ID RAB1_THEAN Reviewed; 220 AA.
AC Q4UB16;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Ras-related protein Rab-1;
DE AltName: Full=Small GTP-binding protein rab1;
GN Name=rab1; ORFNames=TA18180;
OS Theileria annulata.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=5874;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ankara;
RX PubMed=15994557; DOI=10.1126/science.1110418;
RA Pain A., Renauld H., Berriman M., Murphy L., Yeats C.A., Weir W.,
RA Kerhornou A., Aslett M., Bishop R., Bouchier C., Cochet M., Coulson R.M.R.,
RA Cronin A., de Villiers E.P., Fraser A., Fosker N., Gardner M., Goble A.,
RA Griffiths-Jones S., Harris D.E., Katzer F., Larke N., Lord A., Maser P.,
RA McKellar S., Mooney P., Morton F., Nene V., O'Neil S., Price C.,
RA Quail M.A., Rabbinowitsch E., Rawlings N.D., Rutter S., Saunders D.,
RA Seeger K., Shah T., Squares R., Squares S., Tivey A., Walker A.R.,
RA Woodward J., Dobbelaere D.A.E., Langsley G., Rajandream M.A., McKeever D.,
RA Shiels B., Tait A., Barrell B.G., Hall N.;
RT "Genome of the host-cell transforming parasite Theileria annulata compared
RT with T. parva.";
RL Science 309:131-133(2005).
CC -!- FUNCTION: Protein transport. Probably involved in vesicular traffic
CC from ER to Golgi (By similarity). {ECO:0000250}.
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; CR940352; CAI75985.1; -; Genomic_DNA.
DR RefSeq; XP_955461.1; XM_950368.1.
DR AlphaFoldDB; Q4UB16; -.
DR SMR; Q4UB16; -.
DR STRING; 5874.Q4UB16; -.
DR GeneID; 3864726; -.
DR KEGG; tan:TA18180; -.
DR VEuPathDB; PiroplasmaDB:TA18180; -.
DR eggNOG; KOG0084; Eukaryota.
DR InParanoid; Q4UB16; -.
DR OMA; IDRYCGF; -.
DR OrthoDB; 8685at2759; -.
DR Proteomes; UP000001950; Chromosome 3.
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 GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR47977:SF26; LD21953P; 1.
DR PANTHER; PTHR47977; RAS-RELATED PROTEIN RAB; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00177; ARF; 1.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00176; RAN; 1.
DR SMART; SM00173; RAS; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51419; RAB; 1.
PE 3: Inferred from homology;
KW Cell membrane; GTP-binding; Lipoprotein; Membrane; Nucleotide-binding;
KW Prenylation; Protein transport; Reference proteome; Transport.
FT CHAIN 1..220
FT /note="Ras-related protein Rab-1"
FT /id="PRO_0000233339"
FT MOTIF 36..44
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 62..66
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 121..124
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 219
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 220 AA; 24543 MW; 38728BFE830FBCC6 CRC64;
MKEYDYLFKI IVIGDSGTGK SSLLLRFADN TYSESYMSTI GVDFKIKTVK IDNTTIKLQI
WDTAGQERFR TITSTYYRGA HGIICVYDVT NKLSFDHITE TWLQDIDKYA TSNVCKLLIG
NKIDLVDSRV VLADEAKHVA EQNNMNYIEA SAKTDSNVEK AFTTIAKALK DKVTQYPSNA
PTSTVNLSNA SKVTTNRGIS DSCQESSVFK KMNFSSGKCT
//
