RABL3_MOUSE
ID RABL3_MOUSE Reviewed; 236 AA.
AC Q9D4V7; Q8BMU2; Q9D0M6;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Rab-like protein 3;
GN Name=Rabl3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=B5/EGFP; TISSUE=Trophoblast stem cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION.
RX PubMed=31406347; DOI=10.1038/s41588-019-0475-y;
RA Nissim S., Leshchiner I., Mancias J.D., Greenblatt M.B., Maertens O.,
RA Cassa C.A., Rosenfeld J.A., Cox A.G., Hedgepeth J., Wucherpfennig J.I.,
RA Kim A.J., Henderson J.E., Gonyo P., Brandt A., Lorimer E., Unger B.,
RA Prokop J.W., Heidel J.R., Wang X.X., Ukaegbu C.I., Jennings B.C.,
RA Paulo J.A., Gableske S., Fierke C.A., Getz G., Sunyaev S.R.,
RA Wade Harper J., Cichowski K., Kimmelman A.C., Houvras Y., Syngal S.,
RA Williams C., Goessling W.;
RT "Mutations in RABL3 alter KRAS prenylation and are associated with
RT hereditary pancreatic cancer.";
RL Nat. Genet. 51:1308-1314(2019).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 2-216 OF WILD-TYPE AND XIAMEN
RP MUTANT IN COMPLEX WITH MAGNESIUM AND GDP OR GTP-GAMMA-S, FUNCTION, SUBUNIT,
RP INTERACTION WITH GPR89, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 43-VAL--ARG-46.
RX PubMed=32220963; DOI=10.1073/pnas.2000703117;
RA Zhong X., Su L., Yang Y., Nair-Gill E., Tang M., Anderton P., Li X.,
RA Wang J., Zhan X., Tomchick D.R., Brautigam C.A., Moresco E.M.Y., Choi J.H.,
RA Beutler B.;
RT "Genetic and structural studies of RABL3 reveal an essential role in
RT lymphoid development and function.";
RL Proc. Natl. Acad. Sci. U.S.A. 117:8563-8572(2020).
CC -!- FUNCTION: Required for KRAS signaling regulation and modulation of cell
CC proliferation (PubMed:31406347). Regulator of KRAS prenylation, and
CC probably prenylation of other small GTPases (By similarity). Required
CC for lymphocyte development and function (PubMed:32220963). Not required
CC for myeloid cell development (PubMed:32220963).
CC {ECO:0000250|UniProtKB:Q5HYI8, ECO:0000269|PubMed:31406347,
CC ECO:0000269|PubMed:32220963}.
CC -!- SUBUNIT: Homodimer (PubMed:32220963). Interacts with GPR89; the
CC interaction stabilizes GPR89 (PubMed:32220963). Interacts with RAP1GDS1
CC (By similarity). {ECO:0000250|UniProtKB:Q5HYI8,
CC ECO:0000269|PubMed:32220963}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D4V7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D4V7-2; Sequence=VSP_029723;
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal. {ECO:0000269|PubMed:32220963}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AK011280; BAB27514.1; -; mRNA.
DR EMBL; AK016099; BAB30113.1; -; mRNA.
DR EMBL; AK028195; BAC25804.1; -; mRNA.
DR EMBL; BC050194; AAH50194.1; -; mRNA.
DR CCDS; CCDS37338.1; -. [Q9D4V7-1]
DR RefSeq; NP_001035964.1; NM_001042499.1. [Q9D4V7-1]
DR PDB; 6VIH; X-ray; 2.99 A; A/B=2-216.
DR PDB; 6VII; X-ray; 2.00 A; A/B=2-216.
DR PDB; 6VIJ; X-ray; 1.95 A; A/B=2-216.
DR PDB; 6VIK; X-ray; 1.70 A; B=2-216.
DR PDBsum; 6VIH; -.
DR PDBsum; 6VII; -.
DR PDBsum; 6VIJ; -.
DR PDBsum; 6VIK; -.
DR AlphaFoldDB; Q9D4V7; -.
DR SMR; Q9D4V7; -.
DR BioGRID; 212342; 1.
DR IntAct; Q9D4V7; 2.
DR STRING; 10090.ENSMUSP00000023524; -.
DR iPTMnet; Q9D4V7; -.
DR PhosphoSitePlus; Q9D4V7; -.
DR EPD; Q9D4V7; -.
DR MaxQB; Q9D4V7; -.
DR PaxDb; Q9D4V7; -.
DR PeptideAtlas; Q9D4V7; -.
DR PRIDE; Q9D4V7; -.
