IDE_DICDI
ID IDE_DICDI Reviewed; 962 AA.
AC Q54JQ2;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Insulin-degrading enzyme homolog;
DE EC=3.4.24.-;
DE AltName: Full=Insulin protease homolog;
DE Short=Insulinase homolog;
DE AltName: Full=Insulysin homolog;
GN ORFNames=DDB_G0287851;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
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DR EMBL; AAFI02000104; EAL63572.1; -; Genomic_DNA.
DR RefSeq; XP_637100.1; XM_632008.1.
DR AlphaFoldDB; Q54JQ2; -.
DR SMR; Q54JQ2; -.
DR STRING; 44689.DDB0187681; -.
DR MEROPS; M16.A14; -.
DR PaxDb; Q54JQ2; -.
DR PRIDE; Q54JQ2; -.
DR EnsemblProtists; EAL63572; EAL63572; DDB_G0287851.
DR GeneID; 8626354; -.
DR KEGG; ddi:DDB_G0287851; -.
DR dictyBase; DDB_G0287851; -.
DR eggNOG; KOG0959; Eukaryota.
DR HOGENOM; CLU_004639_1_1_1; -.
DR InParanoid; Q54JQ2; -.
DR OMA; INQVMEH; -.
DR PhylomeDB; Q54JQ2; -.
DR Reactome; R-DDI-9033241; Peroxisomal protein import.
DR PRO; PR:Q54JQ2; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR Pfam; PF16187; Peptidase_M16_M; 1.
DR SUPFAM; SSF63411; SSF63411; 4.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Zinc.
FT CHAIN 1..962
FT /note="Insulin-degrading enzyme homolog"
FT /id="PRO_0000331124"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 77
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
SQ SEQUENCE 962 AA; 112074 MW; DCBCB4E6A301533F CRC64;
MVANEQQQQQ QEEERKEVKL IQSPNDNNKY RYVKLKNGLE VVLVSDETTD QSSCCLSINI
GSLCNPREIE GLAHFLEHML FLGTEKFPVE KEFVNFIYLN GGSYNGTTSP NKTNYYFTVN
QESFEEALDR FSSFFISPLM NEDAVNRELN AVDSEHNNNM QKDFWRMDRI VNDQFEGHPM
SMFFTGDSST LKRDDIREKV VEFYQRYYSA NLMKVCIFGR ESLDQLEEYA NKYFLPIVNK
DVKVPKLPPL AITSKSIMIE AEPTQDMDLL KFVFPIPDEK LCFSKNYKNA SASILSHILG
HECQGSLFSV LFNKDYAFSL SISSNSFYEN MNKIEIQIHL TKTGLENVDE VIALLFQSFE
FDTPEYFFTE KKLLSEINWK SFQKSAPAST TQAITSNLFR VERPEETLKY NNFLEQFAPE
KIKEIQSYLR PDNMICLFYS STKFKGKTTE IEPHYKIKFN KRYIEQSDFD KWKSFPKNTN
LFLPKENPFL PIDTTIKAPQ DHSIHIPKEV YNNNGVKVYH SLDHRFNSPK ARVNIRFELT
SYGNNQSMVM WNLLKKSLKE VLNEKILYYL SVLDFSMKLQ ILTTHVELQC YCFNDIIFTA
LGKVFDFLMN LDLNDMQFKR IKEKVAKRFL SSHYLSPYQI SMRHLSLHNF NCNSMLLDKQ
EYLKKVTKSE FLNYFKSLFS YINFSAMVVG NASIEDACAF GEKLNSFSNR NSACPGEVFK
LARVNLPSNT ITHQREFLYD TNQTNCSSSI SFLIGQFNRK TYATTLVICS ILGSAYFEEL
RTKKQFGYVV NCAQDCTGNA ISMRCIVQSH TKTPEEIFDA TMEFFVGFEK TLDYFKTSPS
DFKDLIENCQ KQNTVKQQSN SAQSSLYWSF FTFCGDFEFE KKKYEDIGKI TFDDVKQYYL
DHLSPNTANL RIFAAHCYPQ SYQIPDEVKP FGNVKVNLLR KYEHDNFKEN HGYLSSKVNL
QK
