CYFP1_BOVIN
ID CYFP1_BOVIN Reviewed; 51 AA.
AC P85091;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Cytoplasmic FMR1-interacting protein 1;
DE AltName: Full=Specifically Rac1-associated protein 1;
DE Short=Sra-1;
DE AltName: Full=p140sra-1;
DE Flags: Fragments;
GN Name=CYFIP1 {ECO:0000250|UniProtKB:Q7TMB8};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, AND INTERACTION WITH RAC1.
RC TISSUE=Brain {ECO:0000269|PubMed:9417078};
RX PubMed=9417078; DOI=10.1074/jbc.273.1.291;
RA Kobayashi K., Kuroda S., Fukata M., Nakamura T., Nagase T., Nomura N.,
RA Matsuura Y., Yoshida-Kubomura N., Iwamatsu A., Kaibuchi K.;
RT "p140Sra-1 (specifically Rac1-associated protein) is a novel specific
RT target for Rac1 small GTPase.";
RL J. Biol. Chem. 273:291-295(1998).
CC -!- FUNCTION: Component of the CYFIP1-EIF4E-FMR1 complex which binds to the
CC mRNA cap and mediates translational repression. In the CYFIP1-EIF4E-
CC FMR1 complex this subunit is an adapter between EIF4E and FMR1.
CC Promotes the translation repression activity of FMR1 in brain probably
CC by mediating its association with EIF4E and mRNA (By similarity).
CC Regulates formation of membrane ruffles and lamellipodia. Plays a role
CC in axon outgrowth. Binds to F-actin but not to RNA. Part of the WAVE
CC complex that regulates actin filament reorganization via its
CC interaction with the Arp2/3 complex. Actin remodeling activity is
CC regulated by RAC1. Regulator of epithelial morphogenesis (By
CC similarity). As component of the WAVE1 complex, required for BDNF-NTRK2
CC endocytic trafficking and signaling from early endosomes (By
CC similarity). {ECO:0000250|UniProtKB:Q7L576,
CC ECO:0000250|UniProtKB:Q7TMB8}.
CC -!- SUBUNIT: Component of the WAVE1 complex composed of ABI2, CYFIP1 or
CC CYFIP2, BRK1, NCKAP1 and WASF1/WAVE1. Within the complex, a heterodimer
CC containing NCKAP1 and CYFIP1 interacts with a heterotrimer formed by
CC WAVE1, ABI2 and BRK1. Component of the CYFIP1-EIF4E-FMR1 complex which
CC is composed of CYFIP, EIF4E and FMR1. Interacts with FMR1 but does not
CC bind to related proteins FXR1 or FXR2. Interaction with EIF4E
CC stimulates FMR1 binding. Component of the WAVE2 complex composed of
CC ABI1, CYFIP1/SRA1, NCKAP1/NAP1 (NCKAP1l/HEM1 in hematopoietic cells)
CC and WASF2/WAVE2. Interacts with the active GTP-bound form of RAC1.
CC Interacts through its C-terminus with the C-terminus of DPYSL2/CRMP2
CC which is necessary for DPYSL2-induced axon outgrowth. Interacts with
CC NYAP1, NYAP2 and MYO16. Interacts with TMEM108 (via N-terminus); the
CC interaction associates TMEM108 with the WAVE1 complex (By similarity).
CC {ECO:0000250|UniProtKB:Q7L576, ECO:0000250|UniProtKB:Q7TMB8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7TMB8}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q7TMB8}. Cell
CC projection, lamellipodium {ECO:0000250|UniProtKB:Q7TMB8}. Cell
CC projection, ruffle {ECO:0000250|UniProtKB:Q7TMB8}. Synapse, synaptosome
CC {ECO:0000250|UniProtKB:Q7TMB8}. Note=Highly expressed in the
CC perinuclear region (By similarity). Enriched in synaptosomes (By
CC similarity). Also enriched in membrane ruffles and at the tips of
CC lamellipodia (By similarity). {ECO:0000250|UniProtKB:Q7TMB8}.
CC -!- SIMILARITY: Belongs to the CYFIP family. {ECO:0000255}.
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DR AlphaFoldDB; P85091; -.
DR SMR; P85091; -.
DR CORUM; P85091; -.
DR PRIDE; P85091; -.
DR OrthoDB; 108507at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0005845; C:mRNA cap binding complex; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0001726; C:ruffle; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IDA:UniProtKB.
DR GO; GO:0048675; P:axon extension; ISS:UniProtKB.
DR GO; GO:0030032; P:lamellipodium assembly; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0031529; P:ruffle organization; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW Actin-binding; Cell projection; Cell shape; Cytoplasm;
KW Developmental protein; Differentiation; Direct protein sequencing;
KW Neurogenesis; Reference proteome; Synapse; Synaptosome.
FT CHAIN <1..>51
FT /note="Cytoplasmic FMR1-interacting protein 1"
FT /id="PRO_0000279705"
FT NON_CONS 8..9
FT /evidence="ECO:0000303|PubMed:9417078"
FT NON_CONS 14..15
FT /evidence="ECO:0000303|PubMed:9417078"
FT NON_CONS 20..21
FT /evidence="ECO:0000303|PubMed:9417078"
FT NON_CONS 30..31
FT /evidence="ECO:0000303|PubMed:9417078"
FT NON_CONS 34..35
FT /evidence="ECO:0000303|PubMed:9417078"
FT NON_CONS 47..48
FT /evidence="ECO:0000303|PubMed:9417078"
FT NON_TER 1
FT /evidence="ECO:0000303|PubMed:9417078"
FT NON_TER 51
FT /evidence="ECO:0000303|PubMed:9417078"
SQ SEQUENCE 51 AA; 6047 MW; C81106ABFE2E1081 CRC64;
MYLTPSEKRI NLSKVHPTDK LADQIFAYYK EGERDGKDEI IKNVPLKRIR K
