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Lethal(2) giant larvae protein homolog 1 (LLGL) (DLG4) (Hugl-1) (Human homolog to the D-lgl gene protein)

 L2GL1_HUMAN             Reviewed;        1064 AA.
Q15334; A7MBM7; O00188; Q58F11; Q86UK6;
18-APR-2006, integrated into UniProtKB/Swiss-Prot.
22-SEP-2009, sequence version 3.
20-JUN-2018, entry version 149.
RecName: Full=Lethal(2) giant larvae protein homolog 1;
Short=LLGL;
AltName: Full=DLG4;
AltName: Full=Hugl-1;
AltName: Full=Human homolog to the D-lgl gene protein;
Name=LLGL1; Synonyms=DLG4, HUGL, HUGL1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
INTERACTION WITH MYOSIN II HEAVY CHAIN, AND VARIANTS GLY-148 AND
HIS-550.
TISSUE=Brain;
PubMed=7542763;
Strand D.J., Unger S., Corvi R., Hartenstein K., Schenkel H.,
Kalmes A., Merdes G., Neumann B., Kreig-Schneider F., Coy J.F.,
Poustka A., Schwab M., Mechler B.;
"A human homologue of the Drosophila tumour suppressor gene l(2)gl
maps to 17p11.2-12 and codes for a cytoskeletal protein that
associates with nonmuscle myosin II heavy chain.";
Oncogene 11:291-301(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLY-148.
TISSUE=Brain;
PubMed=8565641;
Koyama K., Fukushima Y., Inazawa J., Tomotsune D., Takahashi N.,
Nakamura Y.;
"The human homologue of the murine Llglh gene (LLGL) maps within the
Smith-Magenis syndrome region in 17p11.2.";
Cytogenet. Cell Genet. 72:78-82(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-148.
TISSUE=Fetal brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH PARD6B/PAR-6 AND PRKCI/APKC, SUBCELLULAR LOCATION,
AND PHOSPHORYLATION AT SER-663.
PubMed=12725730; DOI=10.1016/S0960-9822(03)00244-6;
Yamanaka T., Horikoshi Y., Sugiyama Y., Ishiyama C., Suzuki A.,
Hirose T., Iwamatsu A., Shinohara A., Ohno S.;
"Mammalian Lgl forms a protein complex with PAR-6 and aPKC
independently of PAR-3 to regulate epithelial cell polarity.";
Curr. Biol. 13:734-743(2003).
[5]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=15735678; DOI=10.1038/sj.onc.1208520;
Schimanski C.C., Schmitz G., Kashyap A., Bosserhoff A.K., Bataille F.,
Schafer S.C., Lehr H.A., Berger M.R., Galle P.R., Strand S.,
Strand D.;
"Reduced expression of Hugl-1, the human homologue of Drosophila
tumour suppressor gene lgl, contributes to progression of colorectal
cancer.";
Oncogene 24:3100-3109(2005).
[6]
FUNCTION, TISSUE SPECIFICITY, AND INVOLVEMENT IN COLORECTAL CANCER AND
MELANOMA.
PubMed=16170365; DOI=10.1038/sj.onc.1209008;
Kuphal S., Wallner S., Schimanski C.C., Bataille F., Hofer P.,
Strand S., Strand D., Bosserhoff A.K.;
"Expression of Hugl-1 is strongly reduced in malignant melanoma.";
Oncogene 25:103-110(2006).
[7]
INTERACTION WITH DCAF1.
PubMed=20644714; DOI=10.1371/journal.pbio.1000422;
Tamori Y., Bialucha C.U., Tian A.G., Kajita M., Huang Y.C., Norman M.,
Harrison N., Poulton J., Ivanovitch K., Disch L., Liu T., Deng W.M.,
Fujita Y.;
"Involvement of Lgl and Mahjong/VprBP in cell competition.";
PLoS Biol. 8:E1000422-E1000422(2010).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
-!- FUNCTION: Cortical cytoskeleton protein found in a complex
involved in maintaining cell polarity and epithelial integrity.
Involved in the regulation of mitotic spindle orientation,
proliferation, differentiation and tissue organization of
neuroepithelial cells. Involved in axonogenesis through RAB10
activation thereby regulating vesicular membrane trafficking
toward the axonal plasma membrane. {ECO:0000269|PubMed:15735678,
ECO:0000269|PubMed:16170365}.
