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FAS3_DROME
ID   FAS3_DROME              Reviewed;         508 AA.
AC   P15278; Q8SXX9; Q9VJ89;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 192.
DE   RecName: Full=Fasciclin-3;
DE   AltName: Full=Fasciclin III;
DE            Short=FAS III;
DE   Flags: Precursor;
GN   Name=Fas3; ORFNames=CG5803;
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] (ISOFORM A), AND PYROGLUTAMATE FORMATION AT
RP   GLN-21.
RX   PubMed=2509076; DOI=10.1016/0092-8674(89)90293-6;
RA   Snow P.M., Bieber A.J., Goodman C.S.;
RT   "Fasciclin III: a novel homophilic adhesion molecule in Drosophila.";
RL   Cell 59:313-323(1989).
RN   [2]
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   [3]
RP   GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
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).
CC   -!- FUNCTION: Mediates cell adhesion in a Ca(2+)-independent manner. It
CC       plays a role in axon outgrowth, guidance and fasciculation of the
CC       developing nervous system.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A;
CC         IsoId=P15278-1; Sequence=Displayed;
CC       Name=B;
CC         IsoId=P15278-2; Sequence=VSP_007949, VSP_007950;
CC   -!- TISSUE SPECIFICITY: Expressed on different subsets of axon bundles
CC       (fascicles) in insect embryos.
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DR   EMBL; M27813; AAA28532.1; -; mRNA.
DR   EMBL; AE014134; AAF53665.2; -; Genomic_DNA.
DR   EMBL; AE014134; AAN11002.1; -; Genomic_DNA.
DR   EMBL; AY075516; AAL68324.1; -; mRNA.
DR   PIR; A33378; A33378.
DR   RefSeq; NP_001286039.1; NM_001299110.1. [P15278-2]
DR   RefSeq; NP_724106.1; NM_165249.4. [P15278-2]
DR   RefSeq; NP_724107.1; NM_165250.4. [P15278-1]
DR   AlphaFoldDB; P15278; -.
DR   BioGRID; 61092; 13.
DR   DIP; DIP-21336N; -.
DR   STRING; 7227.FBpp0111717; -.
DR   GlyGen; P15278; 3 sites.
DR   SwissPalm; P15278; -.
DR   PaxDb; P15278; -.
DR   DNASU; 35097; -.
DR   EnsemblMetazoa; FBtr0081051; FBpp0080604; FBgn0000636. [P15278-1]
DR   EnsemblMetazoa; FBtr0081052; FBpp0080605; FBgn0000636. [P15278-2]
DR   EnsemblMetazoa; FBtr0340580; FBpp0309467; FBgn0000636. [P15278-2]
DR   GeneID; 35097; -.
DR   KEGG; dme:Dmel_CG5803; -.
DR   CTD; 35097; -.
DR   FlyBase; FBgn0000636; Fas3.
DR   VEuPathDB; VectorBase:FBgn0000636; -.
DR   eggNOG; ENOG502QWSY; Eukaryota.
DR   GeneTree; ENSGT00940000169499; -.
DR   InParanoid; P15278; -.
DR   PhylomeDB; P15278; -.
DR   BioGRID-ORCS; 35097; 0 hits in 1 CRISPR screen.
DR   ChiTaRS; Fas3; fly.
DR   GenomeRNAi; 35097; -.
DR   PRO; PR:P15278; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0000636; Expressed in wing disc and 48 other tissues.
DR   ExpressionAtlas; P15278; baseline and differential.
DR   Genevisible; P15278; DM.
DR   GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:FlyBase.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0055037; C:recycling endosome; IDA:FlyBase.
DR   GO; GO:0005920; C:smooth septate junction; IDA:FlyBase.
DR   GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR   GO; GO:0007411; P:axon guidance; IEP:FlyBase.
DR   GO; GO:0007413; P:axonal fasciculation; TAS:FlyBase.
DR   GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; TAS:FlyBase.
DR   GO; GO:0008039; P:synaptic target recognition; IDA:FlyBase.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR013162; CD80_C2-set.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF08205; C2-set_2; 1.
DR   SUPFAM; SSF48726; SSF48726; 2.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Developmental protein;
KW   Differentiation; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW   Membrane; Neurogenesis; Phosphoprotein; Pyrrolidone carboxylic acid;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..20
FT   CHAIN           21..508
FT                   /note="Fasciclin-3"
FT                   /id="PRO_0000014760"
FT   TOPO_DOM        21..346
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        347..370
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        371..508
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          44..106
FT                   /note="Ig-like V-type"
FT   DOMAIN          126..223
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          236..310
FT                   /note="Ig-like C2-type 2"
FT   REGION          381..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..412
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         21
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000305|PubMed:2509076"
FT   MOD_RES         382
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         459
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        160
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        257
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        300
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        150..211
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   VAR_SEQ         391..401
FT                   /note="SDTESADIKAT -> KTNNSSMLNLY (in isoform B)"
FT                   /evidence="ECO:0000303|PubMed:12537569"
FT                   /id="VSP_007949"
FT   VAR_SEQ         402..508
FT                   /note="Missing (in isoform B)"
FT                   /evidence="ECO:0000303|PubMed:12537569"
FT                   /id="VSP_007950"
SQ   SEQUENCE   508 AA;  55884 MW;  6E39EA0580697D4F CRC64;
     MSRIVFICLA AILTDALTWA QVNVEPNTAL LNEGDRTELL CRYGRSINYC RIEIPGEQKV
     LNLSPEWSKT PGFTYFGAGL TAGQCGVSIE RVKASNNGQV KCSLGVEGEE LSGTIDLVVA
     LRPQQPIIEL LSRPNREGYF NEGTEFRARC SVRDGRPPAN ISWYIDNMPA NKRTTPLEVM
     SSTNDNVELS TSVQEIQWHL SPEDSNRKLV CRSHHQTDRE SVPPQEAAYI INVRYAPVHQ
     PDAAVYGLYL EHTAIVNITI RASPQPKIEW TIDGAIVGQG RTDGRYSAYE PQYLGNDEYN
     VTLAIAGLTL EDTTKIYNLR ASNELGLTDY QVRISSSSKP PSSSLDVAAI VGIVVAVAVL
     VLVVLLIVFA RATGRWCFGG KSIKTPTNET SDTESADIKA TSTATATTTM GGVGVSAEEE
     ETVNEQESPQ EQQQQQQKKA KRLPAFAAAI LRRFNEKDSR KYKDNQESLN IVEGSVQEIP
     ATNNAIDGND NEPKAIVWQS TSPVWTFK
 
 
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