLK
VLVELSQERN ENIPALVYET GKGSDSNLKL GLGDFIFYSL LISRAALVHM SCVFSTFIAI
LTGLFLTLLC LAIFKKALPA LPISIFLGIL FYYLSNNFLT PFIEALTLSQ IFV
