RUFY3_PONAB
ID RUFY3_PONAB Reviewed; 469 AA.
AC Q5R4V2;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Protein RUFY3 {ECO:0000305};
GN Name=RUFY3 {ECO:0000250|UniProtKB:Q9D394};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a role in the generation of neuronal polarity formation
CC and axon growth. Implicated in the formation of a single axon by
CC developing neurons. May inhibit the formation of additional axons by
CC inhibition of PI3K in minor neuronal processes. Plays a role in the
CC formation of F-actin-enriched protrusive structures at the cell
CC periphery. Plays a role in cytoskeletal organization by regulating the
CC subcellular localization of FSCN1 and DBN1 at axonal growth cones.
CC Promotes gastric cancer cell migration and invasion in a PAK1-dependent
CC manner. {ECO:0000250|UniProtKB:Q5FVJ0, ECO:0000250|UniProtKB:Q7L099,
CC ECO:0000250|UniProtKB:Q9D394}.
CC -!- SUBUNIT: Interacts with PAK1. Interacts (via C-terminus) with Ras-
CC related Rab-5 proteins. Interacts (via C-terminus) with Ras-related
CC Rap-2 proteins. Interacts with PIK3CA and PIK3R1. Interacts (via N-
CC terminus) with FSCN1; this interaction induces neuron axon development.
CC Interacts with DBN1. {ECO:0000250|UniProtKB:Q5FVJ0,
CC ECO:0000250|UniProtKB:Q7L099, ECO:0000250|UniProtKB:Q9D394}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7L099}.
CC Endomembrane system {ECO:0000250|UniProtKB:Q7L099}. Cell projection,
CC invadopodium {ECO:0000250|UniProtKB:Q7L099}. Perikaryon
CC {ECO:0000250|UniProtKB:Q9D394}. Cell projection
CC {ECO:0000250|UniProtKB:Q9D394}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:Q9D394}. Cell projection, filopodium
CC {ECO:0000250|UniProtKB:Q9D394}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:Q9D394}. Note=Colocalizes with PAK1, F-actin,
CC myosins and integrins in invadopodia at the cell periphery. Colocalized
CC with Ras-related Rab-5 proteins in cytoplasmic vesicles. Accumulates in
CC axon growth cones in a F-actin-dependent manner. Colocalized with FSCN1
CC and F-actin at filipodia and lamellipodia of axonal growth cones.
CC Colocalized with DBN1 and F-actin at transitional domain of the axonal
CC growth cone. {ECO:0000250|UniProtKB:Q5FVJ0,
CC ECO:0000250|UniProtKB:Q7L099, ECO:0000250|UniProtKB:Q9D394}.
CC -!- PTM: Phosphorylated by PAK1. {ECO:0000250|UniProtKB:Q7L099}.
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DR EMBL; CR861139; CAH93214.1; -; mRNA.
DR RefSeq; NP_001126891.1; NM_001133419.1.
DR AlphaFoldDB; Q5R4V2; -.
DR SMR; Q5R4V2; -.
DR STRING; 9601.ENSPPYP00000016540; -.
DR GeneID; 100173906; -.
DR KEGG; pon:100173906; -.
DR CTD; 22902; -.
DR eggNOG; KOG4381; Eukaryota.
DR InParanoid; Q5R4V2; -.
DR OrthoDB; 753155at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0030175; C:filopodium; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0050771; P:negative regulation of axonogenesis; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0045773; P:positive regulation of axon extension; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; ISS:UniProtKB.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; ISS:UniProtKB.
DR Gene3D; 1.20.58.900; -; 1.
DR InterPro; IPR004012; Run_dom.
DR InterPro; IPR037213; Run_dom_sf.
DR Pfam; PF02759; RUN; 1.
DR SMART; SM00593; RUN; 1.
DR SUPFAM; SSF140741; SSF140741; 1.
DR PROSITE; PS50826; RUN; 1.
PE 2: Evidence at transcript level;
KW Cell junction; Cell projection; Coiled coil; Cytoplasm;
KW Developmental protein; Differentiation; Membrane; Neurogenesis; Oncogene;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..469
FT /note="Protein RUFY3"
FT /id="PRO_0000245835"
FT DOMAIN 95..227
FT /note="RUN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00178"
FT COILED 267..464
FT /evidence="ECO:0000255"
FT MOD_RES 5
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5FVJ0"
FT MOD_RES 12
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5FVJ0"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D394"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D394"
FT MOD_RES 51
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9D394"
SQ SEQUENCE 469 AA; 52893 MW; BCBD9E7DDF499F43 CRC64;
MSALTPPTDM PTPTTDKITQ AAMETIYLCK FRVSMDGEWL CLRELDDISL TPDPEPTHED
PNYLMANERM NLMNMAKLSI KGLIESALNL GRTLDSDYAP LQQFFVVMEH CLKHGLKAKK
TFLGQNKSFW GPLELVEKLV PEAAEITASV KDLPGLKTPV GRGRAWLRLA LMQKKLSEYM
KALINKKELL SEFYEPNALM MEEEGAIIAG LLVGLNVIDA NFCMKGEDLD SQVGVIDFSM
YLKDGNSSKG TEGDGQITAI LDQKNYVEEL NRHLNATVNN LQAKVDALEK SNTKLTGELA
VANNRIITLQ EEMERVKEES SYILESNRKG PKQDRTAEGQ ALSEARKHLK EETQLRLDVE
KELEMQISMR QEMELAMKML EKDVCEKQDA LVSLRQQLDD LRALKHELAF KLQSSDLGVK
QKSELNSRLE EKTNQMAATI KQLEQSEKDL VKQAKTLNSA ANKLIPKHH
