ID A6HMC4_RAT Unreviewed; 302 AA. AC A6HMC4; DT 28-JUN-2023, integrated into UniProtKB/TrEMBL. DT 28-JUN-2023, sequence version 1. DT 08-NOV-2023, entry version 3. DE RecName: Full=Endoplasmic reticulum junction formation protein lunapark {ECO:0000256|RuleBase:RU367073}; GN Name=Lnp_predicted {ECO:0000313|EMBL:EDL79176.1}; GN ORFNames=rCG_27205 {ECO:0000313|EMBL:EDL79176.1}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|EMBL:EDL79176.1, ECO:0000313|Proteomes:UP000234681}; RN [1] {ECO:0000313|Proteomes:UP000234681} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BN, Sprague-Dawley {ECO:0000313|Proteomes:UP000234681}; RA Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H., RA Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M., RA Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L., Lu F., RA Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C., Sutton G.G., RA Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Plays a role in determining ER morphology. CC {ECO:0000256|RuleBase:RU367073}. CC -!- SUBUNIT: Homodimer; homodimerization requires the C4-type zinc finger CC motif and decreases during mitosis in a phosphorylation-dependent CC manner. {ECO:0000256|RuleBase:RU367073}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004215, ECO:0000256|RuleBase:RU367073}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004215, CC ECO:0000256|RuleBase:RU367073}; Cytoplasmic side CC {ECO:0000256|ARBA:ARBA00004215, ECO:0000256|RuleBase:RU367073}. CC -!- DOMAIN: The C4-type zinc finger motif is necessary both for its ER CC three-way tubular junction localization and formation. CC {ECO:0000256|RuleBase:RU367073}. CC -!- SIMILARITY: Belongs to the lunapark family. CC {ECO:0000256|ARBA:ARBA00009940, ECO:0000256|RuleBase:RU367073}. 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; CH473949; EDL79176.1; -; Genomic_DNA. DR Proteomes; UP000234681; Chromosome 3. DR GO; GO:0098826; C:endoplasmic reticulum tubular network membrane; IEA:UniProtKB-UniRule. DR GO; GO:0042802; F:identical protein binding; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0071788; P:endoplasmic reticulum tubular network maintenance; IEA:UniProtKB-UniRule. DR GO; GO:1903373; P:positive regulation of endoplasmic reticulum tubular network organization; IEA:UniProtKB-UniRule. 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. PE 3: Inferred from homology; KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU367073}; KW Metal-binding {ECO:0000256|RuleBase:RU367073}; KW Zinc {ECO:0000256|RuleBase:RU367073}; KW Zinc-finger {ECO:0000256|RuleBase:RU367073}. FT DOMAIN 128..177 FT /note="Lunapark" FT /evidence="ECO:0000259|Pfam:PF10058" FT REGION 1..121 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 184..302 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..26 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 43..58 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 198..222 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 245..259 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 276..302 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 302 AA; 32862 MW; F700CBB02047B8BC CRC64; MEKETYKTAK LILERFDPDS KKAKEFEPPS AGAAATAKPG QEIRQRTAAQ RNLSPAPANS NQGPPPQVPV SPGPSKDASA PGGPPERTVA PALPRRLGSP ATSVPGMGLH PPGPPLARPV LPRERGALDR IVEYLVGDGP QNRYALICQQ CFSHNGMALK EEFEYIAFRC AYCFFLNPAR KTRPQAPRLP EFSFEKRQAV EGSSSTGPML LESVPSPENQ LTEDSLEEQD DLDNSTEQKD DKIPVTEQTN QVIEETSGPE GSEENQEETE NEETSTNEAK SPVLRSDSVS NLELSEDSVV TK //