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RAB1_THEPA
ID   RAB1_THEPA              Reviewed;         220 AA.
AC   Q9TVU5; Q4MYR6;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Ras-related protein Rab-1;
DE   AltName: Full=Small GTP-binding protein rab1;
DE            Short=TpRab1;
GN   Name=rab1; OrderedLocusNames=TP03_0775;
OS   Theileria parva (East coast fever infection agent).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Theileriidae; Theileria.
OX   NCBI_TaxID=5875;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ISOPRENYLATION AT CYS-219, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=Muguga;
RX   PubMed=10477182; DOI=10.1016/s0166-6851(99)00093-6;
RA   Janoo R.T., Musoke A., Wells C., Bishop R.P.;
RT   "A Rab1 homologue with a novel isoprenylation signal provides insight into
RT   the secretory pathway of Theileria parva.";
RL   Mol. Biochem. Parasitol. 102:131-143(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Muguga;
RX   PubMed=15994558; DOI=10.1126/science.1110439;
RA   Gardner M.J., Bishop R., Shah T., de Villiers E.P., Carlton J.M., Hall N.,
RA   Ren Q., Paulsen I.T., Pain A., Berriman M., Wilson R.J.M., Sato S.,
RA   Ralph S.A., Mann D.J., Xiong Z., Shallom S.J., Weidman J., Jiang L.,
RA   Lynn J., Weaver B., Shoaibi A., Domingo A.R., Wasawo D., Crabtree J.,
RA   Wortman J.R., Haas B., Angiuoli S.V., Creasy T.H., Lu C., Suh B.,
RA   Silva J.C., Utterback T.R., Feldblyum T.V., Pertea M., Allen J.,
RA   Nierman W.C., Taracha E.L.N., Salzberg S.L., White O.R., Fitzhugh H.A.,
RA   Morzaria S., Venter J.C., Fraser C.M., Nene V.;
RT   "Genome sequence of Theileria parva, a bovine pathogen that transforms
RT   lymphocytes.";
RL   Science 309:134-137(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}. Note=Located in the
CC       vicinity of the schizont nucleus within the infected lymphocyte.
CC       {ECO:0000269|PubMed:10477182}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAN30616.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF107763; AAD51133.1; -; Genomic_DNA.
DR   EMBL; AF107762; AAD51132.1; -; mRNA.
DR   EMBL; AAGK01000006; EAN30616.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_762899.1; XM_757806.1.
DR   AlphaFoldDB; Q9TVU5; -.
DR   SMR; Q9TVU5; -.
DR   STRING; 5875.XP_762899.1; -.
DR   EnsemblProtists; EAN30616; EAN30616; TP03_0775.
DR   GeneID; 3499708; -.
DR   KEGG; tpv:TP03_0775; -.
DR   VEuPathDB; PiroplasmaDB:TpMuguga_03g00775; -.
DR   eggNOG; KOG0084; Eukaryota.
DR   InParanoid; Q9TVU5; -.
DR   Proteomes; UP000001949; Unassembled WGS sequence.
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; -; 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   1: Evidence at protein level;
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_0000233340"
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:0000305|PubMed:10477182"
SQ   SEQUENCE   220 AA;  24470 MW;  7CD330F56DF6AFBD CRC64;
     MKEYDYLFKI IVIGDSGTGK SSLLLRFADN TYSESYMSTI GVDFKIKTVK IDNTTIKLQI
     WDTAGQERFR TITSTYYRGA HGIICVYDVT NKLSFDHITE TWLQDIDKYA TSNVCKLLIG
     NKIDLAESRV VSADEAKHVA EQNNMNYIEA SAKTDSNVEK AFTTIAKALK DKVTQYPSNA
     PASTVSLNTA SKVPTNRGLT DSCQESSVFK KMNFSSGKCT
 
 
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