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Database: UniProt
Entry: A0A2H9ZXK8_9ASPA
LinkDB: A0A2H9ZXK8_9ASPA
Original site: A0A2H9ZXK8_9ASPA 
ID   A0A2H9ZXK8_9ASPA        Unreviewed;       554 AA.
AC   A0A2H9ZXK8;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Signal peptide peptidase-like 5 {ECO:0000313|EMBL:PKA48045.1};
DE            EC=3.4.23.- {ECO:0000313|EMBL:PKA48045.1};
GN   Name=SPPL5 {ECO:0000313|EMBL:PKA48045.1};
GN   ORFNames=AXF42_Ash015808 {ECO:0000313|EMBL:PKA48045.1};
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:PKA48045.1, ECO:0000313|Proteomes:UP000236161};
RN   [1] {ECO:0000313|EMBL:PKA48045.1, 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:PKA48045.1};
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; KZ452995; PKA48045.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H9ZXK8; -.
DR   STRING; 1088818.A0A2H9ZXK8; -.
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:SF75; INTRAMEMBRANE PROTEASE (IMPAS) FAMILY; 1.
DR   PANTHER; PTHR12174; SIGNAL PEPTIDE PEPTIDASE; 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:PKA48045.1};
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..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..554
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014169224"
FT   TRANSMEM        192..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        242..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        271..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        312..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        341..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        369..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        424..446
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        458..479
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        491..516
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          82..165
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
SQ   SEQUENCE   554 AA;  60829 MW;  7FF64C8C52E66661 CRC64;
     MRTSGVFGLI TMAVVLPALV SGGDIVHEDD RFPKIPGCSN HFVLVKVQTW INGVEDSEFV
     GVGARFGPTI VSKEKHANRT GLVVSDPHDC CSPPRNEISG DVLLVHRGSC KFTTKAKIAE
     AAGASAILIV NNRRELYKMV CDGNETDLHI KIPAVMLPHD AGASLESVIS SKHSVAVQLY
     SPDRPLVDTA EIFLWLMAVG TILCASIWSA WSSREASIEY EKLLKDAPEE LLNMESTGSS
     GVVDINTLSA ILFVLIASGF LVMLYKFMST WFVEILVVLF CIGGIEGLQT CLVALLSRWF
     KQAGDSFIKV PFFGAVSYLT LAITPFCVAF AVLWAVYRQK AFAWIGQDIL GIALILTVIQ
     IVRVPNLKVG TVLLSCAFLY DIFWVFASHW FFHESVMIVV ARGDRSGEDG VPMLLKIPRM
     FDPWGGYSII GFGDILLPGL LVAFSLRYDW ATKKNVNAGY FLWSMVAYGS GLLITYVALN
     LMDGHGQPAL LYIVPFTLDI IVNGISGQII FLFFIFKTSA GTLLSLGWKR GELKNLWTTG
     QPDRICPHIK ASLQ
//
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