L2GL1_RAT
ID L2GL1_RAT Reviewed; 1036 AA.
AC Q8K4K5;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Lethal(2) giant larvae protein homolog 1;
DE Short=LLGL;
DE AltName: Full=Rgl-1;
GN Name=Llgl1; Synonyms=Rgl1;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=12012002;
RA Kim Y.-S., Baek K.-H., Lee K.Y., Chung H.-M., Lee K.-A., Ko J.J., Cha K.Y.;
RT "The rgl-1 is a legitimate homologue of lethal giant larvae recessive
RT oncogene in rat.";
RL Int. J. Oncol. 20:1219-1225(2002).
RN [2]
RP FUNCTION IN AXON DEVELOPMENT, INTERACTION WITH RAB10, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=21856246; DOI=10.1016/j.devcel.2011.07.007;
RA Wang T., Liu Y., Xu X.H., Deng C.Y., Wu K.Y., Zhu J., Fu X.Q., He M.,
RA Luo Z.G.;
RT "Lgl1 activation of rab10 promotes axonal membrane trafficking underlying
RT neuronal polarization.";
RL Dev. Cell 21:431-444(2011).
CC -!- FUNCTION: Cortical cytoskeleton protein found in a complex involved in
CC maintaining cell polarity and epithelial integrity. Involved in the
CC regulation of mitotic spindle orientation, proliferation,
CC differentiation and tissue organization of neuroepithelial cells.
CC Involved in axonogenesis through RAB10 activation thereby regulating
CC vesicular membrane trafficking toward the axonal plasma membrane.
CC {ECO:0000269|PubMed:21856246}.
CC -!- SUBUNIT: Associated with nonmuscle myosin II heavy chain. Interacts
CC with PRKCI/aPKC, PARD6B/Par-6 and PARD6A. Interacts with STX4A.
CC Interacts with DCAF1 (By similarity). Interacts with RAB10 (GDP-bound
CC form); the interaction is direct and promotes RAB10 association with
CC membranes and activation through competition with the Rab inhibitor
CC GDI1. {ECO:0000250, ECO:0000269|PubMed:21856246}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000269|PubMed:21856246}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000269|PubMed:21856246}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:21856246}. Cell projection, axon
CC {ECO:0000269|PubMed:21856246}. Cytoplasm, cytoskeleton {ECO:0000250}.
CC Note=Localized to the lateral membrane during the polarization and
CC formation cell-cell contacts (By similarity). Enriched in developing
CC axons. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed at high level in the testis and at lower
CC level in ovary, brain, spleen and kidney. {ECO:0000269|PubMed:12012002,
CC ECO:0000269|PubMed:21856246}.
CC -!- PTM: Phosphorylated by PRKCI.
CC -!- MISCELLANEOUS: Complements a salt-sensitive yeast mutant (SOP-deleted
CC mutant) and thus can regulate cation homeostasis.
CC -!- SIMILARITY: Belongs to the WD repeat L(2)GL family. {ECO:0000305}.
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DR EMBL; AF356187; AAM95877.1; -; mRNA.
DR AlphaFoldDB; Q8K4K5; -.
DR SMR; Q8K4K5; -.
DR BioGRID; 248488; 1.
DR STRING; 10116.ENSRNOP00000005366; -.
DR iPTMnet; Q8K4K5; -.
DR PhosphoSitePlus; Q8K4K5; -.
DR PaxDb; Q8K4K5; -.
DR PRIDE; Q8K4K5; -.
DR UCSC; RGD:3012; rat.
DR RGD; 3012; Llgl1.
DR eggNOG; KOG1983; Eukaryota.
DR InParanoid; Q8K4K5; -.
DR PhylomeDB; Q8K4K5; -.
DR PRO; PR:Q8K4K5; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
DR GO; GO:0030864; C:cortical actin cytoskeleton; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005856; C:cytoskeleton; ISO:RGD.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0000137; C:Golgi cis cisterna; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035748; C:myelin sheath abaxonal region; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032588; C:trans-Golgi network membrane; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0045159; F:myosin II binding; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; IMP:UniProtKB.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; ISO:RGD.
DR GO; GO:0051294; P:establishment of spindle orientation; IBA:GO_Central.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IMP:UniProtKB.
