AMPO_MOUSE
ID AMPO_MOUSE Reviewed; 823 AA.
AC Q8BXQ6; Q3UQZ7; Q6P0W6; Q6P394; Q8BHX5;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-JUN-2021, sequence version 3.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Aminopeptidase O;
DE Short=AP-O;
DE EC=3.4.11.- {ECO:0000250|UniProtKB:P15144};
GN Name=Aopep; Synonyms=Onpep;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Retina, and Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP RETRACTED PAPER.
RC STRAIN=C57BL/6J; TISSUE=Lung;
RX PubMed=15687497; DOI=10.1074/jbc.m413222200;
RA Diaz-Perales A., Quesada V., Sanchez L.M., Ugalde A.P., Suarez M.F.,
RA Fueyo A., Lopez-Otin C.;
RT "Identification of human aminopeptidase O, a novel metalloprotease with
RT structural similarity to aminopeptidase B and leukotriene A4 hydrolase.";
RL J. Biol. Chem. 280:14310-14317(2005).
RN [5]
RP RETRACTION NOTICE OF PUBMED:15687497.
RX PubMed=30808004; DOI=10.1074/jbc.w118.007327;
RA Diaz-Perales A., Quesada V., Sanchez L.M., Ugalde A.P., Suarez M.F.,
RA Fueyo A., Lopez-Otin C.;
RL J. Biol. Chem. 294:1433-1433(2019).
RN [6]
RP ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17803194; DOI=10.1002/jcb.21497;
RA Axton R., Wallis J.A., Taylor H., Hanks M., Forrester L.M.;
RT "Aminopeptidase O contains a functional nucleolar localization signal and
RT is implicated in vascular biology.";
RL J. Cell. Biochem. 103:1171-1182(2008).
CC -!- FUNCTION: Aminopeptidase which catalyzes the hydrolysis of amino acid
CC residues from the N-terminus of peptide or protein substrates.
CC {ECO:0000250|UniProtKB:P15144}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P15144};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P15144};
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:17803194}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000305|PubMed:17803194}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms may exist. {ECO:0000269|PubMed:17803194};
CC Name=1;
CC IsoId=Q8BXQ6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BXQ6-3; Sequence=VSP_061019, VSP_061020;
CC -!- TISSUE SPECIFICITY: Expressed in testis, heart, brain, lung, liver,
CC skeletal muscle, kidney and ovary. Expressed in vascular tissues.
CC {ECO:0000269|PubMed:17803194}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
CC -!- CAUTION: A paper describing the expression patterns of this protein has
CC been retracted due to concerns of image manipulation.
CC {ECO:0000305|PubMed:15687497, ECO:0000305|PubMed:30808004}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC36293.1; Type=Miscellaneous discrepancy; Note=Intron retention. This sequence is incomplete at the 5'-end and differs from that shown at positions 658-661.; Evidence={ECO:0000305};
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DR EMBL; AJ810420; CAH17902.1; -; mRNA.
DR EMBL; AK044477; BAC31943.1; -; mRNA.
DR EMBL; AK076298; BAC36293.1; ALT_SEQ; mRNA.
DR EMBL; AK141931; BAE24891.1; -; mRNA.
DR EMBL; AC130827; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC171004; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT009757; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC064132; AAH64132.1; -; mRNA.
DR EMBL; BC065422; AAH65422.1; -; mRNA.
DR EMBL; BC141279; AAI41280.1; -; mRNA.
DR CCDS; CCDS36699.1; -. [Q8BXQ6-1]
DR RefSeq; NP_001276853.1; NM_001289924.1. [Q8BXQ6-1]
DR RefSeq; NP_001276855.1; NM_001289926.1. [Q8BXQ6-1]
DR AlphaFoldDB; Q8BXQ6; -.
DR SMR; Q8BXQ6; -.
DR STRING; 10090.ENSMUSP00000089148; -.
DR MEROPS; M01.028; -.
DR iPTMnet; Q8BXQ6; -.
DR PhosphoSitePlus; Q8BXQ6; -.
DR PaxDb; Q8BXQ6; -.
DR PRIDE; Q8BXQ6; -.
DR ProteomicsDB; 281972; -. [Q8BXQ6-1]
DR ProteomicsDB; 281974; -. [Q8BXQ6-3]
DR Antibodypedia; 985; 87 antibodies from 19 providers.
DR DNASU; 72061; -.
