ID LNP_HUMAN Reviewed; 428 AA. AC Q9C0E8; B7ZLA8; Q2M2V8; Q2YD99; Q658W8; Q8N5V9; Q96MS5; DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 2. DT 27-MAR-2024, entry version 155. DE RecName: Full=Endoplasmic reticulum junction formation protein lunapark {ECO:0000305}; DE AltName: Full=ER junction formation factor lunapark {ECO:0000312|HGNC:HGNC:21610}; GN Name=LNPK {ECO:0000312|HGNC:HGNC:21610}; GN Synonyms=KIAA1715 {ECO:0000312|HGNC:HGNC:21610}, LNP; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=11214970; DOI=10.1093/dnares/7.6.347; RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XIX. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 7:347-355(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4). RC TISSUE=Adrenal cortex, and 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 31-428. RC TISSUE=Stomach; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182; SER-194 AND SER-321, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [8] RP MYRISTOYLATION AT GLY-2. RX PubMed=20213681; DOI=10.1002/pmic.200900783; RA Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E., RA Tsunasawa S., Utsumi T.; RT "Strategy for comprehensive identification of human N-myristoylated RT proteins using an insect cell-free protein synthesis system."; RL Proteomics 10:1780-1793(2010). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-182 AND SER-194, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [11] RP SUBCELLULAR LOCATION. 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). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194; THR-213 AND SER-217, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [13] RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, MYRISTOYLATION AT GLY-2, CLEAVAGE RP OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS RP OF GLY-2 AND 276-CYS--CYS-301, AND MEMBRANE INTEGRATION TARGETING SEQUENCE. RX PubMed=24223779; DOI=10.1371/journal.pone.0078235; RA Moriya K., Nagatoshi K., Noriyasu Y., Okamura T., Takamitsu E., Suzuki T., RA Utsumi T.; RT "Protein N-myristoylation plays a critical role in the endoplasmic RT reticulum morphological change induced by overexpression of protein RT Lunapark, an integral membrane protein of the endoplasmic reticulum."; RL PLoS ONE 8:E78235-E78235(2013). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194; SER-217 AND SER-384, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [15] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=25404289; DOI=10.1073/pnas.1419997111; RA Shemesh T., Klemm R.W., Romano F.B., Wang S., Vaughan J., Zhuang X., RA Tukachinsky H., Kozlov M.M., Rapoport T.A.; RT "A model for the generation and interconversion of ER morphologies."; RL Proc. Natl. Acad. Sci. U.S.A. 111:E5243-E5251(2014). RN [16] RP FUNCTION, SUBCELLULAR LOCATION, AND TOPOLOGY. RX PubMed=25548161; DOI=10.1073/pnas.1423026112; RA Chen S., Desai T., McNew J.A., Gerard P., Novick P.J., Ferro-Novick S.; RT "Lunapark stabilizes nascent three-way junctions in the endoplasmic RT reticulum."; RL Proc. Natl. Acad. Sci. U.S.A. 112:418-423(2015). