ID RSLAA_HUMAN Reviewed; 203 AA.
AC Q92737; Q49AU5; Q6PI03;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 24-JAN-2024, entry version 180.
DE RecName: Full=Ras-like protein family member 10A;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P01116};
DE AltName: Full=Ras-like protein RRP22;
DE AltName: Full=Ras-related protein on chromosome 22;
DE Flags: Precursor;
GN Name=RASL10A; Synonyms=RRP22;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=8975699; DOI=10.1006/geno.1996.0625;
RA Zucman-Rossi J., Legoix P., Thomas G.;
RT "Identification of new members of the Gas2 and Ras families in the 22q12
RT chromosome region.";
RL Genomics 38:247-254(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND ISOPRENYLATION AT CYS-200.
RX PubMed=15833841; DOI=10.1158/0008-5472.can-04-0749;
RA Elam C., Hesson L., Vos M.D., Eckfeld K., Ellis C.A., Bell A., Krex D.,
RA Birrer M.J., Latif F., Clark G.J.;
RT "RRP22 is a farnesylated, nucleolar, Ras-related protein with tumor
RT suppressor potential.";
RL Cancer Res. 65:3117-3125(2005).
CC -!- FUNCTION: Potent inhibitor of cellular proliferation.
CC {ECO:0000269|PubMed:15833841}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000250|UniProtKB:P01116};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:15833841}. Note=May cycle in and out of the
CC nucleolus in a GTP-dependent manner.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q92737-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=Q92737-2; Sequence=VSP_013372;
CC -!- TISSUE SPECIFICITY: Expression appears to be strictly limited to the
CC central nervous system. {ECO:0000269|PubMed:8975699}.
CC -!- PTM: Isoprenylation is essential for nucleolar localization, and the
CC proliferation-inhibiting activity of RASL10A.
CC {ECO:0000269|PubMed:15833841}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; Y07847; CAA69175.1; -; mRNA.
DR EMBL; AC002059; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC022473; AAH22473.1; -; mRNA.
DR EMBL; BC040434; AAH40434.1; -; mRNA.
DR EMBL; BC050739; AAH50739.1; -; mRNA.
DR EMBL; BC058077; AAH58077.1; -; mRNA.
DR CCDS; CCDS13854.1; -. [Q92737-1]
DR RefSeq; NP_006468.1; NM_006477.4. [Q92737-1]
DR AlphaFoldDB; Q92737; -.
DR SMR; Q92737; -.
DR BioGRID; 115877; 13.
DR IntAct; Q92737; 4.
DR STRING; 9606.ENSP00000216101; -.
DR BioMuta; RASL10A; -.
DR DMDM; 3024572; -.
DR MassIVE; Q92737; -.
DR PaxDb; 9606-ENSP00000216101; -.
DR PeptideAtlas; Q92737; -.
DR Antibodypedia; 24486; 135 antibodies from 23 providers.
DR DNASU; 10633; -.
DR Ensembl; ENST00000216101.7; ENSP00000216101.6; ENSG00000100276.10. [Q92737-1]
DR Ensembl; ENST00000401450.3; ENSP00000386095.3; ENSG00000100276.10. [Q92737-2]
DR GeneID; 10633; -.
DR KEGG; hsa:10633; -.
DR MANE-Select; ENST00000216101.7; ENSP00000216101.6; NM_006477.5; NP_006468.1.
DR UCSC; uc003aff.4; human. [Q92737-1]
DR AGR; HGNC:16954; -.
DR CTD; 10633; -.
DR DisGeNET; 10633; -.
DR GeneCards; RASL10A; -.
DR HGNC; HGNC:16954; RASL10A.
DR HPA; ENSG00000100276; Tissue enriched (brain).
DR MIM; 602220; gene.
DR neXtProt; NX_Q92737; -.
DR OpenTargets; ENSG00000100276; -.
DR PharmGKB; PA162400707; -.
DR VEuPathDB; HostDB:ENSG00000100276; -.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000162366; -.
DR HOGENOM; CLU_148762_0_0_1; -.
DR InParanoid; Q92737; -.
DR OMA; WPDSKDW; -.
DR OrthoDB; 19873at2759; -.
DR PhylomeDB; Q92737; -.
DR TreeFam; TF325043; -.
DR PathwayCommons; Q92737; -.
DR SignaLink; Q92737; -.
DR BioGRID-ORCS; 10633; 33 hits in 1150 CRISPR screens.
DR ChiTaRS; RASL10A; human.
DR GenomeRNAi; 10633; -.
DR Pharos; Q92737; Tbio.
DR PRO; PR:Q92737; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q92737; Protein.
DR Bgee; ENSG00000100276; Expressed in amygdala and 115 other cell types or tissues.
DR ExpressionAtlas; Q92737; baseline and differential.
DR Genevisible; Q92737; HS.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; TAS:ProtInc.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:ProtInc.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001806; Small_GTPase.
DR PANTHER; PTHR46350; RAS LIKE FAMILY 10 MEMBER B-RELATED; 1.
DR PANTHER; PTHR46350:SF3; RAS-LIKE PROTEIN FAMILY MEMBER 10A; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00173; RAS; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51421; RAS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; GTP-binding; Hydrolase; Lipoprotein;
KW Membrane; Methylation; Nucleotide-binding; Nucleus; Prenylation;
KW Reference proteome; Tumor suppressor.
FT CHAIN 1..200
FT /note="Ras-like protein family member 10A"
FT /id="PRO_0000082706"
FT PROPEP 201..203
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281360"
FT REGION 1..203
FT /note="Small GTPase-like"
FT MOTIF 33..42
FT /note="Effector region"
FT /evidence="ECO:0000305"
FT BINDING 11..18
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 59..62
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 MOD_RES 200
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 200
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:15833841"
FT VAR_SEQ 116..203
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013372"
FT CONFLICT 25
FT /note="L -> V (in Ref. 3; AAH22473)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 203 AA; 22541 MW; D11B33EE019E2D78 CRC64;
MGGSLRVAVL GAPGVGKTAI IRQFLFGDYP ERHRPTDGPR LYRPAVLLDG AVYDLSIRDG
DVAGPGSSPG GPEEWPDAKD WSLQDTDAFV LVYDICSPDS FDYVKALRQR IAETRPAGAP
EAPILVVGNK RDRQRLRFGP RRALAALVRR GWRCGYLECS AKYNWHVLRL FRELLRCALV
RARPAHPALR LQGALHPARC SLM
//
