ID   APM1A_ORYSJ             Reviewed;         878 AA.
AC   Q6Z6L4; A0A0P0VGK2;
DT   11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Aminopeptidase M1-A;
DE            EC=3.4.11.2;
DE   AltName: Full=Alpha-aminoacylpeptide hydrolase;
GN   OrderedLocusNames=Os02g0218200, LOC_Os02g12650;
GN   ORFNames=OsJ_05906, P0027A02.7;
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 GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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=AK066996; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AP004996; BAD17179.1; -; Genomic_DNA.
DR   EMBL; AP008208; BAF08217.1; -; Genomic_DNA.
DR   EMBL; AP014958; BAS77671.1; -; Genomic_DNA.
DR   EMBL; CM000139; EAZ22251.1; -; Genomic_DNA.
DR   EMBL; AK066996; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_015626085.1; XM_015770599.1.
DR   AlphaFoldDB; Q6Z6L4; -.
DR   SMR; Q6Z6L4; -.
DR   STRING; 4530.OS02T0218200-01; -.
DR   MEROPS; M01.A25; -.
DR   PaxDb; Q6Z6L4; -.
DR   PRIDE; Q6Z6L4; -.
DR   EnsemblPlants; Os02t0218200-01; Os02t0218200-01; Os02g0218200.
DR   GeneID; 4328737; -.
DR   Gramene; Os02t0218200-01; Os02t0218200-01; Os02g0218200.
DR   KEGG; osa:4328737; -.
DR   eggNOG; KOG1046; Eukaryota.
DR   HOGENOM; CLU_003705_0_1_1; -.
DR   InParanoid; Q6Z6L4; -.
DR   OMA; MMEYVAI; -.
DR   OrthoDB; 110058at2759; -.
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000007752; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
DR   ExpressionAtlas; Q6Z6L4; baseline and differential.
DR   Genevisible; Q6Z6L4; 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-A"
FT                   /id="PRO_0000424584"
FT   REGION          105..212
FT                   /note="Required for membrane association"
FT                   /evidence="ECO:0000250"
FT   MOTIF           727..728
FT                   /note="Dileucine internalization motif"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        315
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         278..282
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         314
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         318
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         337
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   SITE            399
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        375
FT                   /note="A -> V (in Ref. 5; AK066996)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        498
FT                   /note="I -> V (in Ref. 5; AK066996)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   878 AA;  98453 MW;  352DD127A17B4167 CRC64;
     MAAAEQSAEQ FRGQARLPGF AAPRRYDLRL VPDLDGCAFT GSVDVSVDVT APTRFLVLNA
     AELEVSPGGV QFKPHGAEQE LHPAEVTNVP EDEILIIRFN EVLPVGEGTL VIAFKGTLND
     KMHGFYRSVY ELNGEKKNMA VTQFEPADAR RCFPCWDEPS FKAIFKITLE VPSETVALSN
     MPVVEEKVNG LIKAVYFQET PIMSTYLVAV IVGMFDYVEA FTTDGTRVRV YTQVGKSAQG
     KFALEVAVKT LVLFKEYFAV PYPLPKMDMI AIPDFASGAM ENYGLVTYRE TALLFDEKHS
     AAANKQRVAV VVAHELAHQW FGNLVTMEWW THLWLNEGFA TWVSYLAADN FFPEWNVWTQ
     FLEESTTGFK LDALAGSHPI EVDVNHVDEI DEIFDAISYR KGAAVIRMLQ SYLGAETFQK
     SLAAYIEKFA YSNAKTEDLW AALEEGSGEP VKTLMHSWTK QQGYPVVNVK LKDGKLEMEQ
     TQFLSSGAEG VGQWVVPITL CCCSYSRQEK FLFNGKQEDF NLSGLVECQK KEDFWIKLNV
     NQTGFYRVSY DEELASRLRY AIEANKLSAA DRYGVLDDTY ALCMAGKQKL VSLLHLIAAY
     KDETEYTVLA RVIDTSLSIV EMVAVAAPEG LGKLKKFLID FLEPFAQRIG WDAKSGEGHL
     DALLRGTLLT ALAELGHEAT INEAVRRFNI FVEDRETPLL PPDVRKAAYV ALMQTVNKSN
     RAGYESLLKI YKETDLSQEK VRILGSLASC PDPDVVRDTL DFMLSPEVRN QDSIFLLRGV
     GAAGHEVAWT WLKEKWDYIS DTFSGTLLTY FVSTTVSPLR TDEMGDDAEE FFKSRTKANI
     ARTVKQSIER VRINAKWVES TRAEANLGNV LKEISHDH