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Protein

Vacuolar membrane protease

Gene

SPCC1919.12c

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

May be involved in vacuolar sorting and osmoregulation.By similarity

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi147 – 1471Zinc 1; catalyticBy similarity
Metal bindingi159 – 1591Zinc 1; catalyticBy similarity
Metal bindingi159 – 1591Zinc 2; catalyticBy similarity
Active sitei191 – 1911Proton acceptorBy similarity
Metal bindingi192 – 1921Zinc 2; catalyticBy similarity
Metal bindingi217 – 2171Zinc 1; catalyticBy similarity
Sitei291 – 2911Transition state stabilizerBy similarity
Metal bindingi292 – 2921Zinc 2; catalyticBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Vacuolar membrane proteaseBy similarity (EC:3.4.-.-Curated)
Alternative name(s):
FXNA-related family protease 1By similarity
Gene namesi
ORF Names:SPCC1919.12cImported
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCC1919.12c.
PomBaseiSPCC1919.12c.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1616CytoplasmicBy similarityAdd
BLAST
Transmembranei17 – 3721Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini38 – 347310VacuolarBy similarityAdd
BLAST
Transmembranei348 – 36821Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini369 – 38618CytoplasmicBy similarityAdd
BLAST
Transmembranei387 – 40721Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini408 – 41710VacuolarBy similarity
Transmembranei418 – 43821Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini439 – 45618CytoplasmicBy similarityAdd
BLAST
Transmembranei457 – 47721Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini478 – 4847VacuolarBy similarity
Transmembranei485 – 50521Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini506 – 56661CytoplasmicBy similarityAdd
BLAST
Transmembranei567 – 58721Helical; Name=7Sequence analysisAdd
BLAST
Topological domaini588 – 60821VacuolarBy similarityAdd
BLAST
Transmembranei609 – 62921Helical; Name=8Sequence analysisAdd
BLAST
Topological domaini630 – 6367CytoplasmicBy similarity
Transmembranei637 – 65721Helical; Name=9Sequence analysisAdd
BLAST
Topological domaini658 – 843186VacuolarBy similarityAdd
BLAST

GO - Cellular componenti

  • cytosol Source: PomBase
  • integral component of membrane Source: UniProtKB-KW
  • vacuolar membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 843843Vacuolar membrane proteasePRO_0000174139Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi96 – 961N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi109 – 1091N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi117 – 1171N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi209 – 2091N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi275 – 2751N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi322 – 3221N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi677 – 6771N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi703 – 7031N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi707 – 7071N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi754 – 7541N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi788 – 7881N-linked (GlcNAc...)PROSITE-ProRule annotation

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiO94479.

Interactioni

Protein-protein interaction databases

BioGridi275729. 4 interactions.
MINTiMINT-4684521.

Structurei

3D structure databases

ProteinModelPortaliO94479.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M28 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

InParanoidiO94479.
OrthoDBiEOG72JWQN.
PhylomeDBiO94479.

