PPCEL_RAT
ID PPCEL_RAT Reviewed; 726 AA.
AC Q5HZA6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Prolyl endopeptidase-like;
DE EC=3.4.21.- {ECO:0000250|UniProtKB:Q4J6C6};
DE AltName: Full=Prolylendopeptidase-like;
GN Name=Prepl;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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=Q5HZA6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5HZA6-2; Sequence=VSP_030409;
CC -!- SIMILARITY: Belongs to the peptidase S9A family. {ECO:0000305}.
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DR EMBL; AABR03049307; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03050672; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC089111; AAH89111.1; -; mRNA.
DR RefSeq; NP_001010951.1; NM_001010951.1. [Q5HZA6-2]
DR RefSeq; XP_008762679.1; XM_008764457.2. [Q5HZA6-2]
DR RefSeq; XP_008762680.1; XM_008764458.2. [Q5HZA6-2]
DR AlphaFoldDB; Q5HZA6; -.
DR SMR; Q5HZA6; -.
DR BioGRID; 256016; 1.
DR STRING; 10116.ENSRNOP00000009660; -.
DR ESTHER; ratno-q5hza6; S9N_PREPL_Peptidase_S9.
DR MEROPS; S09.015; -.
DR iPTMnet; Q5HZA6; -.
DR PhosphoSitePlus; Q5HZA6; -.
DR jPOST; Q5HZA6; -.
DR PaxDb; Q5HZA6; -.
DR PRIDE; Q5HZA6; -.
DR Ensembl; ENSRNOT00000082353; ENSRNOP00000070154; ENSRNOG00000007326. [Q5HZA6-2]
DR GeneID; 298771; -.
DR KEGG; rno:298771; -.
DR UCSC; RGD:1310143; rat. [Q5HZA6-1]
DR CTD; 9581; -.
DR RGD; 1310143; Prepl.
DR VEuPathDB; HostDB:ENSRNOG00000007326; -.
DR eggNOG; KOG2237; Eukaryota.
DR GeneTree; ENSGT00530000063426; -.
DR HOGENOM; CLU_011290_2_1_1; -.
DR InParanoid; Q5HZA6; -.
DR PhylomeDB; Q5HZA6; -.
DR PRO; PR:Q5HZA6; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000007326; Expressed in Ammon's horn and 20 other tissues.
DR ExpressionAtlas; Q5HZA6; baseline and differential.
DR Genevisible; Q5HZA6; RN.
DR GO; GO:0005856; C:cytoskeleton; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Golgi apparatus; Hydrolase;
KW Nucleus; Phosphoprotein; Protease; Reference proteome; Serine protease.
FT CHAIN 1..726
FT /note="Prolyl endopeptidase-like"
FT /id="PRO_0000314864"
FT ACT_SITE 558
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q4J6C6"
FT ACT_SITE 644
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q4J6C6"
FT ACT_SITE 689
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q4J6C6"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 1..88
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030409"
SQ SEQUENCE 726 AA; 83482 MW; 2AE3184F35B38863 CRC64;
MQQTTKLFLG ALKYSIPHLG KCMPKQNYCN VADPYYNRLR LKNYRLTKCL QNKPKISELA
RNIPSRSFSV KDKLEKPESL QKRGINICMD AFEKVRTRLE TQPQEEYEIV NAEIKHGGFV
YYQEGCCLVR SKDEEADSDN YEVLFNLEEL KLEQPFIDCI RVAPDEKYVA AKIRAEDSET
STCIVVKLSD QPAMEASFPN VSSFEWVKDE EDEDVLFYTF QRNLRCHDVY RATFGDNKRN
ERFYTEKDPS YFVFLYLTKD SRFLTLNIMN KTTSEVWLID GLSPWDPPML IQKRIHGMLY
YVEHRDDELY ILTNVGEPTE FKLMRTAADA PAIMNWDLFF TMKRNTKVVD LDMFKDHCVL
FLKHSNLLYV NVIGLADDSV RSLKLPPWAC GFIMDTNSDP KNCPFQLCSP IRPPKYYTYK
FAEGKLFEET GHEDPITKTS RVLRIEAKSK DGKLVPMTVF HKTDSEDLQR KPLLVHVYGA
YGMDLKMNFR PERRVLVDDG WILAYCHVRG GGELGLQWHA DGRLTKKLNG LADLEACIKT
LHSQGFSQPS LTTLSAFSAG GVLVGALCNS KPELLRAVTL EAPFLDVLNT MMDTTLPLTL
EELEEWGNPS SDEKHKNYIK RYCPCQNMKP QHYPSVHITA YENDERVPLK GIVNYTEKLK
EAVAEHSKGA GEGYQPPNIV LDIQPGGNHV IEDSHKKITT QMKFLYDELG LDSTDAFEAL
KKYLKV