DR GO; GO:0035090; P:maintenance of apical/basal cell polarity; ISO:RGD.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:RGD.
DR GO; GO:0032878; P:regulation of establishment or maintenance of cell polarity; IBA:GO_Central.
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; IPR013905; Lgl_C_dom.
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; PF08596; Lgl_C; 1.
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; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cytoplasm; Cytoskeleton; Endosome; Exocytosis;
KW Golgi apparatus; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW WD repeat.
FT CHAIN 1..1036
FT /note="Lethal(2) giant larvae protein homolog 1"
FT /id="PRO_0000232727"
FT REPEAT 38..71
FT /note="WD 1"
FT REPEAT 78..119
FT /note="WD 2"
FT REPEAT 139..175
FT /note="WD 3"
FT REPEAT 199..233
FT /note="WD 4"
FT REPEAT 239..271
FT /note="WD 5"
FT REPEAT 289..331
FT /note="WD 6"
FT REPEAT 339..373
FT /note="WD 7"
FT REPEAT 395..473
FT /note="WD 8"
FT REPEAT 517..592
FT /note="WD 9"
FT REPEAT 601..662
FT /note="WD 10"
FT REPEAT 722..782
FT /note="WD 11"
FT REPEAT 791..843
FT /note="WD 12"
FT REPEAT 848..901
FT /note="WD 13"
FT REPEAT 915..938
FT /note="WD 14"
FT REGION 669..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 980..1002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 662
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15334"
FT MOD_RES 957
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q80Y17"
FT MOD_RES 964
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80Y17"
FT MOD_RES 982
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80Y17"
FT MOD_RES 989
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80Y17"
SQ SEQUENCE 1036 AA; 112495 MW; 4D15B5768FF76023 CRC64;
MMKFRFRRQG ADPQREKLKQ ELFTFHKTVE HGFPNQPSAL AFDPELRIMA IGTRSGAVKI
YGAPGVEFTG LHRDAATVTQ MHFLPGQGRL LTLLDDSSLH LWEIIQRNGC AHLEEGLSFH
PPSRPSFGNA SFPAGLTRVT VVLLAAGDTV VLGTESGSIF FLDVATLALL EGQTLSPDEV
LRSVPDDYRC GKALGPVESL QGHLQDPSKI LIGYSRGLLV IWSQATQSVE HVFLGNQQLE
SLCWGRGGSN IISSHSDGSY AIWSTDTGSP PTLQPTVVTT PYGPFPCKAI NKILWRSCES
GDHFIIFSGG MPRASYGDRH CVSVLRAETL VTLDFTSRVI DFFTVHSTQP EDGFDNPQAL
AVLLEEELVV LDLQTPGWPA VPAPYLAPLH SSAITCSAHV ANVPSKLWAR IVSAGERQSP
QPASSALSWP ITGGRNLAQE PSQRGLLLTG HEDGTVRFWD ASGVALRPLY KLSTAGLFQT
DCEHADSLAQ AVEDDWPPFR KVGCFDPYSD DPRLGIQKVA LCKYTAQMVV AGTAGQVLVL
ELSDVPGEHT VSVASVDLLQ DREGFTWKGH ERLSPHTGPL PWPAGFQPRV LIQCLPPAAV
TAVALHAEWS LVAFGTSHGF GLFDYQRKSP VLARCTLHPN DSLAMEGPLS RVKSLKKSLR
QSFRRIRKSR VSGKKRATTA SSKLQEANAQ LAEQTCPHDV EMTPVQRRIE PRSADDSLSG
VVRCLYFADT FLRDATHHGP TMWAGTNSGS VFAYALEVPA ATAGGEKRPE QAVEAVLGKE
VQLMHRAPVV AIAVLDGRGR PLPEPYEASR DLAQAPDMQG GHAVLIASEE QFKVFTLPKV
SAKTKFKLTA HEGCRVRKVA LATFASVMSE DYAETCLACL TNLGDVHVFS VPGLRPQVHY
SCIRKEDISG IASCVFTRHG QGFYLISPSE FERFSLSARN ITEPLCSLDI SWPQNATQPR
LQESPKLSQA NGTRDIILAP ESCEGSPSSA HSKRADTMEP PEAALSPVSI DSAASGDTML
DTTGDVTVEY VKDFLG
