LNP_HUMAN
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 03-AUG-2022, entry version 146.
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};
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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. [Q9C0E8-3]
DR AlphaFoldDB; Q9C0E8; -.
DR BioGRID; 123333; 295.
DR ELM; Q9C0E8; -.
DR IntAct; Q9C0E8; 48.
DR MINT; Q9C0E8; -.
DR STRING; 9606.ENSP00000272748; -.
DR TCDB; 9.B.390.1.1; the tmcc/tex28 (tm-tex) 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; Q9C0E8; -.
DR PeptideAtlas; Q9C0E8; -.
DR PRIDE; Q9C0E8; -.
DR ProteomicsDB; 7218; -.
DR ProteomicsDB; 80025; -. [Q9C0E8-3]
DR Antibodypedia; 3018; 18 antibodies from 8 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 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; VSFWPWK; -.
DR OrthoDB; 1595535at2759; -.
DR PhylomeDB; Q9C0E8; -.
DR TreeFam; TF315086; -.
DR PathwayCommons; Q9C0E8; -.
DR SignaLink; Q9C0E8; -.
DR BioGRID-ORCS; 80856; 10 hits in 1079 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 185 other tissues.
DR ExpressionAtlas; Q9C0E8; baseline and differential.
DR Genevisible; Q9C0E8; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
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:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of 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; PTHR22166; 1.
DR Pfam; PF10058; zinc_ribbon_10; 1.
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; A-
FT 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; A-
FT 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; A-
FT 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; A-
FT 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; A-
FT 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; A-
FT 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; A-
FT 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; A-
FT 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; A-
FT 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; A-
FT 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
