RABL6_BOVIN
ID RABL6_BOVIN Reviewed; 701 AA.
AC Q08DA0;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Rab-like protein 6;
DE AltName: Full=GTP-binding protein Parf;
DE AltName: Full=Rab-like protein 1;
DE Short=RBEL1;
GN Name=RABL6; Synonyms=PARF;
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 [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May enhance cellular proliferation. May reduce growth
CC inhibitory activity of CDKN2A (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q3YEC7}. Note=Predominantly cytoplasmic.
CC {ECO:0000250|UniProtKB:Q3YEC7}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; BC123865; AAI23866.1; -; mRNA.
DR RefSeq; NP_001070285.1; NM_001076817.1.
DR AlphaFoldDB; Q08DA0; -.
DR SMR; Q08DA0; -.
DR STRING; 9913.ENSBTAP00000001237; -.
DR PaxDb; Q08DA0; -.
DR PRIDE; Q08DA0; -.
DR Ensembl; ENSBTAT00000001237; ENSBTAP00000001237; ENSBTAG00000039573.
DR GeneID; 508218; -.
DR KEGG; bta:508218; -.
DR CTD; 55684; -.
DR VEuPathDB; HostDB:ENSBTAG00000039573; -.
DR VGNC; VGNC:33674; RABL6.
DR eggNOG; KOG0084; Eukaryota.
DR GeneTree; ENSGT00390000016002; -.
DR HOGENOM; CLU_012780_1_0_1; -.
DR InParanoid; Q08DA0; -.
DR OMA; SKWRQSP; -.
DR OrthoDB; 930319at2759; -.
DR TreeFam; TF313974; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000039573; Expressed in retina and 103 other tissues.
DR ExpressionAtlas; Q08DA0; baseline.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR040385; RABL6.
DR PANTHER; PTHR14932; PTHR14932; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51419; RAB; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; GTP-binding; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..701
FT /note="Rab-like protein 6"
FT /id="PRO_0000274222"
FT REGION 39..279
FT /note="Small GTPase-like"
FT REGION 279..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..667
FT /note="Interaction with CDKN2A"
FT /evidence="ECO:0000250"
FT COMPBIAS 282..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..345
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..573
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..625
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..674
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 50..57
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 100..104
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 177..179
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q3YEC7"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3YEC7"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3YEC7"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3YEC7"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U3K5"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U3K5"
FT MOD_RES 552
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3YEC7"
FT MOD_RES 570
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3YEC7"
FT MOD_RES 573
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q3YEC7"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3YEC7"
FT MOD_RES 615
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3YEC7"
SQ SEQUENCE 701 AA; 77097 MW; F719D2989CB1400A CRC64;
MFSALKKLVG SEQAPGRDRN IPAGLQSMNQ ALQRRFAKGV QYNMKIVIRG DRNTGKTALW
HRLQGKKFVE EYIPTQEIQV TSIHWSYKTT DDVVKVEVWD VVDKGKCKKR GDGLKMENDP
QEAESEMALD AEFLDVYKNC NGVVMMFDIT KQWTFNYILR ELPKVPTHVP VCVLGNYRDM
GEHRVILPDD VRDVLDHLDR PPGSSYFRYA ESSMKNSFGL KYLHRFFNIP FLQLQRETLL
RQLETNQLDI DATLEELSVQ QETEDQNYDI FLEMMEARSR GHASPLTTSG QSPSSGSQSP
VVPPSTVSTG SSSPSTPQPV LQPPLQAPPA PPAPAEAPPL PAAPPRRSII ARLFGSTPAT
EAAPPPPEPT PAAEASQKVQ NVEDFVPEDS LDGSFLEDTV PAKDEKRLGA RGPQDSDSDR
ETQAGNPMVA GFQDDVDLED KPPSRPLPPT GPVPSEDITL SSEEEAEEGA GHPKAAVLAP
QKCPEPETRR SSTKALGPPR DAAPRAAKPR PEGPSGKLEE GTDKPVSSES DAEGPIAAQM
LSFVMDDPDF ESDSDAQRRA GEFPVREDLS DLTDEDAGPV QPPAPPKPLA PSFRLKDDSD
LFGLGLEEPG REDSSEQDKE GRPPAKEKKK KKKKGREEED KAAKKRSKHK KSRERADDKG
RDERRRRPRG PQRTALDELE AFLGGGAPSG PLRGGGDYEA L
