ID A8XEJ8_CAEBR Unreviewed; 358 AA.
AC A8XEJ8;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=Presenilin {ECO:0000256|RuleBase:RU361148};
DE EC=3.4.23.- {ECO:0000256|RuleBase:RU361148};
GN Name=hop-1 {ECO:0000313|WormBase:CBG12097};
GN Synonyms=Cbr-hop-1 {ECO:0000313|EMBL:CAP31133.1};
GN ORFNames=CBG12097 {ECO:0000313|WormBase:CBG12097}, CBG_12097
GN {ECO:0000313|EMBL:CAP31133.1};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP31133.1, ECO:0000313|Proteomes:UP000008549};
RN [1] {ECO:0000313|EMBL:CAP31133.1, ECO:0000313|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000313|EMBL:CAP31133.1,
RC ECO:0000313|Proteomes:UP000008549};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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}.
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DR EMBL; HE601540; CAP31133.1; -; Genomic_DNA.
DR RefSeq; XP_002646379.1; XM_002646333.1.
DR AlphaFoldDB; A8XEJ8; -.
DR STRING; 6238.A8XEJ8; -.
DR MEROPS; A22.010; -.
DR EnsemblMetazoa; CBG12097.1; CBG12097.1; WBGene00033101.
DR EnsemblMetazoa; CBG12097.2; CBG12097.2; WBGene00033101.
DR GeneID; 8588376; -.
DR KEGG; cbr:CBG_12097; -.
DR CTD; 8588376; -.
DR WormBase; CBG12097; CBP17385; WBGene00033101; Cbr-hop-1.
DR eggNOG; KOG2736; Eukaryota.
DR HOGENOM; CLU_022975_3_0_1; -.
DR InParanoid; A8XEJ8; -.
DR OMA; ALCMIFV; -.
DR OrthoDB; 2881575at2759; -.
DR Proteomes; UP000008549; Unassembled WGS sequence.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0035253; C:ciliary rootlet; IBA:GO_Central.
DR GO; GO:0043198; C:dendritic shaft; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030426; C:growth cone; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR GO; GO:0042500; F:aspartic endopeptidase activity, intramembrane cleaving; IEA:InterPro.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0042987; P:amyloid precursor protein catabolic process; IBA:GO_Central.
DR GO; GO:0050435; P:amyloid-beta metabolic process; IBA:GO_Central.
DR GO; GO:0006816; P:calcium ion transport; IBA:GO_Central.
DR GO; GO:0018991; P:egg-laying behavior; IEA:EnsemblMetazoa.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IEA:EnsemblMetazoa.
DR GO; GO:0008406; P:gonad development; IEA:EnsemblMetazoa.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0002119; P:nematode larval development; IEA:EnsemblMetazoa.
DR GO; GO:0007220; P:Notch receptor processing; IBA:GO_Central.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:EnsemblMetazoa.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IEA:EnsemblMetazoa.
DR GO; GO:0016485; P:protein processing; IEA:InterPro.
DR GO; GO:0042659; P:regulation of cell fate specification; IEA:EnsemblMetazoa.
DR GO; GO:0040028; P:regulation of vulval development; IEA:EnsemblMetazoa.
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:SF14; PRESENILIN HOP-1; 1.
DR Pfam; PF01080; Presenilin; 2.
DR PRINTS; PR01072; PRESENILIN.
DR SMART; SM00730; PSN; 1.
PE 3: Inferred from homology;
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:UP000008549};
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 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 60..79
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 86..107
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 146..163
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 169..193
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 295..316
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 328..357
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
SQ SEQUENCE 358 AA; 39693 MW; CBFA6BEE9D2DA07D CRC64;
MVRTRRVYSG ATLLRVLYPV ALCMIFVAIN VSICRPPITK TPKVIYGVFH SYDTEESGHV
TLLLMIFLVL TTTMGVVCYK KRLYKAITAY IIANSISLLL VYAFFHFHNL AQACSIPMSV
PSSVFLTFQF GGLGVLSLHW KAHRRLHQFY LVMLAALTAL FLLKNLPDWT VWISIVAISI
WDIVAVLTPC GPLKMLVETA SRRGDNNFPA ILYNSSSYVE TPETPDTTRP HSTQLTEFSN
SSNANLLQSD SLLTTPVIPR RTREVREVEG TIRLGMGDFV FYSLMLGNAA QTSPLTTVLA
CFLSNLVGLT ITLPVVSLSQ TALPALPFPL LIAALFYFSS HVALTPFTNL CSLTLILF
//
