MLP2_YEAST
ID MLP2_YEAST Reviewed; 1679 AA.
AC P40457; D6VVD8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Protein MLP2;
DE AltName: Full=Myosin-like protein 2;
GN Name=MLP2; OrderedLocusNames=YIL149C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION, AND FORMATION OF CHROMATIN EXCLUDING FILAMENTOUS STRUCTURES WITH
RP MLP1.
RX PubMed=10085285; DOI=10.1083/jcb.144.5.839;
RA Strambio-de-Castillia C., Blobel G., Rout M.P.;
RT "Proteins connecting the nuclear pore complex with the nuclear interior.";
RL J. Cell Biol. 144:839-855(1999).
RN [4]
RP FUNCTION, AND INTERACTION WITH NIC96.
RX PubMed=10617624; DOI=10.1074/jbc.275.1.343;
RA Kosova B., Pante N., Rollenhagen C., Podtelejnikov A., Mann M., Aebi U.,
RA Hurt E.C.;
RT "Mlp2p, a component of nuclear pore attached intranuclear filaments,
RT associates with nic96p.";
RL J. Biol. Chem. 275:343-350(2000).
RN [5]
RP FUNCTION, PERINUCLEAR TELOMERE CLUSTERING, DOUBLE-STRAND BREAK REPAIR, AND
RP INTERACTION WITH YKU70 (HDF1).
RX PubMed=10638763; DOI=10.1038/47528;
RA Galy V., Olivo-Marin J.-C., Scherthan H., Doye V., Rascalou N.,
RA Nehrbass U.;
RT "Nuclear pore complexes in the organization of silent telomeric
RT chromatin.";
RL Nature 403:108-112(2000).
RN [6]
RP FUNCTION, PERINUCLEAR-DEPENDENT SILENCING, AND INTERACTION WITH NUP60.
RX PubMed=11862215; DOI=10.1038/ncb756;
RA Feuerbach F., Galy V., Trelles-Sticken E., Fromont-Racine M., Jacquier A.,
RA Gilson E., Olivo-Marin J.-C., Scherthan H., Nehrbass U.;
RT "Nuclear architecture and spatial positioning help establish
RT transcriptional states of telomeres in yeast.";
RL Nat. Cell Biol. 4:214-221(2002).
RN [7]
RP FUNCTION, AND TELOMERE LENGTH REGULATION.
RX PubMed=12490156; DOI=10.1016/s1047-8477(02)00533-6;
RA Hediger F., Dubrana K., Gasser S.M.;
RT "Myosin-like proteins 1 and 2 are not required for silencing or telomere
RT anchoring, but act in the Tel1 pathway of telomere length control.";
RL J. Struct. Biol. 140:79-91(2002).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14718167; DOI=10.1016/s0092-8674(03)01026-2;
RA Galy V., Gadal O., Fromont-Racine M., Romano A., Jacquier A., Nehrbass U.;
RT "Nuclear retention of unspliced mRNAs in yeast is mediated by perinuclear
RT Mlp1.";
RL Cell 116:63-73(2004).
RN [10]
RP IDENTIFICATION IN THE SPINDLE POLE BODY CORE COMPLEX, INTERACTION WITH
RP MLP1; SPC110; SPC42 AND SPC29, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=16027220; DOI=10.1083/jcb.200504140;
RA Niepel M., Strambio-de-Castillia C., Fasolo J., Chait B.T., Rout M.P.;
RT "The nuclear pore complex-associated protein, Mlp2p, binds to the yeast
RT spindle pole body and promotes its efficient assembly.";
RL J. Cell Biol. 170:225-235(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1512, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1670, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, IDENTIFICATION IN THE
RP NUCLEAR PORE COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=24152732; DOI=10.1091/mbc.e13-07-0412;
RA Niepel M., Molloy K.R., Williams R., Farr J.C., Meinema A.C.,
RA Vecchietti N., Cristea I.M., Chait B.T., Rout M.P.,
RA Strambio-De-Castillia C.;
RT "The nuclear basket proteins Mlp1p and Mlp2p are part of a dynamic
RT interactome including Esc1p and the proteasome.";
RL Mol. Biol. Cell 24:3920-3938(2013).
