ID D7KQ50_ARALL Unreviewed; 540 AA.
AC D7KQ50;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:EFH65617.1};
GN ORFNames=ARALYDRAFT_470110 {ECO:0000313|EMBL:EFH65617.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL348713; EFH65617.1; -; Genomic_DNA.
DR RefSeq; XP_002889358.1; XM_002889312.1.
DR AlphaFoldDB; D7KQ50; -.
DR STRING; 81972.D7KQ50; -.
DR MEROPS; A22.A03; -.
DR EnsemblPlants; fgenesh2_kg.1__64__AT1G01650.1; fgenesh2_kg.1__64__AT1G01650.1; fgenesh2_kg.1__64__AT1G01650.1.
DR Gramene; fgenesh2_kg.1__64__AT1G01650.1; fgenesh2_kg.1__64__AT1G01650.1; fgenesh2_kg.1__64__AT1G01650.1.
DR eggNOG; KOG2442; Eukaryota.
DR HOGENOM; CLU_023799_4_1_1; -.
DR OrthoDB; 51438at2759; -.
DR Proteomes; UP000008694; 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:SF102; SIGNAL PEPTIDE PEPTIDASE-LIKE 4; 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};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008694};
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..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..540
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003100959"
FT TRANSMEM 196..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 246..269
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 275..306
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 318..342
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 375..393
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 430..452
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 464..485
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 491..510
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 91..169
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
SQ SEQUENCE 540 AA; 59920 MW; EF64DD1E62E31585 CRC64;
MILWKSLSCF SFVFGLLLYS ASFVSAGDIV HHDDSLPQRP GCNNNFVLVK VPTRVNGSEY
TEFVGVGARF GPTLESKEKH ATLIKLAIAD PPDCCSTPKN KLTGEVILVH RGKCSFTTKT
KVAEAAGASA ILIINNSTDL FKMVCEKGEN VLDITIPVVM LPVDAGRSLE DIVKSNSLVT
LQLYSPKRPA VDVAEVFLWL MAVGTILCAS YWSAWTVREE AIEQDKLLKD GSDELLQLST
TSSRGVVEVT VISAILFVVV ASCFLIMLYK LMSFWFIEVL VVLFCIGGVE GLQTCLVALL
SCFRWFRRFG ESYLKVPILG AVSYLTLAIC PFCIAFAVFW AVKRQYSYAW IGQDILGISL
IITVLQIVRV PNLKVGFVLL SCAFMYDIFW VFVSKWWFRE SVMIVVARGD RSGEDGIPML
LKIPRMFDPW GGYSIIGFGD IILPGLLVTF ALRYDWLANK RLKSGYFLGT MSAYGLGLLI
TYIALNLMDG HGQPALLYIV PFILGTLFVL GHKRGDLKTL WTTGEPDRPC PHVRLQPQSS
//
