GenomeNet

Database: UniProt
Entry: A9P7Y0_POPTR
LinkDB: A9P7Y0_POPTR
Original site: A9P7Y0_POPTR 
ID   A9P7Y0_POPTR            Unreviewed;       540 AA.
AC   A9P7Y0;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=PA domain-containing protein {ECO:0000259|Pfam:PF02225};
OS   Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp.
OS   trichocarpa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX   NCBI_TaxID=3694 {ECO:0000313|EMBL:ABK92483.1};
RN   [1] {ECO:0000313|EMBL:ABK92483.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Outer xylem {ECO:0000313|EMBL:ABK92483.1};
RX   PubMed=18230180; DOI=10.1186/1471-2164-9-57;
RA   Ralph S.G., Chun H.J., Cooper D., Kirkpatrick R., Kolosova N., Gunter L.,
RA   Tuskan G.A., Douglas C.J., Holt R.A., Jones S.J., Marra M.A., Bohlmann J.;
RT   "Analysis of 4,664 high-quality sequence-finished poplar full-length cDNA
RT   clones and their utility for the discovery of genes responding to insect
RT   feeding.";
RL   BMC Genomics 9:57-57(2008).
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; EF144219; ABK92483.1; -; mRNA.
DR   AlphaFoldDB; A9P7Y0; -.
DR   MEROPS; A22.A05; -.
DR   ExpressionAtlas; A9P7Y0; baseline and differential.
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   2: Evidence at transcript level;
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   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..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..540
FT                   /note="PA domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002739865"
FT   TRANSMEM        200..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        259..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        283..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        327..345
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        351..371
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        378..401
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        438..457
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        469..491
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        497..516
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          95..173
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
SQ   SEQUENCE   540 AA;  59051 MW;  31AAA4F7DBC4D758 CRC64;
     MAFPSRRRRR SCSLHAVLLF SFLFLIGLSF AEEASHDGDS PKFPGCDHPY NLVKVKNWAH
     GVEGETFAGI TARFGAFLPK EEKNSYRLTA VFSNPLNGCS PSSSKLSGSI AMAVRGGCDF
     TTKAEVAQSG GAAALLVIND EEELAEMGCE KGTSAQDISI PVVLIPKSGG QSLNKSIVNG
     QKVELLFYAP VRPPVDLSVI FLWIMAVGTV VCASVWSEIA ASEETNERYN ELSPKETSNA
     SAFKDDTEKE VIDINVKSAI VFVITASAFL LLLYFFMSSW FVWLLIVLFC IGGIEGMHNC
     ITTVILRICR NCGRKKLNLP LFGETSLFSL LVLICCVVFS TVWAINRQAS YSWAGQDILG
     ICLMITVLQV ARLPNIKVAT VLLCCAFVYD IFWVFLSPII FHQSVMIAVA RGDNSGGETI
     PMLLRIPRFA DEWGGYDMIG FGDILFPGLL VSFAFRYDKA NKKGIANGYF LWLTIGYGVG
     LFLTYLGLYL MDGHGQPALL YLVPCTLGLC ILLGLVRGEL KDLWNYSSED ASSRASSGLA
//
DBGET integrated database retrieval system