PO121_RAT
ID PO121_RAT Reviewed; 1199 AA.
AC P52591;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Nuclear envelope pore membrane protein POM 121;
DE AltName: Full=Nucleoporin Nup121;
DE AltName: Full=Pore membrane protein of 121 kDa;
DE AltName: Full=p145;
GN Name=Pom121; Synonyms=Nup121;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8335683; DOI=10.1083/jcb.122.3.513;
RA Hallberg E., Wozniak R.W., Blobel G.;
RT "An integral membrane protein of the pore membrane domain of the nuclear
RT envelope contains a nucleoporin-like region.";
RL J. Cell Biol. 122:513-521(1993).
RN [2]
RP PROTEIN SEQUENCE OF 250-256; 365-384 AND 578-603, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=11448991; DOI=10.1083/jcb.200101089;
RA Daigle N., Beaudouin J., Hartnell L., Imreh G., Hallberg E.,
RA Lippincott-Schwartz J., Ellenberg J.;
RT "Nuclear pore complexes form immobile networks and have a very low turnover
RT in live mammalian cells.";
RL J. Cell Biol. 154:71-84(2001).
RN [4]
RP MUTAGENESIS OF ASP-531.
RX PubMed=14729472; DOI=10.1016/j.yexcr.2003.10.019;
RA Kihlmark M., Rustum C., Eriksson C., Beckman M., Iverfeldt K., Hallberg E.;
RT "Correlation between nucleocytoplasmic transport and caspase-3-dependent
RT dismantling of nuclear pores during apoptosis.";
RL Exp. Cell Res. 293:346-356(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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).
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:11448991}. Nucleus membrane
CC {ECO:0000269|PubMed:11448991}; Single-pass membrane protein
CC {ECO:0000269|PubMed:11448991}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11448991}; Single-pass membrane protein
CC {ECO:0000269|PubMed:11448991}. Note=Stably associated with the NPC
CC throughout interphase and the endoplasmic reticulum during metaphase.
CC -!- DOMAIN: Contains F-X-F-G repeats.
CC -!- PTM: Proteolytically cleaved by caspase-3 during apoptosis.
CC -!- SIMILARITY: Belongs to the POM121 family. {ECO:0000305}.
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DR EMBL; Z21513; CAA79725.1; -; mRNA.
DR EMBL; Z21514; CAA79726.1; -; Genomic_DNA.
DR PIR; A40670; A40670.
DR RefSeq; NP_446074.1; NM_053622.1.
DR PDB; 4YI0; X-ray; 1.81 A; A=291-320.
DR PDBsum; 4YI0; -.
DR AlphaFoldDB; P52591; -.
DR SMR; P52591; -.
DR CORUM; P52591; -.
DR STRING; 10116.ENSRNOP00000001968; -.
DR iPTMnet; P52591; -.
DR PhosphoSitePlus; P52591; -.
DR PaxDb; P52591; -.
DR PRIDE; P52591; -.
DR GeneID; 113975; -.
DR KEGG; rno:113975; -.
DR UCSC; RGD:620680; rat.
DR CTD; 9883; -.
DR RGD; 620680; Pom121.
DR eggNOG; ENOG502R5GW; Eukaryota.
DR InParanoid; P52591; -.
DR OrthoDB; 355024at2759; -.
DR PhylomeDB; P52591; -.
DR Reactome; R-RNO-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-RNO-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-RNO-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-RNO-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-RNO-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-RNO-191859; snRNP Assembly.
DR Reactome; R-RNO-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-RNO-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-RNO-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-RNO-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-RNO-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-RNO-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-RNO-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-RNO-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-RNO-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-RNO-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR PRO; PR:P52591; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; ISO:RGD.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IDA:RGD.
DR GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IDA:RGD.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006999; P:nuclear pore organization; IDA:RGD.
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 InterPro; IPR026090; POM121.
DR PANTHER; PTHR23193; PTHR23193; 1.