DR ProteomicsDB; 255069; -. [Q9D4V7-1]
DR ProteomicsDB; 255070; -. [Q9D4V7-2]
DR Antibodypedia; 32810; 45 antibodies from 20 providers.
DR Ensembl; ENSMUST00000023524; ENSMUSP00000023524; ENSMUSG00000022827. [Q9D4V7-1]
DR Ensembl; ENSMUST00000130028; ENSMUSP00000122441; ENSMUSG00000022827. [Q9D4V7-2]
DR GeneID; 67657; -.
DR KEGG; mmu:67657; -.
DR UCSC; uc007zec.1; mouse. [Q9D4V7-1]
DR CTD; 285282; -.
DR MGI; MGI:1914907; Rabl3.
DR VEuPathDB; HostDB:ENSMUSG00000022827; -.
DR eggNOG; ENOG502QT3S; Eukaryota.
DR GeneTree; ENSGT00390000007467; -.
DR HOGENOM; CLU_084875_1_0_1; -.
DR InParanoid; Q9D4V7; -.
DR OMA; EEIWLNC; -.
DR OrthoDB; 1269342at2759; -.
DR PhylomeDB; Q9D4V7; -.
DR TreeFam; TF320841; -.
DR BioGRID-ORCS; 67657; 6 hits in 71 CRISPR screens.
DR ChiTaRS; Rabl3; mouse.
DR PRO; PR:Q9D4V7; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9D4V7; protein.
DR Bgee; ENSMUSG00000022827; Expressed in metanephric ureteric bud and 241 other tissues.
DR Genevisible; Q9D4V7; MM.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0030183; P:B cell differentiation; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0001779; P:natural killer cell differentiation; IMP:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
DR GO; GO:1903059; P:regulation of protein lipidation; ISS:UniProtKB.
DR GO; GO:0046578; P:regulation of Ras protein signal transduction; ISS:UniProtKB.
DR GO; GO:0033077; P:T cell differentiation in thymus; IMP:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; GTP-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..236
FT /note="Rab-like protein 3"
FT /id="PRO_0000312167"
FT REGION 1..235
FT /note="Small GTPase-like"
FT BINDING 16..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:32220963,
FT ECO:0007744|PDB:6VII, ECO:0007744|PDB:6VIJ"
FT BINDING 148..150
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:32220963,
FT ECO:0007744|PDB:6VII, ECO:0007744|PDB:6VIJ"
FT BINDING 179..180
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:32220963,
FT ECO:0007744|PDB:6VII, ECO:0007744|PDB:6VIJ"
FT VAR_SEQ 130..236
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029723"
FT MUTAGEN 43..46
FT /note="Missing: In xiamen; reduced Rabl3 expression,
FT reduced interaction with Gpr89, reduced thermal stability,
FT reduced frequency of CD3+ T cells, increased CD4+-to-CD8+ T
FT cell ratio, higher CD44 expression in CD8+ T cells and
FT increased B cell-to-T cell ratio."
FT /evidence="ECO:0000269|PubMed:32220963"
FT CONFLICT 185
FT /note="S -> P (in Ref. 1; BAC25804)"
FT /evidence="ECO:0000305"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:6VIK"
FT HELIX 19..26
FT /evidence="ECO:0007829|PDB:6VIK"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:6VIK"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:6VIK"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:6VIK"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:6VIK"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:6VIK"
FT STRAND 58..66
FT /evidence="ECO:0007829|PDB:6VIK"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:6VIH"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:6VIK"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:6VIK"
FT HELIX 100..104
FT /evidence="ECO:0007829|PDB:6VIK"
FT HELIX 106..111
FT /evidence="ECO:0007829|PDB:6VIK"
FT HELIX 132..137
FT /evidence="ECO:0007829|PDB:6VII"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:6VIK"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:6VIK"
FT HELIX 154..170
FT /evidence="ECO:0007829|PDB:6VIK"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:6VIK"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:6VIK"
FT HELIX 191..206
FT /evidence="ECO:0007829|PDB:6VIK"
SQ SEQUENCE 236 AA; 26298 MW; DFCE72737C11944B CRC64;
MASLDRVKVL VLGDSGVGKS SLVHLLCHNQ VLGNPSWTVG CSVDIRVHDY KEGTPEEKTY
YIELWDVGGS VGSASSVKST RAVFYNSVNG IILVHDLTNK KSSQNLYRWS LEVLNRDAVP
TGVLVTNGDY DREQFADNQI PLLVIGTKLD QIHETKRHEV LIRTAFLAED FNAEEINLDC
TNPRSSAAGS SNAVKLSRFF DKVIEKRYFF REGNQIPGFS DRKRFGGGAL KNFHCD
