TPP2_SCHPO
ID TPP2_SCHPO Reviewed; 1274 AA.
AC Q9UT05;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Tripeptidyl-peptidase 2 homolog;
DE Short=TPP-2;
DE EC=3.4.14.10 {ECO:0000269|PubMed:9740805};
DE AltName: Full=Multicorn protease;
GN Name=tpp2; ORFNames=SPAP8A3.12c;
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 CATALYTIC ACTIVITY.
RX PubMed=9740805; DOI=10.1016/s0960-9822(07)00423-x;
RA Osmulski P.A., Gaczynska M.;
RT "A new large proteolytic complex distinct from the proteasome is present in
RT the cytosol of fission yeast.";
RL Curr. Biol. 8:1023-1026(1998).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-606, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [4]
RP IDENTIFICATION AS TPP2.
RX PubMed=19467630; DOI=10.1016/j.abb.2009.01.007;
RA Eriksson S., Gutierrez O.A., Bjerling P., Tomkinson B.;
RT "Development, evaluation and application of tripeptidyl-peptidase II
RT sequence signatures.";
RL Arch. Biochem. Biophys. 484:39-45(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal tripeptide from a polypeptide.;
CC EC=3.4.14.10; Evidence={ECO:0000269|PubMed:9740805};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MISCELLANEOUS: The limitation of proteolytic products to tripeptides is
CC achieved by tailoring the size of the substrate-binding cleft: the two
CC negatively charged residues Glu-367 and Glu-393 that are blocking
CC position P4 limit the number of residues that can be accommodated in
CC the binding cleft and thus create a molecular ruler. At the same time,
CC they orient substrates so that the tripeptides are removed exclusively
CC from the N-terminus (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB55179.1; -; Genomic_DNA.
DR PIR; T39249; T39249.
DR RefSeq; NP_594951.1; NM_001020382.2.
DR AlphaFoldDB; Q9UT05; -.
DR SMR; Q9UT05; -.
DR BioGRID; 279609; 2.
DR STRING; 4896.SPAP8A3.12c.1; -.
DR MEROPS; S08.A56; -.
DR iPTMnet; Q9UT05; -.
DR MaxQB; Q9UT05; -.
DR PaxDb; Q9UT05; -.
DR PRIDE; Q9UT05; -.
DR EnsemblFungi; SPAP8A3.12c.1; SPAP8A3.12c.1:pep; SPAP8A3.12c.
DR GeneID; 2543179; -.
DR KEGG; spo:SPAP8A3.12c; -.
DR PomBase; SPAP8A3.12c; tpp2.
DR VEuPathDB; FungiDB:SPAP8A3.12c; -.
DR eggNOG; KOG1114; Eukaryota.
DR HOGENOM; CLU_003084_1_0_1; -.
DR InParanoid; Q9UT05; -.
DR OMA; SLRDFQC; -.
DR PhylomeDB; Q9UT05; -.
DR PRO; PR:Q9UT05; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; NAS:PomBase.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008240; F:tripeptidyl-peptidase activity; IMP:PomBase.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR CDD; cd04857; Peptidases_S8_Tripeptidyl_Aminopeptidase_II; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR022229; Peptidase_S8A_TPPII.
DR InterPro; IPR034051; TPP_II_domain.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF12580; TPPII; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 1: Evidence at protein level;
KW Aminopeptidase; Cytoplasm; Hydrolase; Phosphoprotein; Protease;
KW Reference proteome; Serine protease.
FT CHAIN 1..1274
FT /note="Tripeptidyl-peptidase 2 homolog"
FT /id="PRO_0000310393"
FT DOMAIN 75..570
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 101
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 326
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 512
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT MOD_RES 606
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1274 AA; 142926 MW; 4985CF6C07F429BE CRC64;
MKFRLNANFN FSFRRYCFVQ CRNKYHSHVR YLSSAKKSGI LRNSYNQRTE RYFTNIMIPS
DYSNKFYPVD GVVPKHETQA YEFLKKFPEY DGRGVTVGIL DTGVDPGAPG LSVTTTGLPK
FKNIVDCTGA GDVDTSVEVA AADSNDYLTI TGRSGRTLKL SKEWKNPSKK WKVGCKLAYE
FFPKDLRKRL QKLETEDMNK SNRKLLQDAT DEYAKFKDKF PEAPLDKDNL QTQKELEARI
ECLKQLAEKF DNPGPLYDVV VFHDGEHWRV VIDSDQTGDI YLHKPLADFN VAQEWSTFGS
LDLLSYGVHV YDNGNITSIV AVSGTHGTHV AGIIGANHPE TPELNGAAPG CQLVSLMIGD
GRLDSLETSH AFSRACSEII KNEVDIINIS FGEDAGIPNK GRVIELLRDE LAGKRNVVIV
SSAGNNGPAY TTVGAPGGTT FDVISVGAYV TSGMMQAQYN LLSTVHDTPY TWCSRGPTLD
GDTGVSIYAP GGAITSVPPY SLQNSQLMNG TSMSSPSACG GISLILSALK AQKKPYTAAA
IKKAVMYTSK DLRDDFNTGM LQVDNAYEYL AQSDFQYTGA RSFTINGNIG NSKRGVYLRN
PTEVCSPSRH MFNVAPKFED GEEYEKSHFE VQLSLATTQP WIQAPEYVMM AGTGRGIPVR
VDPTALAPGH HFGKVLAYDA SNESRRCVFE IPVTVMKPSS ISNTCFSLRD VSFEPTLIKR
HFLVPPKGAT YVEIRVKATS ELESTNMLWI SVNQTIPQTK LNEASTELIM PVTQNEVTTK
LVSIDDSYTL ELCMAQWWSS LEPMVLDIDV NFHGIKVVNG KEINLISSQG LKRVDCASIR
RENFKPDITL KDYVDSFKPT NTVIKPLGDR DIMPDGQQLF ELMATYSVEI SEKTELKADF
AVPHNMYDNG FNGLFFMVFD SQKQRVHYGD MYTSSHTLEK GEYLYKFQLL SVDPSTLERF
RNVTLRLTKK LKKPITLPLY ADHIDFCDNK TYERENIDAG VVESFVVGTN IEGEQYASEL
KENSLLTGEL KFGDCEKGTV PVTLVLPPKI STKEDTKLGE KCANIVQLQV DLLSKLADQE
KEKHLKYLQS SYKNSLEVQL AKLDIVKETN ERLSTADSIL SLIDTEALSR YYSCQQKVED
TIPRDVVLEK KMALQRDAFI RALVVKCETF STQGHKDKDN YFQNYQLLLN WLENSDPRVW
QIKKDYYKSQ NQYGLALKAL LELLKENGNS GKMDVAKLLS EEKELLVNLG WNYWHDIVFV
ETVKRVPPYS YALF
