RAB4A_RAT
ID RAB4A_RAT Reviewed; 218 AA.
AC P05714; Q6P6U4;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Ras-related protein Rab-4A;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P20338};
GN Name=Rab4a; Synonyms=Rab4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=3344209; DOI=10.1093/nar/16.3.1204;
RA Zahraoui A., Touchot N., Chardin P., Tavitian A.;
RT "Complete coding sequences of the ras related rab 3 and 4 cDNAs.";
RL Nucleic Acids Res. 16:1204-1204(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INTERACTION WITH GRIPAP1, AND SUBCELLULAR LOCATION.
RX PubMed=20098723; DOI=10.1371/journal.pbio.1000283;
RA Hoogenraad C.C., Popa I., Futai K., Martinez-Sanchez E.,
RA Sanchez-Martinez E., Wulf P.S., van Vlijmen T., Dortland B.R., Oorschot V.,
RA Govers R., Monti M., Heck A.J., Sheng M., Klumperman J., Rehmann H.,
RA Jaarsma D., Kapitein L.C., van der Sluijs P.;
RT "Neuron specific Rab4 effector GRASP-1 coordinates membrane specialization
RT and maturation of recycling endosomes.";
RL PLoS Biol. 8:E1000283-E1000283(2010).
CC -!- FUNCTION: Small GTPase which cycles between an active GTP-bound and an
CC inactive GDP-bound state (By similarity). Involved in protein
CC transport. Plays a role in vesicular traffic. Mediates VEGFR2 endosomal
CC trafficking to enhance VEGFR2 signaling (By similarity). Acts as a
CC regulator of platelet alpha-granule release during activation and
CC aggregation of platelets (By similarity).
CC {ECO:0000250|UniProtKB:P20338, ECO:0000250|UniProtKB:P56371}.
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:P20338};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:P20338};
CC -!- SUBUNIT: Interacts with SGSM1, SGSM2 and SGSM3 (By similarity).
CC Interacts with RAB11FIP1, RABEP1, ZFYVE20 and RUFY1. Interacts
CC (membrane-bound form) with NDRG1; the interaction involves NDRG1 in
CC vesicular recycling of E-cadherin. Interacts (in GTP-bound form) with
CC GRIPAP1 (via N-terminus) (PubMed:20098723). Interacts with RABEP1 and
CC RBSN (By similarity). Does not interact with HPS4 (By similarity).
CC Interacts with RABEP2; this interaction may mediate VEGFR2 cell surface
CC expression (By similarity). {ECO:0000250|UniProtKB:P20338,
CC ECO:0000250|UniProtKB:P56371, ECO:0000269|PubMed:20098723}.
CC -!- INTERACTION:
CC P05714; Q9Y2I1: NISCH; Xeno; NbExp=3; IntAct=EBI-9029299, EBI-2688731;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P20338};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P20338}. Cytoplasm
CC {ECO:0000250|UniProtKB:P20338}. Early endosome membrane
CC {ECO:0000269|PubMed:20098723}; Peripheral membrane protein
CC {ECO:0000305}. Recycling endosome membrane
CC {ECO:0000269|PubMed:20098723}; Peripheral membrane protein
CC {ECO:0000305}. Note=Generally associated with membranes. Cytoplasmic
CC when phosphorylated by CDK1. {ECO:0000250|UniProtKB:P20338}.
CC -!- PTM: Serotonylation of Gln-72 by TGM2 during activation and aggregation
CC of platelets leads to constitutive activation of GTPase activity.
CC {ECO:0000250|UniProtKB:P56371}.
CC -!- PTM: Phosphorylated by CDK1 kinase during mitosis.
CC {ECO:0000250|UniProtKB:P20338}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA30006.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X06890; CAA30006.1; ALT_FRAME; mRNA.
DR EMBL; BC062016; AAH62016.1; -; mRNA.
DR PIR; S01766; S01766.
DR RefSeq; NP_037151.2; NM_013019.2.
