GenomeNet

Database: UniProt
Entry: FAXC_DROME
LinkDB: FAXC_DROME
Original site: FAXC_DROME 
ID   FAXC_DROME              Reviewed;         418 AA.
AC   Q95RI5; Q9VV57;
DT   16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 162.
DE   RecName: Full=Failed axon connections;
GN   Name=fax; ORFNames=CG4609;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=8647396; DOI=10.1093/genetics/141.2.595;
RA   Hill K.K., Bedian V., Juang J.L., Hoffmann F.M.;
RT   "Genetic interactions between the Drosophila Abelson (Abl) tyrosine kinase
RT   and failed axon connections (fax), a novel protein in axon bundles.";
RL   Genetics 141:595-606(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
CC   -!- FUNCTION: Together with Abl, involved in embryonic axonal development.
CC       {ECO:0000269|PubMed:8647396}.
CC   -!- INTERACTION:
CC       Q95RI5; Q9U1K1-1: spir; NbExp=2; IntAct=EBI-147695, EBI-3431623;
CC   -!- DEVELOPMENTAL STAGE: Not detected in pregastrula embryos. Upon
CC       gastrulation, detected in the epidermis and visceral mesoderm. The
CC       expression pattern undergoes a pronounced change, such that epidermal
CC       expression decreases to background levels while mesodermal expression
CC       remains high. Visceral mesoderm expression decreases once formation of
CC       the gut tube is complete. Concurrently, central nervous system
CC       expression intensifies. Also detected in the peripheral nervous system.
CC       {ECO:0000269|PubMed:8647396}.
CC   -!- SIMILARITY: Belongs to the FAX family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY061352; AAL28900.1; -; mRNA.
DR   EMBL; AE014296; AAF49465.2; -; Genomic_DNA.
DR   PIR; S58776; S58776.
DR   RefSeq; NP_524106.3; NM_079382.7.
DR   AlphaFoldDB; Q95RI5; -.
DR   BioGRID; 65132; 75.
DR   DIP; DIP-18589N; -.
DR   IntAct; Q95RI5; 37.
DR   STRING; 7227.FBpp0075170; -.
DR   PaxDb; 7227-FBpp0075170; -.
DR   DNASU; 39826; -.
DR   EnsemblMetazoa; FBtr0075412; FBpp0075170; FBgn0014163.
DR   GeneID; 39826; -.
DR   KEGG; dme:Dmel_CG4609; -.
DR   UCSC; CG4609-RA; d. melanogaster.
DR   AGR; FB:FBgn0014163; -.
DR   CTD; 39826; -.
DR   FlyBase; FBgn0014163; fax.
DR   VEuPathDB; VectorBase:FBgn0014163; -.
DR   eggNOG; KOG4244; Eukaryota.
DR   GeneTree; ENSGT00950000182919; -.
DR   HOGENOM; CLU_044137_0_0_1; -.
DR   InParanoid; Q95RI5; -.
DR   OMA; CFPDWED; -.
DR   OrthoDB; 3684737at2759; -.
DR   PhylomeDB; Q95RI5; -.
DR   SignaLink; Q95RI5; -.
DR   BioGRID-ORCS; 39826; 0 hits in 1 CRISPR screen.
DR   ChiTaRS; fax; fly.
DR   GenomeRNAi; 39826; -.
DR   PRO; PR:Q95RI5; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0014163; Expressed in wing disc and 27 other cell types or tissues.
DR   ExpressionAtlas; Q95RI5; baseline and differential.
DR   Genevisible; Q95RI5; DM.
DR   GO; GO:0005737; C:cytoplasm; HDA:FlyBase.
DR   GO; GO:0005886; C:plasma membrane; HDA:FlyBase.
DR   GO; GO:0007409; P:axonogenesis; IGI:FlyBase.
DR   GO; GO:0036099; P:female germ-line stem cell population maintenance; IMP:FlyBase.
DR   CDD; cd03193; GST_C_Metaxin; 1.
DR   CDD; cd03080; GST_N_Metaxin_like; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR026928; FAX/IsoI-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR033468; Metaxin_GST.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR12289:SF78; FAILED AXON CONNECTIONS; 1.
DR   PANTHER; PTHR12289; METAXIN RELATED; 1.
DR   Pfam; PF17171; GST_C_6; 1.
DR   Pfam; PF17172; GST_N_4; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG01200; SUF1.1; 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
PE   1: Evidence at protein level;
KW   Developmental protein; Reference proteome.
FT   CHAIN           1..418
FT                   /note="Failed axon connections"
FT                   /id="PRO_0000417446"
FT   REGION          1..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          361..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..80
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   418 AA;  47105 MW;  E6D36F42D690AC5B CRC64;
     MASEVAQIPA EETPAVAAAE KSEEPEKSAA PPADSAAAPA AAPAVEKAED ADGEKKDGEA
     GKQDKQQDGE EPKKDEAVAA PVATKSEAPP AQKFNVHKTN FEKDIIYLYQ FSRTPLLPSL
     SPYCLKVETW LRLVGLKYEN VDHKMRFRSK KGQLPFIELN GEEIADSAII IKELSSKYEK
     YLDSGLTAEQ RNVSYATIAM LENHLIWIIF YWRAKYPDNV LKGYKVNLQH ALGLRLPNSI
     LNFFFKITFG RKWFQGTKKL KAHGIGVHSA EEIEEFGKDD LKVLSEMLDC KPFFFGDEPT
     TLDVVAFAVL SQLHYLSKDI AYPLRDYMTE KCPNLIGHVS RMKDKCFPDW DEICTKLDLN
     AHIPKPEPET KEGKEGGEQE KSNEQEGTEG DKIEKELEKD KSNEKESTEE NKEKEETK
//
DBGET integrated database retrieval system