LNP_YEAST
ID LNP_YEAST Reviewed; 278 AA.
AC P38878; D3DLE0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Endoplasmic reticulum junction formation protein lunapark {ECO:0000305};
DE AltName: Full=ER junction formation factor lunapark {ECO:0000250|UniProtKB:Q9C0E8};
GN Name=LNP1; OrderedLocusNames=YHR192W;
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=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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 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 [4]
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 [5]
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RTN1, AND MUTAGENESIS OF
RP CYS-223; CYS-226; CYS-244 AND CYS-247.
RX PubMed=22729086; DOI=10.1038/ncb2523;
RA Chen S., Novick P., Ferro-Novick S.;
RT "ER network formation requires a balance of the dynamin-like GTPase Sey1p
RT and the Lunapark family member Lnp1p.";
RL Nat. Cell Biol. 14:707-716(2012).
CC -!- FUNCTION: Plays a role in tubular endoplasmic reticulum network
CC formation and maintenance. Works in conjunction with the ER shaping
CC proteins (reticulons RTN1 and RTN2, YOP1), and in antagonism to SEY1 to
CC maintain the network in a dynamic equilibrium. May counterbalance SEY1-
CC directed polygon formation by promoting polygon loss through ring
CC closure. {ECO:0000269|PubMed:22729086}.
CC -!- SUBUNIT: Interacts with RTN1; this interaction is negatively regulated
CC by SEY1. Interacts with SEY1 and YOP1. {ECO:0000269|PubMed:22729086}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:22729086}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:22729086}. Note=Localizes to three-way ER tubule
CC junctions. This localization is SEY1-dependent.
CC -!- MISCELLANEOUS: Present with 3390 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the lunapark family. {ECO:0000305}.
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DR EMBL; U00030; AAB68359.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06884.1; -; Genomic_DNA.
DR PIR; S46681; S46681.
DR RefSeq; NP_012062.1; NM_001179323.1.
DR AlphaFoldDB; P38878; -.
DR BioGRID; 36626; 85.
DR DIP; DIP-7382N; -.
DR IntAct; P38878; 3.
DR STRING; 4932.YHR192W; -.
DR TCDB; 8.A.109.1.1; the endoplasmic reticulum junction-forming protein (lunapark) family.
DR MaxQB; P38878; -.
DR PaxDb; P38878; -.
DR PRIDE; P38878; -.
DR EnsemblFungi; YHR192W_mRNA; YHR192W; YHR192W.
DR GeneID; 856599; -.
DR KEGG; sce:YHR192W; -.
DR SGD; S000001235; LNP1.
DR VEuPathDB; FungiDB:YHR192W; -.
DR eggNOG; KOG2846; Eukaryota.
DR HOGENOM; CLU_089708_0_0_1; -.
DR InParanoid; P38878; -.
DR OMA; KEETHYN; -.
DR BioCyc; YEAST:G3O-31220-MON; -.
DR ChiTaRS; LNP1; yeast.
DR PRO; PR:P38878; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38878; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071782; C:endoplasmic reticulum tubular network; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071786; P:endoplasmic reticulum tubular network organization; IMP:SGD.
DR GO; GO:0006999; P:nuclear pore organization; IGI:CACAO.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IGI:SGD.
DR GO; GO:0061709; P:reticulophagy; IMP:SGD.
DR InterPro; IPR040115; Lnp.
DR InterPro; IPR019273; Lunapark_dom.
DR PANTHER; PTHR22166; PTHR22166; 2.
DR Pfam; PF10058; zinc_ribbon_10; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Endoplasmic reticulum; Membrane; Metal-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Zinc; Zinc-finger.
FT CHAIN 1..278
FT /note="Endoplasmic reticulum junction formation protein
FT lunapark"
FT /id="PRO_0000202936"
FT TOPO_DOM 1..45
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..77
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..278
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ZN_FING 223..247
FT /note="C4-type; plays a role in ER morphology"
FT REGION 258..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 107..183
FT /evidence="ECO:0000255"
FT MUTAGEN 223
FT /note="C->A: In lnp1-1; causes aberrant ER morphology; when
FT associaetd with A-226, A-244 and A-247."
FT /evidence="ECO:0000269|PubMed:22729086"
FT MUTAGEN 226
FT /note="C->A: In lnp1-1; causes aberrant ER morphology; when
FT associaetd with A-223, A-244 and A-247."
FT /evidence="ECO:0000269|PubMed:22729086"
FT MUTAGEN 244
FT /note="C->A: In lnp1-1; causes aberrant ER morphology; when
FT associaetd with A-223, A-226 and A-247."
FT /evidence="ECO:0000269|PubMed:22729086"
FT MUTAGEN 247
FT /note="C->A: In lnp1-1; causes aberrant ER morphology; when
FT associaetd with A-223, A-226 and A-244."
FT /evidence="ECO:0000269|PubMed:22729086"
SQ SEQUENCE 278 AA; 32063 MW; D896557EEE805C89 CRC64;
MFSALGKWVR GSRNDKDFVT KYTADLSQIT SQIHQLDVAL KKSQSILSQW QSNLTFYGIA
LTVLALSYTY WEYHGYRPYL VVTALLCIGS LILFKWALTK LYAFYNNNRL RKLAKLRAIH
QKKLEKLKEE THYNATSSII QRFSSGEDQN DDAMVLLDDE LNAKYQELNN LKTELEKFKK
ESHVKGLKKE DSDAWFDKII SVLAGGNELD STSSLSPFKK IICPQCHWKS NCYRLASKPI
IFICPHCNHK IDEVKEREDA IEAKQPAQPS QSEKEKTK
