L2GL2_MOUSE
ID L2GL2_MOUSE Reviewed; 1027 AA.
AC Q3TJ91; B1ATB0; Q6YP20; Q8K1X0;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=LLGL scribble cell polarity complex component 2;
DE AltName: Full=Lethal giant larvae-like protein 2;
DE AltName: Full=Lethal(2) giant larvae protein homolog 2;
GN Name=Llgl2; Synonyms=Llglh2;
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].
RC STRAIN=C57BL/6J;
RA Zhuang D.Z., Yang Y.-C.;
RT "Mammalian homologs of Drosophila gene l(2)gl in hematopoiesis.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Amnion;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1022, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1022, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, and Pancreas;
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: Part of a complex with GPSM2/LGN, PRKCI/aPKC and PARD6B/Par-
CC 6, which may ensure the correct organization and orientation of bipolar
CC spindles for normal cell division. This complex plays roles in the
CC initial phase of the establishment of epithelial cell polarity (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with GPSM2/LGN, PRKCI/aPKC and PARD6B/Par-6. The
CC complex is enhanced during mitosis. Interacts with DCAF1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Localized in the
CC perinuclear structure and faintly at the cell-cell contacts sites in
CC the interphase. Localized at the cell periphery during metaphase.
CC Cortical localization in mitotic cells (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated at Ser-653 by PRKCI. Phosphorylation is enhanced
CC during cell polarization induced by calcium. Phosphorylation may occur
CC during the cell-cell contact-induced cell polarization and may
CC contribute to the segregation of LLGL2 from the PRKCI/aPKC and
CC PARD6B/Par-6 complex (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat L(2)GL family. {ECO:0000305}.
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DR EMBL; AY033650; AAK52346.1; -; mRNA.
DR EMBL; AK167536; BAE39604.1; -; mRNA.
DR EMBL; AL645647; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL645852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC037226; AAH37226.1; -; mRNA.
DR CCDS; CCDS25649.1; -.
DR RefSeq; NP_001239461.1; NM_001252532.1.
DR RefSeq; NP_663413.2; NM_145438.2.
DR AlphaFoldDB; Q3TJ91; -.
DR SMR; Q3TJ91; -.
DR BioGRID; 229887; 1.
DR STRING; 10090.ENSMUSP00000099321; -.
DR iPTMnet; Q3TJ91; -.
DR PhosphoSitePlus; Q3TJ91; -.
DR EPD; Q3TJ91; -.
DR jPOST; Q3TJ91; -.
DR MaxQB; Q3TJ91; -.
DR PaxDb; Q3TJ91; -.
DR PeptideAtlas; Q3TJ91; -.
DR PRIDE; Q3TJ91; -.
DR ProteomicsDB; 252452; -.
DR Antibodypedia; 19581; 211 antibodies from 26 providers.
DR DNASU; 217325; -.
DR Ensembl; ENSMUST00000103032; ENSMUSP00000099321; ENSMUSG00000020782.
DR GeneID; 217325; -.
DR KEGG; mmu:217325; -.
DR UCSC; uc007mit.1; mouse.
DR CTD; 3993; -.
DR MGI; MGI:1918843; Llgl2.
DR VEuPathDB; HostDB:ENSMUSG00000020782; -.
DR eggNOG; KOG1983; Eukaryota.
DR GeneTree; ENSGT00950000182906; -.
DR HOGENOM; CLU_005214_0_0_1; -.
DR InParanoid; Q3TJ91; -.
DR OrthoDB; 122541at2759; -.
DR PhylomeDB; Q3TJ91; -.
DR TreeFam; TF314585; -.
DR BioGRID-ORCS; 217325; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Llgl2; mouse.
DR PRO; PR:Q3TJ91; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q3TJ91; protein.
DR Bgee; ENSMUSG00000020782; Expressed in retinal neural layer and 181 other tissues.
DR ExpressionAtlas; Q3TJ91; baseline and differential.
DR Genevisible; Q3TJ91; MM.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0045159; F:myosin II binding; IBA:GO_Central.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0060670; P:branching involved in labyrinthine layer morphogenesis; IMP:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0051294; P:establishment of spindle orientation; IBA:GO_Central.
DR GO; GO:0016332; P:establishment or maintenance of polarity of embryonic epithelium; IMP:MGI.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0060716; P:labyrinthine layer blood vessel development; IMP:MGI.
DR GO; GO:0015820; P:leucine transport; ISO:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0001890; P:placenta development; IMP:MGI.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:0032878; P:regulation of establishment or maintenance of cell polarity; ISO:MGI.
DR GO; GO:0008593; P:regulation of Notch signaling pathway; IBA:GO_Central.
DR GO; GO:0050708; P:regulation of protein secretion; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR000664; Lethal2_giant.
DR InterPro; IPR013577; LLGL2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF08366; LLGL; 1.
