LNP_MOUSE
ID LNP_MOUSE Reviewed; 425 AA.
AC Q7TQ95; A2ASL9; Q69ZC5; Q6PAQ1; Q6PEN8;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Endoplasmic reticulum junction formation protein lunapark {ECO:0000305};
DE AltName: Full=ER junction formation factor lunapark {ECO:0000250|UniProtKB:Q9C0E8};
DE AltName: Full=Protein ulnaless;
GN Name=Lnpk {ECO:0000312|MGI:MGI:1918115}; Synonyms=Kiaa1715, Lnp, Uln;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J;
RX PubMed=12732147; DOI=10.1016/s0092-8674(03)00310-6;
RA Spitz F., Gonzalez F., Duboule D.;
RT "A global control region defines a chromosomal regulatory landscape
RT containing the HoxD cluster.";
RL Cell 113:405-417(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic tail;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cecum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177 AND SER-411, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Endoplasmic reticulum (ER)-shaping membrane protein that
CC plays a role in determining ER morphology. Involved in the
CC stabilization of nascent three-way ER tubular junctions within the ER
CC network. May also play a role as a curvature-stabilizing protein within
CC three-way ER tubular junction network. May be involved in limb and
CC central nervous system development (PubMed:12732147).
CC {ECO:0000250|UniProtKB:Q9C0E8, ECO:0000269|PubMed:12732147}.
CC -!- SUBUNIT: Homodimer; homodimerization requires the C4-type zinc finger
CC motif and decreases during mitosis in a phosphorylation-dependent
CC manner. {ECO:0000250|UniProtKB:Q9C0E8}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9C0E8}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9C0E8}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9C0E8}. Note=Localizes at endoplasmic reticulum
CC (ER) three-way tubular junctions, which represent crossing-points at
CC which the tubules build a polygonal network.
CC {ECO:0000250|UniProtKB:Q9C0E8}.
CC -!- TISSUE SPECIFICITY: Expressed in most tissues at basal level, with
CC reinforcement in distal limb buds, genital bud, and in parts of the
CC central nervous system. {ECO:0000269|PubMed:12732147}.
CC -!- DEVELOPMENTAL STAGE: Strongly expressed in both limb and genital buds
CC as is the case for Evx2 and Hoxd genes, in particular Hoxd13. In
CC developing limb buds, it is first seen in 10.5 days old fetuses, in the
CC posterior distal bud, to subsequently extend throughout the distal
CC aspect, in presumptive digits. {ECO:0000269|PubMed:12732147}.
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. Transmembrane domain 1 and 2 are probably sufficient to
CC mediate membrane translocation and topology formation in a N-
CC myristoylation-independent manner. Transmembrane domain 2 is sufficient
CC to block the protein secretion pathway. The two coiled-coil domains are
CC necessary for its endoplasmic reticulum (ER) three-way tubular junction
CC localization. The C4-type zinc finger motif is necessary both for its
CC ER three-way tubular junction localization and formation.
CC {ECO:0000250|UniProtKB:Q9C0E8}.
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 {ECO:0000250|UniProtKB:Q9C0E8}.
CC -!- PTM: Phosphorylated. Phosphorylation occurs at Ser-177, Ser-182, Ser-
CC 222, Ser-316 and Ser-380 during interphase. Phosphorylation occurs at
CC Ser-114, Ser-153, Ser-194, Thr-211 and Ser-348 during mitosis; these
CC phosphorylations reduce both its homodimerization and the ER three-way
CC tubular junction formation. {ECO:0000250|UniProtKB:Q9C0E8}.
CC -!- PTM: Subject to proteasomal degradation following phosphorylation
CC during mitosis. {ECO:0000250|UniProtKB:Q9C0E8}.
CC -!- MISCELLANEOUS: Was named 'Lunapark' because the protein sequence
CC contains the word 'LNPARK'.
CC -!- SIMILARITY: Belongs to the lunapark family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32519.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BC060153; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY312281; AAP76388.1; -; mRNA.
DR EMBL; AK173241; BAD32519.1; ALT_INIT; mRNA.
DR EMBL; AK136506; BAE23015.1; -; mRNA.
DR EMBL; AL928644; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC057961; AAH57961.2; -; mRNA.
DR EMBL; BC060153; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS16137.1; -.
DR RefSeq; NP_001103679.1; NM_001110209.1.
DR RefSeq; NP_081409.1; NM_027133.3.
DR RefSeq; XP_006500208.1; XM_006500145.3.
DR RefSeq; XP_006500209.1; XM_006500146.3.
