ID AMPO_RAT Reviewed; 822 AA.
AC P69527; F1LRV1;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-JUN-2021, sequence version 2.
DT 24-JAN-2024, entry version 114.
DE RecName: Full=Aminopeptidase O;
DE Short=AP-O;
DE EC=3.4.11.- {ECO:0000250|UniProtKB:P15144};
GN Name=Aopep; Synonyms=Onpep;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
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
CC {ECO:0000250|UniProtKB:Q8BXQ6}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR EMBL; AJ810421; CAH17903.1; -; mRNA.
DR EMBL; AABR07072530; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07026781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07026783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07026782; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07026785; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07026784; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001012346.1; NM_001012346.1.
DR RefSeq; XP_008769653.1; XM_008771431.2.
DR RefSeq; XP_008769654.1; XM_008771432.2.
DR RefSeq; XP_017455962.1; XM_017600473.1.
DR AlphaFoldDB; P69527; -.
DR SMR; P69527; -.
DR STRING; 10116.ENSRNOP00000023638; -.
DR MEROPS; M01.028; -.
DR PhosphoSitePlus; P69527; -.
DR PaxDb; 10116-ENSRNOP00000023638; -.
DR Ensembl; ENSRNOT00055040036; ENSRNOP00055032487; ENSRNOG00055023304.
DR Ensembl; ENSRNOT00060029756; ENSRNOP00060023973; ENSRNOG00060017408.
DR Ensembl; ENSRNOT00065039930; ENSRNOP00065032461; ENSRNOG00065023363.
DR GeneID; 290963; -.
DR KEGG; rno:290963; -.
DR UCSC; RGD:1309592; rat.
DR AGR; RGD:1309592; -.
DR CTD; 84909; -.
DR RGD; 1309592; Aopep.
DR VEuPathDB; HostDB:ENSRNOG00000017505; -.
DR eggNOG; KOG1047; Eukaryota.
DR HOGENOM; CLU_022467_0_0_1; -.
DR InParanoid; P69527; -.
DR OrthoDB; 3108672at2759; -.
DR PhylomeDB; P69527; -.
DR TreeFam; TF332004; -.
DR Reactome; R-RNO-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR PRO; PR:P69527; -.
DR Proteomes; UP000002494; Chromosome 17.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
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; IEA:UniProtKB-KW.
DR Gene3D; 3.30.2010.30; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 1.25.40.320; Peptidase M1, leukotriene A4 hydrolase/aminopeptidase C-terminal domain; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
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; AMINOPEPTIDASE O; 1.
DR PANTHER; PTHR46627:SF1; AMINOPEPTIDASE O; 1.
DR Pfam; PF09127; Leuk-A4-hydro_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR SMART; SM01263; Leuk-A4-hydro_C; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 2: Evidence at transcript level;
KW Aminopeptidase; Hydrolase; Metal-binding; Metalloprotease; Nucleus;
KW Protease; Reference proteome; Zinc.
FT CHAIN 1..822
FT /note="Aminopeptidase O"
FT /id="PRO_0000095093"
FT MOTIF 692..702
FT /note="Nucleolar localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q8BXQ6"
FT ACT_SITE 481
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P15144,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 480
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT BINDING 484
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT BINDING 503
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT SITE 587
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P15144"
SQ SEQUENCE 822 AA; 93432 MW; 0F800686CCE0FD7E CRC64;
MDINLDPSRD DLPLMANTSH LLVKHYVLDL DVDFGSRVLE GNIVLFFGDG NRCKKQSSSS
QETFQMESEE AYILRTAEPC HVPKMDSNTF SPKMGHREFA VFGKSDQDAF DNDGNHDNKE
HDSESSSSKY CCDTGNHGRE DFLLVLDCCD LSVLKVEEVD VAAVPDLEKF TKAPNLTAAP
EKRRCEIVRD LVALPADAWR EQLDCYTRCS QAPGCGELLF DSDKWSLQIR KKGVPTAADF
PHAIRIWYKT KPEGQSVTWT SDQDGRPCVY TMGSPINNRA LFPCQEPPVA MSTWQATVRA
AASFVVLMSG EKSAKPTPLR EGYMSWHYYV TMPMPASTFT IAVGCWTEMK PKTSPLDDLT
EHTLPLRPSD ADFRYGNTCS HMEYPCRFQS ASAATQNIIP YRVFAPVCLE GACREALLWL
IPSCLSAAHS VLGTHPFSRL DILIVPTNFP SLGMASPHII FLSQSTLTGT SHLCGTRLCH
EIAHAWFGLA IGARDWTEEW LSEGFATHLE DIFWAEAQQL PPHEALEQQE LRACLRWHRL
QDELQNSPEG MQVLRPNKEK TGHVSASGAS VVKNGLNPEK GFMQVHYLKG YFLLRFLART
LGEETYFPFL RKFVHLFHGQ LILSQDFLQM LLESIPENKR FGLSVENIVG DWLECPGIPK
ALQEERKAKD CSPSRLVRQV GSEVAKWIRV NRRPGKRQRR KREAAFEKLS PDQIVLLLEW
LLEQKTLSPQ TLHRLQQTYH LQEQDAEVRH RWCELVIKHK YTKAYDQVKR FLQEDQAMGI
YLYGELMVSE DARLQQLAHR CFELVKGHMD KASAQVVTEM LF
//
