ID M3ZW87_XIPMA Unreviewed; 667 AA.
AC M3ZW87;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Rab proteins geranylgeranyltransferase component A 1-like {ECO:0000313|Ensembl:ENSXMAP00000006481.2};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000006481.2, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000006481.2}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000006481.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the Rab GDI family.
CC {ECO:0000256|ARBA:ARBA00005593}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_014325920.1; XM_014470434.1.
DR AlphaFoldDB; M3ZW87; -.
DR Ensembl; ENSXMAT00000006489.2; ENSXMAP00000006481.2; ENSXMAG00000006439.2.
DR GeneID; 102221052; -.
DR KEGG; xma:102221052; -.
DR CTD; 1121; -.
DR eggNOG; KOG4405; Eukaryota.
DR GeneTree; ENSGT00950000182994; -.
DR HOGENOM; CLU_021695_4_1_1; -.
DR OrthoDB; 197300at2759; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0005968; C:Rab-protein geranylgeranyltransferase complex; IEA:InterPro.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 1.10.405.10; Guanine Nucleotide Dissociation Inhibitor, domain 1; 1.
DR Gene3D; 3.30.519.10; Guanine Nucleotide Dissociation Inhibitor, domain 2; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR018203; GDP_dissociation_inhibitor.
DR InterPro; IPR001738; Rab_escort.
DR PANTHER; PTHR11787; RAB GDP-DISSOCIATION INHIBITOR; 1.
DR PANTHER; PTHR11787:SF4; RAB PROTEINS GERANYLGERANYLTRANSFERASE COMPONENT A; 1.
DR Pfam; PF00996; GDI; 2.
DR PIRSF; PIRSF016550; Rab_ger_ger_transf_A_euk; 2.
DR PRINTS; PR00893; RABESCORT.
DR PRINTS; PR00891; RABGDIREP.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002852}.
FT REGION 105..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..120
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..162
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 667 AA; 74570 MW; 9A16B824217C3E4E CRC64;
MATEDLPSDF DIVILGTGLA ESVVAAACSR VGQRVLHLDR RSYYAANWAS FTFNGLLTWI
QEQNEEPKPE EVRDWSGLTE EGEELIHLSQ ADSASITNLQ VFSYASEEEE EEEAANTTEE
EKAADEEVVK ESSETESADS KEEEEEKEGA GEEEEQANQA EGEEPEADQP HPSSPGQSEP
SREKISYAQL VKEGRRFNID LVSKLMFSRG SLVDLLIKSN VSRYAEFKNV TRILTYRHGN
IEQVPCSRAD VFASRQLSVV EKRKLMRFLT SCVEETEEQT AYHGRPYLEF LRDQQLGDNL
QHFLLHSIAM VAEDTPTEEG LASTRHFLRS LGRYGNTPFL FPVYGLGEIP QCFCRMSAVF
GGIYCLRHSV HCLIVDRDAN RCKAVIDSRG QRISCSHVVM ETSYLDRSKV ATPPRFLSRA
VLITDSSVLP SESNQQISMV TVPPEGGSPA VKMVELSSSS MTCIPGTYLV HLTCRSVGSA
HQDLSPLVTR MFRTTESQEE DRRPSVLWSL YFNMADGMAS QVEGQPLPSN VHICHGPDSA
LGHEDAVQQA ASIFQRILPE EEFCPPAPNP EDIVYDGDNS STGEDRGDMG QDDGQNPEQN
QNQENPDPEQ NQNQENRNQN QENPDPEQNQ NQENRNQNQE NPDQEQNQNQ GNPELQRVGP
EESPSSS
//