ID   CYFIP_DROPS             Reviewed;        1291 AA.
AC   Q299G2;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Cytoplasmic FMR1-interacting protein;
DE   AltName: Full=Specifically Rac1-associated protein 1;
GN   Name=Sra-1 {ECO:0000250|UniProtKB:Q9VF87}; ORFNames=GA18534;
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245;
RN   [1] {ECO:0000312|EMBL:EAL27741.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25 / Tucson 14011-0121.94;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA   Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA   Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA   Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA   Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA   Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA   Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT   gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
CC   -!- FUNCTION: Plays a role in guidance and morphology of central and
CC       peripheral axons and in synaptic morphology. Also required for
CC       formation of cell membrane protrusions and for bristle development (By
CC       similarity). {ECO:0000250|UniProtKB:Q9VF87}.
CC   -!- SUBUNIT: Interacts with Fmr1 and Rac1. Component of the WAVE complex
CC       composed of Hem/Kette, Scar/Wave and Sra-1/Cyfip where it binds through
CC       its C-terminus directly to Hem (By similarity).
CC       {ECO:0000250|UniProtKB:Q9VF87}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9VF87}.
CC       Note=Accumulates in central axons and motor neuron terminals.
CC       {ECO:0000250|UniProtKB:Q9VF87}.
CC   -!- SIMILARITY: Belongs to the CYFIP family. {ECO:0000255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAL27741.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CM000070; EAL27741.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001358600.1; XM_001358563.3.
DR   AlphaFoldDB; Q299G2; -.
DR   SMR; Q299G2; -.
DR   STRING; 7237.FBpp0283849; -.
DR   EnsemblMetazoa; FBtr0285411; FBpp0283849; FBgn0078536.
DR   GeneID; 4801524; -.
DR   KEGG; dpo:Dpse_GA18534; -.
DR   eggNOG; KOG3534; Eukaryota.
DR   HOGENOM; CLU_002688_2_1_1; -.
DR   InParanoid; Q299G2; -.
DR   OMA; MPKVCKL; -.
DR   PhylomeDB; Q299G2; -.
DR   Proteomes; UP000001819; Chromosome 2.
DR   Bgee; FBgn0078536; Expressed in female reproductive system and 2 other tissues.
DR   GO; GO:0045177; C:apical part of cell; IEA:EnsemblMetazoa.
DR   GO; GO:0031209; C:SCAR complex; ISS:UniProtKB.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
DR   GO; GO:0033627; P:cell adhesion mediated by integrin; IEA:EnsemblMetazoa.
DR   GO; GO:0030031; P:cell projection assembly; ISS:UniProtKB.
DR   GO; GO:0060269; P:centripetally migrating follicle cell migration; IEA:EnsemblMetazoa.
DR   GO; GO:0022416; P:chaeta development; ISS:UniProtKB.
DR   GO; GO:0001745; P:compound eye morphogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0051491; P:positive regulation of filopodium assembly; IEA:EnsemblMetazoa.
DR   GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
DR   GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR   GO; GO:0050807; P:regulation of synapse 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   3: Inferred from homology;
KW   Cell shape; Cytoplasm; Developmental protein; Differentiation;
KW   Neurogenesis; Reference proteome.
FT   CHAIN           1..1291
FT                   /note="Cytoplasmic FMR1-interacting protein"
FT                   /id="PRO_0000279715"
FT   REGION          1269..1291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1291 AA;  149362 MW;  4892892A9F05C030 CRC64;
     MTEKITLADA LSNVEVLDEL SLPDEQPCIE AQPCSIIYKA NFDTNFEDRN GFVTGIAKYI
     EEATTHANLN VLLDEGQKHA VMLYTWRCCS RAIPQPKSNE QPNRVEIYEK TVEVLAPEVN
     KLLNFMYFQR KAIEAFSGEV KRLCHAEKRK DFVSEAYLLT LGKFINMFAV LDELKNMKSS
     VKNDYSTYRR AAQFLKVMSD SHTLQESQNL SMFLATQNKI RDTVKDTLEK IVGYEDLLSD
     VVNICVHMFE TKMYLTPEEK HMLVKVMGFG LFLMDSDACN INKLDQKKKI RLDRIDRIFK
     NLEVVPLFGD MQIAPFNYIK RSKHFDSSKW PLSSSNAISP QADLMVHLPQ IREDHVKYIS
     ELARYTNEVT TTVKENPSDA ENRITADLAL RGLQLLSEWT SVVTELYSWK LLHPTDHHQN
     KECPVEAEEY ERATRYNYTS EEKFALIEVI AMIKGLQVLM ARIETVLCEA IRRNIYSELQ
     DFVQLSLREP LRKAVKNKKD LIRSIIMSVR ETSADWQKGY EPTDDPVSKG KKDPDGGFRI
     HVPRLNVGPS STQLYMVRTM LESLTADKSG GKRTLRKDID GNCLMQIETF HNTSFYWSYL
     LNFSDTLQKC CDLSQLWYRE FYLEMTMGRK VNKCMVRHQH NEECKDLITM EKRIQFPIEM
     SMPWILTDHI LQTKEPSMME FVLYPLDLYN DSAHYALTVF RKQFLYDEVE AEVNLCFDQF
     VYKLSEQIFA HYKQLAGSIF LDKRFRLECE VLGFNFQSYP RNNRYETLLK QRHVQLLGRS
     IDLNKLVTQR INANMHKSIE LAISRFEAND ITGIVELEGL LEANRICHKL LSKYLALDNF
     DGMVKEANHN VLAPYGRITL HVFVELNYDF LVNYCYNAAT NRFIRTKVNL SSTQAIQREK
     PPQMSHYYLW GSKQLNAAYS TQYGQYTGFV GSPHFHAMCR LLGYQGIAVV MDIILKDIVK
     PLIQGSLLQF TKTLMIAMPK SCKLPRCEYG SPGVLSYYQA HLTDIVQYPD TKTELFQSFR
     EFGNCIIFCL LIEQALSQEE VCDLLHAALF QNIFPRPFCK ENEKPEAKQK RLEAQFANLQ
     IVSNVEKIGT AKQAMIAREG DLLTRERLCC GLSIFEVILN RVKSYLDDPV WCGPPPANGI
     IHVDECSEFH RLWSALQFVY CIPVRGTEYT IEELFGEGLN WAGCVMIVLL GQQRRFEALD
     FCYHILRVQR VDGKDEDVKG IQLKRMVDRI RRFQVLNSQI FSILNKYLKG GDGEGSNVEH
     VRCFPPPQHP SVISSSSHYQ DPQKLRQSMN N