ID   PO121_MOUSE             Reviewed;        1200 AA.
AC   Q8K3Z9; Q7TSH5;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   24-JAN-2024, entry version 154.
DE   RecName: Full=Nuclear envelope pore membrane protein POM 121;
DE   AltName: Full=Nucleoporin Nup121;
DE   AltName: Full=Pore membrane protein of 121 kDa;
GN   Name=Pom121; Synonyms=Nup121;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Tassabehji M., Cunliffe P.;
RT   "Identification of mouse genes mapping to the Williams syndrome critical
RT   region.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319; SER-322; SER-325;
RP   SER-408 AND SER-409, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244; SER-319; SER-322;
RP   SER-325; SER-370; SER-409; SER-412; SER-413; SER-416 AND SER-417, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Essential component of the nuclear pore complex (NPC). The
CC       repeat-containing domain may be involved in anchoring components of the
CC       pore complex to the pore membrane. When overexpressed in cells induces
CC       the formation of cytoplasmic annulate lamellae (AL) (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000250}.
CC       Nucleus membrane {ECO:0000250}; Single-pass membrane protein
CC       {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-
CC       pass membrane protein {ECO:0000250}. Note=Stably associated with the
CC       NPC throughout interphase and the endoplasmic reticulum during
CC       metaphase. {ECO:0000250}.
CC   -!- DOMAIN: Contains F-X-F-G repeats.
CC   -!- PTM: Proteolytically cleaved by caspase-3 during apoptosis.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the POM121 family. {ECO:0000305}.
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DR   EMBL; AF516680; AAM64199.1; -; mRNA.
DR   EMBL; BC053101; AAH53101.1; -; mRNA.
DR   CCDS; CCDS51662.1; -.
DR   RefSeq; NP_683734.2; NM_148932.2.
DR   AlphaFoldDB; Q8K3Z9; -.
DR   SMR; Q8K3Z9; -.
DR   BioGRID; 223706; 3.
DR   ComplexPortal; CPX-4474; Nuclear pore complex.
DR   STRING; 10090.ENSMUSP00000106801; -.
DR   GlyGen; Q8K3Z9; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8K3Z9; -.
DR   PhosphoSitePlus; Q8K3Z9; -.
DR   SwissPalm; Q8K3Z9; -.
DR   EPD; Q8K3Z9; -.
DR   jPOST; Q8K3Z9; -.
DR   MaxQB; Q8K3Z9; -.
DR   PaxDb; 10090-ENSMUSP00000106801; -.
DR   ProteomicsDB; 289468; -.
DR   Pumba; Q8K3Z9; -.
DR   Ensembl; ENSMUST00000111171.6; ENSMUSP00000106801.3; ENSMUSG00000053293.10.
DR   GeneID; 107939; -.
DR   KEGG; mmu:107939; -.
DR   UCSC; uc008zyi.1; mouse.
DR   AGR; MGI:2137624; -.
DR   CTD; 9883; -.
DR   MGI; MGI:2137624; Pom121.
DR   VEuPathDB; HostDB:ENSMUSG00000053293; -.
DR   eggNOG; ENOG502R5GW; Eukaryota.
DR   GeneTree; ENSGT00940000153253; -.
DR   HOGENOM; CLU_011366_0_0_1; -.
DR   InParanoid; Q8K3Z9; -.
DR   OMA; MPCPQFG; -.
DR   OrthoDB; 3094378at2759; -.
DR   PhylomeDB; Q8K3Z9; -.
DR   TreeFam; TF323517; -.
DR   Reactome; R-MMU-159227; Transport of the SLBP independent Mature mRNA.
DR   Reactome; R-MMU-159230; Transport of the SLBP Dependant Mature mRNA.
DR   Reactome; R-MMU-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR   Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR   Reactome; R-MMU-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR   Reactome; R-MMU-191859; snRNP Assembly.
DR   Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR   Reactome; R-MMU-3232142; SUMOylation of ubiquitinylation proteins.
DR   Reactome; R-MMU-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR   Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR   Reactome; R-MMU-4085377; SUMOylation of SUMOylation proteins.
DR   Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins.
DR   Reactome; R-MMU-4570464; SUMOylation of RNA binding proteins.
DR   Reactome; R-MMU-4615885; SUMOylation of DNA replication proteins.
DR   Reactome; R-MMU-5578749; Transcriptional regulation by small RNAs.
DR   Reactome; R-MMU-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR   BioGRID-ORCS; 107939; 5 hits in 78 CRISPR screens.
DR   ChiTaRS; Pom121; mouse.
DR   PRO; PR:Q8K3Z9; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q8K3Z9; Protein.
DR   Bgee; ENSMUSG00000053293; Expressed in respiratory primordium and 246 other cell types or tissues.