DR Ensembl; ENSMUST00000091560; ENSMUSP00000089148; ENSMUSG00000021458. [Q8BXQ6-1]
DR GeneID; 72061; -.
DR KEGG; mmu:72061; -.
DR UCSC; uc007qxh.1; mouse. [Q8BXQ6-3]
DR UCSC; uc007qxi.2; mouse.
DR CTD; 84909; -.
DR MGI; MGI:1919311; Aopep.
DR VEuPathDB; HostDB:ENSMUSG00000021458; -.
DR eggNOG; KOG1047; Eukaryota.
DR GeneTree; ENSGT00940000155211; -.
DR InParanoid; Q8BXQ6; -.
DR OMA; YERSAVW; -.
DR OrthoDB; 775595at2759; -.
DR TreeFam; TF332004; -.
DR Reactome; R-MMU-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR BioGRID-ORCS; 72061; 3 hits in 72 CRISPR screens.
DR ChiTaRS; 2010111I01Rik; mouse.
DR PRO; PR:Q8BXQ6; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8BXQ6; protein.
DR Bgee; ENSMUSG00000021458; Expressed in lip and 207 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0004177; F:aminopeptidase activity; ISO:MGI.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
DR Gene3D; 1.10.390.10; -; 1.
DR Gene3D; 1.25.40.320; -; 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; IPR033577; AOPep.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR038502; M1_LTA-4_hydro/amino_C_sf.
DR InterPro; IPR015211; Peptidase_M1_C.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR46627; PTHR46627; 1.
DR Pfam; PF09127; Leuk-A4-hydro_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR SMART; SM01263; Leuk-A4-hydro_C; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF63737; SSF63737; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Aminopeptidase; Cytoplasm; Hydrolase; Metal-binding;
KW Metalloprotease; Nucleus; Protease; Reference proteome; Zinc.
FT CHAIN 1..823
FT /note="Aminopeptidase O"
FT /id="PRO_0000095092"
FT MOTIF 693..703
FT /note="Nucleolar localization signal"
FT /evidence="ECO:0000269|PubMed:17803194"
FT ACT_SITE 482
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P15144,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 481
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT BINDING 485
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT BINDING 504
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT SITE 588
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT VAR_SEQ 457..473
FT /note="SPHIIFLSQSTLTGTSH -> RYAAHHGMWNMLKMSRN (in isoform
FT 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_061019"
FT VAR_SEQ 474..823
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_061020"
SQ SEQUENCE 823 AA; 93579 MW; EB7BE0B7C296607C CRC64;
MDIKLDPSRD DLPLMANTSH MLVKHYILDL DVDFGNQVIE GNIVLFFGDG NRFKNQSRST
QETFQMESEE ADIFRTAEPC HVPEMDSSTF SPKMGHRECA VCGKGDQDAF DNDGNHDNQE
RDSEISSSKY CCDTGNHGKR DFLLVLDCCD LSVLKVEEVD VAAVPGLEKF TKAPKLLATP
EKLRCEIVRD LVALPADAWR EQLDCYTRCS QAPGCGELLI DSDNWSLRIR KTGTSTPADF
PRAIRIWYKT KPEGQSVAWT TDQNGRPCVY TMGSPINNRA LFPCQEPPVA MSTWQATVRA
AASFVVLMSG ENSAKPTPLR EGYMSWHYYV TMPMPASTFA IAVGCWTEMK PKASPPDDLM
TEHSLPLSPS EADLRYDNTC NHMEYPCRFQ SASAASQDII PYRVFAPVCL EGACQEALLW
LIPSCLSAAH SVLGTHPFSR LDILIVPTNF PSLGMASPHI IFLSQSTLTG TSHLCGTRLC
HEIAHSWFGL AIGARDWTEE WLSEGFATHL EDIFWAEAQQ LPPHEALEQQ ELRACLRWHR
LQDELRNSPE GMQVLRPNKE ETGHVSASGA SVVKHGLNPE KGFMQVHYLK GYFLLRFLTR
TLGEKIYFPF LRKFVHLFHG QLILSQDFLQ MLLENIPENK RLGLSVENIV RDWLECSGIP
KALQEERKAE DCSPSRLARQ VGSEVAKWIR VNRRPRKRKR GKREVAFEKL SPDQIVLLLE
WLLEQKTLSP QTLHCLQQTY HLPEQDAEVR HRWCELVIKH KYTKAYNQVE RFLLEDQAMG
IYLYGELMVS EDARLQQLAH RCFELVKEHM DRASAQVVTE MLF
