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Database: UniProt
Entry: Q2PEQ9_TRIPR
LinkDB: Q2PEQ9_TRIPR
Original site: Q2PEQ9_TRIPR 
ID   Q2PEQ9_TRIPR            Unreviewed;       537 AA.
AC   Q2PEQ9;
DT   07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT   07-FEB-2006, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=PA domain-containing protein {ECO:0000259|Pfam:PF02225};
OS   Trifolium pratense (Red clover).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Trifolium.
OX   NCBI_TaxID=57577 {ECO:0000313|EMBL:BAE71293.1};
RN   [1] {ECO:0000313|EMBL:BAE71293.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=13679984; DOI=10.1007/s00122-003-1412-z;
RA   Isobe S., Klimenko I., Ivashuta S., Gau M., Kozlov N.N.;
RT   "First RFLP linkage map of red clover ( Trifolium pratense L.) based on
RT   cDNA probes and its transferability to other red clover germplasm.";
RL   Theor. Appl. Genet. 108:105-112(2003).
RN   [2] {ECO:0000313|EMBL:BAE71293.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16769692; DOI=10.1093/dnares/dsi018;
RA   Sato S., Isobe S., Asamizu E., Ohmido N., Kataoka R., Nakamura Y.,
RA   Kaneko T., Sakurai N., Okumura K., Klimenko I., Sasamoto S., Wada T.,
RA   Watanabe A., Kohara M., Fujishiro T., Tabata S.;
RT   "Comprehensive structural analysis of the genome of red clover (Trifolium
RT   pratense L.).";
RL   DNA Res. 12:301-364(2005).
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; AB236841; BAE71293.1; -; mRNA.
DR   AlphaFoldDB; Q2PEQ9; -.
DR   EnsemblPlants; Tp57577_TGAC_v2_mRNA16141; Tp57577_TGAC_v2_mRNA16141; Tp57577_TGAC_v2_gene15618.
DR   Gramene; Tp57577_TGAC_v2_mRNA16141; Tp57577_TGAC_v2_mRNA16141; Tp57577_TGAC_v2_gene15618.
DR   ExpressionAtlas; Q2PEQ9; baseline.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042500; F:aspartic endopeptidase activity, intramembrane cleaving; IEA:InterPro.
DR   CDD; cd02132; PA_GO-like; 1.
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..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..537
FT                   /note="PA domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004213520"
FT   TRANSMEM        254..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        278..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        323..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        347..367
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        374..397
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        429..450
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        462..482
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        494..512
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          92..169
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
SQ   SEQUENCE   537 AA;  58795 MW;  7FE20CF41B83C89B CRC64;
     MPSPSRGRRF FLSVLLVLLF FVTASASDDV KRDDDRAPKS KSCNNPFQLV KVKNWVDGDE
     AITHSGMTAR FGSSLPEKAD NSVRTRVLFS NPTDCCSPST SQLSDSVALC VRGGCDFQIK
     ATIAQSGGAT AVLIINDQED LVEMVCSDTT EANISIPVVM ITKSAGEALN ASLTTGKRVE
     VLLYAPPRPL VDFSVAFLWL VSVGTIVCAS LWSDITTPEK SGERYNELYP KESQNAAAAR
     GGSDKQVVNI NSKAAVIFII SASTFLVLLF FFMSSWFLWL LIVLFCIAGI EGMHNCITTL
     TLRKWENCGE KTVNVPLFGE TSIFSLVVCL FCFAFAVFWA STRHASYSWI FQDTLGICLI
     ITVLQVAQLP NIKVATVLLS CAFAYDIFWV FISPLIFHES VMIAVARGDK AGGEALPMLL
     RFPRFFDTWG GYEMIGFGDI IFPGLLVSFA HRLDKDNKKG ALNGYFLWLV IGYGVGLIFT
     YLGLYLMDGN GQPALLYLVP CTLGVIIILG FARGELKSLW NYGTDSSLST EPADSEV
//
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