DR   ExpressionAtlas; Q8K3Z9; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR   GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR   GO; GO:0005643; C:nuclear pore; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
DR   GO; GO:0017056; F:structural constituent of nuclear pore; ISO:MGI.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0006999; P:nuclear pore organization; ISO:MGI.
DR   GO; GO:0006913; P:nucleocytoplasmic transport; NAS:ComplexPortal.
DR   GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR   GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central.
DR   InterPro; IPR026054; Nucleoporin.
DR   PANTHER; PTHR23193:SF5; NUCLEAR ENVELOPE PORE MEMBRANE PROTEIN POM 121; 1.
DR   PANTHER; PTHR23193; NUCLEAR PORE COMPLEX PROTEIN NUP; 1.
DR   Pfam; PF15229; POM121; 1.
DR   Genevisible; Q8K3Z9; MM.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Membrane; mRNA transport; Nuclear pore complex;
KW   Nucleus; Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW   Translocation; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1200
FT                   /note="Nuclear envelope pore membrane protein POM 121"
FT                   /id="PRO_0000204907"
FT   TRANSMEM        57..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..56
FT                   /note="Cisternal side"
FT                   /evidence="ECO:0000255"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          76..1200
FT                   /note="Pore side"
FT                   /evidence="ECO:0000255"
FT   REGION          91..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          177..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          294..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          345..509
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          530..627
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          640..692
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          706..744
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1075..1151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1173..1200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..322
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        364..422
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        456..482
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        563..589
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        712..742
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            531..532
FT                   /note="Cleavage; by caspase-3"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         83
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A8CG34"
FT   MOD_RES         244
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         319
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         322
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         325
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         345
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96HA1"
FT   MOD_RES         355
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52591"
FT   MOD_RES         367
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A8CG34"
FT   MOD_RES         370
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         408
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355"
FT   MOD_RES         409
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         412
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         413
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         416
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         417
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CONFLICT        500
FT                   /note="Missing (in Ref. 1; AAM64199)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1200 AA;  121022 MW;  C15B5D6C204D445E CRC64;
     MSPAAAAADG GERRRPPLGG REGRSRARGY GGPAGAAALG LALLGLALYL VPAAAALAWL
     AVGASAAWWG LSREPRGPRA LSSFVRDARR HPRPALTASP PPAKSPVNGS LCEPRSPLGG
     PDPAELLLMG SYLGKPGPPE PALRQDPRER PGRRPPARSP PPASAVQRVH HVYPALPTPL
     LRPSRRPPHR DCGPLSSRFV ITPRRRYPIQ QAQYSLLGAL PTVCWNGGHK KAVLSPRNSR
     MVCSPVTVRI APPDSKLFRS SMSEQILDTT LSSPSSNAPD PCAKETVLNA LKEKKKRTVA
     EEDQLHLDGQ ENKRRRHDSG GSGHSAFEPL VANGVPAAFV PKPGSLKRSL ASQSSDDHLN
     KRSRTSSVSS LASACTGGIP SSSRNAITSS YSSTRGISQL WKRSGPTSSP FSSPASSRSQ
     TPERPAKKTR EEEPCQQSSS SPPLVTDKES PGEKVTDTTT GKQQSSWTSP PTPGSSGQRK
     RKIQLLPSRR GDQLTLPPPP ELGYSITAED LDMERKASLQ WFNKVLEDKP DDASASATDG
     PPSTSPPFTF TLPAVGPAAS PASLPAPSSN PLLESLKKMQ ESPAPSSSEP AEAATVAAPS
     PPKTPSLLAP LVSPLAGPLA STSSDSKPAA TFLGLASASS ITPLTDSKSS GVSQAEQSVS
     TPASTASSPT PKPSMLFGML SPPASSSSLA TPAPACASPM FKPIFPATPK SESDSPLPSS
     SSAATTASSS TAPPTAASTT PTFKPIFDKM EPFTAMPLST PFSLKQTTAT ATTTATSAPL
     FTGLGTATST VASGTAASAS KPVFGFGVTT AASTASSTMT STSQSVLFGG APPVTTSSSA
     PALASIFQFG KPLAPAASAA GTSFSQPLAS STQTAASNSG FSGFGSTLTT STSAPATTSQ
     PTLTFSNTVT PTFNIPFSSS AKPALPTYPG ANSQPTFGAT DGATKPALAP SFGSSFTFGN
     SVASAPSAAP APATFGSAAQ PAFGGLKAAA STFGAPASTQ PAFGSTTSVF SFGSATTSGF
     GAAATAATTT QTTNSGSSSS LFGSSAPSPF TFGGSAAPAG SGGFGLSATP GTSSTSGTFS
     FGSGQSGTPG TTTSFGSLSQ NTLGAPSQGS PFAFSVGSTP ESKPVFGGTS TPTFGQSAPA
     PGVGTTGSSL SFGASSTPAQ GFVGVGPFGS AAPSFSIGAG SKTPGARQRL QARRQHTRKK
//