YDZF_SCHPO
ID YDZF_SCHPO Reviewed; 853 AA.
AC Q9P7E9; O13720;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2003, sequence version 2.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Putative dipeptidyl aminopeptidase C14C4.15c;
DE EC=3.4.14.-;
GN ORFNames=SPAC14C4.15c, SPAPJ760.01c;
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; Single-pass type II membrane
CC protein. Note=Lysosome-like vacuoles.
CC -!- SIMILARITY: Belongs to the peptidase S9B family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAB11208.1; -; Genomic_DNA.
DR PIR; T37700; T37700.
DR RefSeq; NP_594920.2; NM_001020352.2.
DR AlphaFoldDB; Q9P7E9; -.
DR SMR; Q9P7E9; -.
DR BioGRID; 278581; 6.
DR STRING; 4896.SPAC14C4.15c.1; -.
DR ESTHER; schpo-C14C4.15C; DPP4N_Peptidase_S9.
DR MEROPS; S09.A93; -.
DR MaxQB; Q9P7E9; -.
DR PaxDb; Q9P7E9; -.
DR PRIDE; Q9P7E9; -.
DR EnsemblFungi; SPAC14C4.15c.1; SPAC14C4.15c.1:pep; SPAC14C4.15c.
DR GeneID; 2542105; -.
DR KEGG; spo:SPAC14C4.15c; -.
DR PomBase; SPAC14C4.15c; -.
DR VEuPathDB; FungiDB:SPAC14C4.15c; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_334677_0_0_1; -.
DR InParanoid; Q9P7E9; -.
DR OMA; DNDHHMP; -.
DR PhylomeDB; Q9P7E9; -.
DR PRO; PR:Q9P7E9; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000329; C:fungal-type vacuole membrane; ISO:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; ISO:PomBase.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0016485; P:protein processing; ISO:PomBase.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
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.
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..853
FT /note="Putative dipeptidyl aminopeptidase C14C4.15c"
FT /id="PRO_0000122423"
FT TOPO_DOM 1..65
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..853
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 719
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 795
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 828
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 483
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 613
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 853 AA; 98342 MW; 38450BA50F8304B6 CRC64;
MNAYEGDTLN NHGKSSTRQH WRKRSAVSSS LEFSSYEESN SPIENTEVLK VSEIEAKKRR
RKKHRYIYLA VCLFFLASVL SCAIIFRFYL HTNRENFSLF KNDSYKQKEP ITVSHFGESI
FLPYHQDIEW ITSTEGTVLY YDQSTFSLSL FYPDGKEYGS NVDSLITSFV LTCKNLHRKR
YSSDMEYIAF SCSKDRRWRH SYYEDVYLVE RATGRIEHLA SDQSKKIVVA EWSPIGHKLV
YGLGSNLFIW ESFSEPPVCI TDQSDLDGLF NGNSDWVYEE EILQSSKAVW WSPDGNCLSY
LSIDDSKVPV HVLPFEQLDS KVEDQNRVNN FFHYSTPKDP IPFVKLFVNC FTDSGESIEV
DSSFPLSTQH RYITDVAWAG NEKLMFVEVL RGNYERVTSL FDLSSRKTTI ENTEVSEHPL
ALTSSLHLKY LSFESLGNLK ERYVRQYFLS NKKRIAIYEL DNPVPIYLTP VNISFLSDLY
LINNTLYFTA ISSGSPFSRV YRLCTKSLIL SEINIQIGSG LFGIKVSNDQ NYLLVNYLGP
EIPKQFIYSI HEDKVSTSND HSKNNLPSDS SSTSLGKVKL ELCNSLETNE ELIITKEKFA
FPSVFFKVIK VKNITAYIQE IRPPNFNPRK RYPTVFHLYG APQSALVTGK YEMDINELMA
SVYNFLVIKV DIVDISDVSG QHLFSDSHEL IIKSWIELLR SYVDTPYIDR HRVGIWGWSF
GGYLTLKILE NADFIKTGAV VAPVTDWRYY DAYYSENLLG AYSKQTTAIY DKTAVHYSEN
FRKLCGLLVL HGTSDDNVHI ENTMQLTKAM VEKGVYNYYP FIVPNANHEF SDPTDYTFLR
EKLSGHFHHA LYC