CC -!- FUNCTION: Together with the closely related MLP1, involved in the
CC structural and functional organization of perinuclear chromatin
CC (PubMed:10638763). MLP1/MLP2 associate with the nuclear pore complex
CC and form filamentous structures along the nuclear periphery
CC (PubMed:10085285, PubMed:24152732, PubMed:10617624). Has a role in the
CC localization of Esc1 to nucleolar regions (PubMed:24152732). Together
CC with MLP1, mediates tethering of the some telomeres to the nuclear
CC periphery, probably mediated by YKU70/YKU80 (HDF1/HDF2) heterodimer and
CC show perinuclear location dependent silencing (PubMed:11862215). MLP1
CC and MLP2 are involved in telomere length regulation but not silencing
CC or telomere anchoring (PubMed:12490156). Plays a role in the
CC incorporation of components into the spindle pole body
CC (PubMed:10617624, PubMed:14718167, PubMed:16027220). Involved in
CC double-strand break repair, probably also mediated by the YKU70/YKU80
CC (HDF1/HDF2) heterodimer (PubMed:10638763, PubMed:14718167,
CC PubMed:16027220). {ECO:0000269|PubMed:10085285,
CC ECO:0000269|PubMed:10617624, ECO:0000269|PubMed:10638763,
CC ECO:0000269|PubMed:11862215, ECO:0000269|PubMed:12490156,
CC ECO:0000269|PubMed:14718167, ECO:0000269|PubMed:16027220,
CC ECO:0000269|PubMed:24152732}.
CC -!- SUBUNIT: Component of the nuclear complex (NPC) (PubMed:24152732). NPC
CC constitutes the exclusive means of nucleocytoplasmic transport
CC (PubMed:24152732). NPCs allow the passive diffusion of ions and small
CC molecules and the active, nuclear transport receptor-mediated
CC bidirectional transport of macromolecules such as proteins, RNAs,
CC ribonucleoparticles (RNPs), and ribosomal subunits across the nuclear
CC envelope (PubMed:24152732). Due to its 8-fold rotational symmetry, all
CC subunits are present with 8 copies or multiples thereof
CC (PubMed:24152732). Interacts with NUP60 and NIC96, which tether it to
CC the nuclear pore complex. Component of the spindle pole body core in
CC which it interacts directly with SPC110, SPC42 and SPC29. Also
CC interacts with YKU70 (HDF1) and MLP1. {ECO:0000269|PubMed:10617624,
CC ECO:0000269|PubMed:10638763, ECO:0000269|PubMed:11862215,
CC ECO:0000269|PubMed:16027220, ECO:0000269|PubMed:24152732}.
CC -!- INTERACTION:
CC P40457; Q02455: MLP1; NbExp=2; IntAct=EBI-25261, EBI-11009;
CC P40457; P32380: SPC110; NbExp=3; IntAct=EBI-25261, EBI-12369;
CC P40457; P33419: SPC29; NbExp=2; IntAct=EBI-25261, EBI-12041;
CC P40457; P36094: SPC42; NbExp=3; IntAct=EBI-25261, EBI-17777;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, microtubule
CC organizing center, spindle pole body. Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:24152732}. Note=Nuclear periphery, excluded from
CC nuclear envelope adjacent to nucleolus.
CC -!- MISCELLANEOUS: Present with 2770 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z38059; CAA86129.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08404.1; -; Genomic_DNA.
DR PIR; S48385; S48385.
DR RefSeq; NP_012117.3; NM_001179497.3.
DR AlphaFoldDB; P40457; -.
DR SMR; P40457; -.
DR BioGRID; 34843; 342.
DR ComplexPortal; CPX-824; Nuclear pore complex.
DR DIP; DIP-2388N; -.
DR IntAct; P40457; 16.
DR MINT; P40457; -.
DR STRING; 4932.YIL149C; -.
DR iPTMnet; P40457; -.
DR MaxQB; P40457; -.
DR PaxDb; P40457; -.
DR PRIDE; P40457; -.
DR EnsemblFungi; YIL149C_mRNA; YIL149C; YIL149C.
DR GeneID; 854657; -.
DR KEGG; sce:YIL149C; -.
DR SGD; S000001411; MLP2.
DR VEuPathDB; FungiDB:YIL149C; -.
DR eggNOG; KOG4674; Eukaryota.
DR GeneTree; ENSGT00940000176562; -.
DR HOGENOM; CLU_002365_0_0_1; -.
DR InParanoid; P40457; -.
DR OMA; TLCEQQE; -.
DR BioCyc; YEAST:G3O-31398-MON; -.
DR PRO; PR:P40457; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40457; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005635; C:nuclear envelope; IDA:SGD.
DR GO; GO:0005643; C:nuclear pore; IBA:GO_Central.
DR GO; GO:0044615; C:nuclear pore nuclear basket; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; IDA:SGD.
DR GO; GO:0005816; C:spindle pole body; IPI:SGD.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IGI:SGD.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IBA:GO_Central.
DR GO; GO:0006406; P:mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:1901925; P:negative regulation of protein import into nucleus during spindle assembly checkpoint; IGI:SGD.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:SGD.
DR GO; GO:0000973; P:post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery; IMP:SGD.
DR GO; GO:0006606; P:protein import into nucleus; IGI:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IGI:SGD.
DR GO; GO:0051300; P:spindle pole body organization; IMP:SGD.
DR GO; GO:0034398; P:telomere tethering at nuclear periphery; IGI:SGD.
DR GO; GO:0000972; P:transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery; IMP:SGD.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; mRNA transport; Nuclear pore complex;
KW Nucleus; Phosphoprotein; Protein transport; Reference proteome;
KW Translocation; Transport.
