MPD2_SCHPO
ID MPD2_SCHPO Reviewed; 992 AA.
AC O36025;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=GYF domain-containing protein mpd2;
GN Name=mpd2; ORFNames=SPAC4F10.13c;
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 FUNCTION.
RX PubMed=15094387; DOI=10.1016/j.bbrc.2004.03.171;
RA Andoh T., Azad A.K., Shigematsu A., Ohshima Y., Tani T.;
RT "The fission yeast ptr1+ gene involved in nuclear mRNA export encodes a
RT putative ubiquitin ligase.";
RL Biochem. Biophys. Res. Commun. 317:1138-1143(2004).
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-175; THR-318; SER-320;
RP SER-509; SER-604; SER-637; SER-775; SER-829; SER-838 AND SER-840, 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 mRNA export from the nucleus.
CC {ECO:0000269|PubMed:15094387}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the SMY2/mpd2 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB11716.1; -; Genomic_DNA.
DR PIR; T38817; T38817.
DR RefSeq; NP_594756.1; NM_001020183.2.
DR AlphaFoldDB; O36025; -.
DR BioGRID; 279865; 36.
DR IntAct; O36025; 2.
DR STRING; 4896.SPAC4F10.13c.1; -.
DR iPTMnet; O36025; -.
DR MaxQB; O36025; -.
DR PaxDb; O36025; -.
DR PRIDE; O36025; -.
DR EnsemblFungi; SPAC4F10.13c.1; SPAC4F10.13c.1:pep; SPAC4F10.13c.
DR GeneID; 2543445; -.
DR KEGG; spo:SPAC4F10.13c; -.
DR PomBase; SPAC4F10.13c; mpd2.
DR VEuPathDB; FungiDB:SPAC4F10.13c; -.
DR eggNOG; KOG1862; Eukaryota.
DR HOGENOM; CLU_292587_0_0_1; -.
DR InParanoid; O36025; -.
DR OMA; RQEFLRW; -.
DR PhylomeDB; O36025; -.
DR PRO; PR:O36025; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISO:PomBase.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR CDD; cd00072; GYF; 1.
DR Gene3D; 3.30.1490.40; -; 1.
DR InterPro; IPR003169; GYF.
DR InterPro; IPR035445; GYF-like_dom_sf.
DR Pfam; PF02213; GYF; 1.
DR SMART; SM00444; GYF; 1.
DR SUPFAM; SSF55277; SSF55277; 1.
DR PROSITE; PS50829; GYF; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; mRNA transport; Phosphoprotein; Reference proteome; Transport.
FT CHAIN 1..992
FT /note="GYF domain-containing protein mpd2"
FT /id="PRO_0000339406"
FT DOMAIN 386..434
FT /note="GYF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00101"
FT REGION 24..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..859
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..983
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 318
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 637
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 775
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 829
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 838
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 840
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 992 AA; 106142 MW; 4751B990B0C39345 CRC64;
MNSEASVFSN MDWSQLAHSL HKKANNSSSS TTGAFPQLTS FTKPTATNGV DSPTSSHIDP
SVSAKLDSQR KLSLKSGNMW DSLNAPSELT SKNPTVSSTT SSANPAIVSN GGSPFYKNPV
VANNPSSTFD MSTNLFNSKN ANTSFTNAFS NEGISPGFLR DCFPSSNSIT TGTASPKLGS
PFNHINRPVL DRSPSSFSQS RSAVSGNMNP GVGTLQQPQR AGSDTFPDLN TSSSNQPGGE
PNVASANTHS LEILSSSAYH PSGSSNGISA GLTQSVASPV GQVDNLADFS QSPLRRGPSR
FPTNSNVPVG NSMSIRDTDS PLNILVDKAK AKASIKENAS QPVAPSASQR EHSAVNSPAA
AMSPSTAMFS SEAFPQHLAS LIPPALLHWL YKDPQNNVQG PFTGVDMHQW YRAGYFPLGL
PIKRLEEEEY YSLAFFIRQV GNQLEPFLVP LSPVTVQNAS WNAQGTDLPL SNYLPESSEQ
NRGGNKHLEL YPSTAEVSNV RNDESKANSL SEISYNQQSE CRSSELNVNE DSANQKEESA
LGTSDNSDMY EKENTPIHHN ESLNQLSKDL GSISLSEETK QEKPSKLKET VESKRLSTGV
QKQSPAASKE IPVTSGSQTT APKPSPWKSL PPKHLPSLDE TISREMSIAS SEALPQVEKS
NSDQPPVAIP STSKTGSPWA KVSDVSTSMA QEIQRMEKQN ENLKSKVASN PVSQTSTNAK
ASTPALASGS IWGSPSVINA WANKPAALKS PLIKKNIQQA ELAQNKQQSS VTTASPRSNA
LNANTPKAAA PSSNVTMKNV TSILETSTFE GEDTWSVVGP GGKIVNQQSP SAQQTTRSPS
KVSATLNAGN SQASTSSKLQ QVVSMSGHSP DFLAWCKISL KGLNEGVNYE EFLDMLLSLP
AENNVETFEI ISDSIYANST IMDGRRFASE FTRRRIADLT GKDGQQSNNK SQSELGNSSG
AWSQVVRNKP KQGTEWNSAF KVVTSKKNKK RV
