ID   PIP_ARATH               Reviewed;         380 AA.
AC   P93732; Q93Y05; Q9SKJ3;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 3.
DT   02-SEP-2026, entry version 166.
DE   RecName: Full=Proline iminopeptidase;
DE            Short=PIP;
DE            EC=3.4.11.5;
DE   AltName: Full=Prolyl aminopeptidase;
DE            Short=PAP;
GN   Name=PIP; OrderedLocusNames=At2g14260; ORFNames=T1O16.15;
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 18-380.
RC   STRAIN=cv. Columbia;
RA   Tamura T., Tamura N., Lottspeich F., Baumeister W.;
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically catalyzes the removal of N-terminal proline
CC       residues from peptides. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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=P93732-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the peptidase S33 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC49560.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AC006304; AAD20113.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC06293.1; -; Genomic_DNA.
DR   EMBL; OZ408684; CAO7034972.1; -; Genomic_DNA.
DR   EMBL; AY059916; AAL24398.1; -; mRNA.
DR   EMBL; AY114690; AAM48009.1; -; mRNA.
DR   EMBL; U72711; AAC49560.1; ALT_INIT; mRNA.
DR   PIR; E84515; E84515.
DR   RefSeq; NP_001325175.1; NM_001335417.1.
DR   RefSeq; NP_179037.2; NM_126994.4. [P93732-1]
DR   RefSeq; NP_973454.1; NM_201725.3.
DR   AlphaFoldDB; P93732; -.
DR   SMR; P93732; -.
DR   BioGRID; 1273; 1.
DR   FunCoup; P93732; 387.
DR   STRING; 3702.P93732; -.
DR   ESTHER; arath-pip; Proline_iminopeptidase.
DR   MEROPS; S33.001; -.
DR   iPTMnet; P93732; -.
DR   PaxDb; 3702-P93732; -.
DR   ProteomicsDB; 234960; -. [P93732-1]
DR   GeneID; 815913; -.
DR   KEGG; ath:AT2G14260; -.
DR   Araport; AT2G14260; -.
DR   TAIR; AT2G14260; PIP.
DR   eggNOG; ENOG502QPPY; Eukaryota.
DR   InParanoid; P93732; -.
DR   PhylomeDB; P93732; -.
DR   BRENDA; 3.4.11.5; 399.
DR   PRO; PR:P93732; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; P93732; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0005737; C:cytoplasm; ISM:TAIR.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR   GO; GO:0004177; F:aminopeptidase activity; IDA:TAIR.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0010038; P:response to metal ion; IEP:TAIR.
DR   GO; GO:1902074; P:response to salt; IEP:TAIR.
DR   GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
DR   FunFam; 3.40.50.1820:FF:000382; Proline iminopeptidase; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR029058; AB_hydrolase_fold.
DR   InterPro; IPR002410; Peptidase_S33.
DR   InterPro; IPR005944; Pro_iminopeptidase.
DR   NCBIfam; TIGR01249; pro_imino_pep_1; 1.
DR   PANTHER; PTHR43722; PROLINE IMINOPEPTIDASE; 1.
DR   PANTHER; PTHR43722:SF1; PROLINE IMINOPEPTIDASE; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   PRINTS; PR00793; PROAMNOPTASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Aminopeptidase; Cytoplasm; Hydrolase; Protease;
KW   Reference proteome.
FT   CHAIN           1..380
FT                   /note="Proline iminopeptidase"
FT                   /id="PRO_0000080853"
FT   DOMAIN          98..360
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        172
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        329
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        357
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        28
FT                   /note="L -> P (in Ref. 5)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        344
FT                   /note="W -> C (in Ref. 5; AAC49560)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   380 AA;  43059 MW;  EC7DA93283639A6D CRC64;
     MNLILASFSL APCFCVRFFP SNHNNLNLLF PGQRKIQVSC GGKSEVLKSD TMEPHEAETF
     VNKRTLYAPI EPYSSGNLKV SDVHTLYWEQ SGKPDGHPVV FLHGGPGGGT APSNRRFFDP
     EFYRIVLFDQ RGAGKSTPHA CLEENTTWDL VNDIEKLREH LKIPEWLVFG GSWGSTLALA
     YSQSHPDKVT GLVLRGIFLL RKKEIDWFYE GGAAAIYPDA WEEFRDLIPE NERGSSLVDA
     YHKRLNSDDL EIQYAAARAW TKWEMMTAYL RPNLENVQKA EDDKFSLAFA RIENHYFVNK
     GFFPSDSHLL DNVDKIRHIK TTIVQGRYDV CCPMMSAWDL HKAWPEAELK IVYDAGHSAN
     EPGISAELVV ANEKMKALMG
//