FT CHAIN 1..1679
FT /note="Protein MLP2"
FT /id="PRO_0000096502"
FT REGION 1495..1521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1632..1679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 32..176
FT /evidence="ECO:0000255"
FT COILED 233..466
FT /evidence="ECO:0000255"
FT COILED 516..1064
FT /evidence="ECO:0000255"
FT COILED 1099..1491
FT /evidence="ECO:0000255"
FT MOTIF 417..433
FT /note="Bipartite nuclear localization signal 1"
FT MOTIF 639..655
FT /note="Bipartite nuclear localization signal 2"
FT MOTIF 1433..1449
FT /note="Bipartite nuclear localization signal 3"
FT COMPBIAS 1632..1657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1658..1672
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1512
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 1670
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 1679 AA; 195141 MW; 298950CC52202D8F CRC64;
MEDKISEFLN VPFESLQGVT YPVLRKLYKK IAKFERSEEE VTKLNVLVDE IKSQYYSRIS
KLKQLLDESS EQKNTAKEEL NGLKDQLNEE RSRYRREIDA LKKQLHVSHE AMREVNDEKR
VKEEYDIWQS RDQGNDSLND DLNKENKLLR RKLMEMENIL QRCKSNAISL QLKYDTSVQE
KELMLQSKKL IEEKLSSFSK KTLTEEVTKS SHVENLEEKL YQMQSNYESV FTYNKFLLNQ
NKQLSQSVEE KVLEMKNLKD TASVEKAEFS KEMTLQKNMN DLLRSQLTSL EKDCSLRAIE
KNDDNSCRNP EHTDVIDELI DTKLRLEKSK NECQRLQNIV MDCTKEEEAT MTTSAVSPTV
GKLFSDIKVL KRQLIKERNQ KFQLQNQLED FILELEHKTP ELISFKERTK SLEHELKRST
ELLETVSLTK RKQEREITSL RQKINGCEAN IHSLVKQRLD LARQVKLLLL NTSAIQETAS
PLSQDELISL RKILESSNIV NENDSQAIIT ERLVEFSNVN ELQEKNVELL NCIRILADKL
ENYEGKQDKT LQKVENQTIK EAKDAIIELE NINAKMETRI NILLRERDSY KLLASTEENK
ANTNSVTSME AAREKKIREL EAELSSTKVE NSAIIQNLRK ELLIYKKSQC KKKTTLEDFE
NFKGLAKEKE RMLEEAIDHL KAELEKQKSW VPSYIHVEKE RASTELSQSR IKIKSLEYEI
SKLKKETASF IPTKESLTRD FEQCCKEKKE LQMRLKESEI SHNENKMDFS SKEGQYKAKI
KELENNLERL RSDLQSKIQE IESIRSCKDS QLKWAQNTID DTEMKMKSLL TELSNKETTI
EKLSSEIENL DKELRKTKFQ YKFLDQNSDA STLEPTLRKE LEQIQVQLKD ANSQIQAYEE
IISSNENALI ELKNELAKTK ENYDAKIELE KKEKWAREED LSRLRGELGE IRALQPKLKE
GALHFVQQSE KLRNEVERIQ KMIEKIEKMS TIVQLCKKKE MSQYQSTMKE NKDLSELVIR
LEKDAADCQA ELTKTKSSLY SAQDLLDKHE RKWMEEKADY ERELISNIEQ TESLRVENSV
LIEKVDDTAA NNGDKDHLKL VSLFSNLRHE RNSLETKLTT CKRELAFVKQ KNDSLEKTIN
DLQRTQTLSE KEYQCSAVII DEFKDITKEV TQVNILKENN AILQKSLKNV TEKNREIYKQ
LNDRQEEISR LQRDLIQTKE QVSINSNKIL VYESEMEQCK QRYQDLSQQQ KDAQKKDIEK
LTNEISDLKG KLSSAENANA DLENKFNRLK KQAHEKLDAS KKQQAALTNE LNELKAIKDK
LEQDLHFENA KVIDLDTKLK AHELQSEDVS RDHEKDTYRT LMEEIESLKK ELQIFKTANS
SSDAFEKLKV NMEKEKDRII DERTKEFEKK LQETLNKSTS SEAEYSKDIE TLKKEWLKEY
EDETLRRIKE AEENLKKRIR LPSEERIQKI ISKRKEELEE EFRKKLKENA GSLTFLDNKG
SGEDAEEELW NSPSKGNSER PSAVAGFINQ KNLKPQEQLK NVKNDVSFND SQSMVTNKEN
NIVDSSAAGN KAIPTFSFGK PFFSSNTSSL QSFQNPFTAS QSNINTNAPL RTLNIQPEVA
VKAAINFSNV TDLTNNSTDG AKITEIGSTS KRPIESGTSS DPDTKKVKES PANDQASNE
