PPCEL_PONAB
ID PPCEL_PONAB Reviewed; 727 AA.
AC Q5RAK4; Q5R5G9; Q5RDT7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Prolyl endopeptidase-like;
DE EC=3.4.21.- {ECO:0000250|UniProtKB:Q4J6C6};
DE AltName: Full=Prolylendopeptidase-like;
GN Name=PREPL;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain cortex, and Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Serine peptidase whose precise substrate specificity remains
CC unclear (By similarity). Does not cleave peptides after a arginine or
CC lysine residue (By similarity). Regulates trans-Golgi network
CC morphology and sorting by regulating the membrane binding of the AP-1
CC complex (By similarity). May play a role in the regulation of synaptic
CC vesicle exocytosis (By similarity). {ECO:0000250|UniProtKB:Q4J6C6}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with the AP-1 complex (By
CC similarity). {ECO:0000250|UniProtKB:Q4J6C6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q4J6C6}. Golgi apparatus, trans-Golgi network
CC {ECO:0000250|UniProtKB:Q8C167}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q8C167}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q8C167}. Nucleus {ECO:0000250|UniProtKB:Q4J6C6}.
CC Note=Co-localizes with AP-1 in the trans-Golgi network (By similarity).
CC Co-localizes with MAP2 and ACTB on the cytoskeleton (By similarity).
CC Co-localizes with STX6 and GOSR2 at the Golgi apparatus (By
CC similarity). {ECO:0000250|UniProtKB:Q8C167}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5RAK4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5RAK4-2; Sequence=VSP_030408;
CC -!- SIMILARITY: Belongs to the peptidase S9A family. {ECO:0000305}.
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DR EMBL; CR857812; CAH90070.1; -; mRNA.
DR EMBL; CR859011; CAH91206.1; -; mRNA.
DR EMBL; CR859512; CAH91680.1; -; mRNA.
DR EMBL; CR860890; CAH92997.1; -; mRNA.
DR RefSeq; NP_001124991.1; NM_001131519.1.
DR RefSeq; NP_001128804.1; NM_001135332.1.
DR RefSeq; XP_009235604.1; XM_009237329.1. [Q5RAK4-2]
DR RefSeq; XP_009235605.1; XM_009237330.1. [Q5RAK4-2]
DR RefSeq; XP_009235606.1; XM_009237331.1. [Q5RAK4-2]
DR AlphaFoldDB; Q5RAK4; -.
DR SMR; Q5RAK4; -.
DR STRING; 9601.ENSPPYP00000013906; -.
DR ESTHER; ponpy-q5rak4; S9N_PREPL_Peptidase_S9.
DR MEROPS; S09.015; -.
DR Ensembl; ENSPPYT00000014469; ENSPPYP00000013906; ENSPPYG00000012449. [Q5RAK4-2]
DR Ensembl; ENSPPYT00000036766; ENSPPYP00000038225; ENSPPYG00000012449. [Q5RAK4-1]
DR GeneID; 100171865; -.
DR GeneID; 100189711; -.
DR KEGG; pon:100171865; -.
DR CTD; 9581; -.
DR eggNOG; KOG2237; Eukaryota.
DR GeneTree; ENSGT00530000063426; -.
DR HOGENOM; CLU_011290_2_1_1; -.
DR InParanoid; Q5RAK4; -.
DR OrthoDB; 1124637at2759; -.
DR Proteomes; UP000001595; Chromosome 2A.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
DR GO; GO:0008233; F:peptidase activity; ISS:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISS:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR023302; Pept_S9A_N.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002470; Peptidase_S9A.
DR Pfam; PF00326; Peptidase_S9; 1.
DR Pfam; PF02897; Peptidase_S9_N; 1.
DR PRINTS; PR00862; PROLIGOPTASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Golgi apparatus; Hydrolase;
KW Nucleus; Protease; Reference proteome; Serine protease.
FT CHAIN 1..727
FT /note="Prolyl endopeptidase-like"
FT /id="PRO_0000314863"
FT ACT_SITE 559
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q4J6C6"
FT ACT_SITE 645
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q4J6C6"
FT ACT_SITE 690
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q4J6C6"
FT VAR_SEQ 1..89
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_030408"
FT CONFLICT 122
FT /note="Y -> C (in Ref. 1; CAH90070)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="Missing (in Ref. 1; CAH91206)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="E -> G (in Ref. 1; CAH91206)"
FT /evidence="ECO:0000305"
FT CONFLICT 644
FT /note="N -> D (in Ref. 1; CAH91206)"
FT /evidence="ECO:0000305"
FT CONFLICT 684
FT /note="I -> M (in Ref. 1; CAH90070)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 727 AA; 83941 MW; E3F2B486E81D2403 CRC64;
MQQKTKLFLQ ALKYSIPHLG KCMQKQHLNH YNFADHYYNR IKLKKYHLTK CLQNKPKISE
LARNIPSRSF SCKDLQPVKQ ENEKPLPENM DAFEKVRTKL ETQPQEEYEI INVEVKHGGF
VYYQEGCCLV RSKDEEADND NYEVLFNLEE LKLDQPFIDC IRVAPDEKYV AAKIRTEDSE
ASTCVIIKLS DQPVMEASFP NVSSFEWVKD EEDEDVLFYT FQRNLRCHDV YRATFGDNKR
NERFYTEKDP SYFVFLYLTK DSRFLTINIM NKTTSEVWLI DGLSPWDPPV LIQKRIHGVL
YYVEHRDDEL YILTNVGEPT EFKLMRTAAD TPAIMNWDLF FTMKRNTKVI DLDMFKDHCV
LFLKHSNLLY VNVIGLADDS VRSLKLPPWA CGFIMDTNSD PKNCPFQLCS PIRPPKYYTY
KFAEGKLFEE TGHEDPITKT SRVLRLEAKS KDGKLVPMTV FHKTDSEDLQ KKPLLVQVYG
AYGIDLKMNF RPERRVLVDD GWILAYCHVR GGGELGLQWH ADGRLTKKLN GLADLEACIK
TLHGQGFSQP SLTTLTAFSA GGVLAGALCN SNPELLRAVT LEAPFLDVLN TMMDTTLPLT
LEELEEWGNP SSDEKHKNYI KHYCPYQNIK PQHYPSIHIT AYENDERVPL KGIVSYTEKL
KEAIAEHAKD TGEGYQSPNI ILDIQPGGNH VIEDSHKKIT AQIKFLYEEL GLDSTSVFED
LKKYLKF
