ID   RAB9B_PONAB             Reviewed;         201 AA.
AC   Q5R4W9;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Ras-related protein Rab-9B;
GN   Name=RAB9B;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the transport of proteins between the endosomes
CC       and the trans Golgi network. {ECO:0000250|UniProtKB:P24408}.
CC   -!- SUBUNIT: Interacts (GTP-bound form) with SGSM1; the GDP-bound form has
CC       much lower affinity for SGSM1. The GTP-bound form but not the GDP-bound
CC       form interacts with HPS4 and the BLOC-3 complex (heterodimer of HPS1
CC       and HPS4) but does not interact with HPS1 alone.
CC       {ECO:0000250|UniProtKB:Q9NP90}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle,
CC       phagosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250};
CC       Cytoplasmic side {ECO:0000250}. Note=Recruited to phagosomes containing
CC       S.aureus or Mycobacterium. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; CR861121; CAH93197.1; -; mRNA.
DR   RefSeq; NP_001126880.1; NM_001133408.1.
DR   AlphaFoldDB; Q5R4W9; -.
DR   SMR; Q5R4W9; -.
DR   STRING; 9601.ENSPPYP00000023047; -.
DR   PRIDE; Q5R4W9; -.
DR   Ensembl; ENSPPYT00000024017; ENSPPYP00000023047; ENSPPYG00000020591.
DR   GeneID; 100173893; -.
DR   KEGG; pon:100173893; -.
DR   CTD; 51209; -.
DR   eggNOG; KOG0394; Eukaryota.
DR   GeneTree; ENSGT00940000160481; -.
DR   HOGENOM; CLU_041217_10_6_1; -.
DR   InParanoid; Q5R4W9; -.
DR   OMA; NRKAPRS; -.
DR   OrthoDB; 1172019at2759; -.
DR   TreeFam; TF326442; -.
DR   Proteomes; UP000001595; Chromosome X.
DR   GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
DR   GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0032482; P:Rab protein signal transduction; IEA:InterPro.
DR   CDD; cd04116; Rab9; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR041824; Rab9.
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; Cytoplasmic vesicle; GTP-binding; Lipoprotein; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..201
FT                   /note="Ras-related protein Rab-9B"
FT                   /id="PRO_0000121144"
FT   MOTIF           36..44
FT                   /note="Effector region"
FT                   /evidence="ECO:0000250"
FT   BINDING         14..22
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP90"
FT   BINDING         33..34
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP90"
FT   BINDING         38..39
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP90"
FT   BINDING         65
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP90"
FT   BINDING         124..127
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP90"
FT   BINDING         155..156
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NP90"
FT   MOD_RES         34
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BHH2"
FT   LIPID           200
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           201
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   201 AA;  22689 MW;  AF32AA8E834DD19C CRC64;
     MSGKSLLLKV ILLGDGGVGK SSLMNRYVTN KFDSQAFHTI GVEFLNRDLE VDGRFVTLQI
     WDTAGQERFK SLRTPFYRGA DCCLLTFSVD DRQSFENLGN WQKEFIYYAD VKDPEHFPFV
     VLGNKVDKED RQVTTEEAQA WCMENGDYPY LETSAKDDTN VTVAFEEAVR QVLAVEEQLE
     HCMLGHTIDL NSGSKAGSSC C