General information | DisProt: | DP00458 | Name: | Rab proteins geranylgeranyltransferase component A 1 | Synonym(s): | RAE1_RAT
Rab escort protein 1
REP-1
Choroideraemia protein homolog
| First appeared in release: | Release 3.1 (03/31/2006) | UniProt: | P37727 | UniGene: | Rn.10191 | SwissProt: | RAE1_RAT | TrEMBL: | | NCBI (GI): | 585775 | Source organism: | Rattus norvegicus (Rat) | Sequence length: | 650 | Percent disordered: | 24% | Homologues: | |
Native sequence |
10 20 30 40 50 60 | | | | | | MADNLPSDFD VIVIGTGLPE SIIAAACSRS GQRVLHVDSR SYYGGNWASF SFSGLLSWLK - 60 EYQENNDVVT ENSMWQEQIL ENEEAIPLSS KDKTIQHVEV FCYASQDLHK DVEEAGALQK - 120 NHASVTSAQS AEAAEAAETS CLPTAVEPLS MGSCEIPAEQ SQCPGPESSP EVNDAEATGK - 180 KENSDAKSST EEPSENVPKV QDNTETPKKN RITYSQIIKE GRRFNIDLVS QLLYSRGLLI - 240 DLLIKSNVSR YAEFKNITRI LAFREGTVEQ VPCSRADVFN SKQLTMVEKR MLMKFLTFCV - 300 EYEEHPDEYR AYEGTTFSEY LKTQKLTPNL QYFVLHSIAM TSETTSCTVD GLKATKKFLQ - 360 CLGRYGNTPF LFPLYGQGEL PQCFCRMCAV FGGIYCLRHS VQCLVVDKES RKCKAVIDQF - 420 GQRIISKHFI IEDSYLSENT CSRVQYRQIS RAVLITDGSV LKTDADQQVS ILAVPAEEPG - 480 SFGVRVIELC SSTMTCMKGT YLVHLTCMSS KTAREDLERV VQKLFTPYTE IEAENEQVEK - 540 PRLLWALYFN MRDSSDISRD CYNDLPSNVY VCSGPDSGLG NDNAVKQAET LFQQICPNED - 600 FCPAPPNPED IVLDGDSSQQ EVPESSVTPE TNSETPKEST VLGNPEEPSE
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Functional narrative |
Binds unprenylated Rab proteins, presents it to the catalytic Rab GGTase dimer, and remains bound to it after the geranylgeranyl transfer reaction. The component A is thought to be regenerated by transferring its prenylated Rab back to the donor membrane.
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Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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Region 1 | Type: | Disordered | Name: | | Location: | 66 - 69 | Length: | 4 | Region sequence: |
NDVV | Modification type: | Complex
| PDB: | | Structural/functional type: | Relationship to function unknown | Functional classes: | Unknown
| Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (KSCN 100 mM; Namalonate 100 mM; PEG 3350 (17-20%))
| References:
- Pylypenko O, Rak A, Reents R, Niculae A, Sidorovitch V, Cioaca MD, Bessolitsyna E, Thoma NH, Waldmann H, Schlichting I, Goody RS, Alexandrov K. "Structure of Rab escort protein-1 in complex with Rab geranylgeranyltransferase." Mol Cell. 2003; 11(2): 483-94. PubMed: 12620235
- Rak A, Reents R, Pylypenko O, Niculae A, Sidorovitch V, Thoma NH, Waldmann H, Schlichting I, Goody RS, Alexandrov K. "Crystallization and preliminary X-ray diffraction analysis of the Rab escort protein-1 in complex with Rab geranylgeranyltransferase." J Struct Biol. 2001; 136(2): 158-61. PubMed: 11886217
| Comments:
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Region 2 | Type: | Disordered | Name: | | Location: | 108 - 208 | Length: | 101 | Region sequence: |
LHKDVEEAGALQKNHASVTSAQSAEAAEAAETSCLPTAVEPLSMGSCEIPAEQSQCPGPE SSPEVNDAEATGKKENSDAKSSTEEPSENVPKVQDNTETPK | Modification type: | Complex
| PDB: | | Structural/functional type: | Relationship to function unknown | Functional classes: | Unknown
| Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (KSCN 100 mM; Namalonate 100 mM; PEG 3350 (17-20%))
| References:
- Pylypenko O, Rak A, Reents R, Niculae A, Sidorovitch V, Cioaca MD, Bessolitsyna E, Thoma NH, Waldmann H, Schlichting I, Goody RS, Alexandrov K. "Structure of Rab escort protein-1 in complex with Rab geranylgeranyltransferase." Mol Cell. 2003; 11(2): 483-94. PubMed: 12620235
- Rak A, Reents R, Pylypenko O, Niculae A, Sidorovitch V, Thoma NH, Waldmann H, Schlichting I, Goody RS, Alexandrov K. "Crystallization and preliminary X-ray diffraction analysis of the Rab escort protein-1 in complex with Rab geranylgeranyltransferase." J Struct Biol. 2001; 136(2): 158-61. PubMed: 11886217
| Comments:
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Region 3 | Type: | Disordered | Name: | | Location: | 343 - 344 | Length: | 2 | Region sequence: |
ET | Modification type: | Complex
| PDB: | | Structural/functional type: | Relationship to function unknown | Functional classes: | Unknown
| Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (KSCN 100 mM; Namalonate 100 mM; PEG 3350 (17-20%))
| References:
