MDN1_SCHPO
ID MDN1_SCHPO Reviewed; 4717 AA.
AC O94248;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Midasin;
DE AltName: Full=Dynein-related AAA-ATPase mdn1;
DE AltName: Full=MIDAS-containing protein;
GN Name=mdn1; ORFNames=SPCC737.08;
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-593, 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: Nuclear chaperone required for maturation and nuclear export
CC of pre-60S ribosome subunits. Functions at successive maturation steps
CC to remove ribosomal factors at critical transition points, first
CC driving the exit of early pre-60S particles from the nucleolus and then
CC driving late pre-60S particles from the nucleus.
CC {ECO:0000250|UniProtKB:Q12019}.
CC -!- SUBUNIT: Associates with pre-60S ribosomes in the nucleoplasm.
CC {ECO:0000250|UniProtKB:Q12019}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:Q12019}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q12019}.
CC -!- SIMILARITY: Belongs to the midasin family. {ECO:0000305}.
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DR EMBL; CU329672; CAA20864.1; -; Genomic_DNA.
DR PIR; T41581; T41581.
DR RefSeq; NP_588370.1; NM_001023361.2.
DR PDB; 6OR5; EM; 4.00 A; A=1-4717.
DR PDB; 6OR6; EM; 5.30 A; A=1-4717.
DR PDB; 6ORB; EM; 7.70 A; A=1-4717.
DR PDBsum; 6OR5; -.
DR PDBsum; 6OR6; -.
DR PDBsum; 6ORB; -.
DR SMR; O94248; -.
DR BioGRID; 276054; 2.
DR STRING; 4896.SPCC737.08.1; -.
DR iPTMnet; O94248; -.
DR MaxQB; O94248; -.
DR PaxDb; O94248; -.
DR PRIDE; O94248; -.
DR EnsemblFungi; SPCC737.08.1; SPCC737.08.1:pep; SPCC737.08.
DR GeneID; 2539491; -.
DR KEGG; spo:SPCC737.08; -.
DR PomBase; SPCC737.08; mdn1.
DR VEuPathDB; FungiDB:SPCC737.08; -.
DR eggNOG; KOG1808; Eukaryota.
DR HOGENOM; CLU_000050_0_2_1; -.
DR InParanoid; O94248; -.
DR OMA; ELGPPNI; -.
DR PhylomeDB; O94248; -.
DR PRO; PR:O94248; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:PomBase.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IPI:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; EXP:PomBase.
DR GO; GO:0005509; F:calcium ion binding; ISM:PomBase.
DR GO; GO:2000200; P:regulation of ribosomal subunit export from nucleus; IBA:GO_Central.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IMP:PomBase.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 6.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR040848; AAA_lid_7.
DR InterPro; IPR011704; ATPase_dyneun-rel_AAA.
DR InterPro; IPR012099; Midasin.
DR InterPro; IPR041190; Midasin_AAA_lid_5.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF07728; AAA_5; 8.
DR Pfam; PF17865; AAA_lid_5; 1.
DR Pfam; PF17867; AAA_lid_7; 3.
DR PIRSF; PIRSF010340; Midasin; 1.
DR SMART; SM00382; AAA; 5.
DR SUPFAM; SSF52540; SSF52540; 6.