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [18] RP FUNCTION, SUBUNIT, PHOSPHORYLATION AT SER-114; SER-153; SER-177; SER-182; RP SER-194; THR-211; SER-217; SER-227; SER-321; SER-353 AND SER-384, RP PROTEASOMAL DEGRADATION, MUTAGENESIS OF GLY-2; SER-177; THR-179; SER-182; RP SER-194; SER-202; THR-211; THR-213; SER-218; SER-227 AND SER-231, DOMAIN, RP AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=27619977; DOI=10.7554/elife.18605; RA Wang S., Tukachinsky H., Romano F.B., Rapoport T.A.; RT "Cooperation of the ER-shaping proteins atlastin, lunapark, and reticulons RT to generate a tubular membrane network."; RL Elife 5:0-0(2016). RN [19] RP FUNCTION, INVOLVEMENT IN NEDEHCC, AND VARIANT NEDEHCC 251-ARG--GLU-428 DEL. RX PubMed=30032983; DOI=10.1016/j.ajhg.2018.06.011; RA Breuss M.W., Nguyen A., Song Q., Nguyen T., Stanley V., James K.N., RA Musaev D., Chai G., Wirth S.A., Anzenberg P., George R.D., Johansen A., RA Ali S., Zia-Ur-Rehman M., Sultan T., Zaki M.S., Gleeson J.G.; RT "Mutations in LNPK, encoding the endoplasmic reticulum junction stabilizer RT Lunapark, cause a recessive neurodevelopmental syndrome."; RL Am. J. Hum. Genet. 103:296-304(2018). CC -!- FUNCTION: Endoplasmic reticulum (ER)-shaping membrane protein that CC plays a role in determining ER morphology (PubMed:30032983). Involved CC in the stabilization of nascent three-way ER tubular junctions within CC the ER network (PubMed:24223779, PubMed:25404289, PubMed:25548161, CC PubMed:27619977). May also play a role as a curvature-stabilizing CC protein within the three-way ER tubular junction network CC (PubMed:25404289). May be involved in limb development (By similarity). CC Is involved in central nervous system development (PubMed:30032983). CC {ECO:0000250|UniProtKB:Q7TQ95, ECO:0000269|PubMed:24223779, CC ECO:0000269|PubMed:25404289, ECO:0000269|PubMed:25548161, CC ECO:0000269|PubMed:27619977, ECO:0000269|PubMed:30032983}. CC -!- SUBUNIT: Homodimer; homodimerization requires the C4-type zinc finger CC motif and decreases during mitosis in a phosphorylation-dependent CC manner (PubMed:27619977). {ECO:0000269|PubMed:27619977}. CC -!- INTERACTION: CC Q9C0E8-2; P04083: ANXA1; NbExp=3; IntAct=EBI-11024283, EBI-354007; CC Q9C0E8-2; Q53G59: KLHL12; NbExp=6; IntAct=EBI-11024283, EBI-740929; CC Q9C0E8-2; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-11024283, EBI-11742507; CC Q9C0E8-2; Q9BVI4: NOC4L; NbExp=3; IntAct=EBI-11024283, EBI-395927; CC Q9C0E8-2; P26367: PAX6; NbExp=3; IntAct=EBI-11024283, EBI-747278; CC Q9C0E8-2; O60664: PLIN3; NbExp=3; IntAct=EBI-11024283, EBI-725795; CC Q9C0E8-2; P08247: SYP; NbExp=3; IntAct=EBI-11024283, EBI-9071725; CC Q9C0E8-2; O95070: YIF1A; NbExp=3; IntAct=EBI-11024283, EBI-2799703; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:22729086, ECO:0000269|PubMed:24223779, CC ECO:0000269|PubMed:25404289, ECO:0000269|PubMed:25548161, CC ECO:0000269|PubMed:27619977}; Multi-pass membrane protein CC {ECO:0000269|PubMed:22729086, ECO:0000269|PubMed:24223779}; Cytoplasmic CC side {ECO:0000269|PubMed:24223779, ECO:0000269|PubMed:25548161}. CC Note=Localizes at endoplasmic reticulum (ER) three-way tubular CC junctions, which represent crossing-points at which the tubules build a CC polygonal network (PubMed:22729086, PubMed:24223779, PubMed:25404289, CC PubMed:25548161, PubMed:27619977). {ECO:0000269|PubMed:22729086, CC ECO:0000269|PubMed:24223779, ECO:0000269|PubMed:25404289, CC ECO:0000269|PubMed:25548161, ECO:0000269|PubMed:27619977}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q9C0E8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9C0E8-2; Sequence=VSP_020239; CC Name=3; CC IsoId=Q9C0E8-3; Sequence=VSP_020238; CC Name=4; CC IsoId=Q9C0E8-4; Sequence=VSP_054427; CC -!