DR AlphaFoldDB; Q7TQ95; -.
DR SMR; Q7TQ95; -.
DR IntAct; Q7TQ95; 1.
DR STRING; 10090.ENSMUSP00000066891; -.
DR iPTMnet; Q7TQ95; -.
DR PhosphoSitePlus; Q7TQ95; -.
DR SwissPalm; Q7TQ95; -.
DR EPD; Q7TQ95; -.
DR jPOST; Q7TQ95; -.
DR MaxQB; Q7TQ95; -.
DR PaxDb; Q7TQ95; -.
DR PeptideAtlas; Q7TQ95; -.
DR PRIDE; Q7TQ95; -.
DR ProteomicsDB; 290135; -.
DR Antibodypedia; 3018; 18 antibodies from 8 providers.
DR Ensembl; ENSMUST00000064503; ENSMUSP00000066891; ENSMUSG00000009207.
DR GeneID; 69605; -.
DR KEGG; mmu:69605; -.
DR UCSC; uc008kdq.2; mouse.
DR CTD; 80856; -.
DR MGI; MGI:1918115; Lnpk.
DR VEuPathDB; HostDB:ENSMUSG00000009207; -.
DR eggNOG; KOG2846; Eukaryota.
DR GeneTree; ENSGT00390000001859; -.
DR InParanoid; Q7TQ95; -.
DR OMA; VSFWPWK; -.
DR OrthoDB; 1595535at2759; -.
DR PhylomeDB; Q7TQ95; -.
DR TreeFam; TF315086; -.
DR BioGRID-ORCS; 69605; 0 hits in 69 CRISPR screens.
DR ChiTaRS; Lnpk; mouse.
DR PRO; PR:Q7TQ95; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q7TQ95; protein.
DR Bgee; ENSMUSG00000009207; Expressed in manus and 239 other tissues.
DR ExpressionAtlas; Q7TQ95; baseline and differential.
DR Genevisible; Q7TQ95; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0071782; C:endoplasmic reticulum tubular network; IBA:GO_Central.
DR GO; GO:0098826; C:endoplasmic reticulum tubular network membrane; ISS:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007596; P:blood coagulation; IMP:MGI.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IGI:MGI.
DR GO; GO:0035115; P:embryonic forelimb morphogenesis; IMP:MGI.
DR GO; GO:0007029; P:endoplasmic reticulum organization; ISO:MGI.
DR GO; GO:0071788; P:endoplasmic reticulum tubular network maintenance; ISS:UniProtKB.
DR GO; GO:0071786; P:endoplasmic reticulum tubular network organization; IBA:GO_Central.
DR GO; GO:1903373; P:positive regulation of endoplasmic reticulum tubular network organization; ISS:UniProtKB.
DR GO; GO:0032330; P:regulation of chondrocyte differentiation; IMP:MGI.
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 Coiled coil; Developmental protein; Endoplasmic reticulum; 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:0000250|UniProtKB:Q9C0E8"
FT CHAIN 2..425
FT /note="Endoplasmic reticulum junction formation protein
FT lunapark"
FT /id="PRO_0000248311"
FT TOPO_DOM 2..45
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..77
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..425
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT ZN_FING 271..296
FT /note="C4-type; plays a role in ER morphology"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT REGION 144..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 15..41
FT /evidence="ECO:0000255"
FT COILED 101..128
FT /evidence="ECO:0000255"
FT COMPBIAS 166..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT MOD_RES 211
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0E8"
SQ SEQUENCE 425 AA; 47500 MW; 829A31984BB48DD6 CRC64;
MGGLFSRWRA KPSTVEVLEN IDKEIQALEE FREKNQRLQK LWVGRLIIYS SILYLFTCLI
VYLWYLPDEF TARLVMTLPF FAFPLIIWTL RTVLIFFFSK RTERNNEALD DLKSQKKKIL
EEVMEKETYK TAKLILERFD PDSKKAKEFE PPSAGAAVTA KPGQEIRQRT AAQRNLSPAP
ASSSQGPPPQ GPVSPGPAKD ASAPGGPPER TVAPALPRRL GSPATSVPGM GLHPPGPPLA
RPILPRERGA LDRIVEYLVG DGPQNRYALI CQQCFSHNGM ALKEEFEYIA FRCAYCFFLN
PARKTRPQAP RLPEFSFEKR QAVEGSSSTG PTLLESVPSA ESQLIEDSLE EQDVLDNSTE
QRDDKIPVTE QTSQVIEKTS GPEEPAENQE ETENEETSTN EAKSPVLRAD SVPNLEPSEE
SLVTK
