RB11A_LOTJA
ID RB11A_LOTJA Reviewed; 226 AA.
AC Q40191;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Ras-related protein Rab11A;
DE Flags: Precursor;
GN Name=RAB11A;
OS Lotus japonicus (Lotus corniculatus var. japonicus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; robinioid clade; Loteae; Lotus.
OX NCBI_TaxID=34305;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Gifu / B-129; TISSUE=Root nodule;
RX PubMed=9076991; DOI=10.1046/j.1365-313x.1997.11020237.x;
RA Borg S., Brandstrup B., Jensen T.J., Poulsen C.;
RT "Identification of new protein species among 33 different small GTP-binding
RT proteins encoded by cDNAs from Lotus japonicus, and expression of
RT corresponding mRNAs in developing root nodules.";
RL Plant J. 11:237-250(1997).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; Z73949; CAA98177.1; -; mRNA.
DR AlphaFoldDB; Q40191; -.
DR SMR; Q40191; -.
DR OMA; DICHLVV; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
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 Cell membrane; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation.
FT CHAIN 1..223
FT /note="Ras-related protein Rab11A"
FT /id="PRO_0000121168"
FT PROPEP 224..226
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370819"
FT MOTIF 46..54
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 24..32
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62491"
FT BINDING 43..49
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62491"
FT BINDING 72..76
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62491"
FT BINDING 130..133
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62491"
FT BINDING 160..162
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62491"
FT MOD_RES 223
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 222
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 223
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 226 AA; 24842 MW; B4DD4C7E66029567 CRC64;
MASGGGYGDA NAKIDYVFKV VLIGDSAVGK SQILARFARN EFSLDSKSTI GVEFQTRTLV
IDHKTVKAQI WDTAGQERYR AVTSAYYRGA VGAMLVYDIT KRQTFDHIPR WLEELRNHAD
KNIVIILIGN KCDLVNQRDV PTEDAKEFAE KEGLFFLETS ALEATNVESA FTTVLTEIYN
IVNKKSLAAD ESQGNGNSAS LSGQKIIIPG PAQEIPAKRN MCCQAS