CYFP1_DANRE
ID CYFP1_DANRE Reviewed; 1253 AA.
AC Q90YM8; Q58ES3;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Cytoplasmic FMR1-interacting protein 1 homolog;
GN Name=cyfip1 {ECO:0000312|ZFIN:ZDB-GENE-030131-8557};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1] {ECO:0000312|EMBL:AAG61253.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11438699; DOI=10.1073/pnas.151231598;
RA Schenck A., Bardoni B., Moro A., Bagni C., Mandel J.-L.;
RT "A highly conserved protein family interacting with the fragile X mental
RT retardation protein (FMRP) and displaying selective interactions with FMRP-
RT related proteins FXR1P and FXR2P.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:8844-8849(2001).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAH91781.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-510.
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH91781.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in formation of membrane ruffles and lamellipodia
CC protrusions and in axon outgrowth. Binds to F-actin but not to RNA (By
CC similarity). {ECO:0000250|UniProtKB:Q7L576,
CC 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 EMBL; AY017342; AAG61253.1; -; mRNA.
DR EMBL; BC091781; AAH91781.1; -; mRNA.
DR RefSeq; NP_997924.1; NM_212759.1.
DR AlphaFoldDB; Q90YM8; -.
DR SMR; Q90YM8; -.
DR STRING; 7955.ENSDARP00000095008; -.
DR PaxDb; Q90YM8; -.
DR GeneID; 336613; -.
DR KEGG; dre:336613; -.
DR CTD; 23191; -.
DR ZFIN; ZDB-GENE-030131-8557; cyfip1.
DR eggNOG; KOG3534; Eukaryota.
DR InParanoid; Q90YM8; -.
DR OrthoDB; 108507at2759; -.
DR PhylomeDB; Q90YM8; -.
DR Reactome; R-DRE-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-DRE-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-DRE-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-DRE-6798695; Neutrophil degranulation.
DR Reactome; R-DRE-9013149; RAC1 GTPase cycle.
DR Reactome; R-DRE-9013404; RAC2 GTPase cycle.
DR Reactome; R-DRE-9013408; RHOG GTPase cycle.
DR Reactome; R-DRE-9013423; RAC3 GTPase cycle.
DR PRO; PR:Q90YM8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISS:ZFIN.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0031209; C:SCAR complex; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0048675; P:axon extension; ISS:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR GO; GO:0030031; P:cell projection assembly; IBA:GO_Central.
DR GO; GO:0030032; P:lamellipodium assembly; ISS:UniProtKB.
DR GO; GO:0099563; P:modification of synaptic structure; IBA:GO_Central.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0006417; P:regulation of translation; IBA:GO_Central.
DR GO; GO:0031529; P:ruffle organization; ISS:UniProtKB.
DR InterPro; IPR009828; CYRIA/CYRIB_Rac1-bd.
DR InterPro; IPR008081; Cytoplasmic_FMR1-int.
DR PANTHER; PTHR12195; PTHR12195; 1.
DR Pfam; PF07159; DUF1394; 1.
DR Pfam; PF05994; FragX_IP; 1.
DR PIRSF; PIRSF008153; FMR1_interacting; 1.
DR PRINTS; PR01698; CYTOFMRPINTP.
PE 2: Evidence at transcript level;
KW Actin-binding; Cell projection; Cell shape; Cytoplasm;
KW Developmental protein; Differentiation; Neurogenesis; Reference proteome;
KW Synapse; Synaptosome.
FT CHAIN 1..1253
FT /note="Cytoplasmic FMR1-interacting protein 1 homolog"
FT /id="PRO_0000279708"
FT CONFLICT 260
FT /note="R -> K (in Ref. 2; AAH91781)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="A -> T (in Ref. 2; AAH91781)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="T -> A (in Ref. 2; AAH91781)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="G -> D (in Ref. 2; AAH91781)"
FT /evidence="ECO:0000305"
FT CONFLICT 505..510
FT /note="NVVQSV -> KKKKKK (in Ref. 2; AAH91781)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1253 AA; 145174 MW; ABE478AAB264B32D CRC64;
MASTVTLEDA LSNVDLLEEL PLPDQQPCIE PLPSSLIYQP NFNTNFEDRN AFVTGIARYI
EQATVHSSMN DMLEEGQQYA VMLYTWRCCS RAIPQVKCNE QPNRVEIYEK TVEVLEPEVN
KLMNFMYFQR TAIDRFCGEV RRLCHAERRK DFVSEAYLLT LGKFINMFAV LDELKNMKCS
VKNDHSAYKR AAQFLRKMSE PSSIQESQNL SMFLANHNKI TQSLQQQLEV INGYDELLAD
IVNLCVDYYE NKMYLTPSER HMLLKVMGFG LYLMDGSNSN IYKLEAKKRI NLTKIDKFFK
QLQVVPLFGD MQIELARYIK TSAHYEENKS RWSCTSTGSS PQYNVCEQMI QIREGHMRFI
SELARYSNSE VVTGSGRQDA QKTDSEYRKL FDLALQGLQL LSQWSAQIME VYSWKLVHPT
DKYSNKECPD NAEEYERATR YNYTSEEKFA LVEVLAMIKG LQVLMGRMES VFNHAIRHTI
YSALQDFAQV TLREPLRQAI KKKKNVVQSV LQAIRKTVCD WETGREPHND PALRGEKDPK
GGFDIKVPRR AVGPSSTQLY MVRTMLESLV ADKSGSKKTL RSSLEGPTIL DIEKFHRESF
FYTHLLNFSE TLQQCCDLSQ LWFREFFLEL TMGRRIQFPI EMSMPWILTD HILETKEASM
MEYVLYSLDL YNDSAHYALT KFKKQFLYDE IEAEVNLCFD QFVYKLADQI FAYYKVIAGS
LLLDKRLRAE CKNQGANISW PSSNRYETLL KQRHVQLLGR SIDLNRLITQ RVSSALYKSL
ELAISRFESE DLTSIMELEG LLDINRMTHK LLSKYLTLDS IDAMFREANH NVSAPYGRIT
LHVFWELNYD FLPNYCYNGS TNRFVRTILP FSQEFQRDKP PNAQPQYLYG SKALNLAYSS
IYSLYRNFVG PPHIKAICRL LGYQGIAVVM EELLKVVKSL LQGTILQYVK TLMEVMPKIC
RLPRHEYGSP GILEFFHHQL KDIVEYAELK SVCFQNLREV GNALLFCLLT EQSLSQEEVC
DLLHAAPFQN ILPRVHVKEG ERLDAKMKRL EAKYTALHLV PLIERLGTPQ QIAIAREGDL
LTKERLCCGL SIFEVILTRV RAYLDDPIWR GPLPSNGVMH VDECVEFHRL WSAMQFVYCI
PVGAHEFTVE QCFGDGLNWA GCMIITLLGQ HRRFDILDFS YHLLKVQKHD GKDEIIKSVP
LKKMVDRIRK FQILNDEIFA ILNKYLKSGD GENMPVEHVR CFQPPIHQSL ASN
