RAB7A_PAROT
ID RAB7A_PAROT Reviewed; 206 AA.
AC Q95UJ0;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Ras-related protein Rab-7a {ECO:0000303|PubMed:22030555};
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P51149};
GN Name=Rab7a {ECO:0000312|EMBL:AAU95464.1};
GN Synonyms=Rab7 {ECO:0000312|EMBL:AAL08054.2};
OS Paramecium octaurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=43137;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RC STRAIN=299s {ECO:0000312|EMBL:AAL08054.2};
RX PubMed=12799062; DOI=10.1016/s0248-4900(03)00012-1;
RA Surmacz L., Wiejak J., Wyroba E.;
RT "Evolutionary conservancy of the endocytic and trafficking machinery in the
RT unicellular eukaryote Paramecium.";
RL Biol. Cell 95:69-74(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=299s {ECO:0000312|EMBL:AAU95464.1};
RX PubMed=16365637;
RA Surmacz L., Wiejak J., Wyroba E.;
RT "Cloning of two genes encoding Rab7 in Paramecium.";
RL Acta Biochim. Pol. 53:149-156(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=299s {ECO:0000312|EMBL:ACJ09042.1};
RA Osinska M., Wypych E., Wiejak J., Wyroba E.;
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION,
RP INDUCTION, AND PHOSPHORYLATION AT SER-17; SER-23; THR-34; THR-40; THR-64;
RP SER-72; TYR-78 AND TYR-88.
RC STRAIN=299s {ECO:0000269|PubMed:22030555};
RX PubMed=22030555;
RA Osinska M., Wiejak J., Wypych E., Bilski H., Bartosiewicz R., Wyroba E.;
RT "Distinct expression, localization and function of two Rab7 proteins
RT encoded by paralogous genes in a free-living model eukaryote.";
RL Acta Biochim. Pol. 58:597-607(2011).
CC -!- FUNCTION: Small GTPase which cycles between active GTP-bound and
CC inactive GDP-bound states. In its active state, binds to a variety of
CC effector proteins playing a key role in the regulation of endo-
CC lysosomal trafficking. Governs early-to-late endosomal maturation,
CC microtubule minus-end as well as plus-end directed endosomal migration
CC and positioning, and endosome-lysosome transport through different
CC protein-protein interaction cascades (By similarity). Involved in
CC lipophagy, a cytosolic lipase-independent autophagic pathway (By
CC similarity). Plays a role in phagocyte formation and acidification
CC (PubMed:22030555). {ECO:0000250|UniProtKB:P51149,
CC ECO:0000250|UniProtKB:P51150, ECO:0000269|PubMed:22030555}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000250|UniProtKB:P51149};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:P51149};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome membrane
CC {ECO:0000269|PubMed:12799062, ECO:0000269|PubMed:22030555}; Peripheral
CC membrane protein {ECO:0000269|PubMed:12799062,
CC ECO:0000269|PubMed:22030555}; Cytoplasmic side {ECO:0000305}. Late
CC endosome membrane {ECO:0000250|UniProtKB:P51149}; Peripheral membrane
CC protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Lysosome
CC membrane {ECO:0000250|UniProtKB:P51149}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle,
CC autophagosome membrane {ECO:0000250|UniProtKB:P51149}; Peripheral
CC membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Lipid
CC droplet {ECO:0000250|UniProtKB:P51150}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:P51150}.
CC -!- INDUCTION: Expression increases two-fold during phagocytosis (at
CC protein level). {ECO:0000269|PubMed:22030555}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000255}.
CC -!- CAUTION: Phosphorylation has been demonstrated on peptides which are
CC common to both Rab7a and Rab7b. {ECO:0000305}.
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DR EMBL; AY050242; AAL08054.2; -; Genomic_DNA.
DR EMBL; AY744503; AAU95464.1; -; mRNA.
DR EMBL; FJ358492; ACJ09042.1; -; Genomic_DNA.
DR AlphaFoldDB; Q95UJ0; -.
DR SMR; Q95UJ0; -.
DR iPTMnet; Q95UJ0; -.
DR GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032419; C:extrinsic component of lysosome membrane; ISS:GO_Central.
DR GO; GO:0031902; C:late endosome membrane; ISS:GO_Central.
DR GO; GO:0005811; C:lipid droplet; ISS:GO_Central.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IDA:UniProtKB.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0099638; P:endosome to plasma membrane protein transport; ISS:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0061724; P:lipophagy; ISS:GO_Central.
DR GO; GO:0090383; P:phagosome acidification; IMP:UniProtKB.
DR GO; GO:0090382; P:phagosome maturation; IMP: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.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW Autophagy; Cytoplasmic vesicle; Endosome; GTP-binding; Hydrolase;
KW Lipid degradation; Lipid droplet; Lipid metabolism; Lipoprotein; Lysosome;
KW Membrane; Nucleotide-binding; Phosphoprotein; Prenylation.
FT CHAIN 1..206
FT /note="Ras-related protein Rab-7a"
FT /id="PRO_0000421471"
FT MOTIF 37..45
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 15..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9NRW1"
FT BINDING 34..40
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 63..67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9NRW1"
FT BINDING 125..128
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9NRW1"
FT BINDING 157..158
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22030555"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22030555"
FT MOD_RES 34
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22030555"
FT MOD_RES 40
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22030555"
FT MOD_RES 64
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22030555"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22030555"
FT MOD_RES 78
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:22030555"
FT MOD_RES 88
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:22030555"
FT LIPID 205
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P62822"
FT LIPID 206
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P62822"
SQ SEQUENCE 206 AA; 23217 MW; 48CB4E47D8D4CF80 CRC64;
MASQKKQLFK IIILGDSGVG KTSLMNQYVN ARFTQQYRAT VGADFMAKEV MIDDRMVTLQ
IWDTAGQERF QSLGGAFYRG ADCCVLVYDI TNPKSFDSLD SWRDEFLMQG QPKDPEHFPF
VVLGNKLDKA TERKVQESKA QQWCKSHGNI QFFEVSAKDA TNIEQAFQDI AKAAASQEKD
EEIFFPTTVT LTKQSQKPQA KQGGCC