Family and domain databases

InterProiIPR007484. Peptidase_M28.
[Graphical view]
PfamiPF04389. Peptidase_M28. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O94479-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTNSRRHIFE RICAKAFQSS LTCSIFGFTV LLILYLLDWK RIAQVPGPNL
60 70 80 90 100
LKDLEFQRAW NDLEYISSLP HPYNSKQNEH VRSYILKSMR ELEATNQSYI
110 120 130 140 150
TVIDDTLTNI TFESTDNDTL TYFEGDNILV KFEGKSKDLF PILLSAHFDS
160 170 180 190 200
VSTGYGATDD GMGVATVMAI ARYYAKNQPN RDLIININNA EEDYLFGAKA
210 220 230 240 250
FASHKLSKNV TAFVNLEGAG SGGKAMLFRS SNGHVSSAYF KGNHYPLASI
260 270 280 290 300
LGNDFFKRGV IRSQTDYIVY EKMHNHTAGL DIAFYENRDI YHTRKDDINH
310 320 330 340 350
LMPSSLRHMM YTASNAVKNL LNDSKSDLTK FRKPMFFLAF GKYWQLNLPI
360 370 380 390 400
YQVLNIIFAV ICPIVLLLTL IRFPSLYEQL KKPRYTVCFV VSCIFVSIFD
410 420 430 440 450
TLTVLLLTWI NPYVINSHTG LILALFYLTN LIALAFSFRA AATHSKLSSE
460 470 480 490 500
DLSSIEIVFI WYAQILWYLV FIVSVILSIY FQLGSTYWVT LSYLCTFTCC
510 520 530 540 550
IMTIIRINYF VDNVVTTQTT HEEDALIGSS INTSSHQHYG STLNSTPHRR
560 570 580 590 600
NSIALSNRAH VKLIDNIWTV IYFIFNVPFP VFLCYDILVE TILPAGSQTL
610 620 630 640 650
TDSVFSSKLY KLVIFVVFLS LVNSGPFIFR ALSKKSLAVL TMLWITLFVQ
660 670 680 690 700
ALSVNPFTES APLKLSFVQM YDMDRMNNTV YVKNISPFTQ DVLSLNPHFL
710 720 730 740 750
FSNGSCNTSL CYYESTDPDF GGLKTPMSIH IEREKHQLDI SINSGSKWCY
760 770 780 790 800
VDFNTSVFFE AINGNSISGM YSSVRMGQRS FYAPYTLNLT ITEVVKAEVT
810 820 830 840
CLYDDIHEGI IPAYNTFVEH LPSWVAGVKA STGLLKVKSS IVI
Length:843
Mass (Da):95,647
Last modified:May 1, 1999 - v1
Checksum:i80E1A404253574E3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti521 – 5288HEEDALIG → IQRRRTDW in BAA87092 (PubMed:10759889).Curated
Sequence conflicti624 – 63916SGPFI…KSLAV → QWTFHISCLVKKVACC in BAA87121 (PubMed:10759889).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAA22643.1.
AB027788 Genomic DNA. Translation: BAA87092.1.
AB027817 Genomic DNA. Translation: BAA87121.1.
PIRiT41237.
RefSeqiNP_588494.1. NM_001023484.2.

Genome annotation databases

EnsemblFungiiSPCC1919.12c.1; SPCC1919.12c.1:pep; SPCC1919.12c.
GeneIDi2539157.
KEGGispo:SPCC1919.12c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAA22643.1.
AB027788 Genomic DNA. Translation: BAA87092.1.
AB027817 Genomic DNA. Translation: BAA87121.1.
PIRiT41237.
RefSeqiNP_588494.1. NM_001023484.2.

3D structure databases

ProteinModelPortaliO94479.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi275729. 4 interactions.
MINTiMINT-4684521.

Proteomic databases

MaxQBiO94479.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPCC1919.12c.1; SPCC1919.12c.1:pep; SPCC1919.12c.
GeneIDi2539157.
KEGGispo:SPCC1919.12c.

Organism-specific databases

EuPathDBiFungiDB:SPCC1919.12c.
PomBaseiSPCC1919.12c.

Phylogenomic databases

InParanoidiO94479.
OrthoDBiEOG72JWQN.
PhylomeDBiO94479.

Miscellaneous databases

NextBioi20800329.
PROiO94479.

Family and domain databases

InterProiIPR007484. Peptidase_M28.
[Graphical view]
PfamiPF04389. Peptidase_M28. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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. "Large-scale screening of intracellular protein localization in living fission yeast cells by the use of a GFP-fusion genomic DNA library."
    Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T., Hiraoka Y.
    Genes Cells 5:169-190(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 521-705, SUBCELLULAR LOCATION.
    Strain: ATCC 38364 / 968.

Entry informationi

Entry nameiPFF1_SCHPO
AccessioniPrimary (citable) accession number: O94479
Secondary accession number(s): Q9UU46
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: May 1, 1999
Last modified: December 9, 2015
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.