-!- SUBUNIT: Associated with nonmuscle myosin II heavy chain.
Interacts with PRKCI/aPKC, PARD6B/Par-6 and PARD6A. Interacts with
STX4A (By similarity). Interacts with RAB10 (GDP-bound form); the
interaction is direct and promotes RAB10 association with
membranes and activation through competition with the Rab
inhibitor GDI1 (By similarity). Interacts with DCAF1.
{ECO:0000250, ECO:0000269|PubMed:12725730,
ECO:0000269|PubMed:20644714, ECO:0000269|PubMed:7542763}.
-!- SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250}. Golgi
apparatus, trans-Golgi network membrane {ECO:0000250}. Golgi
apparatus membrane {ECO:0000250}. Cell projection, axon
{ECO:0000250}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:12725730, ECO:0000269|PubMed:7542763}.
Note=Localized to the lateral membrane during the polarization and
formation cell-cell contacts. Enriched in developping axons (By
similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in brain, kidney, and muscle but is
barely seen in heart and placenta. Down-regulated or lost in all
cell lines and in most of the tumor samples analyzed. Loss was
associated with advanced stage of the disease.
{ECO:0000269|PubMed:15735678, ECO:0000269|PubMed:16170365,
ECO:0000269|PubMed:7542763}.
-!- PTM: Phosphorylated at least at Ser-663 by PRKCI.
{ECO:0000269|PubMed:12725730}.
-!- MISCELLANEOUS: Down-regulation of LLGL1 is associated with the
progression of colorectal cancer and melanoma. Located within the
Smith-Magenis syndrome region on chromosome 17; deleted in
patients with this syndrome.
-!- MISCELLANEOUS: Expression increases cell adhesion and decreases
cell migration. Substitutes for Drosophila l(2)gl tumor suppressor
function in vivo.
-!- SIMILARITY: Belongs to the WD repeat L(2)GL family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA19516.1; Type=Frameshift; Positions=205, 216, 737, 740, 794, 799, 866, 872, 881, 945, 968, 1024; Evidence={ECO:0000305};
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EMBL; X86371; CAA60130.1; -; mRNA.
EMBL; D50550; BAA19516.1; ALT_FRAME; mRNA.
EMBL; BC028037; AAH28037.1; -; mRNA.
EMBL; BC151838; AAI51839.1; -; mRNA.
CCDS; CCDS32586.1; -.
PIR; I38171; I38171.
RefSeq; NP_004131.3; NM_004140.3.
UniGene; Hs.513983; -.
ProteinModelPortal; Q15334; -.
BioGrid; 110183; 35.
CORUM; Q15334; -.
IntAct; Q15334; 38.
MINT; Q15334; -.
STRING; 9606.ENSP00000321537; -.
iPTMnet; Q15334; -.
PhosphoSitePlus; Q15334; -.
SwissPalm; Q15334; -.
BioMuta; LLGL1; -.
DMDM; 259016343; -.
EPD; Q15334; -.
MaxQB; Q15334; -.
PaxDb; Q15334; -.
PeptideAtlas; Q15334; -.
PRIDE; Q15334; -.
ProteomicsDB; 60533; -.
DNASU; 3996; -.
Ensembl; ENST00000316843; ENSP00000321537; ENSG00000131899.
Ensembl; ENST00000640494; ENSP00000492144; ENSG00000284137.
GeneID; 3996; -.
KEGG; hsa:3996; -.
UCSC; uc002gsp.4; human.
CTD; 3996; -.
DisGeNET; 3996; -.
EuPathDB; HostDB:ENSG00000131899.10; -.
GeneCards; LLGL1; -.
HGNC; HGNC:6628; LLGL1.
HPA; HPA022924; -.
HPA; HPA023569; -.
MIM; 600966; gene.
neXtProt; NX_Q15334; -.
OpenTargets; ENSG00000131899; -.
PharmGKB; PA30396; -.
eggNOG; KOG1983; Eukaryota.
eggNOG; ENOG410XS6Z; LUCA.
GeneTree; ENSGT00390000000018; -.
HOGENOM; HOG000115700; -.
HOVERGEN; HBG052711; -.
InParanoid; Q15334; -.
KO; K06094; -.
OMA; GHLRDPT; -.
OrthoDB; EOG091G01L0; -.
PhylomeDB; Q15334; -.
TreeFam; TF314585; -.
GeneWiki; LLGL1; -.
GenomeRNAi; 3996; -.
