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IDE2_ARATH
ID   IDE2_ARATH              Reviewed;         966 AA.
AC   F4J3D9; B6EUA3; Q9SCM5;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   16-MAR-2016, sequence version 2.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Insulin-degrading enzyme-like 2;
DE            EC=3.4.24.-;
DE   AltName: Full=Insulysin-like 2;
GN   OrderedLocusNames=At3g57470 {ECO:0000312|Araport:AT3G57470};
GN   ORFNames=T8H10.70 {ECO:0000312|EMBL:CAB66104.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=F4J3D9-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AEE79658.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB66104.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL133248; CAB66104.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE79658.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE79659.2; -; Genomic_DNA.
DR   PIR; T46183; T46183.
DR   RefSeq; NP_001319782.1; NM_001339871.1. [F4J3D9-1]
DR   RefSeq; NP_567049.3; NM_115607.4.
DR   AlphaFoldDB; F4J3D9; -.
DR   SMR; F4J3D9; -.
DR   STRING; 3702.AT3G57470.2; -.
DR   MEROPS; M16.A01; -.
DR   iPTMnet; F4J3D9; -.
DR   PaxDb; F4J3D9; -.
DR   PRIDE; F4J3D9; -.
DR   ProteomicsDB; 228792; -. [F4J3D9-1]
DR   EnsemblPlants; AT3G57470.2; AT3G57470.2; AT3G57470. [F4J3D9-1]
DR   GeneID; 824914; -.
DR   Gramene; AT3G57470.2; AT3G57470.2; AT3G57470. [F4J3D9-1]
DR   KEGG; ath:AT3G57470; -.
DR   Araport; AT3G57470; -.
DR   TAIR; locus:2103523; AT3G57470.
DR   eggNOG; KOG0959; Eukaryota.
DR   HOGENOM; CLU_004639_1_1_1; -.
DR   OMA; MDKGGEI; -.
DR   OrthoDB; 1008844at2759; -.
DR   PRO; PR:F4J3D9; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; F4J3D9; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
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   Alternative splicing; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Reference proteome; Zinc.
FT   CHAIN           1..966
FT                   /note="Insulin-degrading enzyme-like 2"
FT                   /id="PRO_0000435732"
FT   ACT_SITE        74
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   ACT_SITE        145
FT                   /evidence="ECO:0000305"
FT   BINDING         71
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         75
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         152
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   966 AA;  110688 MW;  B8585989213448D3 CRC64;
     MAVGMENATA SGECGEILKP RTDKREYRRI VLKNSLEVLL ISDPETDKCA ASMNVSVGSF
     TDPEGLEGLA HFLEHMLFYA SEKYPEEDSY SKYITEHGGS TNAYTSSEDT NYHFDINTDS
     FYEALDRFAQ FFIQPLMSTD ATMREIKAVD SEHQNNLLSD SWRMAQLQKH LSREDHPYHK
     FSTGNMDTLH VRPEENGVDT RSELIKFYDE HYSANIMHLV VYGKENLDKT QGLVEALFQG
     IRNTNQGIPR FPGQPCTLDH LQVLVKAVPI MQGHELSVSW PVTPSISHYE EAPCRYLGDL
     IGHEGEGSLF HALKILGWAT GLYAGEADWS MEYSFFNVSI DLTDAGHEHM QDILGLLFEY
     IKVLQQSGVS QWIFDELSAI CEAEFHYQAK IDPISYAVDI SSNMKIYPTK HWLVGSSLPS
     KFNPAIVQKV LDELSPNNVR IFWESNKFEG QTDKVEPWYN TAYSLEKITK FTIQEWMQSA
     PDVNLLLPTP NVFIPTDFSL KDLKDKDIFP VLLRKTSYSR LWYKPDTKFF KPKAYVKMDF
     NCPLAVSSPD AAVLSDIFVW LLVDYLNEYA YYAQAAGLDY GLSLSDNGFE LSLAGFNHKL
     RILLEAVIQK IAKFEVKPDR FSVIKETVTK AYQNNKFQQP HEQATNYCSL VLQDQIWPWT
     EELDALSHLE AEDLANFVPM LLSRTFVECY IAGNVEKDEA ESMVKHIEDV LFTDSKPICR
     PLFPSQFLTN RVTELGTGMK HFYYQEGSNS SDENSALVHY IQVHKDEFSM NSKLQLFELI
     AKQDTFHQLR TIEQLGYITS LSLSNDSGVY GVQFIIQSSV KGPGHIDSRV ESLLKDLESK
     FYNMSDEEFK SNVTNLIDMK LEKDKNLDEE SWFYWAEIQT GTLKFNRIDA EVAALRLLKK
     DEWIDFFDEY IKVDAPNKKS LSICVYGNQH LKEMRNDKDK IPSTSIEIED IVCFRKSQPL
     YGSLKL
 
 
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