- TISSUE SPECIFICITY: Expressed in neural precursor cells, where it is CC detected at the growth-cone-like structure and branching sites of CC neurite-like processes. {ECO:0000269|PubMed:30032983}. CC -!- DOMAIN: The transmembrane domain 1 and 2 function as a signal-anchor CC and stop-transfer sequence, respectively, generating a double-spanning CC integral membrane protein with a N- and C-terminal cytoplasmic CC orientation (PubMed:24223779). Transmembrane domain 1 and 2 are CC probably sufficient to mediate membrane translocation and topology CC formation in a N-myristoylation-independent manner (PubMed:24223779). CC Transmembrane domain 2 is sufficient to block the protein secretion CC pathway (PubMed:24223779). The two coiled-coil domains are necessary CC for its endoplasmic reticulum (ER) three-way tubular junction CC localization (PubMed:27619977). The C4-type zinc finger motif is CC necessary both for its ER three-way tubular junction localization and CC formation (PubMed:24223779, PubMed:27619977). CC {ECO:0000269|PubMed:24223779, ECO:0000269|PubMed:27619977}. CC -!- PTM: Myristoylated; myristoylation is necessary for the endoplasmic CC reticulum (ER) three-way ER tubular junction formation, but is not CC required neither for membrane translocation, membrane topology CC formation, nor for the specific localization to ER membranes CC (PubMed:24223779). {ECO:0000269|PubMed:24223779}. CC -!- PTM: Phosphorylated. Phosphorylation occurs at Ser-177, Ser-182, Ser- CC 217, Ser-227, Ser-321 and Ser-384 during interphase (PubMed:27619977). CC Phosphorylation occurs at Ser-114, Ser-153, Ser-194, Thr-211 and Ser- CC 353 during mitosis; these phosphorylations reduce both its CC homodimerization and the ER three-way tubular junction formation CC (PubMed:27619977). {ECO:0000269|PubMed:27619977}. CC -!- PTM: Subject to proteasomal degradation following phosphorylation CC during mitosis (PubMed:27619977). {ECO:0000269|PubMed:27619977}. CC -!- DISEASE: Neurodevelopmental disorder with epilepsy and hypoplasia of CC the corpus callosum (NEDEHCC) [MIM:618090]: An autosomal recessive CC disorder characterized by severe psychomotor delay, intellectual CC disability, hypotonia, epilepsy, and corpus callosum hypoplasia. Some CC patients show mild cerebellar hypoplasia and atrophy. CC {ECO:0000269|PubMed:30032983}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the lunapark family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB21806.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB051502; BAB21806.1; ALT_INIT; mRNA. DR EMBL; AK056532; BAB71207.1; -; mRNA. DR EMBL; AC016751; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC016915; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC031530; AAH31530.1; -; mRNA. DR EMBL; BC105132; AAI05133.1; -; mRNA. DR EMBL; BC105134; AAI05135.1; -; mRNA. DR EMBL; BC110329; AAI10330.1; -; mRNA. DR EMBL; BC143681; AAI43682.1; -; mRNA. DR EMBL; AL832947; CAH56306.1; -; mRNA. DR CCDS; CCDS33332.1; -. [Q9C0E8-1] DR CCDS; CCDS77488.1; -. [Q9C0E8-3] DR CCDS; CCDS77489.1; -. [Q9C0E8-4] DR RefSeq; NP_001291937.1; NM_001305008.1. DR RefSeq; NP_001291938.1; NM_001305009.1. [Q9C0E8-4] DR RefSeq; NP_001291940.1; NM_001305011.1. [Q9C0E8-3] DR RefSeq; NP_085153.1; NM_030650.2. [Q9C0E8-1] DR RefSeq; XP_006712846.1; XM_006712783.2. [Q9C0E8-1] DR RefSeq; XP_016860544.1; XM_017005055.1. DR AlphaFoldDB; Q9C0E8; -. DR BioGRID; 123333; 301. DR ELM; Q9C0E8; -. DR IntAct; Q9C0E8; 50. DR