DNPEP_SCHPO
ID DNPEP_SCHPO Reviewed; 467 AA.
AC O36014; P78925;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Aspartyl aminopeptidase 1;
DE EC=3.4.11.21;
GN Name=aap1; ORFNames=SPAC4F10.02;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 76-467.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=20044953; DOI=10.5483/bmbrep.2009.42.12.812;
RA Lee S., Kim J.S., Yun C.H., Chae H.Z., Kim K.;
RT "Aspartyl aminopeptidase of Schizosaccharomyces pombe has a molecular
RT chaperone function.";
RL BMB Rep. 42:812-816(2009).
CC -!- FUNCTION: Aspartyl aminopeptidase that is able to remove aspartyl
CC residue at N-terminus of angiotensin I. Acts also as a chaperone and
CC efficiently suppressed the thermal aggregation of citrate synthase.
CC {ECO:0000269|PubMed:20044953}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal aspartate or glutamate from a
CC peptide, with a preference for aspartate.; EC=3.4.11.21;
CC Evidence={ECO:0000269|PubMed:20044953};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Tetrahedron-shaped homododecamer built from six homodimers.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the peptidase M18 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB11706.1; -; Genomic_DNA.
DR EMBL; D89276; BAA13937.1; -; mRNA.
DR PIR; T38806; T38806.
DR PIR; T43206; T43206.
DR RefSeq; NP_594745.1; NM_001020172.2.
DR PDB; 7DDE; EM; 2.26 A; A/C/E/G/I/K/M/O/Q/S/V/X=1-467.
DR PDBsum; 7DDE; -.
DR AlphaFoldDB; O36014; -.
DR SMR; O36014; -.
DR BioGRID; 280020; 2.
DR STRING; 4896.SPAC4F10.02.1; -.
DR MaxQB; O36014; -.
DR PaxDb; O36014; -.
DR EnsemblFungi; SPAC4F10.02.1; SPAC4F10.02.1:pep; SPAC4F10.02.
DR GeneID; 2543605; -.
DR KEGG; spo:SPAC4F10.02; -.
DR PomBase; SPAC4F10.02; aap1.
DR VEuPathDB; FungiDB:SPAC4F10.02; -.
DR eggNOG; KOG2596; Eukaryota.
DR HOGENOM; CLU_019532_2_0_1; -.
DR OMA; GPILKVN; -.
DR PhylomeDB; O36014; -.
DR BRENDA; 3.4.11.21; 5613.
DR PRO; PR:O36014; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000324; C:fungal-type vacuole; IBA:GO_Central.
DR GO; GO:0000328; C:fungal-type vacuole lumen; IDA:PomBase.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IDA:PomBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IDA:PomBase.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.30.250.10; -; 1.
DR InterPro; IPR001948; Peptidase_M18.
DR InterPro; IPR023358; Peptidase_M18_dom2.
DR PANTHER; PTHR28570; PTHR28570; 1.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
PE 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Chaperone; Cytoplasm; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Reference proteome; Zinc.
FT CHAIN 1..467
FT /note="Aspartyl aminopeptidase 1"
FT /id="PRO_0000173454"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 365
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 372
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 431
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 76..77
FT /note="KP -> MI (in Ref. 2; BAA13937)"
FT /evidence="ECO:0000305"
FT CONFLICT 262..263
FT /note="FC -> SG (in Ref. 2; BAA13937)"
FT /evidence="ECO:0000305"
FT TURN 2..4
FT /evidence="ECO:0007829|PDB:7DDE"
FT HELIX 5..17
FT /evidence="ECO:0007829|PDB:7DDE"
FT HELIX 22..35
FT /evidence="ECO:0007829|PDB:7DDE"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:7DDE"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:7DDE"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:7DDE"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:7DDE"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:7DDE"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:7DDE"
FT STRAND 92..103
FT /evidence="ECO:0007829|PDB:7DDE"
FT STRAND 106..116
FT /evidence="ECO:0007829|PDB:7DDE"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:7DDE"
FT STRAND 127..136
FT /evidence="ECO:0007829|PDB:7DDE"
FT STRAND 142..156
FT /evidence="ECO:0007829|PDB:7DDE"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:7DDE"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:7DDE"
FT TURN 175..178
FT /evidence="ECO:0007829|PDB:7DDE"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:7DDE"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:7DDE"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:7DDE"
FT HELIX 204..215
FT /evidence="ECO:0007829|PDB:7DDE"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:7DDE"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:7DDE"
FT STRAND 227..236
FT /evidence="ECO:0007829|PDB:7DDE"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:7DDE"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:7DDE"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:7DDE"
FT HELIX 258..270
FT /evidence="ECO:0007829|PDB:7DDE"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:7DDE"
FT STRAND 282..290
FT /evidence="ECO:0007829|PDB:7DDE"
FT TURN 292..295
FT /evidence="ECO:0007829|PDB:7DDE"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:7DDE"
FT HELIX 306..315
FT /evidence="ECO:0007829|PDB:7DDE"
FT HELIX 323..329
FT /evidence="ECO:0007829|PDB:7DDE"
FT STRAND 332..336
FT /evidence="ECO:0007829|PDB:7DDE"
FT HELIX 344..349
FT /evidence="ECO:0007829|PDB:7DDE"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:7DDE"
FT STRAND 362..365
FT /evidence="ECO:0007829|PDB:7DDE"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:7DDE"
FT HELIX 376..389
FT /evidence="ECO:0007829|PDB:7DDE"
FT STRAND 393..396
FT /evidence="ECO:0007829|PDB:7DDE"
FT HELIX 409..416
FT /evidence="ECO:0007829|PDB:7DDE"
FT STRAND 419..424
FT /evidence="ECO:0007829|PDB:7DDE"
FT STRAND 426..429
FT /evidence="ECO:0007829|PDB:7DDE"
FT STRAND 432..439
FT /evidence="ECO:0007829|PDB:7DDE"
FT HELIX 440..454
FT /evidence="ECO:0007829|PDB:7DDE"
FT HELIX 456..459
FT /evidence="ECO:0007829|PDB:7DDE"
FT STRAND 460..464
FT /evidence="ECO:0007829|PDB:7DDE"
SQ SEQUENCE 467 AA; 51741 MW; 4A162926DBE3D086 CRC64;
MTATAKSCAL DFLDFVNASP TPYHAVQNLA EHYMSHGFQY LSEKSDWQSK IEPGNSYFVT
RNKSSIIAFS IGKKWKPGNG FSIIATHTDS PTLRLKPKSQ KSAYGYLQVG VEKYGGGIWH
TWFDRDLSLA GRVMVEEEDG RVIQYNVHID RPLLRIPTLA IHLDPSANSS FSFNMETEFV
PLIGLENELA KEETSDNGDK YHHPVLLSLL ANEISKSLET TIDPSKIVDF ELILGDAEKA
RLGGIHEEFV FSPRLDNLGM TFCASQALTK SLENNSLDNE SCVRVVPSFD HEEIGSVSAQ
GAESTFLPAV LQRICELGKE SSLFSISMVK SFLVSADMAH AMHPNYSSRY ENSNTPFLNK
GTVIKVNANQ RYTTNSAGIV LLKKVAQLAD VPIQSFVVRN DSPCGSTIGP KLAAMTGMRT
LDLGNPMLSM HSCREMCGSK DFEYAVVLFS SFFQNFANLE EKIIIDE
