ID A0A1U8B5A9_NELNU Unreviewed; 464 AA.
AC A0A1U8B5A9;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Probable membrane metalloprotease ARASP2, chloroplastic {ECO:0000313|RefSeq:XP_010276130.1};
GN Name=LOC104610955 {ECO:0000313|RefSeq:XP_010276130.1};
OS Nelumbo nucifera (Sacred lotus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Proteales; Nelumbonaceae; Nelumbo.
OX NCBI_TaxID=4432 {ECO:0000313|Proteomes:UP000189703, ECO:0000313|RefSeq:XP_010276130.1};
RN [1] {ECO:0000313|RefSeq:XP_010276130.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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 RefSeq; XP_010276130.1; XM_010277828.2.
DR AlphaFoldDB; A0A1U8B5A9; -.
DR STRING; 4432.A0A1U8B5A9; -.
DR GeneID; 104610955; -.
DR KEGG; nnu:104610955; -.
DR eggNOG; ENOG502QT40; Eukaryota.
DR InParanoid; A0A1U8B5A9; -.
DR OrthoDB; 3675515at2759; -.
DR Proteomes; UP000189703; Unplaced.
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:UniProtKB-KW.
DR CDD; cd00989; PDZ_metalloprotease; 1.
DR CDD; cd06163; S2P-M50_PDZ_RseP-like; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004387; Pept_M50_Zn.
DR InterPro; IPR008915; Peptidase_M50.
DR PANTHER; PTHR42837:SF2; MEMBRANE METALLOPROTEASE ARASP2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR42837; REGULATOR OF SIGMA-E PROTEASE RSEP; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000313|RefSeq:XP_010276130.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000189703};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 194..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 434..451
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 214..281
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 464 AA; 50154 MW; C84C221CB82FAE4D CRC64;
MLINVSTSPP TPSLSFLIRL SNPKLNGSDF PLKSRTHLSK SFYSSSSSSS CHSLCYHSSS
SYFRTHDANH LFYLKRRYQH GKRDSFRSLA IPGFELGSLE GPQSVLEAAA VLTAIILVHE
SGHFLAAYLQ GIHVSKFAVG FGPILAKFNS NNVEYSIRAF PLGGFVGFPD NDPESDIPVD
DENLLKNRPI FDRVLVISAG VIANIIFAYG IIFGQVLSVG LPVQEAFPGV LVPEVRAYSA
AARDGLLPGD VILAVNGIEL PRTGPAAVSE LVDIIKNNPK KNVFLKVGRG KQDLEIGVTP
DESFDGSGRI GVQLSPNVKI TKIRPKNLLD AMNYAGREFW GLSFNVLDSL KQTFLNFSQS
ASKVSGPVAI IAVGAEVARS NTDGLFQFAA ILNLNLAVIN LLPLPALDGG SLALLLVEAA
RGGRKLPQEV EQRIMSSGIM VVILLGLFLI IRDTLNLDFI KELL
//
