PO152_YEAST
ID PO152_YEAST Reviewed; 1337 AA.
AC P39685; D6VZV2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Nucleoporin POM152;
DE AltName: Full=Nuclear pore protein POM152;
DE AltName: Full=P150;
DE AltName: Full=Pore membrane protein POM152;
GN Name=POM152; OrderedLocusNames=YMR129W; ORFNames=YM9553.05;
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 [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION,
RP AND REPEATS.
RC STRAIN=ATCC 200060 / W303;
RX PubMed=8138573; DOI=10.1083/jcb.125.1.31;
RA Wozniak R.W., Blobel G., Rout M.P.;
RT "POM152 is an integral protein of the pore membrane domain of the yeast
RT nuclear envelope.";
RL J. Cell Biol. 125:31-42(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [3]
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 [4]
RP FUNCTION, AND INTERACTION WITH NUP188.
RX PubMed=8682855; DOI=10.1083/jcb.133.6.1153;
RA Nehrbass U., Rout M.P., Maguire S., Blobel G., Wozniak R.W.;
RT "The yeast nucleoporin Nup188p interacts genetically and physically with
RT the core structures of the nuclear pore complex.";
RL J. Cell Biol. 133:1153-1162(1996).
RN [5]
RP FUNCTION, AND TOPOLOGY.
RX PubMed=9988776; DOI=10.1074/jbc.274.8.5252;
RA Tcheperegine S.E., Marelli M., Wozniak R.W.;
RT "Topology and functional domains of the yeast pore membrane protein
RT Pom152p.";
RL J. Biol. Chem. 274:5252-5258(1999).
RN [6]
RP FUNCTION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10684247; DOI=10.1083/jcb.148.4.635;
RA Rout M.P., Aitchison J.D., Suprapto A., Hjertaas K., Zhao Y., Chait B.T.;
RT "The yeast nuclear pore complex: composition, architecture, and transport
RT mechanism.";
RL J. Cell Biol. 148:635-651(2000).
RN [7]
RP FUNCTION, AND DE NOVO NPC ASSEMBLY.
RX PubMed=11352933; DOI=10.1083/jcb.153.4.709;
RA Marelli M., Lusk C.P., Chan H., Aitchison J.D., Wozniak R.W.;
RT "A link between the synthesis of nucleoporins and the biogenesis of the
RT nuclear envelope.";
RL J. Cell Biol. 153:709-724(2001).
RN [8]
RP REVIEW.
RX PubMed=12791264; DOI=10.1016/s1534-5807(03)00162-x;
RA Suntharalingam M., Wente S.R.;
RT "Peering through the pore: nuclear pore complex structure, assembly, and
RT function.";
RL Dev. Cell 4:775-789(2003).
RN [9]
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 [10]
RP PHOSPHORYLATION BY CDC28.
RX PubMed=14574415; DOI=10.1038/nature02062;
RA Ubersax J.A., Woodbury E.L., Quang P.N., Paraz M., Blethrow J.D., Shah K.,
RA Shokat K.M., Morgan D.O.;
RT "Targets of the cyclin-dependent kinase Cdk1.";
RL Nature 425:859-864(2003).
RN [11]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [14]
RP IDENTIFICATION BY 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Functions as a component of the nuclear pore complex (NPC).
CC NPC components, collectively referred to as nucleoporins (NUPs), can
CC play the role of both NPC structural components and of docking or
CC interaction partners for transiently associated nuclear transport
CC factors. POM152 is important for the de novo assembly of NPCs.
CC {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:11352933,
CC ECO:0000269|PubMed:8682855, ECO:0000269|PubMed:9988776}.
CC -!- SUBUNIT: Component of the nuclear pore complex (NPC). NPC constitutes
CC the exclusive means of nucleocytoplasmic transport. NPCs allow the
CC passive diffusion of ions and small molecules and the active, nuclear
CC transport receptor-mediated bidirectional transport of macromolecules
CC such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal
CC subunits across the nuclear envelope. Due to its 8-fold rotational
CC symmetry, all subunits are present with 8 copies or multiples thereof.
CC Interacts with NUP188. {ECO:0000269|PubMed:10684247,
CC ECO:0000269|PubMed:8682855}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:10684247}. Nucleus membrane; Multi-pass membrane
CC protein. Note=Central core structure of the nuclear pore complex.
CC -!- PTM: The N-terminus is blocked.