PRO; PR:Q15334; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000131899; -.
CleanEx; HS_DLG4; -.
CleanEx; HS_LLGL1; -.
ExpressionAtlas; Q15334; baseline and differential.
Genevisible; Q15334; HS.
GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
GO; GO:0030864; C:cortical actin cytoskeleton; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; TAS:ProtInc.
GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
GO; GO:0000137; C:Golgi cis cisterna; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0032588; C:trans-Golgi network membrane; ISS:UniProtKB.
GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IDA:UniProtKB.
GO; GO:0017137; F:Rab GTPase binding; IBA:GO_Central.
GO; GO:0005198; F:structural molecule activity; TAS:ProtInc.
GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
GO; GO:0030866; P:cortical actin cytoskeleton organization; IDA:UniProtKB.
GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
GO; GO:0006893; P:Golgi to plasma membrane transport; ISS:UniProtKB.
GO; GO:0065003; P:protein-containing complex assembly; IDA:UniProtKB.
GO; GO:0017157; P:regulation of exocytosis; IBA:GO_Central.
GO; GO:0050708; P:regulation of protein secretion; IBA:GO_Central.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR000664; Lethal2_giant.
InterPro; IPR013577; LLGL2.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF08366; LLGL; 1.
Pfam; PF00400; WD40; 1.
PRINTS; PR00962; LETHAL2GIANT.
SMART; SM00320; WD40; 5.
SUPFAM; SSF50978; SSF50978; 4.
PROSITE; PS00678; WD_REPEATS_1; 2.
PROSITE; PS50082; WD_REPEATS_2; 1.
1: Evidence at protein level;
Cell projection; Complete proteome; Cytoplasm; Cytoskeleton; Endosome;
Exocytosis; Golgi apparatus; Membrane; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; WD repeat.
CHAIN 1 1064 Lethal(2) giant larvae protein homolog 1.
/FTId=PRO_0000232725.
REPEAT 38 71 WD 1.
REPEAT 78 119 WD 2.
REPEAT 139 176 WD 3.
REPEAT 200 234 WD 4.
REPEAT 240 272 WD 5.
REPEAT 290 332 WD 6.
REPEAT 340 374 WD 7.
REPEAT 396 474 WD 8.
REPEAT 518 593 WD 9.
REPEAT 602 663 WD 10.
REPEAT 723 783 WD 11.
REPEAT 792 844 WD 12.
REPEAT 849 902 WD 13.
REPEAT 916 939 WD 14.
MOD_RES 663 663 Phosphoserine.
{ECO:0000269|PubMed:12725730}.
MOD_RES 958 958 Phosphothreonine.
{ECO:0000250|UniProtKB:Q80Y17}.
MOD_RES 967 967 Phosphoserine.
{ECO:0000250|UniProtKB:Q80Y17}.
MOD_RES 985 985 Phosphoserine.
{ECO:0000250|UniProtKB:Q80Y17}.
VARIANT 148 148 S -> G (in dbSNP:rs2290505).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:7542763,
ECO:0000269|PubMed:8565641}.
/FTId=VAR_058710.
VARIANT 550 550 Q -> H (in dbSNP:rs1063683).
{ECO:0000269|PubMed:7542763}.
/FTId=VAR_058711.
CONFLICT 5 5 R -> P (in Ref. 1; CAA60130).
{ECO:0000305}.
CONFLICT 152 152 A -> G (in Ref. 2; BAA19516).
{ECO:0000305}.
CONFLICT 159 159 S -> SS (in Ref. 1; CAA60130).
{ECO:0000305}.
CONFLICT 194 194 A -> D (in Ref. 1; CAA60130).
{ECO:0000305}.
CONFLICT 206 206 R -> Q (in Ref. 1; CAA60130).
{ECO:0000305}.
CONFLICT 216 216 S -> D (in Ref. 2; BAA19516).
{ECO:0000305}.
CONFLICT 223 223 W -> R (in Ref. 1; CAA60130).
{ECO:0000305}.
CONFLICT 226 227 AS -> SR (in Ref. 2; BAA19516).
{ECO:0000305}.
CONFLICT 337 338 TS -> HF (in Ref. 1; CAA60130).
{ECO:0000305}.
CONFLICT 400 400 H -> Y (in Ref. 2; BAA19516).
{ECO:0000305}.
CONFLICT 486 486 A -> S (in Ref. 1; CAA60130).
