ID A0A1U7ZSB1_NELNU Unreviewed; 955 AA.
AC A0A1U7ZSB1;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Insulin-degrading enzyme-like 1, peroxisomal isoform X3 {ECO:0000313|RefSeq:XP_010257147.1};
GN Name=LOC104597372 {ECO:0000313|RefSeq:XP_010257147.1};
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_010257147.1};
RN [1] {ECO:0000313|RefSeq:XP_010257147.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR RefSeq; XP_010257147.1; XM_010258845.2.
DR AlphaFoldDB; A0A1U7ZSB1; -.
DR GeneID; 104597372; -.
DR OrthoDB; 129328at2759; -.
DR Proteomes; UP000189703; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR InterPro; IPR032632; Peptidase_M16_M.
DR PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR Pfam; PF16187; Peptidase_M16_M; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000189703};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 7..131
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 163..337
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 345..625
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 629..816
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 955 AA; 110302 MW; 1A7F0D5C82AC8B9F CRC64;
MLFFFDKRAA ASMNVCVGSF SNPEGLDGLA HFLEHMLFYA SEKYPLEDSY SKYIAEHGGS
TNAFTSSERT NYHFDINTDC FEEALDRFAQ FFIKPLMSPD ATMREIKAVD SENQKNLLSD
VWRMNQLQKH LCTEAHPYHK FSTGNWDTLE VRPKARGIDI RCELIKFYEE RYSANLMQLV
VYGKESLDKI QSLVENKFQE IPNTNRSCFS FPGQPCTPEH LQILVKAVPI MQGHKLRIIW
PITPSIHYYK EGPCRYLGHL IGHKGEGSLF LILKKLGWAI SLSAGEGDFT REFSFFKVVI
DLTDAGHEHM GEIVGLLFKY IILLQQSGVK KWVFDEISAI CETVFHYKDK IPPINYVVNV
ASNMKLYPPK DWLVASSLPL NFNPGTIQMV LDELTMNNVR IFWESKKFEG HTDMLEPWYG
TAYAVMKLTD SMIQKWIDTA PNDCLHLPAP NLFIPTDLSL KDVQGKAKYP VLLRKSAYSR
LWYKPDTMFF TPKAYIRIDF NCPYASHSPE AQILTYIFTQ LLMDYLNEYA YDAQVAGLHY
AIYLKDTGFQ VIVLGYNHKM RILLETVVQK IAEFKVKPDR FAVVKESVTK EYENFKFQQP
YQQALYYCST ILEDHSWPWS EKLEALPHLE ADDLAKFSPV MLSRAFLECY IAGNFDQNEA
ESVIKHIEDT LFKCPQPISK QLSPSEHLAT RTIKLESSLS YFYPIEGLNQ SDKNSALVHY
IQVHQDDSVL NVKLQLFSLI AKQAAFHQLR SVEQLGYITV LMQRNDFGIR GLQFIIQSTE
KDPQEVDLRV EAFLKVFESK LHVMTNDEFK SNVNALIDMK LERHKNLREE SSFYWKEIVY
GTLKFDRKES EVAALEQLTQ QELIDFFNEY IKVGAPRKKI LSVQVYGGLH SDGYKLAKSE
RIQPQSVRID DIFSFRRSRP LYGSFKGGLG HMKLQMFQPG CTVTVREPPL MQHCS
//
