ID A0A0S3RQS3_PHAAN Unreviewed; 541 AA.
AC A0A0S3RQS3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=PA domain-containing protein {ECO:0000259|Pfam:PF02225};
GN Name=Vigan.04G002300 {ECO:0000313|EMBL:BAT82937.1};
GN ORFNames=VIGAN_04002300 {ECO:0000313|EMBL:BAT82937.1};
OS Vigna angularis var. angularis.
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; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT82937.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT82937.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(2015).
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; AP015037; BAT82937.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3RQS3; -.
DR Proteomes; UP000291084; Chromosome 4.
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 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:UP000291084};
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..541
FT /note="PA domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006617289"
FT TRANSMEM 261..279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 285..308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 329..347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 380..398
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 440..459
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 471..494
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 500..518
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 102..174
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
SQ SEQUENCE 541 AA; 59014 MW; F0B2D0A422E46522 CRC64;
MQTKTMSPPG LPVLLLLLFF IATATAAATA AADNDAKRDD QRAPKSQSCN NPFQLVKVEN
WIDGVEGRIY NGVTARFGSL LPEKPENSVR TPAIFSNPVD CCSNSTSKLS GSVALCIRGG
CDFTVKAEFA QAGGATGMLV INDAEDLFEM VCSNSSEANI SIPVVMITKS AGEGLNNSLI
SGRKVEILLY APPRPLVDFS VAFLWLMSVG TIVCASLWSD FTSPEKSDER YNELCPKESS
IAETARDDFD KEIVHIDSKG AIIFVIAAST FLVLLFFFMS SWFVWVLIVL FCIGGIEGMH
NCIVSLTVRK GRSCGQKTVS VPLFGETSIF SLVVLLFCVT FAVFWAATRQ ESYSWIGQDI
LGICLMITVL QLARLPNIKV ATVLLCCAFV YDIFWVFISP VIFHESVMIA VARGDKAGGE
AIPMLLRFPR LFDPWGGYDM IGFGDILFPG LLVSFAHRFD KDNGRGASNG YFLWLVIGYG
IGLVFTYLGL YLMNGNGQPA LLYLVPCTLG VTVILGCIRG ELKNLWNYGT DPSLSTEHSE
V
//
