APM1B_ORYSJ
ID APM1B_ORYSJ Reviewed; 875 AA.
AC Q0J5V5; A0A0P0XFB8; Q6ZIV5;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Aminopeptidase M1-B;
DE EC=3.4.11.2;
DE AltName: Full=Alpha-aminoacylpeptide hydrolase;
GN OrderedLocusNames=Os08g0398700, LOC_Os08g30810;
GN ORFNames=OJ1051_A08.7, OJ1198_B10.19;
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].
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=BAC99372.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAC99434.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP003904; BAC99372.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP003947; BAC99434.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008214; BAF23660.1; -; Genomic_DNA.
DR EMBL; AP014964; BAT05325.1; -; Genomic_DNA.
DR EMBL; AK120068; BAG99861.1; -; mRNA.
DR RefSeq; XP_015649943.1; XM_015794457.1.
DR AlphaFoldDB; Q0J5V5; -.
DR SMR; Q0J5V5; -.
DR STRING; 4530.OS08T0398700-01; -.
DR MEROPS; M01.A25; -.
DR PaxDb; Q0J5V5; -.
DR PRIDE; Q0J5V5; -.
DR EnsemblPlants; Os08t0398700-01; Os08t0398700-01; Os08g0398700.
DR GeneID; 4345501; -.
DR Gramene; Os08t0398700-01; Os08t0398700-01; Os08g0398700.
DR KEGG; osa:4345501; -.
DR eggNOG; KOG1046; Eukaryota.
DR HOGENOM; CLU_003705_0_1_1; -.
DR InParanoid; Q0J5V5; -.
DR OMA; HDMAGFY; -.
DR OrthoDB; 110058at2759; -.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR ExpressionAtlas; Q0J5V5; baseline and differential.
DR Genevisible; Q0J5V5; 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..875
FT /note="Aminopeptidase M1-B"
FT /id="PRO_0000424585"
FT REGION 96..203
FT /note="Required for membrane association"
FT /evidence="ECO:0000250"
FT MOTIF 722..723
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 875 AA; 97904 MW; 7D4AE0B3231D8600 CRC64;
MAASPEQFRG QARLPRCASP LSYDLRLRPD LAACAFSGSA AVAVAVSAPT RFLVLNAAEL
AVDGSSVRFQ DLVPSEVVQF EEDEIVVIGF GQDLPIGEGV LKMDFTGTLN DQMRGFYRSK
YEYKGESRNM AVTQFEAADA RRCFPCWDEP AFKAKFKLTL EVPSELVALS NMPVIKETVH
GPLKTVYYEE SPLMSTYLVA IVVGLFDYIE GSTLEGTKVR VYTQVGKSNQ GKFALDVAVK
SLDLFKDYFA TPYPLPKLDM VAIPDFAAGA MENYGLVTYR ETALLYDELL SSASNKQQVA
ITVAHELAHQ WFGNLVTMEW WTHLWLNEGF ASWVSYLAVE ALFPEWNNWT QFLDETTSGL
RLDALAESHP IEVDINHASE IDAIFDSISY DKGASVIRML QSYLGAERFQ KALASYIKKY
AYSNAKTEDL WAVLEEESGE PVKDLMTTWT KQQGYPVIYA KLDGHDLHLE QAQFLSDGSS
GPGLWIVPIT SCCGSYDAQK KFLLKGKTDK VHIDLTASQN AGGEKGENCW IKLNVDQTGF
YRVKYDDELA AGLEKAIKAN KLSLMDKIGI VEDSYSLSVA RKQTLTSLLR LLNAYRNESD
YTVLSHVTSV CLGIDKISVD ATPELSRDIK QLLINLLLSA AKTLGWDPKE GESHLDVMLR
SLLLIALVKL GHDETINEGV RRFHIFIKDR KTNILPPDTR KASYLAVMRT VTTSSRAGYD
ALLKIYRETA EAQEKSRILG SLSSCLDKDI VLEALNFMLT DEVRNQDAFY VLGGISLEGR
EVAWAWLKEN WDHVLKTWPS SSLISDFVKS TVSRFTTEEK AAEVSEFFAG KTKPSFERAL
KQSLERVRIS ARWIESIRSE PNLAQTVNEL LQHDM
