APE1_SCHPO
ID APE1_SCHPO Reviewed; 882 AA.
AC Q9USX1; Q9HGK4;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Aminopeptidase 1;
DE EC=3.4.11.-;
DE AltName: Full=Aminopeptidase I;
GN Name=ape1; ORFNames=SPBC1921.05;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Villa L., Suarez-Rendueles P.;
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP GENE NAME, AND FUNCTION.
RX PubMed=1897317; DOI=10.1002/yea.320070512;
RA Arbesu M.J., Gascon S., Suarez-Rendueles P.;
RT "Isolation and characterization of Schizosaccharomyces pombe mutants
RT lacking aminopeptidase activity.";
RL Yeast 7:525-531(1991).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR EMBL; AF281863; AAG01326.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB58971.1; -; Genomic_DNA.
DR PIR; T39789; T39789.
DR RefSeq; NP_595998.1; NM_001021906.2.
DR AlphaFoldDB; Q9USX1; -.
DR SMR; Q9USX1; -.
DR BioGRID; 277173; 22.
DR STRING; 4896.SPBC1921.05.1; -.
DR MEROPS; M01.A29; -.
DR iPTMnet; Q9USX1; -.
DR MaxQB; Q9USX1; -.
DR PaxDb; Q9USX1; -.
DR PRIDE; Q9USX1; -.
DR EnsemblFungi; SPBC1921.05.1; SPBC1921.05.1:pep; SPBC1921.05.
DR GeneID; 2540648; -.
DR KEGG; spo:SPBC1921.05; -.
DR PomBase; SPBC1921.05; -.
DR VEuPathDB; FungiDB:SPBC1921.05; -.
DR eggNOG; KOG1046; Eukaryota.
DR HOGENOM; CLU_003705_0_1_1; -.
DR InParanoid; Q9USX1; -.
DR OMA; MMEYVAI; -.
DR PhylomeDB; Q9USX1; -.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR Reactome; R-SPO-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR PRO; PR:Q9USX1; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000328; C:fungal-type vacuole lumen; IDA:PomBase.
DR GO; GO:0005771; C:multivesicular body; IDA:PomBase.
DR GO; GO:0061957; C:NVT complex; IPI:PomBase.
DR GO; GO:0070006; F:metalloaminopeptidase activity; ISM:PomBase.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0120113; P:cytoplasm to vacuole transport by the NVT pathway; IMP:PomBase.
DR GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
DR GO; GO:0016485; P:protein processing; NAS:PomBase.
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 3: Inferred from homology;
KW Aminopeptidase; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Zinc.
FT CHAIN 1..882
FT /note="Aminopeptidase 1"
FT /id="PRO_0000095103"
FT ACT_SITE 317
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 281..285
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT SITE 402
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CONFLICT 90..91
FT /note="ER -> DA (in Ref. 1; AAG01326)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="G -> A (in Ref. 1; AAG01326)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="G -> A (in Ref. 1; AAG01326)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="G -> P (in Ref. 1; AAG01326)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="G -> A (in Ref. 1; AAG01326)"
FT /evidence="ECO:0000305"
FT CONFLICT 475
FT /note="T -> N (in Ref. 1; AAG01326)"
FT /evidence="ECO:0000305"
FT CONFLICT 503
FT /note="W -> C (in Ref. 1; AAG01326)"
FT /evidence="ECO:0000305"
FT CONFLICT 593
FT /note="G -> A (in Ref. 1; AAG01326)"
FT /evidence="ECO:0000305"
FT CONFLICT 611
FT /note="P -> S (in Ref. 1; AAG01326)"
FT /evidence="ECO:0000305"
FT CONFLICT 622
FT /note="R -> A (in Ref. 1; AAG01326)"
FT /evidence="ECO:0000305"
FT CONFLICT 665
FT /note="D -> N (in Ref. 1; AAG01326)"
FT /evidence="ECO:0000305"
FT CONFLICT 715
FT /note="F -> I (in Ref. 1; AAG01326)"
FT /evidence="ECO:0000305"
FT CONFLICT 720
FT /note="R -> A (in Ref. 1; AAG01326)"
FT /evidence="ECO:0000305"
FT CONFLICT 746
FT /note="C -> S (in Ref. 1; AAG01326)"
FT /evidence="ECO:0000305"
FT CONFLICT 814..815
FT /note="MR -> IA (in Ref. 1; AAG01326)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 882 AA; 99446 MW; 98729E353AB7B865 CRC64;
MQVTIPKSTS KEDDKNRNLL PKNVKPIHYD LSLYPDLETF TYGGKVVVTL DVLEDSNSIT
LHGINLRILT AALEWGSQTV WASEVSYGDE RIVLQFPSTV PANSVAVLTL PFTARISSGM
EGFYRSSYVD SDGNTKYLAT TQMEPTSARR AFPCWDEPAL KATFTIDITA KENYTILSNM
NAVEETVKDG LKTARFAETC RMSTYLLAWI VAELEYVEYF TPGKHCPRLP VRVYTTPGFS
EQGKFAAELG AKTLDFFSGV FGEPYPLPKC DMVAIPDFEA GAMENWGLVT YRLAAILVSE
DSAATVIERV AEVVQHELAH QWFGNLVTMQ FWDGLWLNEG FATWMSWFSC NHFYPEWKVW
ESYVTDNLQS ALSLDALRSS HPIEVPIMHD YEINQIFDAI SYSKGSCVIR MVSKYVGEDT
FIKGIQKYIS KHRYGNTVTE DLWAALSAES GQDISSTMHN WTKKTGYPVL SVSETNDGEL
LIEQHRFLST GDVKPEEDTV IYWAPLKLKT MKDGKAVVDE KAVLSDRSKK IKVDKEALES
YKLNSEQSGI YRVNYSADHL KKLSQIAVEK PDYLSVEDRA GLIADVASLS RAGYGKVSST
LDLIKTWKDE PNFVVFAEML ARLNGIKSTL RFESSDIIAA MKKLVLEVSA TKAHSLGWEF
KANDDHIIRQ FKSTVYNYAG LFGDDKVVKD ALSKFDAYAS GNKSAINDNL RSAVFNIAIR
YGGAKSWDQL LEIYTKTNDP YVRNSCLRAF GVTEDEKYIQ KTLDLTLDPI VKEQDIYLIL
VTLSTHKNGV LAMWKFATSN WDKLLSRLPV AGTMRGYVVR FVTSGFTHAS AIDKIKEFFA
DKDTKLYERA LQQSLDTISA NSSFIDKSLD DITRWLKENR YM