DR PRINTS; PR00962; LETHAL2GIANT.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 2.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Exocytosis; Phosphoprotein;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1..1027
FT /note="LLGL scribble cell polarity complex component 2"
FT /id="PRO_0000232729"
FT REPEAT 36..69
FT /note="WD 1"
FT REPEAT 76..117
FT /note="WD 2"
FT REPEAT 132..169
FT /note="WD 3"
FT REPEAT 193..227
FT /note="WD 4"
FT REPEAT 233..268
FT /note="WD 5"
FT REPEAT 282..324
FT /note="WD 6"
FT REPEAT 332..366
FT /note="WD 7"
FT REPEAT 388..464
FT /note="WD 8"
FT REPEAT 508..583
FT /note="WD 9"
FT REPEAT 592..653
FT /note="WD 10"
FT REPEAT 715..771
FT /note="WD 11"
FT REPEAT 780..832
FT /note="WD 12"
FT REPEAT 837..890
FT /note="WD 13"
FT REPEAT 904..927
FT /note="WD 14"
FT REGION 654..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..967
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 653
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P1M3"
FT MOD_RES 971
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P1M3"
FT MOD_RES 1022
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CONFLICT 154
FT /note="F -> L (in Ref. 1; AAK52346)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="H -> N (in Ref. 1; AAK52346)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="A -> G (in Ref. 1; AAK52346)"
FT /evidence="ECO:0000305"
FT CONFLICT 480
FT /note="I -> S (in Ref. 1; AAK52346 and 3; AAH37226)"
FT /evidence="ECO:0000305"
FT CONFLICT 683..685
FT /note="IKA -> TKT (in Ref. 1; AAK52346)"
FT /evidence="ECO:0000305"
FT CONFLICT 742
FT /note="G -> S (in Ref. 1; AAK52346)"
FT /evidence="ECO:0000305"
FT CONFLICT 756..760
FT /note="RRTDE -> KKINK (in Ref. 1; AAK52346)"
FT /evidence="ECO:0000305"
FT CONFLICT 765
FT /note="E -> K (in Ref. 1; AAK52346)"
FT /evidence="ECO:0000305"
FT CONFLICT 791
FT /note="L -> I (in Ref. 2; BAE39604)"
FT /evidence="ECO:0000305"
FT CONFLICT 956
FT /note="L -> P (in Ref. 1; AAK52346 and 3; AAH37226)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1027 AA; 114323 MW; 1F36BE1E818CC5BC CRC64;
MRRFLRTGHD PARERLKRDL FQFNKTVEHG FPHQPSALGY SPSLRILAIG TRSGAVKLYG
APGVEFMGLH KENNAVLQIH FLPGQCQLVT LLDDNSLHLW SLKVKGGVSE LQEEESFTLR
GPPGAAPSAT QVTEILPHSS GELLYLGTES GNVFVVQLPG FRTLHDRTIC SDEVLQWLPE
EARHRRVFEM VEALQEHPRD PNQILIGYSR GLVVIWDLQG SRALSHFLSS QQLENASWQR
DGCLIVTCHS DGSHCQWPVS SDTQNPEPLR SSIPYGPFPC KAITKIFWLT TRQGLPFTIF
QGGMPRASYG DRHCISVVHN GQQTAFDFTS RVIDFTVLSE ADPAAAFDDP YALVVLAEEE
LVVIDLQTPG WPPVQLPYLA SLHCSAITCS HHVSNIPLKL WERIIAAGSR QNSHFSTMEW
PIDGGTSLAP PPPQRDLLLT GHEDGTVRFW DASGVCLRLL YKLSTVRVFL TDTDPSENLI
AQGEDEWPPL RKVGSFDPYS DDPRLGIQKI FLCKYSGYLA VAGTAGQVLV LELNDEAAEH
AVEQVEADLL QDQEGYRWKG HERLAARPGP VCFEAGFQPF VLVQCQPPAV VTSLALHSEW
RLVAFGTSHG FGLFDHQQRR QVFVKCTLHP SDQLALEGPL SRVKSLKKSL RQSFRRMRRS
RVSSHKRRPG GPTGEAQAQA VNIKAERTGL QNMELAPVQR KIEARSAEDS FTGFVRTLYF
ADTYLRDSSR HCPSLWAGTN GGTVYAFSLR VPPAERRTDE PVRAEQAKEI QLMHRAPVVG
ILVLDGHNVP LPEPLEVAHD LSKSPDMQGS HQLLVVSEEQ FKVFTLPKVS AKLKLKLTAL
EGSRVRRVGV AHFGSCRAED YGEHHLAVLT NLGDIQVVSM PLLKPQVRYS CIRREDVSGI
ASCVFTKYGQ GFYLISPSEF ERFSLSTKWL VEPRCLVDST KAKKHNRPSN GNGTGLKMTS
SGHVRNSKSQ SDGDEKKPGP VMEHALLNDA WVLKEIQSTL EGDRRSYGNW HPHRVAVGCR
LSNGEAE
