APQ12_YEAST
ID APQ12_YEAST Reviewed; 138 AA.
AC P40532; D6VVP2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Nuclear membrane organization protein APQ12;
GN Name=APQ12; OrderedLocusNames=YIL040W;
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4]
RP FUNCTION.
RX PubMed=15273328; DOI=10.1261/rna.7420504;
RA Baker K.E., Coller J., Parker R.;
RT "The yeast Apq12 protein affects nucleocytoplasmic mRNA transport.";
RL RNA 10:1352-1358(2004).
RN [5]
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 [6]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=17724120; DOI=10.1083/jcb.200702120;
RA Scarcelli J.J., Hodge C.A., Cole C.N.;
RT "The yeast integral membrane protein Apq12 potentially links membrane
RT dynamics to assembly of nuclear pore complexes.";
RL J. Cell Biol. 178:799-812(2007).
RN [7]
RP FUNCTION.
RX PubMed=20016074; DOI=10.1242/jcs.055046;
RA Hodge C.A., Choudhary V., Wolyniak M.J., Scarcelli J.J., Schneiter R.,
RA Cole C.N.;
RT "Integral membrane proteins Brr6 and Apq12 link assembly of the nuclear
RT pore complex to lipid homeostasis in the endoplasmic reticulum.";
RL J. Cell Sci. 123:141-151(2010).
CC -!- FUNCTION: Involved in the regulation of lipid homeostasis in the
CC endoplasmic reticulum, thereby impacting nuclear pore complex
CC biogenesis and localization, and nucleocytoplasmic mRNA transport.
CC {ECO:0000269|PubMed:15273328, ECO:0000269|PubMed:17724120,
CC ECO:0000269|PubMed:20016074}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane; Multi-pass membrane protein.
CC Endoplasmic reticulum membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the APQ12 family. {ECO:0000305}.
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DR EMBL; Z46861; CAA86911.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08508.1; -; Genomic_DNA.
DR PIR; S49938; S49938.
DR RefSeq; NP_012224.1; NM_001179390.1.
DR AlphaFoldDB; P40532; -.
DR SMR; P40532; -.
DR BioGRID; 34950; 500.
DR DIP; DIP-5412N; -.
DR STRING; 4932.YIL040W; -.
DR TCDB; 9.A.34.1.1; the nuclear pore complex biogenesis (npc-b) family.
DR MaxQB; P40532; -.
DR PaxDb; P40532; -.
DR PRIDE; P40532; -.
DR TopDownProteomics; P40532; -.
DR EnsemblFungi; YIL040W_mRNA; YIL040W; YIL040W.
DR GeneID; 854771; -.
DR KEGG; sce:YIL040W; -.
DR SGD; S000001302; APQ12.
DR VEuPathDB; FungiDB:YIL040W; -.
DR HOGENOM; CLU_1856860_0_0_1; -.
DR InParanoid; P40532; -.
DR OMA; TCIGIYM; -.
DR BioCyc; YEAST:G3O-31312-MON; -.
DR PRO; PR:P40532; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40532; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IDA:SGD.
DR GO; GO:0005635; C:nuclear envelope; IDA:SGD.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055088; P:lipid homeostasis; IMP:SGD.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006998; P:nuclear envelope organization; IMP:SGD.
DR InterPro; IPR024316; APQ12.
DR Pfam; PF12716; Apq12; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; mRNA transport; Nucleus;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..138
FT /note="Nuclear membrane organization protein APQ12"
FT /id="PRO_0000202992"
FT TOPO_DOM 1..39
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..67
FT /note="Perinuclear space"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 138 AA; 16508 MW; 5DDA578B8469CDAF CRC64;
MDATQPQYEL SVVTQCLKSA IDVIQWLIPT ITKFSQSHPL VFQLLFIFFT FYVFYKLLMN
FITLVKRFLY LTLVVTCIGI YMRGSQQFLT VDLLNFYNFV MSNRYYAFKI YTLFINALER
EINTVYHLAQ MKMEQLLK
