VID27_SCHPO
ID VID27_SCHPO Reviewed; 801 AA.
AC Q1MTR3; O74334; Q9US95;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Vacuolar import and degradation protein 27;
GN Name=vid27; ORFNames=SPBC1685.14c;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 159-339.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; SER-415 AND THR-478, AND
RP IDENTIFICATION BY 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: Has a role in the negative regulation of gluconeogenesis.
CC Required for vacuolar catabolite degradation of fructose-1,6-
CC bisphosphatase (FBPase) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the VID27 family. {ECO:0000305}.
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DR EMBL; CU329671; CAA20062.2; -; Genomic_DNA.
DR EMBL; AB027933; BAA87237.1; -; Genomic_DNA.
DR PIR; T39530; T39530.
DR RefSeq; NP_595218.1; NM_001021125.2.
DR AlphaFoldDB; Q1MTR3; -.
DR BioGRID; 276509; 6.
DR STRING; 4896.SPBC1685.14c.1; -.
DR iPTMnet; Q1MTR3; -.
DR MaxQB; Q1MTR3; -.
DR PaxDb; Q1MTR3; -.
DR PRIDE; Q1MTR3; -.
DR EnsemblFungi; SPBC1685.14c.1; SPBC1685.14c.1:pep; SPBC1685.14c.
DR GeneID; 2539965; -.
DR KEGG; spo:SPBC1685.14c; -.
DR PomBase; SPBC1685.14c; vid27.
DR VEuPathDB; FungiDB:SPBC1685.14c; -.
DR eggNOG; KOG2395; Eukaryota.
DR HOGENOM; CLU_007002_0_0_1; -.
DR InParanoid; Q1MTR3; -.
DR OMA; PFIITWS; -.
DR PRO; PR:Q1MTR3; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005635; C:nuclear envelope; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR011044; Quino_amine_DH_bsu.
DR InterPro; IPR040458; Vid27.
DR InterPro; IPR013863; VID27_C.
DR InterPro; IPR040979; Vid27_N.
DR InterPro; IPR040768; Vid27_PH.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR31913; PTHR31913; 1.
DR Pfam; PF08553; VID27; 1.
DR Pfam; PF17748; VID27_N; 1.
DR Pfam; PF17747; VID27_PH; 1.
DR SUPFAM; SSF50969; SSF50969; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..801
FT /note="Vacuolar import and degradation protein 27"
FT /id="PRO_0000339146"
FT REGION 372..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..420
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 478
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 801 AA; 92427 MW; 90FA9BDA22DCB4ED CRC64;
MFMLKSLGKY IWGNTNSTEI VQIPYGQLYS VHENYRECMF KDASASIRRT TAEFQYQLVI
QRAYEEGEEE LEDDGDEAED EQSFLLDEKL HLRFDVNKDS ITIMWDNPDF QDGTLYEFTC
ENCLQEGVAY TFEMVALQCM YERKYRQSHE KATLADLEQF SNPITRPSKE VDSLENIVTK
LDLESEDLMR LKKQEQLDDE IAKKYLLGQQ EAEEPLVQQQ TSIVNPEKEE VTKTENIKSL
EGELMGTISA ELHLFDAVEE VFILQDPNVE ASVFDLGDWN YWFTISTEEK TWLSQSVDAD
MNPVFSFEHL SFIWNYFDAN SNAFSWLLRF DSQVRMEQFQ ELLMRALWES LNQQRWLKID
DEQRDYVMET FHEDEELEDS EDEEFARQQL LSRKEEEEEE DEEASDFEDS FADFSDGEAD
DLDESRWRKE AAKEHNSLLA VGYKNDRSYV VRNNKIGVFK HVDEKGLKFQ TALNNLSTPK
GKSLRPSKLM LHNQDSSILF QTENAPHSLY HMDIEYGKIV DEWKVHDDVP LVTFTPDNKF
AQMTAEQTLI GLSNNSIFRI DPRVEGNKLV AEQFKQYATK NDFSSAATTE NGYIAVASNK
GDIRLFDRIG VNAKTALPAL GEAIIGVDVT ASGDFVLATC KTYILLIDTR IKEGRYAGRL
GFERNFAKDK KPKPKRLQLS PQHIAMMQRE LKGGASFTPA KFNTGIDAKE TTIVSSIGPF
LISWNLDRVK RGFTDSYKIR RYDANVQAED FRFGTDRSLI VALPDDVAMV DKSSLRRPTR
ESICTPVKKL RSKHDIVNAP Y