ID A0A158QYA4_NIPBR Unreviewed; 584 AA.
AC A0A158QYA4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Presenilin hop-1 (inferred by orthology to a C. elegans protein) {ECO:0000313|WBParaSite:NBR_0000815601-mRNA-1};
GN ORFNames=NBR_LOCUS8157 {ECO:0000313|EMBL:VDL71746.1};
OS Nippostrongylus brasiliensis (Rat hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Heligmosomidae; Nippostrongylus.
OX NCBI_TaxID=27835 {ECO:0000313|Proteomes:UP000038043, ECO:0000313|WBParaSite:NBR_0000815601-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:NBR_0000815601-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDL71746.1, ECO:0000313|Proteomes:UP000271162}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase A22A family.
CC {ECO:0000256|ARBA:ARBA00008604}.
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DR EMBL; UYSL01019969; VDL71746.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A158QYA4; -.
DR STRING; 27835.A0A158QYA4; -.
DR WBParaSite; NBR_0000815601-mRNA-1; NBR_0000815601-mRNA-1; NBR_0000815601.
DR Proteomes; UP000038043; Unplaced.
DR Proteomes; UP000271162; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW.
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; 2.
DR SMART; SM00730; PSN; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Notch signaling pathway {ECO:0000256|ARBA:ARBA00022976};
KW Reference proteome {ECO:0000313|Proteomes:UP000271162};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 114..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 225..247
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 267..289
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 344..365
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 517..545
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 31..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 584 AA; 65614 MW; A8665D115FB26BDA CRC64;
MSKNSTSTED TKDLAKVGLC RTFMASEALL SKHVPCLQRS KETTSAETTA EGKKATNTGR
TSGETATNEK TADKTTSKEP SNQRSPEKGK QSGEEADGET KSTRARRMYG PRDMVKVFIP
VSICMLIVVV CVRNVEIFKT DHVLPTPYVL YREVEVEPTT KLWQSGLNAA FLMAIIIIVT
LLIVGLFYFK CYLKCALFRG KVSSKSLTFT FSVSIRVHYV RNVHAANYCI VFSILVSRAY
VTDFSITLNP TERTPYSLIL RELDVPVSSV TFLFVLYNMA ILAMLCIFWK GPMKVQQVSV
YYFMKYIGTD SRVPWFNLWR ITLIIISAMV ALTIMVILPQ WTCWVLLIVL ALWDLFAVLT
PCGPLKILVE IAEKRGEDLM PALIYTGSVS EGGNSQVSTQ KTQTDDENAN KPEPGVESLR
VPNFAKSQEE EERNIRLGLG DFIFYSLLVG TAAKNGDWTT TMACYVAILT GLGFTLTIDR
VANHTDELIL EIRQTLNGTT YVLNDLGDAV AMLLDQLYLL LIWTLIFLVP ILCISIMLCG
IACLLRSTRR PVRYIPHYPH IPIVREDYNS SKVFREAEED ETIE
//
