APM1C_ORYSJ
ID APM1C_ORYSJ Reviewed; 878 AA.
AC Q0J2B5; Q6K4E8;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 11-DEC-2013, sequence version 2.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Aminopeptidase M1-C;
DE EC=3.4.11.2;
DE AltName: Full=Alpha-aminoacylpeptide hydrolase;
GN OrderedLocusNames=Os09g0362500, LOC_Os09g19790; ORFNames=OJ1506_A04.10;
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 9-878.
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=BAD23405.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP005572; BAD23405.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008215; BAF24900.2; -; Genomic_DNA.
DR EMBL; AP014965; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK068165; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015612451.1; XM_015756965.1.
DR AlphaFoldDB; Q0J2B5; -.
DR SMR; Q0J2B5; -.
DR STRING; 4530.OS09T0362500-01; -.
DR MEROPS; M01.A25; -.
DR PaxDb; Q0J2B5; -.
DR PRIDE; Q0J2B5; -.
DR GeneID; 4346854; -.
DR KEGG; osa:4346854; -.
DR eggNOG; KOG1046; Eukaryota.
DR HOGENOM; CLU_003705_0_1_1; -.
DR InParanoid; Q0J2B5; -.
DR OrthoDB; 110058at2759; -.
DR Proteomes; UP000000763; Chromosome 9.
DR Proteomes; UP000059680; Chromosome 9.
DR Genevisible; Q0J2B5; OS.
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..878
FT /note="Aminopeptidase M1-C"
FT /id="PRO_0000424586"
FT REGION 102..209
FT /note="Required for membrane association"
FT /evidence="ECO:0000250"
FT MOTIF 726..727
FT /note="Dileucine internalization motif"
FT /evidence="ECO:0000255"
FT ACT_SITE 312
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 275..279
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 311
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 334
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT SITE 396
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CONFLICT 304
FT /note="N -> D (in Ref. 4; AK068165)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 878 AA; 98683 MW; FADC3B652EA19C5B CRC64;
MAPAPAPAGS ADQFRGQARL PRFAAPRRYE LRLRPDLDAC VFTGDASVVV DVSAPTRFLV
LNAADLAVDR ASIRFQGLAP TEVSLFEDDE ILVLEFDGEL PLGEGVLAMD FNGTLNDQMR
GFYRSKYEYK GETKNMAVTQ FEAVDARRCF PCWDEPAFKA KFKLTLEVPS ELVALSNMPV
ACETIAGPIK TIHYEESPLM STYLVAIVVG LFDYVEGVTS EGNKVRVYTQ VGKSSQGKFA
LDIGVKSLNF YKDYFDTPYP LPKLDMVAIP DFAAGAMENY GLVTYREVSL LFDEQSSSAS
FKQNVAITVA HELAHQWFGN LVTMEWWTHL WLNEGFATWM SHLSVDSFFP QWNIWTQFLD
STTSALKLDS QAESHPIEVE IHHASEVDEI FDAISYDKGA SVIRMLQSYL GAERFQKALT
SYIKKYAYSN AKTEDLWAVL EEVSGEPVKD LMTTWTKQQG YPVISVKLKG HDLELEQDQF
LLNGTSGAGI WIVPITLGCC SHDKQKRLLL KHKHDNIKAI VSQCDSRQKG GNFWIKLNID
ETGFYRVKYD DELTAALRNA LQAKKLSLMD EIGIVDDAHA LSIACKQTLS SLLHLLYAFR
DEADYSVLSH INSVTSSVAK ISIDATPDLA GDIKQLFIKL LLPPAKKLGW DPKDGESHLN
AMLRPMLLVA LVQLGHDKTI NEGFRRFQIF FDDRNTSLLT PDTRKAAYLS VMHNVSSTNR
SGYDALLKVY RKSAEGEEKL RVLGTLSSCQ DKDIVLESLN LIFTDEVRNQ DAYRVLGGVI
IEARETAWSW LKENWDRISE AFSGSSLISD FIRSIVTLFT SKEKEAEISQ FFATRTKPGY
ERTLKQSLER VLINARWIEG IRGEAKLAQT VHELLHKP
