RAB28_RAT
ID RAB28_RAT Reviewed; 221 AA.
AC P51158;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Ras-related protein Rab-28;
DE Flags: Precursor;
GN Name=Rab28;
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].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=8647132; DOI=10.1111/j.1432-1033.1996.0833p.x;
RA Brauers A., Schuermann A., Massmann S., Muehl-Zuerbes P., Becker W.,
RA Kainulainen H., Lie C., Joost H.-G.;
RT "Alternative mRNA splicing of the novel GTPase Rab28 generates isoforms
RT with different C-termini.";
RL Eur. J. Biochem. 237:833-840(1996).
RN [2]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23746546; DOI=10.1016/j.ajhg.2013.05.005;
RG European Retinal Disease Consortium;
RA Roosing S., Rohrschneider K., Beryozkin A., Sharon D., Weisschuh N.,
RA Staller J., Kohl S., Zelinger L., Peters T.A., Neveling K., Strom T.M.,
RA van den Born L.I., Hoyng C.B., Klaver C.C., Roepman R., Wissinger B.,
RA Banin E., Cremers F.P., den Hollander A.I.;
RT "Mutations in RAB28, encoding a farnesylated small GTPase, are associated
RT with autosomal-recessive cone-rod dystrophy.";
RL Am. J. Hum. Genet. 93:110-117(2013).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, cytoskeleton,
CC cilium basal body {ECO:0000269|PubMed:23746546}. Note=Expressed in the
CC basal body and ciliary rootlet of the photoreceptors.
CC -!- TISSUE SPECIFICITY: Testis, brain, and to much lower levels heart,
CC skeletal muscle and fat cells. Expressed in the retina.
CC {ECO:0000269|PubMed:23746546}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; X78606; CAA55340.1; -; mRNA.
DR PIR; S65476; S65476.
DR RefSeq; NP_446430.1; NM_053978.1.
DR AlphaFoldDB; P51158; -.
DR SMR; P51158; -.
DR STRING; 10116.ENSRNOP00000050260; -.
DR iPTMnet; P51158; -.
DR PhosphoSitePlus; P51158; -.
DR Ensembl; ENSRNOT00000081033; ENSRNOP00000071725; ENSRNOG00000017074.
DR GeneID; 117049; -.
DR KEGG; rno:117049; -.
DR CTD; 9364; -.
DR RGD; 620891; Rab28.
DR eggNOG; KOG0078; Eukaryota.
DR GeneTree; ENSGT00940000161833; -.
DR HOGENOM; CLU_041217_10_4_1; -.
DR InParanoid; P51158; -.
DR OMA; YIYGSHA; -.
DR OrthoDB; 1144210at2759; -.
DR PhylomeDB; P51158; -.
DR TreeFam; TF313852; -.
DR PRO; PR:P51158; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000017074; Expressed in quadriceps femoris and 20 other tissues.
DR ExpressionAtlas; P51158; baseline and differential.
DR Genevisible; P51158; RN.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0035253; C:ciliary rootlet; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:RGD.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:1901998; P:toxin transport; ISO:RGD.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell membrane; Cell projection; Cytoplasm; Cytoskeleton;
KW GTP-binding; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW Phosphoprotein; Prenylation; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P51157"
FT CHAIN 2..218
FT /note="Ras-related protein Rab-28"
FT /id="PRO_0000121229"
FT PROPEP 219..221
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000396724"
FT MOTIF 41..49
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 19..27
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 68..72
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 129..132
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 159..161
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P51157"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51157"
FT MOD_RES 218
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 218
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 221 AA; 24772 MW; 2220A1F0B0EBFFB8 CRC64;
MSDSEEESQD RQLKIVVLGD GTSGKTSLAT CFAQETFGKQ YKQTIGLDFF LRRITLPGNL
NVTLQVWDIG GQTIGGKMLD KYIYGAQGIL LVYDITNYQS FENLEDWYSV VKTVSEESET
QPLVALVGNK IDLEHMRTVK PDKHLRFCQE NGFSSHFVSA KTGDSVFLCF QKVAAEILGI
KLNKAEIEQS QRVVKADIVN YNQEPMSRTV NPPRSSMCAV Q
