L2GL1_BOVIN
ID L2GL1_BOVIN Reviewed; 1036 AA.
AC Q8MKF0;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Lethal(2) giant larvae protein homolog 1;
DE Short=LLGL;
DE AltName: Full=Bgl-1;
DE AltName: Full=Giant larvae-1;
GN Name=LLGL1; Synonyms=BGL1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=11894119;
RA Baek K.-H., Kim Y.-S., Jung S., Lee K.Y., Choi H.-K., Kim K.-S.;
RT "Molecular cloning and characterization of bovine bgl-1, a novel family
RT member of WD-40 repeat-containing lethal giant larvae tumor suppressor
RT genes.";
RL Int. J. Oncol. 20:739-744(2002).
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 (By
CC similarity). {ECO:0000250}.
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 RAB10 (GDP-bound form); the interaction is direct and
CC promotes RAB10 association with membranes and activation through
CC competition with the Rab inhibitor GDI1. Interacts with DCAF1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250}. Golgi
CC apparatus, trans-Golgi network membrane {ECO:0000250}. Cell projection,
CC axon {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}. Cytoplasm,
CC cytoskeleton {ECO:0000250}. Note=Localized to the lateral membrane
CC during the polarization and formation cell-cell contacts. Enriched in
CC developing axons (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in brain, ovary,
CC testis, with moderate expression in lever, uterus, lung and kidney.
CC {ECO:0000269|PubMed:11894119}.
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; AF435571; AAM20906.1; -; mRNA.
DR AlphaFoldDB; Q8MKF0; -.
DR SMR; Q8MKF0; -.
DR PRIDE; Q8MKF0; -.
DR InParanoid; Q8MKF0; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0000137; C:Golgi cis cisterna; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032588; C:trans-Golgi network membrane; ISS:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR GO; GO:0045159; F:myosin II binding; IBA:GO_Central.
DR GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
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:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; ISS:UniProtKB.
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; 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; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
PE 2: Evidence at transcript 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_0000232724"
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 667..688
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 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; 112663 MW; F936C94F70EB5719 CRC64;
MMKFRFRRQG ADPQREKLKQ ELFAFHKTVE HGFPNQPSAL AFDPELRIMA IGTRSGAVKI
YGAPGVEFTG LHRDAATVTQ MHFLPGQGRL LTLLDDSSLH LWEIIQRNGC AHLEEGLSFH
PPSRPSFDNA SFPAGLTRVT VVLLAAGDTV VLGTESGSIF FLDVATLALL EGQTLSPDEV
LRSVPDDYRC GKALGPVESL QGHLQDPSKI LIGYSRGLLV IWSQATQSVE HVFLGNQQLE
SLCWGRGGSN IISSHSDGSY AIWSTDTGSP PTLQPTVVTT PYGPFPCKAI NKILWRSCES
GDHFIIFSGG MPRASYGDRH CVCVLRAETL VTLDFTSRVI DFFTVHSTQP EDECDNPQAL
AVLLEEELVV LDLQTPGWPA VPAPYLAPLH SSAITCSAHV ANVPSKLWAR IVSAGEQQSP
QPASSALSWP ITGGRNLAQE PSQRGLLLTG HEDGTVRFWD ASGVALRPLY KLSTAGLFQT
DCEHADSLAQ AVEDDWPPFR KVGCFDPYSD DPRLGIQKVA LCKYTAQMVV AGTAGQVLVL
ELSEVPAEHA VSVANVDLLQ DREGFTWKGH ERLNPHTGLL PWPAGFQPRM LIQCLPPAAV
TAVTLHAEWS LVAFGTSHGF GLFDYQRKSP VLARCTLHPN DSLAMEGPLS RVKSLKKSLR
QSFRRIRKSR VSGKKRTPAA SSKLQEANAQ LAEQTCPHDL EMTPVQRRIE PRSADDSLSG
VVRCLYFADT FLRDATHHGP TMWAGTNSGS VFAYALEVPA ATAGGEKRPE QAVEAVLGKE
VQLMHRAPVV AIAVLDGRGR PLPEPYEASR DLAQAPDMQG GHAVLIASEE QFKVFTLPKV
SAKTKFKLTA HEGCRVRKVA LATFASVMSE DYAETCLACL TNLGDVHVFA VPGLRPQVHY
SCIRKEDISG IASCVFTRHG QGFYLISPSE FERFSLSARN ITEPLCSLDI SWPQNATQPR
LQESPKLSQA NGTRDIILAP ESCEGSPSSA HSKRADTMEP PEAALSPVSI DSAASGDTML
DTTGDVTVEY VKDFLG
