VPS54_SCHPO
ID VPS54_SCHPO Reviewed; 949 AA.
AC O14093;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Vacuolar protein sorting-associated protein 54;
GN Name=vps54; ORFNames=SPAC2F3.10;
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).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Involved in retrograde transport from early and late
CC endosomes to late Golgi by linking the vesicle through the t-SNARE TGL1
CC to the Golgi, leading to the membrane fusion between late Golgi and
CC endosomal vesicles. Seems also to be involved in protein transport from
CC Golgi to the plasma membrane and is required for the integrity of the
CC actin cytoskeleton (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the Golgi-associated retrograde protein (GARP)
CC complex, also called VFT (VPS fifty-three) complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:16823372}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16823372}. Endosome membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the VPS54 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB16266.1; -; Genomic_DNA.
DR PIR; T38543; T38543.
DR RefSeq; NP_594389.1; NM_001019811.2.
DR AlphaFoldDB; O14093; -.
DR BioGRID; 278219; 1.
DR STRING; 4896.SPAC2F3.10.1; -.
DR iPTMnet; O14093; -.
DR MaxQB; O14093; -.
DR PaxDb; O14093; -.
DR PRIDE; O14093; -.
DR EnsemblFungi; SPAC2F3.10.1; SPAC2F3.10.1:pep; SPAC2F3.10.
DR GeneID; 2541725; -.
DR KEGG; spo:SPAC2F3.10; -.
DR PomBase; SPAC2F3.10; vps54.
DR VEuPathDB; FungiDB:SPAC2F3.10; -.
DR eggNOG; KOG2115; Eukaryota.
DR HOGENOM; CLU_003094_1_0_1; -.
DR InParanoid; O14093; -.
DR OMA; IRIVQLR; -.
DR PhylomeDB; O14093; -.
DR PRO; PR:O14093; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000938; C:GARP complex; ISO:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0006896; P:Golgi to vacuole transport; ISO:PomBase.
DR GO; GO:0006886; P:intracellular protein transport; IC:PomBase.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISO:PomBase.
DR InterPro; IPR039745; Vps54.
DR InterPro; IPR012501; Vps54_C.
DR PANTHER; PTHR12965; PTHR12965; 1.
DR Pfam; PF07928; Vps54; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Endosome; Golgi apparatus; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..949
FT /note="Vacuolar protein sorting-associated protein 54"
FT /id="PRO_0000339878"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 243..312
FT /evidence="ECO:0000255"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 949 AA; 107951 MW; 1373BC059D713114 CRC64;
MERISSAPSI SLGYPPTESS AHLAPSFSDS ATSTLSFKSL LEDPVNPIRP VYTPTRTEIT
PVTLSPIPIT PVREFQPYLH EISQEYARYS KQKRASLRRY LEKHGKLEGS MKESSINGSL
LRRSSVSTIL RPASESSYPN SNSETITYDI DDNVNPSSSL VDNFSISSVP SVFFQSDFNL
DDPQIFDVVS EHIDITQTSD APNSNRNLLL NNSMLQEKIS WYLDTVELHL LQEIENASDS
FPMIIDNLKQ LKKETRDNVE ETKHLLEKLT EVNVMCDRHM DAISSEELAC HQLTQLKKVV
QTLEDIYSEH KKVSEDVKDQ RFLEAINGIN SIVTQLKKKS TELNVDLLSL PSVKSLREEH
KVLYHTVSQS VVQQFSKFLT SDMHKFSTIL DSNELKDIYL SKNRLIPSVT KSLPSAMEFD
ADFLHEVDVC IDCLTLTDSL QAALTLYKTA VFEAFENLAQ QYFTDGVEMR SVRKSSDLRR
SLSAASLSSL SDSSRRSSSA ANPFQSMSIT EFAEMLTNIY FSSLECLRRI RSQIKVLIDI
LSKKDTKQYH LSVILNDLMA TSSDVVTQQV TTINNLRFRV LDTYPPNNVI YLFSLHIIFH
NELESLCGIT QSSFIPTIMR QLLDWFKNFQ RYSTQKLASS FERELWEAIP VEPSCQDLAN
RVFECSGNTP VEWTRLLSPE AEKEDENHRV HHVKVSEDCT ATVSFGKQSL HIVRSSVTLL
ETLDDYGKLL AHFSRLAPEF QTGMLDMFRT LNSRVYQLIL GAGTVRSSGL SKVLGKHIAL
ASQTIALFQL SLNSMCRYLS RVTGTRLTNE TNKLDQDFTV HHLQIHDKFV SLMRERVAIS
CSQIASLSWD IDSPHGYIID LSKSLIKLYK VLHRYSQRDC VEVIPDVIRM FEDRLQLELT
DIARNPSKWP GVRIDLSYFY DMMASKCGYA GDRTLLEKFE RTPEQQEAA
