ELF1_SCHPO
ID ELF1_SCHPO Reviewed; 1057 AA.
AC O14134;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=mRNA export factor elf1;
GN Name=elf1; ORFNames=SPAC3C7.08c;
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 [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF GLY-731.
RX PubMed=12110682; DOI=10.1074/jbc.m205415200;
RA Kozak L., Gopal G., Yoon J.H., Sauna Z.E., Ambudkar S.V., Thakurta A.G.,
RA Dhar R.;
RT "Elf1p, a member of the ABC class of ATPases, functions as a mRNA export
RT factor in Schizosacchromyces pombe.";
RL J. Biol. Chem. 277:33580-33589(2002).
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).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-733; SER-1041 AND SER-1053,
RP AND 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 direct role in the mRNA export process. Appears to act
CC within the rae1 mediated mRNA export pathway.
CC {ECO:0000269|PubMed:12110682}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12110682}. Nucleus
CC {ECO:0000269|PubMed:12110682}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family.
CC EF3 subfamily. {ECO:0000305}.
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DR EMBL; CU329670; CAB16738.1; -; Genomic_DNA.
DR PIR; T38694; T38694.
DR RefSeq; NP_593609.1; NM_001019040.2.
DR AlphaFoldDB; O14134; -.
DR SMR; O14134; -.
DR BioGRID; 279515; 13.
DR STRING; 4896.SPAC3C7.08c.1; -.
DR iPTMnet; O14134; -.
DR MaxQB; O14134; -.
DR PaxDb; O14134; -.
DR PRIDE; O14134; -.
DR EnsemblFungi; SPAC3C7.08c.1; SPAC3C7.08c.1:pep; SPAC3C7.08c.
DR GeneID; 2543082; -.
DR KEGG; spo:SPAC3C7.08c; -.
DR PomBase; SPAC3C7.08c; elf1.
DR VEuPathDB; FungiDB:SPAC3C7.08c; -.
DR eggNOG; KOG0062; Eukaryota.
DR eggNOG; KOG1242; Eukaryota.
DR HOGENOM; CLU_002848_0_1_1; -.
DR InParanoid; O14134; -.
DR OMA; VQKFDDH; -.
DR PhylomeDB; O14134; -.
DR PRO; PR:O14134; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; NAS:PomBase.
DR GO; GO:0005524; F:ATP binding; IDA:PomBase.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:PomBase.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:PomBase.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF00385; Chromo; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00298; CHROMO; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
DR PROSITE; PS50013; CHROMO_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; mRNA transport; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transport.
FT CHAIN 1..1057
FT /note="mRNA export factor elf1"
FT /id="PRO_0000093460"
FT DOMAIN 440..659
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 692..1019
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 820..869
FT /note="Chromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT REGION 1020..1057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1040
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 477..484
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 726..733
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 733
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1041
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1053
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 731
FT /note="G->D: No mRNA transport."
FT /evidence="ECO:0000269|PubMed:12110682"
SQ SEQUENCE 1057 AA; 116701 MW; 60DF5AE9DFC9D9F3 CRC64;
MTSSVLIQGY EEDDVLKLLQ ELLDAETSQS CADVGKKIAQ LFSNDNPLVT LKTTGFLDGL
ERAARNKKSG FHREAAMIGF ATVIKNLGTP SEVVFLPYLP TILDSFSDRG EVVRQAAKMA
AQALLDCLPA GAVETRLIPS LISYLDDSSI KWPSKVAALQ LLGSLASSSP KAVADYMAAL
IPCIKERMHD TKPEISRAAI TCMLNLCSVV ENNDIIPHIP KLVDCMAHPE TLEACIKDLS
ATTFVATVES VALAVLVPIL KRALAQRSQS MLRLTVIITD NLCKLVPDPA EASDFLPELI
PDVERIAQTA AMPEVRALAS HALTTLNKAA AAQAAKAANN SEKQALDSAC KELREAVLKN
TSVPHELANS IIDYVCDALA ALYKSNNFDK DKWTSQLGVL YLSPLVGEEL ASQISSKIYD
DLHAFYKSLN SVDGISNLTI EEEELVNTDF SLAYGGRLLL SHTNLHLYRG HRYGVVGHNG
CGKSTLLRAI GDYKVENFPS PDEVKTCFVA HSLQGEDTSM AILDFVAQDK ALLTMNVTRQ
EAADALHSVG FTAEMQENPV ASLSGGWKMK LELARAMLQK ADILLLDEPT NHLDVANIAW
LEAYLTSQKN ITCLIVSHDS SFLDHVCTDI IHYEGVKNQA KKLGYYQGNL SAFVKVKPEA
KSYYTLTATN EKFVFPPPGI LTGVRSNTRL ILKMTNASYT YPNAKKKSLD NVTVGLSLSS
RVAILGPNGA GKSTLIKVLI GEVIPQEGKV FKHPNLRVGY VAQHAFHHLD QHLEKTPSQY
IQWRYAGGQD REVSEKESRK LTEEDRAQLQ RDITVNGERR RVEALIGRQK LKKSFQYEIK
WFGKPHKYNT WVSREILLEN GFQKFVQAFD DMESSREGLG FRELIPEDIR AHFEDVGLPG
DIADYSPISS LSGGQKVKVV IAACLWNNPQ LLVLDEPTNF LDRDALGGLA VAIRDWEGGV
VMISHNEEFV SALCPEHWHV EAGKVTGKGK TAVDDGKFED LSEKDLKKIE AKATKKKKLT
RNEIKAKERR ARERELAWLQ SPKGTEKPKS FFSDDEE