MINT; Q9C0E8; -. DR STRING; 9606.ENSP00000440905; -. DR TCDB; 8.A.109.1.5; the endoplasmic reticulum junction-forming protein (lunapark) family. DR iPTMnet; Q9C0E8; -. DR PhosphoSitePlus; Q9C0E8; -. DR SwissPalm; Q9C0E8; -. DR BioMuta; LNPK; -. DR DMDM; 114149979; -. DR CPTAC; CPTAC-1616; -. DR EPD; Q9C0E8; -. DR jPOST; Q9C0E8; -. DR MassIVE; Q9C0E8; -. DR MaxQB; Q9C0E8; -. DR PaxDb; 9606-ENSP00000272748; -. DR PeptideAtlas; Q9C0E8; -. DR ProteomicsDB; 7218; -. DR ProteomicsDB; 80025; -. [Q9C0E8-3] DR Pumba; Q9C0E8; -. DR Antibodypedia; 3018; 29 antibodies from 10 providers. DR DNASU; 80856; -. DR Ensembl; ENST00000272748.9; ENSP00000272748.4; ENSG00000144320.14. [Q9C0E8-1] DR Ensembl; ENST00000409660.5; ENSP00000386237.1; ENSG00000144320.14. [Q9C0E8-3] DR Ensembl; ENST00000544803.5; ENSP00000440905.1; ENSG00000144320.14. [Q9C0E8-4] DR GeneID; 80856; -. DR KEGG; hsa:80856; -. DR MANE-Select; ENST00000272748.9; ENSP00000272748.4; NM_030650.3; NP_085153.1. DR UCSC; uc002ukc.2; human. [Q9C0E8-1] DR AGR; HGNC:21610; -. DR CTD; 80856; -. DR DisGeNET; 80856; -. DR GeneCards; LNPK; -. DR HGNC; HGNC:21610; LNPK. DR HPA; ENSG00000144320; Low tissue specificity. DR MalaCards; LNPK; -. DR MIM; 610236; gene. DR MIM; 618090; phenotype. DR neXtProt; NX_Q9C0E8; -. DR OpenTargets; ENSG00000144320; -. DR PharmGKB; PA134938939; -. DR VEuPathDB; HostDB:ENSG00000144320; -. DR eggNOG; KOG2846; Eukaryota. DR GeneTree; ENSGT00390000001859; -. DR HOGENOM; CLU_036951_0_0_1; -. DR InParanoid; Q9C0E8; -. DR OMA; CGYFNPS; -. DR OrthoDB; 2918653at2759; -. DR PhylomeDB; Q9C0E8; -. DR TreeFam; TF315086; -. DR PathwayCommons; Q9C0E8; -. DR SignaLink; Q9C0E8; -. DR SIGNOR; Q9C0E8; -. DR BioGRID-ORCS; 80856; 11 hits in 1157 CRISPR screens. DR ChiTaRS; LNPK; human. DR GenomeRNAi; 80856; -. DR Pharos; Q9C0E8; Tbio. DR PRO; PR:Q9C0E8; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q9C0E8; Protein. DR Bgee; ENSG00000144320; Expressed in calcaneal tendon and 187 other cell types or tissues. DR ExpressionAtlas; Q9C0E8; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0071782; C:endoplasmic reticulum tubular network; IBA:GO_Central. DR GO; GO:0098826; C:endoplasmic reticulum tubular network membrane; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; NAS:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0007596; P:blood coagulation; IEA:Ensembl. DR GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl. DR GO; GO:0035115; P:embryonic forelimb morphogenesis; IEA:Ensembl. DR GO; GO:0007029; P:endoplasmic reticulum organization; IMP:UniProtKB. DR GO; GO:0071788; P:endoplasmic reticulum tubular network maintenance; IMP:UniProtKB. DR GO; GO:0071786; P:endoplasmic reticulum tubular network organization; IBA:GO_Central. DR GO; GO:0060173; P:limb development; NAS:UniProtKB. DR GO; GO:1903373; P:positive regulation of endoplasmic reticulum tubular network organization; IMP:UniProtKB. DR GO; GO:0032330; P:regulation of chondrocyte differentiation; IEA:Ensembl. DR InterPro; IPR040115; Lnp. DR InterPro; IPR019273; Lunapark_dom. DR PANTHER; PTHR22166; ENDOPLASMIC RETICULUM JUNCTION FORMATION PROTEIN LUNAPARK; 1. DR PANTHER; PTHR22166:SF12; ENDOPLASMIC RETICULUM JUNCTION FORMATION PROTEIN LUNAPARK; 1. DR Pfam; PF10058; zinc_ribbon_10; 1. DR Genevisible; Q9C0E8; HS. PE 1: Evidence at protein level; KW Alternative splicing; Coiled coil; Developmental protein; Disease variant; KW Endoplasmic reticulum; Epilepsy; Intellectual disability; Lipoprotein; KW Membrane; Metal-binding; Myristate; Phosphoprotein; Reference proteome; KW Transmembrane; Transmembrane helix; Zinc; Zinc-finger. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:20213681, FT ECO:0000269|PubMed:24223779" FT CHAIN 2..428 FT /note="Endoplasmic reticulum junction formation protein FT lunapark" FT /id="PRO_0000248310" FT TOPO_DOM 2..45 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:24223779" FT TRANSMEM 46..66 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 67..77 FT /note="Lumenal" FT /evidence="ECO:0000269|PubMed:24223779" FT TRANSMEM 78..98 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 99..428 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:24223779, FT ECO:0000269|PubMed:25548161" FT ZN_FING 276..301 FT /note="C4-type; plays a role in ER morphology" FT /evidence="ECO:0000269|PubMed:24223779, FT ECO:0000269|PubMed:27619977" FT REGION 143..247 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 356..428 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 16..41 FT /evidence="ECO:0000255" FT COILED 102..128 FT /evidence="ECO:0000255" FT COMPBIAS 166..180 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 181..204 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 114 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:27619977" FT MOD_RES 153 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:27619977" FT MOD_RES 177 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:27619977, FT ECO:0007744|PubMed:20068231" FT MOD_RES 182 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:27619977, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231" FT MOD_RES 194 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:27619977, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 211 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:27619977" FT MOD_RES 213 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 217 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:27619977, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 227 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:27619977" FT MOD_RES 321 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:27619977, FT ECO:0007744|PubMed:18691976" FT MOD_RES 353 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:27619977" FT MOD_RES 384 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:27619977, FT ECO:0007744|PubMed:24275569" FT MOD_RES 414 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q7TQ95" FT LIPID 2 FT /note="N-myristoyl glycine" FT /evidence="ECO:0000269|PubMed:20213681, FT ECO:0000269|PubMed:24223779" FT VAR_SEQ 1..123 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_020238" FT VAR_SEQ 1..9 FT /note="MGGLFSRWR -> MEGK (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_020239" FT VAR_SEQ 235 FT /note="M -> MEMGLPHIAQAGLEHLSSSDLSTSTSQSAGIT (in isoform FT 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_054427" FT VARIANT 251..428 FT /note="Missing (in NEDEHCC)" FT /evidence="ECO:0000269|PubMed:30032983" FT /id="VAR_081176" FT MUTAGEN 2 FT /note="G->A: Abolishes myristoylation. Inhibits three-way FT ER tubular junction formation. Does not inhibit FT transmembrane domain 1-induced membrane translocation." FT /evidence="ECO:0000269|PubMed:24223779, FT ECO:0000269|PubMed:27619977" FT MUTAGEN 177 FT /note="S->A: Inhibits phosphorylation and degradation in FT mitosis and prevents homodimerization