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Database: UniProt
Entry: A0A2I0A2B6_9ASPA
LinkDB: A0A2I0A2B6_9ASPA
Original site: A0A2I0A2B6_9ASPA 
ID   A0A2I0A2B6_9ASPA        Unreviewed;       552 AA.
AC   A0A2I0A2B6;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Signal peptide peptidase-like 2 {ECO:0000313|EMBL:PKA49663.1};
DE            EC=3.4.23.- {ECO:0000313|EMBL:PKA49663.1};
GN   Name=SPPL2 {ECO:0000313|EMBL:PKA49663.1};
GN   ORFNames=AXF42_Ash004204 {ECO:0000313|EMBL:PKA49663.1};
OS   Apostasia shenzhenica.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC   Apostasioideae; Apostasia.
OX   NCBI_TaxID=1088818 {ECO:0000313|EMBL:PKA49663.1, ECO:0000313|Proteomes:UP000236161};
RN   [1] {ECO:0000313|EMBL:PKA49663.1, ECO:0000313|Proteomes:UP000236161}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Shenzhen {ECO:0000313|Proteomes:UP000236161};
RC   TISSUE=Stem {ECO:0000313|EMBL:PKA49663.1};
RX   PubMed=28902843; DOI=10.1038/nature23897;
RA   Zhang G.Q., Liu K.W., Li Z., Lohaus R., Hsiao Y.Y., Niu S.C., Wang J.Y.,
RA   Lin Y.C., Xu Q., Chen L.J., Yoshida K., Fujiwara S., Wang Z.W., Zhang Y.Q.,
RA   Mitsuda N., Wang M., Liu G.H., Pecoraro L., Huang H.X., Xiao X.J., Lin M.,
RA   Wu X.Y., Wu W.L., Chen Y.Y., Chang S.B., Sakamoto S., Ohme-Takagi M.,
RA   Yagi M., Zeng S.J., Shen C.Y., Yeh C.M., Luo Y.B., Tsai W.C.,
RA   Van de Peer Y., Liu Z.J.;
RT   "The Apostasia genome and the evolution of orchids.";
RL   Nature 549:379-383(2017).
CC   -!- FUNCTION: Intramembrane-cleaving aspartic protease (I-CLiP) that
CC       cleaves type II membrane signal peptides in the hydrophobic plane of
CC       the membrane. {ECO:0000256|ARBA:ARBA00003012}.
CC   -!- SUBCELLULAR LOCATION: Endosome membrane
CC       {ECO:0000256|ARBA:ARBA00004337}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004337}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the peptidase A22B family.
CC       {ECO:0000256|ARBA:ARBA00006859}.
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DR   EMBL; KZ452037; PKA49663.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I0A2B6; -.
DR   OrthoDB; 51438at2759; -.
DR   Proteomes; UP000236161; Unassembled WGS sequence.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042500; F:aspartic endopeptidase activity, intramembrane cleaving; IEA:InterPro.
DR   Gene3D; 3.50.30.30; -; 1.
DR   InterPro; IPR046450; PA_dom_sf.
DR   InterPro; IPR003137; PA_domain.
DR   InterPro; IPR007369; Peptidase_A22B_SPP.
DR   InterPro; IPR006639; Preselin/SPP.
DR   PANTHER; PTHR12174; SIGNAL PEPTIDE PEPTIDASE; 1.
DR   PANTHER; PTHR12174:SF90; SIGNAL PEPTIDE PEPTIDASE-LIKE 3; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF04258; Peptidase_A22B; 1.
DR   SMART; SM00730; PSN; 1.
DR   SUPFAM; SSF52025; PA domain; 1.
PE   3: Inferred from homology;
KW   Endosome {ECO:0000256|ARBA:ARBA00022753};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:PKA49663.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000236161};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..38
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           39..552
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014116561"
FT   TRANSMEM        210..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        269..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        293..319
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        331..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        361..381
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        388..411
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        447..466
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        478..500
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        506..525
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          114..182
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
SQ   SEQUENCE   552 AA;  60924 MW;  907854D1F5D3E79D CRC64;
     MTSPGGPVHP LRPSLLFRLV IFLVTCFVGL RNAPFAAASD DVSHDDEFAH KSEACNKEFQ
     LVKVRNWVDG DESMDIVGLS ARFGAFLPRH ASEAHQWPAT AANPLNCCAN LTSKLGNSIA
     IAKRGDCTFT TKAVVAQTGG ATGLLVINDS EDLYKMVCSE NDTSLNLTIP VVMIPKSAGD
     KLTKLLNDGR KVVVLLYSPR RPVVDFSATF LWLMAVGTIV CASLWAEFIA CDQVDERYNQ
     LTLKQDQPGT EMSSREHEKE VLEINSRGAI IFVIAASAFL MLLFYFMSSW FVLLLVVLFC
     IGGVEGMHIC LVSLILRVFK YCGQKTVRLP FFGEVLVLSV VMLPLCAAFA IFWAANRHAS
     YAWIGQDILG ICLMVTVLQM ARLPNIKVAS ALLCCAFVYD IFWVFVSPLI FHESVMIAVA
     RGDNSGEAIP MLLRTPRFFD PWGGYDMIGF GDILFPGLLI AFSYRYDRAN KKSIVSGYFV
     WLTIGYAFGL FLTYLALFLM DGHGQPALLY LVPCTLGLII ILGWVRGELG DLWNYGKIRS
     SDNAPITETG EA
//
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