ID B5X1U6_SALSA Unreviewed; 447 AA.
AC B5X1U6;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Presenilin {ECO:0000256|RuleBase:RU361148};
DE EC=3.4.23.- {ECO:0000256|RuleBase:RU361148};
GN Name=PSN2 {ECO:0000313|EMBL:ACI33277.1};
GN Synonyms=psn2 {ECO:0000313|RefSeq:NP_001133459.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|EMBL:ACI33277.1};
RN [1] {ECO:0000313|EMBL:ACI33277.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain {ECO:0000313|EMBL:ACI33277.1};
RG cGRASP (B.F. Koop & W.S. Davidson);
RA Leong J., von Schalburg K., Cooper G., Moore R., Holt R., Davidson W.S.,
RA Koop B.F.;
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACI33277.1, ECO:0000313|RefSeq:NP_001133459.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain {ECO:0000313|EMBL:ACI33277.1};
RX PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA Koop B.F.;
RT "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT evolutionary pressures on a post-tetraploidization genome.";
RL BMC Genomics 11:279-279(2010).
RN [3] {ECO:0000313|EMBL:ACI33277.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain {ECO:0000313|EMBL:ACI33277.1};
RG cGRASP (B.F. Koop & W.S. Davidson);
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|RefSeq:NP_001133459.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Probable subunit of the gamma-secretase complex, an
CC endoprotease complex that catalyzes the intramembrane cleavage of
CC integral membrane proteins such as Notch receptors.
CC {ECO:0000256|RuleBase:RU361148}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU361148}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU361148}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU361148}. Golgi apparatus membrane
CC {ECO:0000256|RuleBase:RU361148}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU361148}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- DOMAIN: The PAL motif is required for normal active site conformation.
CC {ECO:0000256|RuleBase:RU361148}.
CC -!- SIMILARITY: Belongs to the peptidase A22A family.
CC {ECO:0000256|ARBA:ARBA00008604, ECO:0000256|RuleBase:RU361148}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BT045015; ACI33277.1; -; mRNA.
DR RefSeq; NP_001133459.1; NM_001139987.1.
DR STRING; 8030.ENSSSAP00000052694; -.
DR MEROPS; A22.002; -.
DR PaxDb; 8030-ENSSSAP00000052694; -.
DR GeneID; 100194958; -.
DR KEGG; sasa:100194958; -.
DR CTD; 100194958; -.
DR OMA; WTTITFC; -.
DR OrthoDB; 205653at2759; -.
DR Proteomes; UP000087266; Chromosome ssa12.
DR Bgee; ENSSSAG00000051966; Expressed in spleen and 16 other cell types or 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:0042500; F:aspartic endopeptidase activity, intramembrane cleaving; 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; Presenilin; 1.
DR InterPro; IPR001108; Peptidase_A22A.
DR InterPro; IPR006639; Preselin/SPP.
DR InterPro; IPR042524; Presenilin_C.
DR PANTHER; PTHR10202; PRESENILIN; 1.
DR PANTHER; PTHR10202:SF13; PRESENILIN-2; 1.
DR Pfam; PF01080; Presenilin; 1.
DR PRINTS; PR01072; PRESENILIN.
DR SMART; SM00730; PSN; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU361148};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW ECO:0000256|RuleBase:RU361148}; Hydrolase {ECO:0000256|RuleBase:RU361148};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361148};
KW Notch signaling pathway {ECO:0000256|ARBA:ARBA00022976,
KW ECO:0000256|RuleBase:RU361148}; Protease {ECO:0000256|RuleBase:RU361148};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361148};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361148}.
FT TRANSMEM 85..103
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 137..158
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 165..187
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 226..242
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 248..266
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 384..405
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 412..429
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 447 AA; 50081 MW; B3D12F749A4535D4 CRC64;
MSTSDSDEDS YNERTALVAS EIPSVPSYQQ DPDQPQPADM EPRRRPVAPE PAAEPPSLDR
SAVEREPVDL EEEEELTLKY GAKHVIMLFV PVTLCMVVVV ATIKSVSFYT EKNGQQLIYT
PFTEDTDTVG ERLLNSVLNT IIMISVIVVM TIFLVVLYKY RCYKFIHGWL ILSSLMLLFW
FSFMYLGEVF KTYNLAMDYP TVAMIIWNFG AVGMICIHWK GPLQLQQAYL IAISALMALV
FIKYLPEWSA WVILGAISVY DLVAVLCPKG PLRMLVETAQ ERNEPIFPAL IYSSAMIWMV
GMANPARNAE PTNQDTDEEA HQSEGSALAR DWVEPETQVS SGMNRSYSTE DDLDEEDRGV
KLGLGDFIFY SVLVGKAAAT GGDWNTTLAC FVAILIGLCL TLLLLAIFKK ALPALPISIT
FGLVFYFSTD NLVRPFMDNL AAHQFYI
//