and three-way ER FT tubular junction formations; when associated with A-179; FT A-182; A-194; A-202; A-211; A-213; A-218; A-227 and A-231." FT /evidence="ECO:0000269|PubMed:27619977" FT MUTAGEN 177 FT /note="S->D: Inhibits phosphorylation and degradation in FT mitosis but does not prevent homodimerization and three-way FT ER tubular junction formations; when associated with A-179; FT A-182; A-194; A-202; A-211; A-213; A-218; A-227 and A-231." FT /evidence="ECO:0000269|PubMed:27619977" FT MUTAGEN 179 FT /note="T->A: Inhibits phosphorylation and degradation in FT mitosis and prevents homodimerization and three-way ER FT tubular junction formations; when associated with A-177; FT A-182; A-194; A-202; A-211; A-213; A-218; A-227 and A-231." FT /evidence="ECO:0000269|PubMed:27619977" FT MUTAGEN 179 FT /note="T->D: Inhibits phosphorylation and degradation in FT mitosis but does not prevent homodimerization and three-way FT ER tubular junction formations; when associated with A-177; FT A-182; A-194; A-202; A-211; A-213; A-218; A-227 and A-231." FT /evidence="ECO:0000269|PubMed:27619977" FT MUTAGEN 182 FT /note="S->A: Inhibits phosphorylation and degradation in FT mitosis and prevents homodimerization and three-way ER FT tubular junction formations; when associated with A-177; FT A-179; A-194; A-202; A-211; A-213; A-218; A-227 and A-231." FT /evidence="ECO:0000269|PubMed:27619977" FT MUTAGEN 182 FT /note="S->D: Inhibits phosphorylation and degradation in FT mitosis but does not prevent homodimerization and three-way FT ER tubular junction formations; when associated with A-177; FT A-179; A-194; A-202; A-211; A-213; A-218; A-227 and A-231." FT /evidence="ECO:0000269|PubMed:27619977" FT MUTAGEN 194 FT /note="S->A: Inhibits phosphorylation and degradation in FT mitosis and prevents homodimerization and three-way ER FT tubular junction formations; when associated with A-177; FT A-179; A-182; A-202; A-211; A-213; A-218; A-227 and A-231." FT /evidence="ECO:0000269|PubMed:27619977" FT MUTAGEN 194 FT /note="S->D: Inhibits phosphorylation and degradation in FT mitosis but does not prevent homodimerization and three-way FT ER tubular junction formations; when associated with A-177; FT A-179; A-182; A-202; A-211; A-213; A-218; A-227 and A-231." FT /evidence="ECO:0000269|PubMed:27619977" FT MUTAGEN 202 FT /note="S->A: Inhibits phosphorylation and degradation in FT mitosis and prevents homodimerization and three-way ER FT tubular junction formations; when associated with A-177; FT A-179; A-182; A-194; A-211; A-213; A-218; A-227 and A-231." FT /evidence="ECO:0000269|PubMed:27619977" FT MUTAGEN 202 FT /note="S->D: Inhibits phosphorylation and degradation in FT mitosis but does not prevent homodimerization and three-way FT ER tubular junction formations; when associated with A-177; FT A-179; A-182; A-194; A-211; A-213; A-218; A-227 and A-231." FT /evidence="ECO:0000269|PubMed:27619977" FT MUTAGEN 211 FT /note="T->A: Inhibits phosphorylation and degradation in FT mitosis and prevents homodimerization and three-way ER FT tubular junction formations; when associated with A-177; FT A-179; A-182; A-194; A-202; A-213; A-218; A-227 and A-231." FT /evidence="ECO:0000269|PubMed:27619977" FT MUTAGEN 211 FT /note="T->D: Inhibits phosphorylation and degradation in FT mitosis but does not prevent homodimerization and three-way FT ER tubular junction formations; when associated with A-177; FT