YEA8_SCHPO
ID YEA8_SCHPO Reviewed; 793 AA.
AC O14073;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=Putative dipeptidyl aminopeptidase C2E11.08;
DE EC=3.4.14.-;
GN ORFNames=SPAC2E11.08, SPACUNK4.08;
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).
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250}; Single-pass type
CC II membrane protein {ECO:0000250}. Note=Lysosome-like vacuoles.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S9B family. {ECO:0000305}.
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DR EMBL; CU329670; CAA20138.1; -; Genomic_DNA.
DR PIR; T41703; T41703.
DR RefSeq; NP_593970.1; NM_001019397.2.
DR AlphaFoldDB; O14073; -.
DR SMR; O14073; -.
DR BioGRID; 278879; 2.
DR STRING; 4896.SPACUNK4.08.1; -.
DR ESTHER; schpo-C2E11.08; DPP4N_Peptidase_S9.
DR MEROPS; S09.006; -.
DR MaxQB; O14073; -.
DR PaxDb; O14073; -.
DR EnsemblFungi; SPACUNK4.08.1; SPACUNK4.08.1:pep; SPACUNK4.08.
DR GeneID; 2542415; -.
DR KEGG; spo:SPACUNK4.08; -.
DR PomBase; SPACUNK4.08; -.
DR VEuPathDB; FungiDB:SPACUNK4.08; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_006105_0_1_1; -.
DR InParanoid; O14073; -.
DR OMA; AYVWKND; -.
DR PhylomeDB; O14073; -.
DR PRO; PR:O14073; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; ISO:PomBase.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0016485; P:protein processing; ISO:PomBase.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002471; Pept_S9_AS.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002469; Peptidase_S9B_N.
DR Pfam; PF00930; DPPIV_N; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE 3: Inferred from homology;
KW Aminopeptidase; Glycoprotein; Hydrolase; Membrane; Protease;
KW Reference proteome; Serine protease; Signal-anchor; Transmembrane;
KW Transmembrane helix; Vacuole.
FT CHAIN 1..793
FT /note="Putative dipeptidyl aminopeptidase C2E11.08"
FT /id="PRO_0000122422"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..793
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 647
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT ACT_SITE 722
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT ACT_SITE 755
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 535
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 761
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 793 AA; 91305 MW; 20B707F97F231463 CRC64;
MNDFSFEDKG LISRSGFGSR HVRRVVKALA LIFSLLILYL TISNVSDSPP KRDSLSLDDI
VLQKYKPSYK QVNWIDSQGL KDTFLVKYGD LINIQDPYNL NKTLFSVSDL VYNGIQLDYD
SYSISFDAKY VLVSVNKSQR WRHSSFAQYY LYNTETKDVN MLGQDNEHWT ISLAEWSPTG
HQLSFVYNND LYVRKNDGNV QRLTYDGTVD VFNGLTDWIY EEEVLSSPST IWWSPDSDKI
AFLKLNESEI PTYHYPLYTA ELDPSLPEFD YNKDMAIKYP KPGNPNPSVS LFVADLNSNA
SSNFSLWHNE PLAEPVVQNV LWVNTSSVLV QFTNRNSTCI TARLLDTELK SIHTVKTECL
EEGWYEVQQS AKMFPLNNSL VWENWSDGYF DILALDDYNH LAFIPFNGSS PIYLTSGAWD
VTDGPIHIDG DFGNVYFLAT LKDSTERHLY YVSLDTLEIY GITDNGEDEG YYSTSFSPFG
DFYVLNYHGP DVPWQELRST KDKDYCLSLE TNSRLKQQLS SITLPSVEYG KLTFNDTTFN
FMERRPRNFD VNKKYPVLFF AYGGPGSQQV AKLFRVDFQA YLASHPDFEF IVVTLDGRGT
GFNGNAFRYS VSRHLGEWES YDQGQAGKFW ADLPFVDENH VGIWGWSYGG YLTLKTLETQ
DVFSYGMAVA PVTDWRLYDS VYTERYMDLP QYNKEGYKNS QIHDYEKFKQ LKRFFVAHGT
GDDNVHFQHS MHLMDGLNLA NCYNYDMAVF PDSAHSISYH NASLSIYHRL SEWIGDALGR
IDPSTGVRQH RWD
