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RAB34_RAT
ID   RAB34_RAT               Reviewed;         259 AA.
AC   Q5U1Y1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Ras-related protein Rab-34;
GN   Name=Rab34;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
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).
CC   -!- FUNCTION: Transport protein involved in the redistribution of lysosomes
CC       to the peri-Golgi region (By similarity). Plays a role in the
CC       maturation of phagosomes that engulf pathogens, such as S.aureus and
CC       M.tuberculosis. Plays a role in the fusion of phagosomes with lysosomes
CC       (By similarity). Acts also as a positive regulator of hedgehog
CC       signaling and regulates ciliary function (By similarity).
CC       {ECO:0000250|UniProtKB:Q64008, ECO:0000250|UniProtKB:Q9BZG1}.
CC   -!- SUBUNIT: Interacts with RILP. {ECO:0000250|UniProtKB:Q9BZG1}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q64008}. Golgi
CC       apparatus {ECO:0000250|UniProtKB:Q64008}. Cytoplasmic vesicle,
CC       phagosome {ECO:0000250|UniProtKB:Q9BZG1}. Cytoplasmic vesicle,
CC       phagosome membrane {ECO:0000250|UniProtKB:Q9BZG1}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:Q9BZG1}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:Q9BZG1}. Cell projection, cilium
CC       {ECO:0000250|UniProtKB:Q64008}. Note=Recruited to phagosomes containing
CC       S.aureus or Mycobacterium. {ECO:0000250|UniProtKB:Q9BZG1}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; BC086400; AAH86400.1; -; mRNA.
DR   RefSeq; NP_001012140.1; NM_001012140.1.
DR   AlphaFoldDB; Q5U1Y1; -.
DR   SMR; Q5U1Y1; -.
DR   IntAct; Q5U1Y1; 1.
DR   STRING; 10116.ENSRNOP00000036566; -.
DR   iPTMnet; Q5U1Y1; -.
DR   PhosphoSitePlus; Q5U1Y1; -.
DR   jPOST; Q5U1Y1; -.
DR   PaxDb; Q5U1Y1; -.
DR   PRIDE; Q5U1Y1; -.
DR   Ensembl; ENSRNOT00000037016; ENSRNOP00000036566; ENSRNOG00000023375.
DR   GeneID; 360571; -.
DR   KEGG; rno:360571; -.
DR   CTD; 83871; -.
DR   RGD; 1305058; Rab34.
DR   eggNOG; KOG0094; Eukaryota.
DR   InParanoid; Q5U1Y1; -.
DR   OrthoDB; 1048146at2759; -.
DR   PhylomeDB; Q5U1Y1; -.
DR   TreeFam; TF326626; -.
DR   Reactome; R-RNO-8873719; RAB geranylgeranylation.
DR   PRO; PR:Q5U1Y1; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR   GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR   GO; GO:0005769; C:early endosome; ISO:RGD.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR   GO; GO:0031985; C:Golgi cisterna; ISO:RGD.
DR   GO; GO:0005795; C:Golgi stack; ISO:RGD.
DR   GO; GO:0005770; C:late endosome; ISO:RGD.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR   GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
DR   GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0001726; C:ruffle; ISO:RGD.
DR   GO; GO:0031982; C:vesicle; ISO:RGD.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0030742; F:GTP-dependent protein binding; ISO:RGD.
DR   GO; GO:0003924; F:GTPase activity; ISO:RGD.
DR   GO; GO:0019001; F:guanyl nucleotide binding; ISO:RGD.
DR   GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR   GO; GO:0019882; P:antigen processing and presentation; ISO:RGD.
DR   GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR   GO; GO:0071333; P:cellular response to glucose stimulus; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0006897; P:endocytosis; ISO:RGD.
DR   GO; GO:0043001; P:Golgi to plasma membrane protein transport; ISO:RGD.
DR   GO; GO:0007041; P:lysosomal transport; ISO:RGD.
DR   GO; GO:0032418; P:lysosome localization; ISO:RGD.
DR   GO; GO:0090382; P:phagosome maturation; ISS:UniProtKB.
DR   GO; GO:0090385; P:phagosome-lysosome fusion; ISS:UniProtKB.
DR   GO; GO:1900426; P:positive regulation of defense response to bacterium; ISO:RGD.
DR   GO; GO:1905171; P:positive regulation of protein localization to phagocytic vesicle; ISO:RGD.
DR   GO; GO:0050714; P:positive regulation of protein secretion; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0045880; P:positive regulation of smoothened signaling pathway; ISS:UniProtKB.
DR   GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
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   Acetylation; Cell projection; Cilium biogenesis/degradation; Cytoplasm;
KW   Cytoplasmic vesicle; Golgi apparatus; GTP-binding; Lipoprotein; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..259
FT                   /note="Ras-related protein Rab-34"
FT                   /id="PRO_0000315238"
FT   MOTIF           81..89
FT                   /note="Effector region"
FT                   /evidence="ECO:0000250"
FT   BINDING         59..66
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         107..111
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         166..169
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZG1"
FT   MOD_RES         241
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZG1"
FT   LIPID           257
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000255"
FT   LIPID           258
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   259 AA;  29103 MW;  17593A92727B8389 CRC64;
     MNILAPVRRD RVLAELPQCL KKEAALHVRK DFHPRVTCAC QEHRTGTVGF KISKVIVVGD
     LSVGKTCLIN RFCKDTFDKN YKATIGVDFE MERFEVLGVP FSLQLWDTAG QERFKCIAST
     YYRGAQAIII VFNLNDVASL EHSKQWLADA LKENDPSNVL LFLVGSKKDL STPAQYSLME
     KDALKVAQEI KAEYWSVSSL TGENVREFFF RVAALTFEAN VLAELEKSGS RHIGDVVRIN
     SDDKNLYLTA SKKKATCCP
 
 
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