ALM1_SCHPO
ID ALM1_SCHPO Reviewed; 1727 AA.
AC Q9UTK5; O13313; Q9UTT8;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Nucleoporin alm1 {ECO:0000303|PubMed:28974540};
DE AltName: Full=Abnormal long morphology protein 1;
DE AltName: Full=Sp8;
GN Name=alm1 {ECO:0000303|PubMed:10660053};
GN ORFNames=SPAC1486.04c {ECO:0000312|PomBase:SPAC1486.04c};
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 [MRNA] OF 495-1727, AND CHARACTERIZATION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=10660053; DOI=10.1007/pl00008660;
RA Jimenez M., Petit T., Gancedo C., Goday C.;
RT "The alm1+ gene from Schizosaccharomyces pombe encodes a coiled-coil
RT protein that associates with the medial region during mitosis.";
RL Mol. Gen. Genet. 262:921-930(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 644-834.
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1706, 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).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=28974540; DOI=10.1083/jcb.201612194;
RA Salas-Pino S., Gallardo P., Barrales R.R., Braun S., Daga R.R.;
RT "The fission yeast nucleoporin Alm1 is required for proteasomal degradation
RT of kinetochore components.";
RL J. Cell Biol. 216:3591-3608(2017).
CC -!- FUNCTION: Maintains the proteasome and its anchor cut8 at the nucleus
CC envelope and is required for kinetochore component proteostasis
CC (PubMed:28974540). Proper kinetochore stoichiometry ensures the correct
CC attachment of kinetochores to spindle microtubules during cytokinesis
CC (PubMed:28974540, PubMed:10660053). Required for the localization of
CC spindle assembly checkpoint (SAC) protein mad2 and bub1 to the nucleus
CC envelope during interphase, but not their localization during mitosis
CC (PubMed:28974540). {ECO:0000269|PubMed:10660053,
CC ECO:0000269|PubMed:28974540}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:28974540}. Nucleus envelope
CC {ECO:0000269|PubMed:28974540}.
CC -!- DISRUPTION PHENOTYPE: Decreases cut8 localization to the nuclear
CC envelope (PubMed:28974540). Increases kinetochore component protein
CC levels, including cnp3 (PubMed:28974540). Asynchronous kinetochore
CC segregation during metaphase, with lagging kinetochores present during
CC anaphase B (PubMed:28974540). Increases spindle assembly checkpoint
CC (SAC) activation and results in mitotic metaphase/anaphase transition
CC delay (PubMed:28974540). Abnormal chromosome segregation; lagging
CC mitotic chromosomes during anaphase B and unequal mitotic sister
CC chromatid segregation (PubMed:28974540). Sensitive to thiabendazole
CC (PubMed:28974540). Simultaneous disruption of spindle assembly
CC checkpoint (SAC) proteins bub1 or mad2 results in a growth defect
CC (PubMed:28974540). {ECO:0000269|PubMed:28974540}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB65416.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CU329670; CAB62414.1; -; Genomic_DNA.
DR EMBL; AF010473; AAB65416.1; ALT_INIT; mRNA.
DR EMBL; AB028012; BAA87316.1; -; Genomic_DNA.
DR PIR; T43527; T43527.
DR PIR; T50073; T50073.
DR RefSeq; NP_594092.1; NM_001019516.2.
DR AlphaFoldDB; Q9UTK5; -.
DR SMR; Q9UTK5; -.
DR BioGRID; 279328; 220.
DR STRING; 4896.SPAC1486.04c.1; -.
DR iPTMnet; Q9UTK5; -.
DR MaxQB; Q9UTK5; -.
DR PaxDb; Q9UTK5; -.
DR PRIDE; Q9UTK5; -.
DR EnsemblFungi; SPAC1486.04c.1; SPAC1486.04c.1:pep; SPAC1486.04c.
DR GeneID; 2542883; -.
DR KEGG; spo:SPAC1486.04c; -.
DR PomBase; SPAC1486.04c; alm1.
DR VEuPathDB; FungiDB:SPAC1486.04c; -.
DR eggNOG; KOG4674; Eukaryota.
DR HOGENOM; CLU_240701_0_0_1; -.
DR InParanoid; Q9UTK5; -.
DR OMA; TLCEQQE; -.
DR PhylomeDB; Q9UTK5; -.
DR PRO; PR:Q9UTK5; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005635; C:nuclear envelope; IDA:PomBase.
DR GO; GO:0005643; C:nuclear pore; EXP:PomBase.
DR GO; GO:0044615; C:nuclear pore nuclear basket; IMP:PomBase.
DR GO; GO:0140602; C:nucleolar ring; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0017056; F:structural constituent of nuclear pore; EXP:PomBase.
DR GO; GO:0006406; P:mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Coiled coil; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Translocation; Transport.
