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Database: UniProt
Entry: A0A210QTX2_MIZYE
LinkDB: A0A210QTX2_MIZYE
Original site: A0A210QTX2_MIZYE 
ID   A0A210QTX2_MIZYE        Unreviewed;       515 AA.
AC   A0A210QTX2;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Presenilin {ECO:0000256|RuleBase:RU361148};
DE            EC=3.4.23.- {ECO:0000256|RuleBase:RU361148};
GN   ORFNames=KP79_PYT10275 {ECO:0000313|EMBL:OWF52175.1};
OS   Mizuhopecten yessoensis (Japanese scallop) (Patinopecten yessoensis).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Pectinida; Pectinoidea; Pectinidae;
OC   Mizuhopecten.
OX   NCBI_TaxID=6573 {ECO:0000313|EMBL:OWF52175.1, ECO:0000313|Proteomes:UP000242188};
RN   [1] {ECO:0000313|Proteomes:UP000242188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PY_sf001 {ECO:0000313|Proteomes:UP000242188};
RX   PubMed=28812685; DOI=10.1038/s41559-017-0120;
RA   Wang S., Zhang J., Jiao W., Li J., Xun X., Sun Y., Guo X., Huan P.,
RA   Dong B., Zhang L., Hu X., Sun X., Wang J., Zhao C., Wang Y., Wang D.,
RA   Huang X., Wang R., Lv J., Li Y., Zhang Z., Liu B., Lu W., Hui Y., Liang J.,
RA   Zhou Z., Hou R., Li X., Liu Y., Li H., Ning X., Lin Y., Zhao L., Xing Q.,
RA   Dou J., Li Y., Mao J., Guo H., Dou H., Li T., Mu C., Jiang W., Fu Q.,
RA   Fu X., Miao Y., Liu J., Yu Q., Li R., Liao H., Li X., Kong Y., Jiang Z.,
RA   Chourrout D., Li R., Bao Z.;
RT   "Scallop genome provides insights into evolution of bilaterian karyotype
RT   and development.";
RL   Nat. Ecol. Evol. 1:120-120(2017).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OWF52175.1}.
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DR   EMBL; NEDP02001917; OWF52175.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A210QTX2; -.
DR   STRING; 6573.A0A210QTX2; -.
DR   EnsemblMetazoa; XM_021494179.1; XP_021349854.1; LOC110448115.
DR   EnsemblMetazoa; XM_021494180.1; XP_021349855.1; LOC110448115.
DR   OrthoDB; 205653at2759; -.
DR   Proteomes; UP000242188; Unassembled WGS sequence.
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   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:UP000242188};
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        102..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361148"
FT   TRANSMEM        156..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361148"
FT   TRANSMEM        184..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361148"
FT   TRANSMEM        216..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361148"
FT   TRANSMEM        243..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361148"
FT   TRANSMEM        267..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361148"
FT   TRANSMEM        305..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361148"
FT   TRANSMEM        454..476
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361148"
FT   TRANSMEM        483..505
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361148"
FT   REGION          1..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          326..424
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..87
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        369..386
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..419
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   515 AA;  56767 MW;  C4454EBBB072BDA2 CRC64;
     MSTTVIESDD SAGETRPLMS TGTAYSGRRS QPVTRDQYEN FDDGRTRDNQ GNGIGMDVNH
     EDEADETRAE IRPARQPQRR RGTSGEGEED EDEVMLYGAK HVIMLFAPVT VCMIVVVASI
     SSVTFYTKKS GYLIYTPFHD GDKPDSTTGT KVWQSLANAM ILLGVVIVMT IFLLLLYKYR
     CYKVIHGWLV GSSLMLLFLF SYLYIEVVLQ AYNVPIDYIT VALLIWNFGV MGMICIHWKG
     PLILQQAYLI IISALMSLIF IKYLPDWTTW VLLGVMVIWD LVAVLCPKGP LRMLVETAQK
     RNEPIFPALI YSSTMIWTVG IGMAEGNPKK KKKSKKSKKD TQTDAATGGA SLAVDNGSDD
     DDDSGFTRNS AHEQVLARNS TDSAEARNAV AALADRPTQP ATARPSRQAA PSNSRDSQAS
     AQQDEERGIK LGLGDFIFYS VLVGKASSYG DWNTTLACFV AILIGLCFTL LLLAIFKKAL
     PALPISITFG LIFNFATSEI MAPFLDRLAS GQVYV
//
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