LEM2_SCHPO
ID LEM2_SCHPO Reviewed; 688 AA.
AC Q10109;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Lap-Emerin-Man domain protein 2;
DE Short=LEM domain protein 2;
GN Name=lem2; Synonyms=heh1; ORFNames=SPAC18G6.10;
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 SUBCELLULAR LOCATION.
RX PubMed=18692466; DOI=10.1016/j.cell.2008.06.022;
RA King M.C., Drivas T.G., Blobel G.;
RT "A network of nuclear envelope membrane proteins linking centromeres to
RT microtubules.";
RL Cell 134:427-438(2008).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-683 AND SER-684, 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.
RX PubMed=20404563; DOI=10.4161/cc.9.9.11526;
RA Rumpf C., Cipak L., Novatchkova M., Li Z., Polakova S., Dudas A.,
RA Kovacikova I., Miadokova E., Ammerer G., Gregan J.;
RT "High-throughput knockout screen in Schizosaccharomyces pombe identifies a
RT novel gene required for efficient homolog disjunction during meiosis I.";
RL Cell Cycle 9:1802-1808(2010).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28242692; DOI=10.1073/pnas.1613916114;
RA Gu M., LaJoie D., Chen O.S., von Appen A., Ladinsky M.S., Redd M.J.,
RA Nikolova L., Bjorkman P.J., Sundquist W.I., Ullman K.S., Frost A.;
RT "LEM2 recruits CHMP7 for ESCRT-mediated nuclear envelope closure in fission
RT yeast and human cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E2166-E2175(2017).
CC -!- FUNCTION: Nucleus inner membrane protein involved in meiosis
CC (PubMed:20404563). Plays a role in regulating nuclear envelope (NE)
CC morphology and nuclear integrity, particularly during spindle pole body
CC (SPB) extrusion or insertion through the NE, and perhaps during
CC karyokinesis (PubMed:28242692). {ECO:0000269|PubMed:20404563,
CC ECO:0000269|PubMed:28242692}.
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:18692466}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:16823372,
CC ECO:0000269|PubMed:18692466}.
CC -!- DISRUPTION PHENOTYPE: Modest growth deficit (PubMed:28242692).
CC Suppresses slow growth rates of spores and severe nuclear envelope (NE)
CC morphology defects of vps4 mutants (PubMed:18692466).
CC {ECO:0000269|PubMed:18692466, ECO:0000269|PubMed:28242692}.
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DR EMBL; CU329670; CAA92388.1; -; Genomic_DNA.
DR PIR; T37923; T37923.
DR RefSeq; NP_593673.1; NM_001019105.2.
DR PDB; 5YCA; X-ray; 1.57 A; C=261-279.
DR PDBsum; 5YCA; -.
DR AlphaFoldDB; Q10109; -.
DR SMR; Q10109; -.
DR BioGRID; 279001; 140.
DR STRING; 4896.SPAC18G6.10.1; -.
DR iPTMnet; Q10109; -.
DR MaxQB; Q10109; -.
DR PaxDb; Q10109; -.
DR PRIDE; Q10109; -.
DR EnsemblFungi; SPAC18G6.10.1; SPAC18G6.10.1:pep; SPAC18G6.10.
DR GeneID; 2542544; -.
DR KEGG; spo:SPAC18G6.10; -.
DR PomBase; SPAC18G6.10; lem2.
DR VEuPathDB; FungiDB:SPAC18G6.10; -.
DR HOGENOM; CLU_408346_0_0_1; -.
DR InParanoid; Q10109; -.
DR OMA; HAFCYPN; -.
DR PRO; PR:Q10109; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0061638; C:CENP-A containing chromatin; IDA:PomBase.
DR GO; GO:0034506; C:chromosome, centromeric core domain; IDA:CACAO.
DR GO; GO:0099115; C:chromosome, subtelomeric region; IDA:PomBase.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; IDA:PomBase.
DR GO; GO:0140599; C:mitotic nuclear bridge midzone membrane domain; IDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0005635; C:nuclear envelope; IDA:PomBase.
