LLPH_MOUSE
ID LLPH_MOUSE Reviewed; 130 AA.
AC Q9D945; Q3KQP9;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Protein LLP homolog;
DE AltName: Full=Protein LAPS18-like;
GN Name=Llph;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Pancreas, and Visual cortex;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Mammary gland;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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).
RN [4]
RP FUNCTION, INTERACTION WITH CTCF; MYO1C; RNA POLYMERASE II AND TBP,
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND
RP INDUCTION BY EXTRACELLULAR POTASSIUM.
RX PubMed=26961175; DOI=10.1038/srep22892;
RA Yu N.K., Kim H.F., Shim J., Kim S., Kim D.W., Kwak C., Sim S.E., Choi J.H.,
RA Ahn S., Yoo J., Choi S.L., Jang D.J., Lim C.S., Lee Y.S., Kang C.,
RA Choi S.Y., Kaang B.K.;
RT "A transducible nuclear/nucleolar protein, mLLP, regulates neuronal
RT morphogenesis and synaptic transmission.";
RL Sci. Rep. 6:22892-22892(2016).
CC -!- FUNCTION: In hippocampal neurons, regulates dendritic and spine growth
CC and synaptic transmission. {ECO:0000269|PubMed:26961175}.
CC -!- SUBUNIT: Interacts with CTCF, MYO1C and with the transcriptional
CC machinery, including RNA polymerase II and TBP.
CC {ECO:0000269|PubMed:26961175}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:26961175}.
CC Chromosome {ECO:0000250|UniProtKB:Q9BRT6}. Note=Cell-permeable protein.
CC 22 hours after injection in the hippocampal area CA1, internalized by
CC most cells at the injection site (PubMed:26961175). Localizes at the
CC chromosome periphery during mitosis (By similarity).
CC {ECO:0000250|UniProtKB:Q9BRT6, ECO:0000269|PubMed:26961175}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D945-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D945-2; Sequence=VSP_022719;
CC -!- TISSUE SPECIFICITY: Widely expressed, with high levels in testis and
CC spleen and low levels in heart. In the brain, expressed in the cortex
CC and hippocampus, and at very low levels in the cerebellum.
CC {ECO:0000269|PubMed:26961175}.
CC -!- DEVELOPMENTAL STAGE: Strongly expressed in the brain in early
CC developmental stages. Expression gradually decreases during
CC development, from very high levels at 13 dpc down to hardly detectable
CC in the adult at day 20 postnatal and later on (at protein level).
CC {ECO:0000269|PubMed:26961175}.
CC -!- INDUCTION: In the hippocampal neurons, down-regulated by sustained
CC activity induced by increased extracellular potassium concentration for
CC a prolonged time (2 - 5 hours) (at protein level).
CC {ECO:0000269|PubMed:26961175}.
CC -!- SIMILARITY: Belongs to the learning-associated protein family.
CC {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; AK004503; BAC25084.1; -; mRNA.
DR EMBL; AK007375; BAB24995.1; -; mRNA.
DR EMBL; AK158700; BAE34617.1; -; mRNA.
DR EMBL; BC024098; AAH24098.1; -; mRNA.
DR EMBL; BC096681; AAH96681.1; -; mRNA.
DR EMBL; BC106103; AAI06104.1; -; mRNA.
DR CCDS; CCDS24206.1; -. [Q9D945-1]
DR RefSeq; NP_079707.1; NM_025431.2. [Q9D945-1]
DR RefSeq; XP_006514017.1; XM_006513954.1. [Q9D945-1]
DR AlphaFoldDB; Q9D945; -.
DR SMR; Q9D945; -.
DR STRING; 10090.ENSMUSP00000020444; -.
DR iPTMnet; Q9D945; -.
DR PhosphoSitePlus; Q9D945; -.
DR EPD; Q9D945; -.
DR MaxQB; Q9D945; -.
DR PaxDb; Q9D945; -.
DR PeptideAtlas; Q9D945; -.
DR PRIDE; Q9D945; -.
DR ProteomicsDB; 292337; -. [Q9D945-1]
DR ProteomicsDB; 292338; -. [Q9D945-2]
DR Antibodypedia; 53204; 108 antibodies from 19 providers.
DR DNASU; 66225; -.
DR Ensembl; ENSMUST00000020444; ENSMUSP00000020444; ENSMUSG00000020224. [Q9D945-1]
DR Ensembl; ENSMUST00000130198; ENSMUSP00000118254; ENSMUSG00000020224. [Q9D945-1]
DR GeneID; 66225; -.
DR KEGG; mmu:66225; -.
DR UCSC; uc007hfa.1; mouse. [Q9D945-1]
DR CTD; 84298; -.
DR MGI; MGI:1913475; Llph.
DR VEuPathDB; HostDB:ENSMUSG00000020224; -.
DR eggNOG; KOG4811; Eukaryota.
DR GeneTree; ENSGT00390000012979; -.
DR HOGENOM; CLU_134502_0_0_1; -.
DR InParanoid; Q9D945; -.
DR OMA; PVWMNPR; -.
DR PhylomeDB; Q9D945; -.
DR TreeFam; TF314654; -.
DR BioGRID-ORCS; 66225; 7 hits in 69 CRISPR screens.
DR ChiTaRS; Llph; mouse.
DR PRO; PR:Q9D945; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9D945; protein.
DR Bgee; ENSMUSG00000020224; Expressed in morula and 104 other tissues.
DR ExpressionAtlas; Q9D945; baseline and differential.
DR Genevisible; Q9D945; MM.
DR GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0001099; F:basal RNA polymerase II transcription machinery binding; IDA:UniProtKB.
DR GO; GO:0097484; P:dendrite extension; IMP:UniProtKB.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; IMP:UniProtKB.
DR InterPro; IPR018784; LAPS18-like.
DR PANTHER; PTHR34253; PTHR34253; 1.
DR Pfam; PF10169; Laps; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosome; Coiled coil; Isopeptide bond; Nucleus;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..130
FT /note="Protein LLP homolog"
FT /id="PRO_0000274347"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 10..78
FT /evidence="ECO:0000255"
FT COMPBIAS 1..18
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..123
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 78
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BRT6"
FT VAR_SEQ 69
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022719"
SQ SEQUENCE 130 AA; 15391 MW; CD4991D7360EC23E CRC64;
MAKSLRSKWK RKMRAEKRKK NAPRELNRLK SILRVDGDAL MKDVEEIATV VVAKPRQEKM
QCEEGRCDGA DEEKDDMKME TEIKRNRKTL LDQHGQYPVW MNQRQRKRLK AKREKKRGKS
RAKAAKGLAW
