VGL1_SCHPO
ID VGL1_SCHPO Reviewed; 1291 AA.
AC O59810;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 2.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Vigilin 1;
DE AltName: Full=KH domain-containing protein vgl1;
GN Name=vgl1; ORFNames=SPCC550.14;
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 REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
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-115; SER-934 AND THR-935, 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).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20547592; DOI=10.1093/nar/gkq555;
RA Wen W.L., Stevenson A.L., Wang C.Y., Chen H.J., Kearsey S.E., Norbury C.J.,
RA Watt S., Bahler J., Wang S.W.;
RT "Vgl1, a multi-KH domain protein, is a novel component of the fission yeast
RT stress granules required for cell survival under thermal stress.";
RL Nucleic Acids Res. 38:6555-6566(2010).
CC -!- FUNCTION: Required for cell survival under thermal stress.
CC {ECO:0000269|PubMed:20547592}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum. Cytoplasm. Note=Under
CC thermal stress, relocalizes from the ER to cytoplasmic foci that are
CC distinct from P-bodies but contain stress granule markers.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329672; CAA19118.2; -; Genomic_DNA.
DR PIR; T41389; T41389.
DR RefSeq; NP_588106.2; NM_001023097.2.
DR AlphaFoldDB; O59810; -.
DR SMR; O59810; -.
DR BioGRID; 275990; 7.
DR STRING; 4896.SPCC550.14.1; -.
DR iPTMnet; O59810; -.
DR MaxQB; O59810; -.
DR PaxDb; O59810; -.
DR PRIDE; O59810; -.
DR EnsemblFungi; SPCC550.14.1; SPCC550.14.1:pep; SPCC550.14.
DR GeneID; 2539425; -.
DR KEGG; spo:SPCC550.14; -.
DR PomBase; SPCC550.14; vgl1.
DR VEuPathDB; FungiDB:SPCC550.14; -.
DR eggNOG; KOG2208; Eukaryota.
DR HOGENOM; CLU_003293_1_1_1; -.
DR InParanoid; O59810; -.
DR OMA; ARSDIMN; -.
DR PRO; PR:O59810; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005844; C:polysome; IDA:PomBase.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0008298; P:intracellular mRNA localization; ISO:PomBase.
DR GO; GO:0000280; P:nuclear division; IBA:GO_Central.
DR GO; GO:0043488; P:regulation of mRNA stability; NAS:PomBase.
DR Gene3D; 3.30.1370.10; -; 10.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR Pfam; PF00013; KH_1; 8.
DR SMART; SM00322; KH; 13.
DR SUPFAM; SSF54791; SSF54791; 11.
DR PROSITE; PS50084; KH_TYPE_1; 11.
PE 1: Evidence at protein level;
KW Cytoplasm; Endoplasmic reticulum; Phosphoprotein; Reference proteome;
KW Repeat; RNA-binding; Stress response.
FT CHAIN 1..1291
FT /note="Vigilin 1"
FT /id="PRO_0000310368"
FT DOMAIN 166..229
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 236..328
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 339..405
FT /note="KH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 416..486
FT /note="KH 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 575..644
FT /note="KH 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 658..726
FT /note="KH 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 741..798
FT /note="KH 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 808..883
FT /note="KH 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 894..957
FT /note="KH 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 967..1040
FT /note="KH 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 1050..1114
FT /note="KH 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 1219..1280
FT /note="KH 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 845..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 934
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 935
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1291 AA; 142613 MW; 533B859E10BA357E CRC64;
MEHLSNLEQP TTMDSYDFQK LTNDENLQGT ESQVPSGSKS ASTNGLLSAA SSAAGSSFGL
TPSAILQQKH ENAQQGKKQN NSKSFSKKPA IDVHSEDAFP TLLSKTGPSK PRIVSWVRKT
ASNTSVAGSD SVSRDKIPFS ASSRASSTKS TLSSVKETDF VTETLILSPD NQAPRMSFVG
KPNSVAEIVR TVMHQTSTRI NVSTASKTKN TTFLIQGKTS AVKAARRQIL KLIGRRETKT
MPCPVFVVGA IIGTNGQNLK SIMDRTSTRI QIPKRNNTAN ESSDDAKKPE KEENSAASTL
DDLEPQYEMT TITIEGDFEG VELAQKDIEA IINERTSNTT VRISHISTEL YSLLRGPDGK
NIKELEEGRD LKVQIPFAYL DPSAPVNPIV LSGEKSAVRE CALYLQGQAE ELLRTTIPTM
LPIPRRQHRF INGEKGVGIQ DILRKSGCSV ILPPINGDSD VVSVRGPALN ISEGIRLTLE
RANSTIVDAV NITTAYASSK NPFDIASIVA RLFLRSRKLI PLEEECAVQY HLPKREELQS
NSNKTVIIEI SGKSQEAVRE GRAKLLALVN QFPESKFYKV TIDPLLQRYV IGSKGKNLQK
LRNEHQVELL VGEYGEEDPD VIVCYIGADD GKSPDQIQKE LADLAESVKS SAEASAKIVS
EIIQVPSVYH KHIVGPKGTT LNAIIGKSEE NVIVQLGKVS YRPDSTDDDV YIRGFSKDVE
RVVSEIKQVV RDAKNHEILH SHVEEFDFPA QYSKNVIGKN GSNVSSLRED LGVQINVEEG
HIRIQGIKKN VEETAARIKS QIEALIDDTI LRVNIPNDFH RQLIGSNGKY VRRLEEKFSV
RVRFPREDDS SNSTGNELMK PTSPDEVVIR GGKKSVAAAK QELLELYEYE KSIAYTSTID
IPSKAVSRVV GRNGSTVENI RTQFDVKIDI GDVSTEETTP VSVRGAKADV ENAIKEISAI
AEEVKNLVEK VIKIDREYHR YLIGPNGSKL QNTIKECGGS TDKTETARLI SFSNGNSEEE
RNSVVLRGDK EIVEALETRL LEIVEELKNQ VEEKIEVPQR CISSIIGRMG STRRDIERKT
STMLNIPNVL DPEETVTITI VGSPENCEKA KEMIQEKVAS QYTQMITVPD TVYESIMKGI
LMKKLRSDLK VFVDTPEIKP VQPTEVVLED HEDGVFPWKL VTHDYTGSSS SEWAVRGHKE
NVEKAIASLE KSIKQVMENC IAYLGIPTNL HRRIIGSGGS IINKIRKIAQ VKIDVPRTPG
DEIVVVQGSR AGVVKAKDLI FERLQENQNQ E