CC -!- PTM: Phosphorylated by CDC28. {ECO:0000269|PubMed:14574415}.
CC -!- MISCELLANEOUS: Present with 3410 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z31592; CAA83469.1; -; Genomic_DNA.
DR EMBL; Z48622; CAA88554.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10026.1; -; Genomic_DNA.
DR PIR; A53824; A53824.
DR RefSeq; NP_013848.1; NM_001182630.1.
DR PDB; 5TVZ; NMR; -; A=718-820.
DR PDBsum; 5TVZ; -.
DR AlphaFoldDB; P39685; -.
DR SASBDB; P39685; -.
DR SMR; P39685; -.
DR BioGRID; 35306; 150.
DR ComplexPortal; CPX-824; Nuclear pore complex.
DR DIP; DIP-1520N; -.
DR IntAct; P39685; 5.
DR MINT; P39685; -.
DR STRING; 4932.YMR129W; -.
DR TCDB; 1.I.1.1.1; the nuclear pore complex (npc) family.
DR iPTMnet; P39685; -.
DR MaxQB; P39685; -.
DR PaxDb; P39685; -.
DR PRIDE; P39685; -.
DR DNASU; 855159; -.
DR EnsemblFungi; YMR129W_mRNA; YMR129W; YMR129W.
DR GeneID; 855159; -.
DR KEGG; sce:YMR129W; -.
DR SGD; S000004736; POM152.
DR VEuPathDB; FungiDB:YMR129W; -.
DR eggNOG; ENOG502QQ5B; Eukaryota.
DR HOGENOM; CLU_002415_0_0_1; -.
DR InParanoid; P39685; -.
DR OMA; FDVFYTF; -.
DR BioCyc; YEAST:G3O-32822-MON; -.
DR PRO; PR:P39685; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P39685; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005635; C:nuclear envelope; IC:ComplexPortal.
DR GO; GO:0005641; C:nuclear envelope lumen; IDA:SGD.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034399; C:nuclear periphery; HDA:SGD.
DR GO; GO:0005643; C:nuclear pore; IDA:SGD.
DR GO; GO:0070762; C:nuclear pore transmembrane ring; IDA:SGD.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IDA:SGD.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IGI:SGD.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006999; P:nuclear pore organization; IGI:SGD.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:SGD.
DR GO; GO:0006606; P:protein import into nucleus; IDA:SGD.
DR GO; GO:0030474; P:spindle pole body duplication; IGI:SGD.
DR InterPro; IPR037701; Pom152.
DR PANTHER; PTHR28206; PTHR28206; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glycoprotein; Membrane;
KW mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Translocation;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1337
FT /note="Nucleoporin POM152"
FT /id="PRO_0000204910"
FT TOPO_DOM 1..110
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258,
FT ECO:0000305|PubMed:9988776"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..148
FT /note="Perinuclear space"
FT /evidence="ECO:0000305|PubMed:16847258,
FT ECO:0000305|PubMed:9988776"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258,
FT ECO:0000305|PubMed:9988776"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..1337
FT /note="Perinuclear space"
FT /evidence="ECO:0000269|PubMed:16847258,
FT ECO:0000305|PubMed:9988776"
FT REPEAT 390..413
FT /note="1"
FT /evidence="ECO:0000269|PubMed:8138573"
FT REPEAT 626..650
