APM1D_ORYSJ
ID APM1D_ORYSJ Reviewed; 873 AA.
AC Q6K4E7; Q0J2B3;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Aminopeptidase M1-D;
DE EC=3.4.11.2;
DE AltName: Full=Alpha-aminoacylpeptide hydrolase;
GN OrderedLocusNames=Os09g0362800, LOC_Os09g19800/LOC_Os09g19820;
GN ORFNames=OJ1506_A04.11;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 472-873.
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a
CC peptide, amide or arylamide. Xaa is preferably Ala, but may be most
CC amino acids including Pro (slow action). When a terminal hydrophobic
CC residue is followed by a prolyl residue, the two may be released as
CC an intact Xaa-Pro dipeptide.; EC=3.4.11.2;
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:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Microsome membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=The
CC dileucine internalization motif may be involved in intracellular
CC sequestration.
CC -!- DOMAIN: Dileucine motif seems to be involved in protein-protein
CC interactions. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK068512; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=BAF24902.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP005572; BAD23406.1; -; Genomic_DNA.
DR EMBL; AP008215; BAF24902.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014965; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK068512; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015611913.1; XM_015756427.1.
DR AlphaFoldDB; Q6K4E7; -.
DR SMR; Q6K4E7; -.
DR STRING; 4530.OS09T0362800-02; -.
DR MEROPS; M01.A25; -.
DR PaxDb; Q6K4E7; -.
DR PRIDE; Q6K4E7; -.
DR GeneID; 4346856; -.
DR KEGG; osa:4346856; -.
DR eggNOG; KOG1046; Eukaryota.
DR InParanoid; Q6K4E7; -.
DR OrthoDB; 110058at2759; -.
DR Proteomes; UP000000763; Chromosome 9.
DR Proteomes; UP000059680; Chromosome 9.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.10.390.10; -; 1.
DR Gene3D; 2.60.40.1730; -; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; SSF63737; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Aminopeptidase; Cytoplasm; Endoplasmic reticulum; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Microsome; Protease; Reference proteome;
KW Zinc.
FT CHAIN 1..873
FT /note="Aminopeptidase M1-D"
FT /id="PRO_0000424587"
FT REGION 96..203
FT /note="Required for membrane association"
FT /evidence="ECO:0000250"
FT MOTIF 721..722
FT /note="Dileucine internalization motif"
FT /evidence="ECO:0000255"
FT ACT_SITE 306
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 269..273
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 328
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT SITE 390
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 873 AA; 98513 MW; EF7BDE7FF4AF0667 CRC64;
MAAAAAEFRG QARLPRFAAP RRYELRLRPD LAACVFSGEA SVAVDVSAPT RFLVLNAADL
AVDRASIRFQ GLAPAEVSVF EEDEILVLEF AGELPLGEGV LAMRFNGTLN DQMRGFYRSK
YEYKGETKNM AVTQFESVDA RRCFPCWDEP SFKAKFKLTL EVPSELVALS NMPIVNEKIA
GPIKTVEYEE SPVMSTYLVA IVVGLFDYIE GVTSEGNKVR VYTQVGKSNQ GKFALDVGVK
SLNLYKEFFD TPYPLPKLDM VAIPDFTNGA MENYGLVTYR EIYLLFDEQS SSASTKQNVA
ITVAHELAHQ WFGNLVTMEW WTHLWLNEGF ATWMSYLAVD SFFPEWNIWT QFLDSTTSAL
KLDSLAESHP IEVEIHHASE IDSIFDSISY DKGASVIRML QSYLGAERFQ KALASYIKKY
AYSNAKTEDL WAVLEEVSGE PVKNLMTTWT KKQGYPVIGV KLKGHDVELE QDQFLLDGSS
DSGMWIVPIT LGCNSHDMQK RFLLKHKFSD IKGINSQYDD QDRQNSGNFW IKLNIDETGF
YRVKYDDELT TALRNALQMK KLSLMDKIGI VEDAHALSIA GKQTLSSLLH LLYACRDEDD
FSVLSHINSV TSSVAKISID ATPELAGEIK QLFIKLLLPT AEKLGWDPKN SESHLDAMLR
PVLLVGLVQL GHDKTISEGV RRFQIFFDDR NTSLPPDTRK AAYLSVMHNV SSTNRSGYDA
LLKIYRESTE VEERLNVLGI LSSCQDKDIV LESLNFIFTD EVRNQDAYLV LRSVIIDARE
TAWSWLKENW DRITKTFAAS AILSDYVKSI VTLFTSKEKE AEISQFFATR TKPGFKRALK
QSLENVRISA RWVDGIRGEA ELAQTVHDLL IKL
