RB40L_HUMAN
ID RB40L_HUMAN Reviewed; 278 AA.
AC P0C0E4; Q495H3;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Ras-related protein Rab-40A-like;
DE AltName: Full=Ras-like GTPase;
GN Name=RAB40AL; Synonyms=RLGP;
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 [GENOMIC DNA], SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=12145744; DOI=10.1086/342208;
RA Saito-Ohara F., Fukuda Y., Ito M., Agarwala K.L., Hayashi M., Matsuo M.,
RA Imoto I., Yamakawa K., Nakamura Y., Inazawa J.;
RT "The Xq22 inversion breakpoint interrupted a novel Ras-like GTPase gene in
RT a patient with Duchenne muscular dystrophy and profound mental
RT retardation.";
RL Am. J. Hum. Genet. 71:637-645(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT GLY-59, AND
RP CHARACTERIZATION OF VARIANT GLY-59.
RX PubMed=22581972; DOI=10.1136/jmedgenet-2011-100575;
RA Bedoyan J.K., Schaibley V.M., Peng W., Bai Y., Mondal K., Shetty A.C.,
RA Durham M., Micucci J.A., Dhiraaj A., Skidmore J.M., Kaplan J.B.,
RA Skinner C., Schwartz C.E., Antonellis A., Zwick M.E., Cavalcoli J.D.,
RA Li J.Z., Martin D.M.;
RT "Disruption of RAB40AL function leads to Martin--Probst syndrome, a rare X-
RT linked multisystem neurodevelopmental human disorder.";
RL J. Med. Genet. 49:332-340(2012).
RN [5]
RP VARIANT GLY-59.
RX PubMed=25044830; DOI=10.1002/humu.22620;
RA Oldak M., Sciezynska A., Mlynarski W., Borowiec M., Ruszkowska E.,
RA Szulborski K., Pollak A., Kosinska J., Mueller-Malesinska M., Stawinski P.,
RA Szaflik J.P., Ploski R.;
RT "Evidence against RAB40AL being the locus for Martin-Probst X-linked
RT deafness-intellectual disability syndrome.";
RL Hum. Mutat. 35:1171-1174(2014).
RN [6]
RP VARIANT GLY-59.
RX PubMed=25370018; DOI=10.1007/s00431-014-2452-x;
RA Oldak M., Ruszkowska E., Pollak A., Sobczyk-Kopciol A., Kowalewski C.,
RA Piwonska A., Drygas W., Ploski R.;
RT "A note of caution on the diagnosis of Martin-Probst syndrome by the
RT detection of the p.D59G mutation in the RAB40AL gene.";
RL Eur. J. Pediatr. 174:693-696(2015).
RN [7]
RP VARIANT GLY-59.
RX PubMed=26300074; DOI=10.3892/mmr.2015.4215;
RA Bianco A.M., Faletra F., Vozzi D., Girardelli M., Knowles A., Tommasini A.,
RA Zauli G., Marcuzzi A.;
RT "Two-gene mutation in a single patient: Biochemical and functional analysis
RT for a correct interpretation of exome results.";
RL Mol. Med. Report. 12:6128-6132(2015).
CC -!- FUNCTION: May be a substrate-recognition component of a SCF-like ECS
CC (Elongin-Cullin-SOCS-box protein) E3 ubiquitin ligase complex which
CC mediates the ubiquitination and subsequent proteasomal degradation of
CC target proteins. {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm
CC {ECO:0000269|PubMed:22581972}. Mitochondrion
CC {ECO:0000269|PubMed:12145744, ECO:0000269|PubMed:22581972}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, lung, heart, skeletal muscle,
CC kidney and liver. Highest expression in brain. Expressed in fetal brain
CC and kidney. {ECO:0000269|PubMed:12145744, ECO:0000269|PubMed:22581972}.
CC -!- DOMAIN: The SOCS box domain mediates the interaction with the Elongin
CC BC complex, an adapter module in different E3 ubiquitin ligase
CC complexes. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; Z95624; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC101169; AAI01170.1; -; mRNA.
DR EMBL; BC101170; AAI01171.1; -; mRNA.
DR EMBL; BC101171; AAI01172.1; -; mRNA.
DR EMBL; BC101172; AAI01173.1; -; mRNA.
DR CCDS; CCDS35353.1; -.
DR RefSeq; NP_001027004.1; NM_001031834.1.
DR AlphaFoldDB; P0C0E4; -.
DR SMR; P0C0E4; -.