DR SUPFAM; SSF53300; SSF53300; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chaperone; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..4717
FT /note="Midasin"
FT /id="PRO_0000363386"
FT DOMAIN 4505..4707
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REGION 149..384
FT /note="AAA-ATPase protomer 1"
FT /evidence="ECO:0000255"
FT REGION 458..797
FT /note="AAA-ATPase protomer 2"
FT /evidence="ECO:0000255"
FT REGION 871..1131
FT /note="AAA-ATPase protomer 3"
FT /evidence="ECO:0000255"
FT REGION 1157..1448
FT /note="AAA-ATPase protomer 4"
FT /evidence="ECO:0000255"
FT REGION 1552..1811
FT /note="AAA-ATPase protomer 5"
FT /evidence="ECO:0000255"
FT REGION 1858..2106
FT /note="AAA-ATPase protomer 6"
FT /evidence="ECO:0000255"
FT REGION 2173..3925
FT /note="Linker"
FT /evidence="ECO:0000250|UniProtKB:Q12019"
FT REGION 3898..3924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3936..4283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4295..4365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3947..3961
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3973..3992
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4030..4046
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4047..4065
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4081..4102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4103..4192
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4209..4228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4310..4342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 159..166
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 474..481
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 901..908
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 1193..1200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 1566..1573
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 1876..1883
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 4717 AA; 537787 MW; B2B08A69419EF502 CRC64;
MDVLIEWVAI YPQIYDILEH INYVPSNTLQ RLRLHQPWSK IDYDVWFLYA SDEIRETCKV
KYYGETKTYG EVFVLENERI SQLHRLFVSW TVSERAEHLK NLLFDAGLSN LPLVELGGNV
FFNSHVPLPC SLVLTKSTQE NLNRITPYLV QKRPILLAGP EGIGKKFLIT QIAAKLGQQI
IRIHLSDSTD PKMLIGTYTS PKPGEFEWQP GVLTQAVITG KWILFTNIEH APSEVLSVLL
PLLEKRQLVI PSRGETIYAK GSFQMFATSS MKTKILGQRL WQILDLTYQP DECVEVVSTL
YPVLSIICPT LYSVYKDIFD LFSQRSFLAT SKIYRRLCLR DFYKFIKRVA FLYHKFMIPS