DR GO; GO:0031965; C:nuclear membrane; EXP:PomBase.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:PomBase.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:PomBase.
DR GO; GO:0033553; C:rDNA heterochromatin; IDA:PomBase.
DR GO; GO:0140449; F:centromere-nuclear envelope anchor activity; IDA:PomBase.
DR GO; GO:0019237; F:centromeric DNA binding; EXP:PomBase.
DR GO; GO:0003682; F:chromatin binding; IDA:PomBase.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:PomBase.
DR GO; GO:0062239; F:heterochromatin-nuclear membrane anchor activity; IDA:PomBase.
DR GO; GO:0140698; P:attachment of telomeric heterochromatin to nuclear envelope; IMP:PomBase.
DR GO; GO:0072766; P:centromere clustering at the mitotic interphase nuclear envelope; IMP:PomBase.
DR GO; GO:0070828; P:heterochromatin organization; EXP:PomBase.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007084; P:mitotic nuclear membrane reassembly; IMP:PomBase.
DR GO; GO:0071765; P:nuclear inner membrane organization; IGI:PomBase.
DR GO; GO:0071763; P:nuclear membrane organization; IMP:PomBase.
DR GO; GO:0140462; P:pericentric heterochromatin organization; IMP:PomBase.
DR GO; GO:0097355; P:protein localization to heterochromatin; IMP:CACAO.
DR GO; GO:0140464; P:silent mating-type cassette heterochromatin organization; IMP:PomBase.
DR Gene3D; 1.10.10.1180; -; 1.
DR InterPro; IPR025856; HeH/LEM_domain.
DR InterPro; IPR044780; Heh2/Src1.
DR InterPro; IPR041885; MAN1_winged_helix_dom.
DR InterPro; IPR018996; MSC.
DR PANTHER; PTHR47808; PTHR47808; 1.
DR Pfam; PF12949; HeH; 1.
DR Pfam; PF09402; MSC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Meiosis; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..688
FT /note="Lap-Emerin-Man domain protein 2"
FT /id="PRO_0000116460"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 547..567
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 62..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 683
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT HELIX 261..273
FT /evidence="ECO:0007829|PDB:5YCA"
SQ SEQUENCE 688 AA; 78179 MW; 3CB29ED7B7A5DEA2 CRC64;
MDNWEDPNFE LRNLRVIDLK KILHESGVSF PVNARKIEYI RMVDRIRKNK LSSGPQHLLS
HLQKEENSNT SKASSSEDEI APKYLYPSSP SKSTKKPHNE TEPLLSPQFI DKPSNIETPV
KIESPHVSQN NTFQSYSELS PNVETSLTMK TPPAHASTPK FRSHKSHRVA VPMSFMDSSA
LHTSPAFSER LKLLSSSNNF SPQLRSPKIS HRLQTSATSS PLQHKRPFTN VPERVSRDIE
FAPLDSARPS ESSSPYSEVD SAEEDDELFQ NYVLQQTRKE SKLWSFIKKV FHDIKYANYR
LLHNLRAFPG ISAISSSYLV HIFMILLGVV AAIFLALLRE KMFTAGFCDS GASGSSASIL
GISFPSLCRT CPPNAICPSP NYVECKPGYV LYEPWYSSLG FWPSKYCVSD TSREESVNIF
REECLSVLRS WNAILHCSNN SSDLLERNMS YNAHPYVADN LNISSDHISF PSKPFALGLL
HDTLLERKSP TLGLEMFEDL FKASLAVLSE TNEVVMDSKL ICYDSWAGIP LRCRLKQQLI
KFVWRNKVFL FGILALSGVI FKLINFFRTR SIVAKYLPSA SRFCVESLKR QKANYQMSRS
QEPVIPLIEM HDILFHGNGP LEQIHMTKAT ARTLWEAIVE RVEQVGSVRT RESEVDGEWT
RVWEWVGTNT LDFQTDRSFI NTTSPLRE