{ECO:0000305}.
CONFLICT 580 580 P -> L (in Ref. 1; CAA60130).
{ECO:0000305}.
CONFLICT 588 588 Q -> L (in Ref. 2; BAA19516).
{ECO:0000305}.
CONFLICT 590 590 R -> C (in Ref. 1; CAA60130).
{ECO:0000305}.
CONFLICT 624 629 FDYQRK -> L (in Ref. 1; CAA60130).
{ECO:0000305}.
CONFLICT 686 686 Q -> L (in Ref. 2; BAA19516).
{ECO:0000305}.
CONFLICT 781 782 EV -> KE (in Ref. 2; BAA19516).
{ECO:0000305}.
CONFLICT 782 782 V -> L (in Ref. 1; CAA60130).
{ECO:0000305}.
CONFLICT 799 799 Missing (in Ref. 1; CAA60130).
{ECO:0000305}.
CONFLICT 818 818 D -> H (in Ref. 1; CAA60130).
{ECO:0000305}.
CONFLICT 860 860 V -> VV (in Ref. 1; CAA60130).
{ECO:0000305}.
CONFLICT 871 871 E -> R (in Ref. 2; BAA19516).
{ECO:0000305}.
CONFLICT 894 894 Missing (in Ref. 2; BAA19516).
{ECO:0000305}.
CONFLICT 898 898 Q -> E (in Ref. 1; CAA60130).
{ECO:0000305}.
CONFLICT 945 945 P -> G (in Ref. 1; CAA60130).
{ECO:0000305}.
CONFLICT 1060 1064 AILIK -> CI (in Ref. 1; CAA60130).
{ECO:0000305}.
SEQUENCE 1064 AA; 115418 MW; 9318D6736934E4D5 CRC64;
MMKFRFRRQG ADPQREKLKQ ELFAFNKTVE HGFPNQPSAL AFDPELRIMA IGTRSGAVKI
YGAPGVEFTG LHRDAATVTQ MHFLTGQGRL LSLLDDSSLH LWEIVHHNGC AHLEEALSFQ
LPSRPGFDGA SAPLSLTRVT VVLLVAASDI AALGTEGSSV FFLDVTTLTL LEGQTLAPGE
VLRSVPDDYR CGKALGPVES LQGHLRDPTK ILIGYSRGLL VIWNQASQCV DHIFLGNQQL
ESLCWGRDSS TVVSSHSDGS YAVWSVDAGS FPTLQPTVAT TPYGPFPCKA INKILWRNCE
SGGHFIIFSG GMPRASYGDR HCVSVLRAET LVTLDFTSRI IDFFTVHSTR PEDEFDDPQA
LAVLLEEELV VLDLQTPGWP AVPAPYLAPL HSSAITCSAH VASVPAKLWA RIVSAGEQQS
PQPVSSALSW PITGGRNLAQ EPSQRGLLLT GHEDGTVRFW DASGVALRPL YKLSTAGLFQ
TDCEHADSLA QAAEDDWPPF RKVGCFDPYS DDPRLGVQKV ALCKYTAQMV VAGTAGQVLV
LELSDVPVEQ AVSVAIIDLL QDREGFTWKG HERLSPRTGP LPWPAGFQPR VLVQCLPPAA
VTAVTLHTEW SLVAFGTSHG FGLFDYQRKS PVLARCTLHP NDSLAMEGPL SRVKSLKKSL
RQSFRRIRKS RVSGKKRAAN ASSKLQEANA QLAEQACPHD VEMTPVQRRI EPRSADDSLS
GVVRCLYFAD TFLRDGAHHG PTMWAGTNSG SVFAYALEVP AAAVGGEKRP EQAVEAVLGK
EVQLMHRAPV VAIAVLDGRG RPLPEPYEAS RDLAQAPDMQ GGHAVLIASE EQFKVFTLPK
VSAKTKFKLT AHEGCRVRKV ALATFASVAC EDYAETCLAC LTNLGDVHVF SVPGLRPQVH
YSCIRKEDIS GIASCVFTRH GQGFYLISPS EFERFSLSAR NITEPLCSLD INWPRDATQA
SYRIRESPKL SQANGTPSIL LAPQSLDGSP DPAHSMGPDT PEPPEAALSP MSIDSATSAD
TTLDTTGDVT VEDVKDFLGS SEESEKNLRN LAEDEAHACA ILIK


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