RAB1A_LYMST
ID RAB1A_LYMST Reviewed; 205 AA.
AC Q05974;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Ras-related protein Rab-1A;
GN Name=RAB1A;
OS Lymnaea stagnalis (Great pond snail) (Helix stagnalis).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC Lymnaeidae; Lymnaea.
OX NCBI_TaxID=6523;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8223561; DOI=10.1111/j.1432-1033.1993.tb18239.x;
RA Agterberg M., van Die I., Yang H., Andriessen J.A., van Tetering A.,
RA van den Eijnden D.H., Ploegh H.L.;
RT "Isolation and characterization of three cDNAs coding for Rab proteins from
RT the albumen gland of the mollusc Lymnaea stagnalis.";
RL Eur. J. Biochem. 217:241-246(1993).
CC -!- FUNCTION: Probably required for transit of protein from the ER through
CC Golgi compartment. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:P62820}.
CC Endoplasmic reticulum {ECO:0000250|UniProtKB:P62820}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; X72688; CAA51233.1; -; mRNA.
DR PIR; S38339; S38339.
DR AlphaFoldDB; Q05974; -.
DR SMR; Q05974; -.
DR PRIDE; Q05974; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
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 Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; GTP-binding;
KW Lipoprotein; Nucleotide-binding; Prenylation; Protein transport; Transport.
FT CHAIN 1..205
FT /note="Ras-related protein Rab-1A"
FT /id="PRO_0000121060"
FT REGION 183..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 40..48
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT COMPBIAS 185..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 18..26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 36..43
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 66..70
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 124..127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 154..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT LIPID 204
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 205
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 205 AA; 22760 MW; D5E0BDDCBB4A26FF CRC64;
MSTMNPDYDY LFKLLLIGDS GVGKSCLLLR FADDTYTESY ISTIGVDFKI RTIELDGKTI
KLQIWDTAGQ ERFRTITSSY YRGAHGIIVV YDVTDQESFN NVKQWLQEID RYASENVNKL
LVGNKSDLTT KKVVDFTTAK EYADQLGIPF LETSAKNATN VEQAFMTMAA EIKNRMGPIT
AASDSKPSVK INSSTPVSAN KGGCC