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Database: UniProt
Entry: M3ZW87_XIPMA
LinkDB: M3ZW87_XIPMA
Original site: M3ZW87_XIPMA 
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}.
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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
//
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