DR BioGRID; 129420; 26.
DR IntAct; P0C0E4; 11.
DR STRING; 9606.ENSP00000218249; -.
DR iPTMnet; P0C0E4; -.
DR PhosphoSitePlus; P0C0E4; -.
DR BioMuta; RAB40AL; -.
DR DMDM; 83287760; -.
DR MassIVE; P0C0E4; -.
DR PaxDb; P0C0E4; -.
DR PeptideAtlas; P0C0E4; -.
DR PRIDE; P0C0E4; -.
DR Antibodypedia; 68152; 69 antibodies from 13 providers.
DR DNASU; 282808; -.
DR Ensembl; ENST00000218249.7; ENSP00000218249.5; ENSG00000102128.8.
DR GeneID; 282808; -.
DR KEGG; hsa:282808; -.
DR MANE-Select; ENST00000218249.7; ENSP00000218249.5; NM_001031834.1; NP_001027004.1.
DR UCSC; uc004ejs.4; human.
DR CTD; 282808; -.
DR DisGeNET; 282808; -.
DR GeneCards; RAB40AL; -.
DR HGNC; HGNC:25410; RAB40AL.
DR HPA; ENSG00000102128; Tissue enhanced (brain).
DR MalaCards; RAB40AL; -.
DR MIM; 300405; gene.
DR neXtProt; NX_P0C0E4; -.
DR OpenTargets; ENSG00000102128; -.
DR PharmGKB; PA142671103; -.
DR VEuPathDB; HostDB:ENSG00000102128; -.
DR eggNOG; KOG0078; Eukaryota.
DR GeneTree; ENSGT00940000166416; -.
DR HOGENOM; CLU_041217_11_0_1; -.
DR InParanoid; P0C0E4; -.
DR OMA; STHNRNS; -.
DR OrthoDB; 1065856at2759; -.
DR PhylomeDB; P0C0E4; -.
DR TreeFam; TF323230; -.
DR PathwayCommons; P0C0E4; -.
DR SignaLink; P0C0E4; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 282808; 5 hits in 616 CRISPR screens.
DR GenomeRNAi; 282808; -.
DR Pharos; P0C0E4; Tbio.
DR PRO; PR:P0C0E4; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P0C0E4; protein.
DR Bgee; ENSG00000102128; Expressed in stromal cell of endometrium and 53 other tissues.
DR Genevisible; P0C0E4; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
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 InterPro; IPR001496; SOCS_box.
DR InterPro; IPR036036; SOCS_box-like_dom_sf.
DR Pfam; PF00071; Ras; 1.
DR Pfam; PF07525; SOCS_box; 1.
DR SMART; SM00174; RHO; 1.
DR SMART; SM00253; SOCS; 1.
DR SMART; SM00969; SOCS_box; 1.
DR SUPFAM; SSF158235; SSF158235; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
DR PROSITE; PS50225; SOCS; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Deafness; GTP-binding; Lipoprotein; Membrane; Mitochondrion;
KW Nucleotide-binding; Palmitate; Prenylation; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..278
FT /note="Ras-related protein Rab-40A-like"
FT /id="PRO_0000121258"
FT DOMAIN 175..228
FT /note="SOCS box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00194"
FT BINDING 21..28
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 69..73
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 126..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 270
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 275
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT VARIANT 59
FT /note="D -> G (renders the protein unstable and disrupts
FT its cytoplasmic localization; dbSNP:rs145606134)"
FT /evidence="ECO:0000269|PubMed:22581972,
FT ECO:0000269|PubMed:25044830, ECO:0000269|PubMed:25370018,
FT ECO:0000269|PubMed:26300074"
FT /id="VAR_068916"
SQ SEQUENCE 278 AA; 31239 MW; DF047F1703217DA4 CRC64;
MSAPGSPDQA YDFLLKFLLV GDRDVGKSEI LESLQDGTAE SPYSHLGGID YKTTTILLDG
QRVKLKLWDT SGQGRFCTIF RSYSRGAQGV ILVYDIANRW SFEGMDRWIK KIEEHAPGVP
KILVGNRLHL AFKRQVPREQ AQAYAERLGV TFFEVSPLCN FNIIESFTEL ARIVLLRHRL
NWLGRPSKVL SLQDLCCRTI VSCTPVHLVD KLPLPIALRS HLKSFSMAKG LNARMMRGLS
YSLTTSSTHK RSSLCKVKIV CPPQSPPKNC TRNSCKIS
