ID A0A0S3R3L1_PHAAN Unreviewed; 337 AA.
AC A0A0S3R3L1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Endopeptidase S2P {ECO:0000256|ARBA:ARBA00032658};
GN Name=Vigan.01G307600 {ECO:0000313|EMBL:BAT75243.1};
GN ORFNames=VIGAN_01307600 {ECO:0000313|EMBL:BAT75243.1};
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:BAT75243.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT75243.1, 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase M50A family.
CC {ECO:0000256|ARBA:ARBA00009989}.
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DR EMBL; AP015034; BAT75243.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3R3L1; -.
DR Proteomes; UP000291084; Chromosome 1.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR InterPro; IPR001193; MBTPS2.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR008915; Peptidase_M50.
DR PANTHER; PTHR13325:SF3; MEMBRANE-BOUND TRANSCRIPTION FACTOR SITE-2 PROTEASE; 1.
DR PANTHER; PTHR13325; PROTEASE M50 MEMBRANE-BOUND TRANSCRIPTION FACTOR SITE 2 PROTEASE; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000291084};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..337
FT /note="Endopeptidase S2P"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006616658"
FT DOMAIN 266..322
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
SQ SEQUENCE 337 AA; 37539 MW; 44D868CC1FB17A38 CRC64;
MCCAACGLAL FFLPLILFPF YTSGHNPKVL NVPPTSPLSG YLAPGDVILS IDDVTIRNSQ
EWLKLNTLTY NVKLNNVNLS HRTGELETVN KMKGYCVPSF MMEEIKITKW LGNQHVCPGE
LTAFVKLCSS NVTLHDGQNK TDLLNIGRSM YCINAKDVVK RNRCGDDRGL ATLRGGGCTC
LQDEFCLAPV QEPGLVWVEI SYSSPSHECL SHEQNRFPFS KTSGVKATNC GGTFIFVGDV
VSMAHSIKLT SYQPRWGPQI VAYFPSILER ILIWTFHTSL ALALFNALPV YLLDGEYILD
ATLSYFTSLS SRKRKKVLRV CLFSSTPPCK YLVRNLD
//