DR PANTHER; PTHR23193:SF43; PTHR23193:SF43; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Endoplasmic reticulum; Membrane;
KW mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Translocation;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1199
FT /note="Nuclear envelope pore membrane protein POM 121"
FT /id="PRO_0000204908"
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..1199
FT /note="Pore side"
FT /evidence="ECO:0000255"
FT REGION 82..197
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 344..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1061..1151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1199
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 457..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..551
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 616..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 531..532
FT /note="Cleavage; by caspase-3"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A8CG34"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K3Z9"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K3Z9"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K3Z9"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K3Z9"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96HA1"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A8CG34"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K3Z9"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K3Z9"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K3Z9"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K3Z9"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K3Z9"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K3Z9"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K3Z9"
FT MUTAGEN 531
FT /note="D->A: Abolishes cleavage."
FT /evidence="ECO:0000269|PubMed:14729472"
SQ SEQUENCE 1199 AA; 120785 MW; 6DC4451B91D5B907 CRC64;
MSPAAAAADG GERRRPPLGV REGRGRTRGC GGPAGAAALG LALLGLALYL VPAAAALAWL
AVGASAAWWG LSREPRGPRG LSSFVRESRR HPRPALTASP LPAKSPVNGS LCEPRSPLGG
PDPAELLLMG SYLGKPGPPE PALPQDPRDR PGRRPPSRSP PSSSTAQRVH HVYPALPTPL
LRPSRRPPHR DCGPLSSRFV ITPRRRYPIQ QAQYSLLGAL PTVCWNGGHK KAVLSARNSR
MVCSPVTVRI APPDSKLFRS PMPEQILSTT LSSPSSNAPD PCAKETVLNA LKEKKKRTVA
EEDQLHLDGQ ENKRRRHDSS GSGHSAFEPL VANGVPAAFV PKPGSLKRSL ASQSSDDHLN
KRSRTSSVSS LTSTCTGGIP SSSRNAITSS YSSTRGVSQL WKRSGPTSSP FSSPASSRSQ
TPERPAKKTR EEEPCHQSSS SAPLVTDKES PGEKVTDPAT GKQQSLWTSP PTPGSSGQRK
RKIQLLPSRR GDQLTLPPPP ELGYSITAED LDMERRASLQ WFNKVLEDKT DDASTPATDT
SPATSPPFTL TLPTVGPAAS PASLPAPSSN PLLESLKKMQ ESPAPSSSEP PEAATVAAPS
PPKTPSLLAP LVSPLTGPLA STSSDSKPTT TFLGLASASS ATPLTDTKAP GVSQAQLCVS
TPAATAPSPT PASTLFGMLS PPASSSSLAT PGPACASPMF KPIFPATPKS ESDNPLPTSS
SAATTTPAST ALPTTATATA HTFKPIFESV EPFAAMPLSP PFSLKQTTAP ATTAATSAPL
LTGLGTATST VATGTTASAS KPVFGFGVTT AASTASTIAS TSQSILFGGA PPVTASSSAP
ALASIFQFGK PLAPAASVAG TSFSQSLASS AQTAASNSSG GFSGFGGTLT TSTSAPATTS
QPTLTFSNTV TPTFNIPFSA SAKPALPTYP GANSQPTFGA TDGATKPALA PSFGSSFTFG
NSVASAPSAA PAPAAFGGAA QPAFGGLKAS ASTFGTPAST QPAFGSTTSV FSFGSATTSG
FGAAAATTQT THSGSSSSLF GSSTPSPFTF GGSAAPAGGG GFGLSATPGT GSTSGTFSFG
SGQSGTTGTT TSFGGSLSQN TLGAPSQSSP FAFSVGSTPE SKPVFGGTST PTFGQSAPAP
GVGTTGSSLS FGAPSTPAQG FVGVGPFGSG APSFSIGAGS KTPGARQRLQ ARRQHTRKK