FT CHAIN 1..1727
FT /note="Nucleoporin alm1"
FT /id="PRO_0000064565"
FT REGION 1423..1459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1477..1500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1656..1727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 57..361
FT /evidence="ECO:0000255"
FT COILED 443..463
FT /evidence="ECO:0000255"
FT COILED 542..740
FT /evidence="ECO:0000255"
FT COILED 804..1106
FT /evidence="ECO:0000255"
FT COILED 1223..1427
FT /evidence="ECO:0000255"
FT COILED 1497..1555
FT /evidence="ECO:0000255"
FT COILED 1601..1664
FT /evidence="ECO:0000255"
FT COMPBIAS 1423..1452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1669..1686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1700..1718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1706
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1727 AA; 197860 MW; F820BF8D9C132644 CRC64;
MSSGGLEDDI QLVHEFLDVS FEDIKPLVSV NGFAVFISAI KTKVKDINAL KDQLVLQEVN
HEHKENVLTK KINFLEQQLQ SSNNQAEESR NLISVLRNEN ESLKTNLENQ NKRFDALTTE
NQSLRRANSE LQEQSKIASE QLSIAKDQIE ALQNENSHLG EQVQSAHQAL SDIEERKKQH
MFASSSSRVK EEILVQEKSA LVSDLASLQS DHSKVCEKLE VSSRQVQDLE KKLAGLAQQN
TELNEKIQLF EQKRSNYSSD GNISKILETD PTSIKELEEE VETQKRLTAL WESKSSELQS
EVAALQEKLT SQQSLYNNVT EELNNNKQQL LISENSLREL QEKYDSVVSE LQVVKENKNT
SVSAGVGLFS PLAQKLSAVQ NPEFSFTKVY SDNMKLQQKV SSLKLQLDRL TNKFSSFCEQ
VKQRIPVVKQ QRSEIVRNNI YMNFLSESLE TSNNNLTKVQ AELLSTKMRQ EACYLQLTAS
RTQCSDLSRE VICLMAELDH LNETKSRNVP ATVQVALDEY AQNPSTASET LVNKELANFS
SIKEAVSKTL ELREKVRALE CDVEIQKQTV QYQISNAVKE NSNTLSEQIK NLESELNSSK
IKNESLLNER NLLKEMLATS RSSILSHNSS AGNIDDKMKS IDESTRELEK NYEVYRNEMT
AIQESLSKRN QDLLSEMEAI RKELENSKYQ QQLSTDRLTN ANNDVEAFKK EAKELRSINQ
NLQDIISRQD QRASKFAEEL LHVNSLAERL KGELNASKGE KDLRKRTQER LISENDKLLA
ERERLMSLVS DLQTFLNQQQ LSDAARKVKF ESEKESLSLS LQKLKESNEK MSNDLHSLQK
SLEKSGIEYS SRIKTLMLEK QSLSEDNRKL LDNQQMMEIK LQELNGVIEL EKQRFSTLEA
KFTQQKNTSY SEREALLESS LSDLQSKHTS LESQYNYSLR NIEQLQAASK LAEEMVERVK
TEYDEYRLQT SESLEKNHLK ITSLEQRIVI LQDEIASSSL RCENITKDSE TRVALLLEEN
KHLNNELSSH RNAEKQHLEK ENDYKQQLLL VTEDLRKTRE DYEKELLRHA DARSTLQKLR
EDYTKALEQV EDLNKEIALK AGINESQPFP ISEKEDPLRQ EVYVLKKQNA MLLTQLQSSN
LNFAEITSPS PDLDSVMKLG LSDLQNHVKR ISKEMEIISC QRQLLFLENK KLKRTVESSN
RVIADLQRGI TEKDVSSTSE SVGERSNYLN MVALLNESNK SLRENLERNE EVITELREKI
ETLKTDLANF RLNKEQLESQ LQTEKAAVKK LENSNEEYKR HNQEILLSLN SSTSTSSDAS
RLKNELVSKE NLIEELNQEI GHLKSELETV KSKSEDLENE RAQNQSKIEQ LELKNTKLAA
AWRTKYEQVV NKSLEKHNQI RQQLSQKTSE LEAKVAECHQ LNEQLNKPSA TPTATTQSEP
STVSLEEFNS TKEELSSTQR KLSEIMDILN TTKEELEKVR QNSNKSEGTS KDTEIPNEEE
MERKKVMQQE VLRLRSRIAK ELQKNELLRK QNQVLQDQVK ALQETVVSSE EAESASVHAD
TKDLENLKKT EEMLSVTFQV IFNESISDFS TSTADFTTFV QKEWEKRREI LQKDVEEQVA
QSHQKQLDNI RKELEMRNKL KLSMLEKNLA RVRAELEQSK KKDSPAILSL EASKNTDSNK
SNSEVPAAQV KEKKLIAKTH SVDTNSPPKR SSSDAGMDVS NDVKKAK
