ID   RAB7B_PAROT             Reviewed;         206 AA.
AC   Q6DUB4;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Ras-related protein Rab-7b {ECO:0000303|PubMed:22030555};
GN   Name=Rab7b {ECO:0000312|EMBL:AAT66502.1};
OS   Paramecium octaurelia.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX   NCBI_TaxID=43137;
RN   [1] {ECO:0000312|EMBL:AAT66502.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=299s {ECO:0000312|EMBL:AAT66502.1};
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   [2] {ECO:0000305}
RP   SUBCELLULAR LOCATION, INDUCTION, GLYCOSYLATION, AND PHOSPHORYLATION AT
RP   SER-17; SER-23; THR-34; THR-40; THR-64; 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   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:22030555}. Note=Localizes to the oral apparatus
CC       where it is associated with microtubules.
CC       {ECO:0000269|PubMed:22030555}.
CC   -!- INDUCTION: Expression increases by 55% during phagocytosis (at protein
CC       level). {ECO:0000269|PubMed:22030555}.
CC   -!- PTM: Glycosylated. {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; AY644723; AAT66502.1; -; mRNA.
DR   EMBL; AY875981; AAW68046.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6DUB4; -.
DR   SMR; Q6DUB4; -.
DR   iPTMnet; Q6DUB4; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR   GO; GO:0031912; C:oral apparatus; IDA:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
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   Cytoplasm; Cytoskeleton; Glycoprotein; GTP-binding; Lipoprotein;
KW   Nucleotide-binding; Phosphoprotein; Prenylation.
FT   CHAIN           1..206
FT                   /note="Ras-related protein Rab-7b"
FT                   /id="PRO_0000421472"
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;  23291 MW;  557C576833CCAB90 CRC64;
     MASQKKQLFK IIILGDSGVG KTSLMNQYVN ARFTQQYRAT VGADFMAKEV MIDDRMVTLQ
     IWDTAGQERF QSLGGAFYRG ADCCVLVYDI TNPKSFDSLD SWRDEFLMQG QPKDPEHFPF
     VVLGNKLDKA TERKVQESKS QQWCKSHGNI QFFEVSAKDA TNIEQAFQDI AKAAASQEKD
     EEIFFPTTVT LTKQDPKKQT KQGGCC