VTC1_SCHPO
ID VTC1_SCHPO Reviewed; 122 AA.
AC Q9UR17;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Vacuolar transporter chaperone 1;
DE AltName: Full=Negative regulator of cdc42;
GN Name=nrf1; Synonyms=vtc1; ORFNames=SPBC21B10.04c;
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 [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10628977; DOI=10.1093/genetics/154.1.155;
RA Murray J.M., Johnson D.I.;
RT "Isolation and characterization of Nrf1p, a novel negative regulator of the
RT Cdc42p GTPase in Schizosaccharomyces pombe.";
RL Genetics 154:155-165(2000).
RN [2]
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 -!- FUNCTION: Component of the vacuolar transporter chaperone (VTC)
CC complex, which plays a role in vacuolar membrane fusion (By
CC similarity). Involved in the control of cell polarity. {ECO:0000250,
CC ECO:0000269|PubMed:10628977}.
CC -!- SUBUNIT: The VTC complex is an integral membrane heterooligomer
CC composed of at least vtc1, vtc2 and vtc4 (By similarity). Interacts
CC with GTP-bound Ras-like cdc42, which is subsequently inactivated.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:10628977};
CC Multi-pass membrane protein {ECO:0000269|PubMed:10628977}.
CC -!- SIMILARITY: Belongs to the VTC1 family. {ECO:0000305}.
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DR EMBL; AF087832; AAD53227.1; -; mRNA.
DR EMBL; CU329671; CAB57926.1; -; Genomic_DNA.
DR PIR; T39923; T39923.
DR RefSeq; NP_595683.1; NM_001021578.2.
DR AlphaFoldDB; Q9UR17; -.
DR BioGRID; 277291; 6.
DR STRING; 4896.SPBC21B10.04c.1; -.
DR iPTMnet; Q9UR17; -.
DR PaxDb; Q9UR17; -.
DR EnsemblFungi; SPBC21B10.04c.1; SPBC21B10.04c.1:pep; SPBC21B10.04c.
DR GeneID; 2540771; -.
DR KEGG; spo:SPBC21B10.04c; -.
DR PomBase; SPBC21B10.04c; nrf1.
DR VEuPathDB; FungiDB:SPBC21B10.04c; -.
DR eggNOG; KOG4580; Eukaryota.
DR HOGENOM; CLU_141247_1_0_1; -.
DR InParanoid; Q9UR17; -.
DR OMA; YALITYH; -.
DR PhylomeDB; Q9UR17; -.
DR PRO; PR:Q9UR17; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0033254; C:vacuolar transporter chaperone complex; ISO:PomBase.
DR GO; GO:0030695; F:GTPase regulator activity; IGI:PomBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006112; P:energy reserve metabolic process; IC:PomBase.
DR GO; GO:0016237; P:lysosomal microautophagy; IBA:GO_Central.
DR GO; GO:0006799; P:polyphosphate biosynthetic process; ISO:PomBase.
DR GO; GO:0006797; P:polyphosphate metabolic process; IBA:GO_Central.
DR GO; GO:2000769; P:regulation of establishment or maintenance of cell polarity regulating cell shape; IGI:PomBase.
DR GO; GO:0007034; P:vacuolar transport; IBA:GO_Central.
DR GO; GO:0042144; P:vacuole fusion, non-autophagic; ISO:PomBase.
DR InterPro; IPR003807; DUF202.
DR Pfam; PF02656; DUF202; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Chaperone; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Vacuole.
FT CHAIN 1..122
FT /note="Vacuolar transporter chaperone 1"
FT /id="PRO_0000057948"
FT TOPO_DOM 1..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..59
FT /note="Vacuolar"
FT /evidence="ECO:0000250"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 122 AA; 13388 MW; 63652ED9D9DEC122 CRC64;
MSTQPLLQTT PGKRIALPVR VEPKVFFANE RTFLSWLSFA VVLGGLSVGL LNFGDRIGKI
SAGLFTIVAI GTMGYALGIY HWRASAIRRR GSGPYDDRLG PTILCFVLLA AIITNFVLRM
LF