A-179; A-182; A-194; A-202; A-213; A-218; A-227 and A-231." FT /evidence="ECO:0000269|PubMed:27619977" FT MUTAGEN 213 FT /note="T->A: Inhibits phosphorylation and degradation in FT mitosis and prevents homodimerization and three-way ER FT tubular junction formations; when associated with A-177; FT A-179; A-182; A-194; A-202; A-211; A-218; A-227 and A-231." FT /evidence="ECO:0000269|PubMed:27619977" FT MUTAGEN 213 FT /note="T->D: Inhibits phosphorylation and degradation in FT mitosis but does not prevent homodimerization and three-way FT ER tubular junction formations; when associated with A-177; FT A-179; A-182; A-194; A-202; A-211; A-218; A-227 and A-231." FT /evidence="ECO:0000269|PubMed:27619977" FT MUTAGEN 218 FT /note="S->A: Inhibits phosphorylation and degradation in FT mitosis and prevents homodimerization and three-way ER FT tubular junction formations; when associated with A-177; FT A-179; A-182; A-194; A-202; A-211; A-213; A-227 and A-231." FT /evidence="ECO:0000269|PubMed:27619977" FT MUTAGEN 218 FT /note="S->D: Inhibits phosphorylation and degradation in FT mitosis but does not prevent homodimerization and three-way FT ER tubular junction formations; when associated with A-177; FT A-179; A-182; A-194; A-202; A-211; A-213; A-227 and A-231." FT /evidence="ECO:0000269|PubMed:27619977" FT MUTAGEN 227 FT /note="S->A: Inhibits phosphorylation and degradation in FT mitosis and prevents homodimerization and three-way ER FT tubular junction formations; when associated with A-177; FT A-179; A-182; A-194; A-202; A-211; A-213; A-218 and A-231." FT /evidence="ECO:0000269|PubMed:27619977" FT MUTAGEN 227 FT /note="S->D: Inhibits phosphorylation and degradation in FT mitosis but does not prevent homodimerization and three-way FT ER tubular junction formations; when associated with A-177; FT A-179; A-182; A-194; A-202; A-211; A-213; A-218 and A-231." FT /evidence="ECO:0000269|PubMed:27619977" FT MUTAGEN 231 FT /note="S->A: Inhibits phosphorylation and degradation in FT mitosis and prevents homodimerization and three-way ER FT tubular junction formations; when associated with A-177; FT A-179; A-182; A-194; A-202; A-211; A-213; A-218 and A-227." FT /evidence="ECO:0000269|PubMed:27619977" FT MUTAGEN 231 FT /note="S->D: Inhibits phosphorylation and degradation in FT mitosis but does not prevent homodimerization and three-way FT ER tubular junction formations; when associated with A-177; FT A-179; A-182; A-194; A-202; A-211; A-213; A-218 and A-227." FT /evidence="ECO:0000269|PubMed:27619977" FT MUTAGEN 276..301 FT /note="CQQCFSHNGMALKEEFEYIAFRCAYC->AQQAFSHNGMALKEEFEYIAFRAA FT YA: No change in N-myristoylation. Inhibits three-way ER FT tubular junction formation." FT /evidence="ECO:0000269|PubMed:24223779" FT CONFLICT 262 FT /note="Y -> H (in Ref. 2; BAB71207)" FT /evidence="ECO:0000305" FT CONFLICT 374 FT /note="E -> G (in Ref. 4; AAH31530)" FT /evidence="ECO:0000305" SQ SEQUENCE 428 AA; 47740 MW; F5BBA4186C2691BF CRC64; MGGLFSRWRT KPSTVEVLES IDKEIQALEE FREKNQRLQK LWVGRLILYS SVLYLFTCLI VYLWYLPDEF TARLAMTLPF FAFPLIIWSI RTVIIFFFSK RTERNNEALD DLKSQRKKIL EEVMEKETYK TAKLILERFD PDSKKAKECE PPSAGAAVTA RPGQEIRQRT AAQRNLSPTP ASPNQGPPPQ VPVSPGPPKD SSAPGGPPER TVTPALSSNV LPRHLGSPAT SVPGMGLHPP GPPLARPILP RERGALDRIV EYLVGDGPQN RYALICQQCF SHNGMALKEE FEYIAFRCAY CFFLNPARKT RPQAPRLPEF SFEKRQVVEG SSSVGPLPSG SVLSSDNQFN EESLEHDVLD DNTEQTDDKI PATEQTNQVI EKASDSEEPE EKQETENEEA SVIETNSTVP GADSIPDPEL SGESLTAE //