DHVVISQELQ DAVFKEAIDM FGAFIPSRDG FDLVVRNVAI ELNIPPEKAL QLRYSIPVFQ
NLEHNINIGR CSLKKLSTIR SCSTNSYAFT SSSLGLLEQL AAGVQTNEPL LLVGETGTGK
TTTIQLLAGL LGQKVTVINM SQQTESSDML GGYKPINAST LGLPLHERFI DIFEQTFSSK
KNAKFISMAS TSARRFRWKT CLKIWKEACK LSKTVLDGQQ PLPNPQKRQK RLSNQVELRN
QWAKFEKEVE DFEKVLTGGS NGFMFSFVEG ALVKAVRSGH WVLLDEINLA SLETLEPIGQ
LLSSYESGIL LSERGDITPI TPHKNFRLFG CMNPSTDVGK RELEPSFRSR FTEIYVHSPD
QNLDDLLSII QKYIGSLCIG NEHVIREVAE LYQVAKSLSL DGSLVDGAGQ RPHYTVRTLS
RTLSYVTEIA PIYGLRRSLY EGFCMSFLTL LDHTSESLLY NHVVRFTLGE LNRDQQNAIL
KQIPKVPDHS SYIAFCHYWL RRGSFPVEEQ EHYIITPFVQ KNLLNIARAC STRMFPILIQ
GPTSSGKTSM IEYVAKKTGH KFVRINNHEH TDLQEYIGTY VTDDNGSLSF REGVLVEALR
NGYWIVLDEL NLAPTDVLEA LNRLLDDNRE LFIPETQVLV KPHPEFMLFA TQNPPGVYAG
RKHLSRAFRN RFLEIHFDDI PENELETILH KRCKIAPSYA AKIVQVFREL SLRRQTTRIF
EQKNSFATLR DLFRWAFREA VGYQQLAENG YMLLAERARD QKDKLAVQEV IEKVMKVKID
TDGIYNLDSM EIFQDMSLKE GPLSKVVWTR PMIRLFCLVW RCLLAKEPVL LVGDTGCGKT
TVCQILAECL HKELHIINAH QDTENGDIIG AQRPVRNRSA VNYSLHSQLC EKFNVQESLD
SIDDLIEKFE KLSSSEKNDN LSNLIERQII KYRSLFEWHD GALVTAMKQG DFFLLDEISL
ADDSVLERLN SVLELSRTLT LVEHSNAAVS LTAKDGFAFF ATMNPGGDYG KKELSPALRN
RFTEIWVPPM VDTEDILKIV EGKLHNNKIE LARPLVEYAK WHANEYLYTD VISIRDVLSA
VEFINACEIL DLNLVLFNAV SMVFIDALGS FTTFSLSNNL ASLHAERQRC FAKLNELAGS
NIMASKSADI SIKFSDSSFF IGDFGIPLGD SVESDSTYSL HTDTTLMNAS KVLRALQVLK
PILLEGSPGV GKTSLITALA RETGHQLVRI NLSDQTDLMD LFGSDVPVEG GEGGQFAWRD
APFLAAMRNG HWVLLDELNL ASQSVLEGLN ACLDHRNEAY IPELDKVFKA HPNFRVFAAQ
NPQHQGGGRK GLPRSFINRF SVVYVEALKE KDMIEIAACN YHQVNEDWRL KIIKFMFRLQ
DNIEKDISFG SFGSPWEFNL RDTLRWLQLL NDAPKYTCVS PADYLEVMVL HRMRTVEDRV
RTCELFKEVF DIDYEPRTIG FSLSSQCFKV GHSLLVRDVE RQKTLLDSQN ILQSQLPVLE
SVITCINKKW PCILVGDTAT GKTCILRLLA AIAGAKIKEM AVNSDTDTMD LIGEYEQIDI
SRKASELFTD LSQQLLNIVI KYRNFDNIFR ETSLYTLTTT SFKTHSQAFT LLQKVVDQLD
QLKIHETLVH SLGDIHEKAR KLLAEFSASP AGRFEWFDGY LLKAVEEGHW FVLDNANLCS
PAVLDRLNSL LEHKGVLIVN EKTTEDGHPK TIKPHPNFRL FLTVNPVYGE LSRAMRNRGV
EIFLLKEALT EIDKKQMSLL EPAPISSAVD TLASNISYIK YVFETMGKIE IDGNYMYIAH
AIILALFSPR QLKLLRKVLL TNPQFSLSIK ADAELLLTLK NLVQKIYCAD YFNHMDLKAS
RFMDIYEYPV QLREVVGLIQ TINDFQSVIL TSHLELPETY ASGLLFVSAH EILDLTEEVN
RLAVSTSNST YLLKSASAVY HNVSSFKGST PSLWNLLNQF SKFLIEIASA NSNIVYKLSY
DVIRHFLKLV VLWKNIYVWT NVPDCDISRF YCYTKMLGEW MFTLTEKTKL LESFLPKDSL
EKFSELQNLS TGLHMQAIWD KWHAFVPRTY DQWSLWNTVD KLLTQYVNAN IPSISMETTA
CEVVGTSLSL LNKVLVENEV GDIYSYLKIL GKGVNELKSS KQVILPENLV NLFNCLASLD
