O14124 (DPEH1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Uncharacterized dipeptidase C3A11.10c
EC=3.4.13.19

Gene names

ORF Names:

SPAC3A11.10c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	409 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Hydrolysis of dipeptides.
Cofactor	Zinc By similarity.
Subunit structure	Interacts with dil1. Ref.2
Sequence similarities	Belongs to the peptidase M19 family.

Ontologies

Keywords
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Aminopeptidase Dipeptidase Hydrolase Metalloprotease Protease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to stress Inferred from expression pattern PubMed 12529438. Source: PomBase proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Golgi apparatus Inferred from direct assay PubMed 16823372. Source: PomBase
Molecular_function	aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW dipeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW dipeptidyl-peptidase activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloexopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 39	39	Potential
	Chain	40 – 409	370	Uncharacterized dipeptidase C3A11.10c		PRO_0000314654
Sites
	Metal binding	67	1	Zinc 1; catalytic By similarity
	Metal binding	69	1	Zinc 1; catalytic By similarity
	Metal binding	181	1	Zinc 1; catalytic By similarity
	Metal binding	181	1	Zinc 2; catalytic By similarity
	Metal binding	250	1	Zinc 2; catalytic By similarity
	Metal binding	271	1	Zinc 2; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	O14124 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 860A95056C6B1CF1	FASTA	409	46,048
	10 20 30 40 50 60 MVSDSKLELP LPVNQQKPRR RRILKVHLLI AALILSAVGY LGKGKWIWTP ERKAHFVLTH 70 80 90 100 110 120 FPLIDGHNDL PIYLRENYDN RLLNISLEHL PGQTDIFRLR QGHVGGQFWS VFVECPSLDS 130 140 150 160 170 180 NSSLSWNRTG EYEAVTQTLQ QIDVVKRMAL YYPKTFSLTD HSGKVKFDFL RNHISSMMGI 190 200 210 220 230 240 EGLHQIAGSP SILRQFYDLG VRYATLAHNC DNVFADAAVD GKRTNKGLSP AGRDIVREMN 250 260 270 280 290 300 RLGMIVDLSH TTPETMHQAL DVSVAPAFFS HSSAKGVYDH PRNVPDDVLI RVKETDGVVM 310 320 330 340 350 360 VNFYPAFISP HPENATIDTV VEHIMHIANV TGSYRHIGLG GDFDGIDMVP KGLEDVSKYP 370 380 390 400 DLFVKLAERG LSITELADIA GRNVLRVWKT TEDLGHSIHE PPLEWEDDF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
[2]	"High-throughput knockout screen in Schizosaccharomyces pombe identifies a novel gene required for efficient homolog disjunction during meiosis I." Rumpf C., Cipak L., Novatchkova M., Li Z., Polakova S., Dudas A., Kovacikova I., Miadokova E., Ammerer G., Gregan J. Cell Cycle 9:1802-1808(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH DIL1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAB16385.1.
PIR	T11632.
RefSeq	NP_594193.1. NM_001019617.2.
3D structure databases
HSSP	HSSP built from PDB template 1ITU based on UniProtKB P16444.
ProteinModelPortal	O14124.
ModBase	Search...
Protein-protein interaction databases
STRING	4896.SPAC3A11.10c-1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC3A11.10c.1; SPAC3A11.10c.1:pep; SPAC3A11.10c.
GeneID	2543080.
KEGG	spo:SPAC3A11.10c.
Organism-specific databases
PomBase	SPAC3A11.10c.
Phylogenomic databases
eggNOG	COG2355.
HOGENOM	HOG000072016.
KO	K01273.
OMA	HIMHIAN.
OrthoDB	EOG4T7CBW.
Family and domain databases
InterPro	IPR008257. Peptidase_M19. [Graphical view]
PANTHER	PTHR10443. PTHR10443. 1 hit.
Pfam	PF01244. Peptidase_M19. 1 hit. [Graphical view]
PROSITE	PS00869. RENAL_DIPEPTIDASE_1. False negative. PS51365. RENAL_DIPEPTIDASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20804108.

Entry information

Entry name

DPEH1_SCHPO

Accession

Primary (citable) accession number: O14124

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	January 1, 1998
Last modified:	April 3, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program