DR AlphaFoldDB; P05714; -.
DR SMR; P05714; -.
DR IntAct; P05714; 1.
DR MINT; P05714; -.
DR STRING; 10116.ENSRNOP00000048878; -.
DR jPOST; P05714; -.
DR PaxDb; P05714; -.
DR PRIDE; P05714; -.
DR DNASU; 25532; -.
DR Ensembl; ENSRNOT00000049337; ENSRNOP00000048878; ENSRNOG00000017467.
DR GeneID; 25532; -.
DR KEGG; rno:25532; -.
DR UCSC; RGD:3529; rat.
DR CTD; 5867; -.
DR RGD; 3529; Rab4a.
DR eggNOG; KOG0086; Eukaryota.
DR GeneTree; ENSGT00940000157464; -.
DR HOGENOM; CLU_041217_23_1_1; -.
DR InParanoid; P05714; -.
DR OMA; STQECGC; -.
DR OrthoDB; 1146851at2759; -.
DR TreeFam; TF300032; -.
DR Reactome; R-RNO-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-RNO-8854214; TBC/RABGAPs.
DR Reactome; R-RNO-8873719; RAB geranylgeranylation.
DR Reactome; R-RNO-8875656; MET receptor recycling.
DR PRO; PR:P05714; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000017467; Expressed in cerebellum and 20 other tissues.
DR Genevisible; P05714; RN.
DR GO; GO:0098993; C:anchored component of synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; ISO:RGD.
DR GO; GO:0070062; C:extracellular exosome; ISO:RGD.
DR GO; GO:0032593; C:insulin-responsive compartment; IDA:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0098837; C:postsynaptic recycling endosome; IDA:SynGO.
DR GO; GO:0055037; C:recycling endosome; IDA:RGD.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031982; C:vesicle; ISO:RGD.
DR GO; GO:0001671; F:ATPase activator activity; IDA:RGD.
DR GO; GO:0051117; F:ATPase binding; IPI:RGD.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:RGD.
DR GO; GO:0003924; F:GTPase activity; IDA:RGD.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:RGD.
DR GO; GO:0019905; F:syntaxin binding; IPI:RGD.
DR GO; GO:0019882; P:antigen processing and presentation; ISO:RGD.
DR GO; GO:0015031; P:protein transport; ISO:RGD.
DR GO; GO:0032482; P:Rab protein signal transduction; IMP:RGD.
DR GO; GO:0030100; P:regulation of endocytosis; ISO:RGD.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; ISO:RGD.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd04113; Rab4; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041819; Rab4.
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; Endosome; GTP-binding; Hydrolase; Lipoprotein; Membrane;
KW Methylation; Nucleotide-binding; Phosphoprotein; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..218
FT /note="Ras-related protein Rab-4A"
FT /id="PRO_0000121095"
FT MOTIF 42..50
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 20..28
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61018"
FT BINDING 68..72
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62820"
FT BINDING 126..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61018"
FT BINDING 156..158
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P61018"
FT MOD_RES 72
FT /note="5-glutamyl serotonin"
FT /evidence="ECO:0000250|UniProtKB:P56371"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20338"
FT MOD_RES 204
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P20338"
FT MOD_RES 218
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 216
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 218
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 52
FT /note="S -> Q (in Ref. 1; CAA30006)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="R -> T (in Ref. 1; CAA30006)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="A -> P (in Ref. 1; CAA30006)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 218 AA; 24409 MW; A576827D571CAD01 CRC64;
MAQTAMSETY DFLFKFLVIG NAGTGKSCLL HQFIEKKFKD DSNHTIGVEF GSKIINVGGK
YVKLQIWDTA GQERFRSVTR SYYRGAAGAL LVYDITSRET YNALTNWLTD ARMLASQNIV
IILCGNKKDL DADREVTFLE ASRFAQENEL MFLETSALTG ENVEEAFMQC ARKILNKIES
GELDPERMGS GIQYGDAALR QLRSPRRTQA PSAQECGC