LLHIFIKYTT SSFFLTDDFV RFIRVCFHSR ISGNLLTLLH GISFDSTKAV APVLTYFDFC
SLTTGNILGR IALAFTSIDE NANLESANIF EHARLALLQH FMDHSSLLAE DSSTKMNLIL
LQRYAVIISI FLDQGKCEKA NDLITKLSLP YEELAENFVS ILEACKAFLV ANSEFISYTY
TERFIHSLRF LKDSWLSSNQ QKMLKNQGMA YIYFASGMLL VYVPDKPFDP ALLPLLTVES
LRHYLESLYK ESQILEIAES LNSGKVNSVM RRLVSTEISN TPNIDSSFST VYRSLNESIV
PLYSELEFFM KSVVLNQYIF ELAMRLSKES NIAVVEEAKS FVTKWKAYIE RIREAYPQFV
DVYELILSFI SFMIYGIELL MFEAKRRLDE RSQILSTLIL TLVDPSSFAR SLSFDDVSNL
IEQIKVLDLN DSIRFEIYLF LASRLCSEKQ HSSDTHSLAN SFVLLANEFY IHNAKIKQKE
LEEIEEKNRL YRQREFNFDK NDYLKVFINY DDEVEPEVEP EVVIERKRFL QLQFAFWSLY
NEIYSEKMNV IPLEQLMNTG SYLAKKIKVK NPDMIASSGF DIVSVVLMMG VKSTNERQYW
TPPVYNFYSD PNPSKAIEVR DLIKIVESRA ISLIKNWPEN FVLRGLKDAI DAILNLSPFS
PIAEYLSKLE RVFHLLSEWE KLASREYSLA NEMDLIKKKI IDWRKFELSN WNNLLKLEEY
KLSERVYPRL YSILQFIILK PFFENSKFTK QNLCESASII VQFITDLTVG EFQLCLKCLL
SFSQHAASLR ICHGIDAMLL NIYHYFEQFL SKVSEAIHTQ KQSLENSIKE RILLMSWKDT
NVYALKESAK KSHAELFKVL HRYREVLRQP VSSYLSQKHD WDSLLDTENN SAMWVAKKVN
LSPSYIEKMD TEIMKLVPVR FSNTPTTLRL MWTLFANVEK PGSTFTNMVS NLITDARELM
KLTPETINDD NLSEIKHLKS RKHLLLTETF KTLKAFGLQY RVKAGIEENL SNLRNLLAVI
PTFPVTSLSI EKVDRSLMKS LDFIPKFQTL AGHQHNDLSV PEVQKGVGLF NSMLSLQLGE
RAQLVEFTNE LLALKNVYSE VGVNGSPLES FNNSSFNEVS SLGYDHDFEN RAQAVSMLCQ
IYAIVIQKHS SISPTASFQS IGHELSRFAD LLSNKLFPSS IPLYASADKV SSIRDQQKGI
NDLIEYCRKK RTELPELSYC FKHLVSLQSL KSISRTQVDL TNDEFLNLMN FVLNLFDSLL
SSIETATKNM RTFKELAETS SFIEMSSCFS KVLRAFNLKF QSMKLSSLKE KLRSSSVDKM
SCQLLMLFLP VCEQFINLAE SVLDYFINVH NSNLDSLSKI STLFFMVANN GFCSPDLPQE
GKSNSGELES GTGLGSGVGA EDITNTLNED DDLEELANEE DTANQSDLDE SEARELESDM
NGVTKDSVVS ENENSDSEEE NQDLDEEVND IPEDLSNSLN EKLWDEPNEE DLLETEQKSN
EQSAANNESD LVSKEDDNKA LEDKDRQEKE DEEEMSDDVG IDDEIQPDIQ ENNSQPPPEN
EDHLDLPEDL KLDEKEGDVS KDSDLEDMDM EAADENKEEA DAEKDEPMQD FEDPLEENNT
LDEDIQQDDF SDLAEDDEKM NEDGFEENVQ ENEESTEDGV KSDEELEQGE VPEDQAIDNH
PKMDAKSTFA SAEADEENTD KGIVGENEEL GEEDGAAESG VRGNGTADGE FSSAEQVQKG
EDTSTPKEAM SEADRQYQSL GDHLREWQQA NRIHEWEDLT ESQSQAFDDS EFMHVKEDEE
EDLQALGNAE KDQIKSIDRD ESANQNPDSM NSTNIAEDEA DEVGDKQLQD GQDISDIKQT
GEDTLPTEFG SINQSEKVFE LSEDEDIEDE LPDYNVKITN LPAAMPIDEA RDLWNKHEDS
TKQLSIELCE QLRLILEPTL ATKMQGDFRT GKRLNMKRII PYIASQFKKD KIWMRRVKPS
KRTYQVMISI DDSKSMSESG STVLALETLA LVTKALSLLE VGQIAVMKFG EQPELLHPFD
KQFSSESGVQ MFSHFTFEQS NTNVLALADA SMKCFNYANT ASHHRSNSDI RQLEIIISDG
ICEDHDSIRK LLRRAQEEKV MIVFVILDNV NTQKKSSILD IKKVYYDTKE DGTMDLKIQP
YIDEFAFDYY LVVRNIEELP QLLSSALRQW FQQMSNT