FT /note="2"
FT /evidence="ECO:0000269|PubMed:8138573"
FT REPEAT 732..755
FT /note="3"
FT /evidence="ECO:0000269|PubMed:8138573"
FT REPEAT 836..859
FT /note="4"
FT /evidence="ECO:0000269|PubMed:8138573"
FT REPEAT 943..966
FT /note="5"
FT /evidence="ECO:0000269|PubMed:8138573"
FT REPEAT 1058..1077
FT /note="6"
FT /evidence="ECO:0000269|PubMed:8138573"
FT REPEAT 1157..1178
FT /note="7"
FT /evidence="ECO:0000269|PubMed:8138573"
FT REPEAT 1253..1276
FT /note="8"
FT /evidence="ECO:0000269|PubMed:8138573"
FT REGION 1..175
FT /note="Pore side"
FT /evidence="ECO:0000305"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..1337
FT /note="Cisternal side"
FT /evidence="ECO:0000305"
FT REGION 390..1276
FT /note="8 X 24 AA approximate repeats"
FT COMPBIAS 13..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:8138573"
FT STRAND 722..726
FT /evidence="ECO:0007829|PDB:5TVZ"
FT STRAND 729..733
FT /evidence="ECO:0007829|PDB:5TVZ"
FT STRAND 737..746
FT /evidence="ECO:0007829|PDB:5TVZ"
FT STRAND 748..763
FT /evidence="ECO:0007829|PDB:5TVZ"
FT STRAND 766..773
FT /evidence="ECO:0007829|PDB:5TVZ"
FT STRAND 776..787
FT /evidence="ECO:0007829|PDB:5TVZ"
FT STRAND 790..800
FT /evidence="ECO:0007829|PDB:5TVZ"
FT TURN 801..803
FT /evidence="ECO:0007829|PDB:5TVZ"
FT STRAND 804..807
FT /evidence="ECO:0007829|PDB:5TVZ"
FT STRAND 813..817
FT /evidence="ECO:0007829|PDB:5TVZ"
SQ SEQUENCE 1337 AA; 151653 MW; A024A42069193898 CRC64;
MEHRYNVFND TPRGNHWMGS SVSGSPRPSY SSRPNVNTTR RFQYSDDEPA EKIRPLRSRS
FKSTESNISD EKSRISERDS KDRYINGDKK VDIYSLPLIS TDVLEISKQR TFAVILFLII
QCYKIYDLVI LKSGLPLSGL LFKNYRFNFI SKYFIIDSFF LYVLPSFNIP RLTFKPWVVY
LQILAMLLLN IFISSDHEFV LISLIMTTWR KLYTKELSVT GSAINHHRIF DSSAHFKGAL
TIKILPENTA MFNPLHESYC LPMDTNLFKI NSIDVPIRIN STEEIEYIEL EYRDLYTNSV
ELRSLSKKDF KIIDNPKSFL KKDQSVLKSH SNDFEEGSTI RYLAVTLQDI GFYQIKKIVD
SKKLNLKIHQ SHLVVPYCPI ASITGTGSND RCIGDSDNVS FEIQGVPPMK LAYSKIVNGQ
TFSYVDSSLQ PEYFESPLQS SKSKQSFTQG ELNDLKWGRN QPVNINLDSS ITQDGKFAYK
IDKITDGLGN VVDFTSLPEE LKKRYDLSYN FNVHEVPRAA LEERFDPKSP TKRSIAIVFE
EIKNWISDIP YVISLSYTDA QDKSKKIMNV TTDSLTKVLQ ADLPGSYNLE YIESKFCPGE
IVGKSNVLVT MPVAPTMEVK SFPILDQCVG QVGLNFELSF TGAPPYYYNT KIYKLENGER
KLYDAKRYTS EGTRNRFSYS PPKEGNYEIV FDTVSNKLFT EPIKLEPVKE YTFKTSMRVK
PSASLKLHHD LKLCLGDHSS VPVALKGQGP FTLTYDIIET FSSKRKTFEI KEIKTNEYVI
KTPVFTTGGD YILSLVSIKD STGCVVGLSQ PDAKIQVRRD IPSAAFNFFE PIKEAKIKHG
SVTEIPLKLS GEGPFTVKFK HMDYDGNIVK EFENKFQNSY KPALKVSKEG LYQLVDIRDS
SCQGNVIYRN SLYKVSFLEK PKFAIQDNHH ITKVTENLFS KEEVCQGMEG TVDLALFGSP
PFILEYDLMA PNGHISTKKI QVATKYASLK LPNQIPGEYI TTIKAIFDGN YGESDIHFRE
HQSELIIKQT VHPIPDVAFA DGGKTLRACA ANVDQISFLE PINLKFLQGE SPFSITFSVY
HESTSRTDQY TIDNIDSENF SFEKLYEGMK LGNHAITIDS VVDANGCVNS LISGPRNQIL
VSITDAPKIH ILDPSTEYCV GDYVAYQLNG VAPFMIKYEF NGIPLKSKER SSQFVRLASE
PGIISITSLQ DSSSQCIVDF TNPKLKSEFD DLSLNIHPIP SVTVSQGNYV TEDIREGDQA
EVIFSFEGTP PFSLTYVRTE ETDGKHGKRR SQVVETHKVT DIYSHEYKVI TSLQGTYEAI
EITDAYCFAK NDLFFNN