- Pylypenko O, Rak A, Reents R, Niculae A, Sidorovitch V, Cioaca MD, Bessolitsyna E, Thoma NH, Waldmann H, Schlichting I, Goody RS, Alexandrov K. "Structure of Rab escort protein-1 in complex with Rab geranylgeranyltransferase." Mol Cell. 2003; 11(2): 483-94. PubMed: 12620235
- Rak A, Reents R, Pylypenko O, Niculae A, Sidorovitch V, Thoma NH, Waldmann H, Schlichting I, Goody RS, Alexandrov K. "Crystallization and preliminary X-ray diffraction analysis of the Rab escort protein-1 in complex with Rab geranylgeranyltransferase." J Struct Biol. 2001; 136(2): 158-61. PubMed: 11886217
| Comments:
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Region 4 | Type: | Disordered | Name: | | Location: | 533 - 538 | Length: | 6 | Region sequence: |
AENEQV | Modification type: | Complex
| PDB: | | Structural/functional type: | Relationship to function unknown | Functional classes: | Unknown
| Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (KSCN 100 mM; Namalonate 100 mM; PEG 3350 (17-20%))
| References:
- Pylypenko O, Rak A, Reents R, Niculae A, Sidorovitch V, Cioaca MD, Bessolitsyna E, Thoma NH, Waldmann H, Schlichting I, Goody RS, Alexandrov K. "Structure of Rab escort protein-1 in complex with Rab geranylgeranyltransferase." Mol Cell. 2003; 11(2): 483-94. PubMed: 12620235
- Rak A, Reents R, Pylypenko O, Niculae A, Sidorovitch V, Thoma NH, Waldmann H, Schlichting I, Goody RS, Alexandrov K. "Crystallization and preliminary X-ray diffraction analysis of the Rab escort protein-1 in complex with Rab geranylgeranyltransferase." J Struct Biol. 2001; 136(2): 158-61. PubMed: 11886217
| Comments:
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Region 5 | Type: | Disordered | Name: | | Location: | 602 - 607 | Length: | 6 | Region sequence: |
CPAPPN | Modification type: | Complex
| PDB: | | Structural/functional type: | Relationship to function unknown | Functional classes: | Unknown
| Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (KSCN 100 mM; Namalonate 100 mM; PEG 3350 (17-20%))
| References:
- Pylypenko O, Rak A, Reents R, Niculae A, Sidorovitch V, Cioaca MD, Bessolitsyna E, Thoma NH, Waldmann H, Schlichting I, Goody RS, Alexandrov K. "Structure of Rab escort protein-1 in complex with Rab geranylgeranyltransferase." Mol Cell. 2003; 11(2): 483-94. PubMed: 12620235
- Rak A, Reents R, Pylypenko O, Niculae A, Sidorovitch V, Thoma NH, Waldmann H, Schlichting I, Goody RS, Alexandrov K. "Crystallization and preliminary X-ray diffraction analysis of the Rab escort protein-1 in complex with Rab geranylgeranyltransferase." J Struct Biol. 2001; 136(2): 158-61. PubMed: 11886217
| Comments:
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Region 6 | Type: | Disordered | Name: | | Location: | 615 - 650 | Length: | 36 | Region sequence: |
GDSSQQEVPESSVTPETNSETPKESTVLGNPEEPSE | Modification type: | Complex
| PDB: | | Structural/functional type: | Relationship to function unknown | Functional classes: | Unknown
| Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (KSCN 100 mM; Namalonate 100 mM; PEG 3350 (17-20%))
| References:
- Pylypenko O, Rak A, Reents R, Niculae A, Sidorovitch V, Cioaca MD, Bessolitsyna E, Thoma NH, Waldmann H, Schlichting I, Goody RS, Alexandrov K. "Structure of Rab escort protein-1 in complex with Rab geranylgeranyltransferase." Mol Cell. 2003; 11(2): 483-94. PubMed: 12620235
- Rak A, Reents R, Pylypenko O, Niculae A, Sidorovitch V, Thoma NH, Waldmann H, Schlichting I, Goody RS, Alexandrov K. "Crystallization and preliminary X-ray diffraction analysis of the Rab escort protein-1 in complex with Rab geranylgeranyltransferase." J Struct Biol. 2001; 136(2): 158-61. PubMed: 11886217
| Comments:
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References |
- Andres DA, Seabra MC, Brown MS, Armstrong SA, Smeland TE, Cremers FP, Goldstein JL. "cDNA cloning of component A of Rab geranylgeranyl transferase and demonstration of its role as a Rab escort protein." Cell. 1993; 73(6): 1091-9. PubMed: 8513495
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Comments |
REP-1 forms a complex with a Rab protein immediately after translation. The Rab protein is then presented to RabGGTase for prenylation. After this step, the modified Rab protein is chaperoned to its target membrane, followed by the release of REP-1 to bind to a new molecule of unprenylated Rab.
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