PSA_ARATH
ID PSA_ARATH Reviewed; 883 AA.
AC Q8H0S9; F4I3R2; Q0WMR3; Q9CAE1; Q9CAJ3;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Puromycin-sensitive aminopeptidase;
DE Short=PSA;
DE EC=3.4.11.14;
DE AltName: Full=Cytosol alanyl aminopeptidase;
DE Short=AAP-S;
DE AltName: Full=Meiotic prophase aminopeptidase 1;
GN Name=MPA1; OrderedLocusNames=At1g63770; ORFNames=F24D7.4, T12P18.21;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 46-180.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP DISRUPTION PHENOTYPE, FUNCTION, ACTIVITY REGULATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=15522847; DOI=10.1105/tpc.104.024992;
RA Sanchez-Moran E., Jones G.H., Franklin F.C., Santos J.L.;
RT "A puromycin-sensitive aminopeptidase is essential for meiosis in
RT Arabidopsis thaliana.";
RL Plant Cell 16:2895-2909(2004).
RN [6]
RP FUNCTION.
RX PubMed=17151235; DOI=10.1534/genetics.106.067595;
RA Pradillo M., Lopez E., Romero C., Sanchez-Moran E., Cunado N., Santos J.L.;
RT "An analysis of univalent segregation in meiotic mutants of Arabidopsis
RT thaliana: a possible role for synaptonemal complex.";
RL Genetics 175:505-511(2007).
CC -!- FUNCTION: Aminopeptidase with broad substrate specificity for several
CC peptides. Involved in proteolytic events essential for cell growth and
CC viability. Plays an essential role during prophase I of meiosis.
CC Required for correct meiotic reconbination in both male and female
CC gametophytes. {ECO:0000269|PubMed:15522847,
CC ECO:0000269|PubMed:17151235}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, preferentially alanine,
CC from a wide range of peptides, amides and arylamides.; EC=3.4.11.14;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Strongly inhibited by puromycin and DAMPAQ-22.
CC {ECO:0000269|PubMed:15522847}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8H0S9-1; Sequence=Displayed;
CC -!- DEVELOPMENTAL STAGE: Expressed in meiocytes during meiotic prophase I.
CC {ECO:0000269|PubMed:15522847}.
CC -!- DISRUPTION PHENOTYPE: Reduced fertility and shorter siliques bearing a
CC lower number of seeds compared with wild-type plants. Cytogenetic
CC characterization of meiosis in the mutant line reveals that both male
CC and female meiosis are defective. {ECO:0000269|PubMed:15522847}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG52429.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG52451.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AEE34146.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC010852; AAG52451.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC011622; AAG52429.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34146.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; ANM60183.1; -; Genomic_DNA.
DR EMBL; AY960336; AAX59049.1; -; mRNA.
DR EMBL; BT002074; AAN72085.1; -; mRNA.
DR EMBL; BT010361; AAQ56804.1; -; mRNA.
DR EMBL; AK229751; BAF01587.1; -; mRNA.
DR RefSeq; NP_001154442.1; NM_001160970.1.
DR RefSeq; NP_001322486.1; NM_001334126.1. [Q8H0S9-1]
DR AlphaFoldDB; Q8H0S9; -.
DR SMR; Q8H0S9; -.
DR BioGRID; 27902; 16.
DR STRING; 3702.AT1G63770.5; -.
DR MEROPS; M01.005; -.
DR iPTMnet; Q8H0S9; -.
DR PaxDb; Q8H0S9; -.
DR PRIDE; Q8H0S9; -.
DR ProMEX; Q8H0S9; -.
DR EnsemblPlants; AT1G63770.7; AT1G63770.7; AT1G63770. [Q8H0S9-1]
DR GeneID; 842681; -.
DR Gramene; AT1G63770.7; AT1G63770.7; AT1G63770. [Q8H0S9-1]
DR KEGG; ath:AT1G63770; -.
DR Araport; AT1G63770; -.
DR eggNOG; KOG1046; Eukaryota.
DR HOGENOM; CLU_007993_2_0_1; -.
DR PRO; PR:Q8H0S9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8H0S9; baseline and differential.
DR Genevisible; Q8H0S9; AT.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.390.10; -; 1.
DR Gene3D; 1.25.50.10; -; 1.
DR Gene3D; 2.60.40.1730; -; 1.
DR Gene3D; 2.60.40.1840; -; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR038438; PepN_Ig-like_sf.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR012779; Peptidase_M1_pepN.
DR InterPro; IPR024601; Peptidase_M1_pepN_C.
DR InterPro; IPR037144; Peptidase_M1_pepN_C_sf.
DR InterPro; IPR035414; Peptidase_M1_pepN_Ig-like.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR46322; PTHR46322; 2.
DR Pfam; PF11940; DUF3458; 1.
DR Pfam; PF17432; DUF3458_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 TIGRFAMs; TIGR02414; pepN_proteo; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Aminopeptidase; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Zinc.
FT CHAIN 1..883
FT /note="Puromycin-sensitive aminopeptidase"
FT /id="PRO_0000424590"
FT ACT_SITE 302
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 265..269
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
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 324
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT SITE 385
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 883 AA; 99159 MW; 2F8589EC07D6DC7C CRC64;
MDAPKEIFLK NYTKPDYYFE TVDLSFSLGE EKTIVSSKIK VSPRVKGSSA ALVLDGHDLK
LLSVKVEGKL LKEGDYQLDS RHLTLPSLPA EESFVLEIDT EIYPHKNTSL EGLYKSSGNF
CTQCEAEGFR KITFYQDRPD IMAKYTCRVE GDKTLYPVLL SNGNLISQGD IEGGRHYALW
EDPFKKPCYL FALVAGQLVS RDDTFTTRSG RQVSLKIWTP AEDLPKTAHA MYSLKAAMKW
DEDVFGLEYD LDLFNIVAVP DFNMGAMENK SLNIFNSKLV LASPETATDA DYAAILGVIG
HEYFHNWTGN RVTCRDWFQL SLKEGLTVFR DQEFSSDMGS RTVKRIADVS KLRIYQFPQD
AGPMAHPVRP HSYIKMDNFY TVTVYEKGAE VVRMYKTLLG TQGFRKGIDL YFERHDEQAV
TCEDFFAAMR DANNADFANF LQWYSQAGTP VVKVVSSYNA DARTFSLKFS QEIPPTPGQP
TKEPTFIPVV VGLLDSSGKD ITLSSVHHDG TVQTISGSST ILRVTKKEEE FVFSDIPERP
VPSLFRGFSA PVRVETDLSN DDLFFLLAHD SDEFNRWEAG QVLARKLMLN LVSDFQQNKP
LALNPKFVQG LGSVLSDSSL DKEFIAKAIT LPGEGEIMDM MAVADPDAVH AVRKFVRKQL
ASELKEELLK IVENNRSTEA YVFDHSNMAR RALKNTALAY LASLEDPAYM ELALNEYKMA
TNLTDQFAAL AALSQNPGKT RDDILADFYN KWQDDYLVVN KWFLLQSTSD IPGNVENVKK
LLDHPAFDLR NPNKVYSLIG GFCGSPVNFH AKDGSGYKFL GDIVVQLDKL NPQVASRMVS
AFSRWKRYDE TRQGLAKAQL EMIMSANGLS ENVFEIASKS LAA
