RAB7_EPICO
ID RAB7_EPICO Reviewed; 207 AA.
AC H9BW96;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Ras-related protein rab7 {ECO:0000305};
GN Name=rab7 {ECO:0000303|PubMed:24161772};
OS Epinephelus coioides (Orange-spotted grouper) (Epinephelus nebulosus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Serranoidei; Serranidae; Epinephelinae;
OC Epinephelini; Epinephelus.
OX NCBI_TaxID=94232 {ECO:0000312|EMBL:AFD97434.1};
RN [1] {ECO:0000312|EMBL:AFD97434.1}
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH VIRAL PROTEINS, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, INDUCTION, ISOPRENYLATION AT CYS-205 AND
RP CYS-207, AND PHYLOGENETIC ANALYSIS.
RX PubMed=24161772; DOI=10.1016/j.fsi.2013.10.002;
RA Fu J., Huang Y., Cai J., Wei S., Ouyang Z., Ye F., Huang X., Qin Q.;
RT "Identification and characterization of Rab7 from orange-spotted grouper,
RT Epinephelus coioides.";
RL Fish Shellfish Immunol. 36:19-26(2014).
CC -!- FUNCTION: Key regulator in endo-lysosomal trafficking. Governs early-
CC to-late endosomal maturation, microtubule minus-end as well as plus-end
CC directed endosomal migration and positioning, and endosome-lysosome
CC transport through different protein-protein interaction cascades. Plays
CC important roles in microbial pathogen infection and survival, as well
CC as in participating in the life cycle of viruses (By similarity).
CC {ECO:0000250|UniProtKB:P51149}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Singapore grouper
CC iridoviral proteins VP69 (ORF69) and VP101 (ORF101).
CC {ECO:0000269|PubMed:24161772}.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000250|UniProtKB:P51149}; Lipid-anchor {ECO:0000305}. Lysosome
CC membrane {ECO:0000269|PubMed:24161772}; Lipid-anchor {ECO:0000305}.
CC Note=Aggregates into the viral factories in cells infected by Singapore
CC grouper iridovirus (SGIV) in the late stages of the infection.
CC {ECO:0000269|PubMed:24161772}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed in liver, spleen,
CC kidney, brain, intestine, heart, skin, muscle, gill and stomach.
CC {ECO:0000269|PubMed:24161772}.
CC -!- INDUCTION: (Microbial infection) Down-regulated at 6 hours post
CC infection, and then up-regulated until 48 hours post infection in
CC spleen cells in response to Singapore grouper iridovirus (SGIV)
CC infection. {ECO:0000269|PubMed:24161772}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; JQ085431; AFD97434.1; -; mRNA.
DR AlphaFoldDB; H9BW96; -.
DR SMR; H9BW96; -.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0045022; P:early endosome to late endosome transport; ISS:UniProtKB.
DR GO; GO:0008333; P:endosome to lysosome transport; ISS:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISS:UniProtKB.
DR GO; GO:0048524; P:positive regulation of viral process; ISS:UniProtKB.
DR GO; GO:0006622; P:protein targeting to lysosome; ISS:UniProtKB.
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.
PE 1: Evidence at protein level;
KW Endosome; GTP-binding; Host-virus interaction; Lipid degradation;
KW Lipid metabolism; Lipoprotein; Lysosome; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Protein transport; Transport.
FT CHAIN 1..207
FT /note="Ras-related protein rab7"
FT /id="PRO_0000438075"
FT MOTIF 37..45
FT /note="Effector region"
FT /evidence="ECO:0000305"
FT BINDING 15..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P51149"
FT BINDING 34..40
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P51149"
FT BINDING 63..67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P51149"
FT BINDING 125..128
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P51149"
FT BINDING 156..157
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P51149"
FT MOD_RES 207
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000305"
FT LIPID 205
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000303|PubMed:24161772"
FT LIPID 207
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000303|PubMed:24161772"
SQ SEQUENCE 207 AA; 23567 MW; 4A3E3F29AE791463 CRC64;
MTSRKKVLLK VIILGDSGVG KTSLMNQYVN KKFSNQYKAT IGADFLTKEV MVDDRLVTMQ
IWDTAGQERF QSLGVAFYRG ADCCVLVFDV TAPNTFKTLD SWRDEFLIQA SPRDPENFPF
VVLGNKIDLE NRQVTTKRAQ AWCQSKNNIP YFETSAKEAI NVEQAFQTIA RNALKQETEV
ELYNEFPEPI KLDRNERAKP SAETCSC
