FAS1_DROME
ID FAS1_DROME Reviewed; 652 AA.
AC P10674;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Fasciclin-1;
DE AltName: Full=Fasciclin I;
DE Short=FAS I;
DE Short=FCN;
DE Flags: Precursor;
GN Name=Fas1; ORFNames=CG6588;
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].
RX PubMed=3370670; DOI=10.1016/0092-8674(88)90574-0;
RA Zinn K., McAllister L., Goodman C.;
RT "Sequence analysis and neuronal expression of fasciclin I in grasshopper
RT and Drosophila.";
RL Cell 53:577-587(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=1545245; DOI=10.1523/jneurosci.12-03-00895.1992;
RA McAllister L., Rehm E.J., Goodman G.S., Zinn K.;
RT "Alternative splicing of micro-exons creates multiple forms of the insect
RT cell adhesion molecule fasciclin I.";
RL J. Neurosci. 12:895-905(1992).
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).
RN [5]
RP GPI-ANCHOR.
RX PubMed=2394715; DOI=10.1016/s0021-9258(18)77229-3;
RA Hortsch M., Goodman C.S.;
RT "Drosophila fasciclin I, a neural cell adhesion molecule, has a
RT phosphatidylinositol lipid membrane anchor that is developmentally
RT regulated.";
RL J. Biol. Chem. 265:15104-15109(1990).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-497, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=17893096; DOI=10.1093/glycob/cwm097;
RA Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
RA Panin V.;
RT "Identification of N-glycosylated proteins from the central nervous system
RT of Drosophila melanogaster.";
RL Glycobiology 17:1388-1403(2007).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-497, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 314-628, AND GLYCOSYLATION AT
RP ASN-441.
RX PubMed=12575939; DOI=10.1016/s0969-2126(03)00002-9;
RA Clout N.J., Tisi D., Hohenester E.;
RT "Novel fold revealed by the structure of a FAS1 domain pair from the insect
RT cell adhesion molecule fasciclin I.";
RL Structure 11:197-203(2003).
CC -!- FUNCTION: Neural cell adhesion molecule.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=Many isoforms are produced by alternative splicing.
CC {ECO:0000269|PubMed:1545245};
CC Name=1;
CC IsoId=P10674-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed on different subsets of axon bundles
CC (fascicles) in insect embryos.
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DR EMBL; M20545; AAA28531.1; -; mRNA.
DR EMBL; M32311; AAA28529.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13715.1; -; Genomic_DNA.
DR PIR; B29900; B29900.
DR RefSeq; NP_732165.1; NM_169725.2. [P10674-1]
DR PDB; 1O70; X-ray; 2.60 A; A=314-628.
DR PDBsum; 1O70; -.
DR AlphaFoldDB; P10674; -.
DR SMR; P10674; -.
DR BioGRID; 67070; 9.
DR IntAct; P10674; 1.
DR STRING; 7227.FBpp0111715; -.
DR GlyGen; P10674; 5 sites.
DR iPTMnet; P10674; -.
DR PaxDb; P10674; -.
DR PRIDE; P10674; -.
DR DNASU; 42025; -.
DR EnsemblMetazoa; FBtr0083333; FBpp0082783; FBgn0285925. [P10674-1]
DR GeneID; 42025; -.
DR KEGG; dme:Dmel_CG6588; -.
DR CTD; 42025; -.
DR FlyBase; FBgn0285925; Fas1.
DR VEuPathDB; VectorBase:FBgn0285925; -.
DR eggNOG; KOG1437; Eukaryota.
DR GeneTree; ENSGT00530000063860; -.
DR InParanoid; P10674; -.
DR PhylomeDB; P10674; -.
DR SignaLink; P10674; -.
DR BioGRID-ORCS; 42025; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Fas1; fly.
DR EvolutionaryTrace; P10674; -.
DR GenomeRNAi; 42025; -.
DR PRO; PR:P10674; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0285925; Expressed in seminal fluid secreting gland and 42 other tissues.
DR ExpressionAtlas; P10674; baseline and differential.
DR Genevisible; P10674; DM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0050839; F:cell adhesion molecule binding; IDA:FlyBase.
DR GO; GO:0007411; P:axon guidance; IGI:FlyBase.
DR GO; GO:0016338; P:calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules; IDA:FlyBase.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:FlyBase.
DR GO; GO:0008038; P:neuron recognition; IDA:FlyBase.
DR Gene3D; 2.30.180.10; -; 4.
DR InterPro; IPR036378; FAS1_dom_sf.
DR InterPro; IPR000782; FAS1_domain.
DR Pfam; PF02469; Fasciclin; 4.
DR SMART; SM00554; FAS1; 4.
DR SUPFAM; SSF82153; SSF82153; 4.
DR PROSITE; PS50213; FAS1; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Reference proteome;
KW Repeat; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..625
FT /note="Fasciclin-1"
FT /id="PRO_0000008772"
FT PROPEP 626..652
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000008773"
FT DOMAIN 22..144
FT /note="FAS1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT DOMAIN 166..310
FT /note="FAS1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT DOMAIN 317..463
FT /note="FAS1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT DOMAIN 467..616
FT /note="FAS1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT LIPID 625
FT /note="GPI-anchor amidated alanine"
FT /evidence="ECO:0000255"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12575939"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096,
FT ECO:0000269|PubMed:19349973"
FT HELIX 330..342
FT /evidence="ECO:0007829|PDB:1O70"
FT HELIX 346..352
FT /evidence="ECO:0007829|PDB:1O70"
FT STRAND 355..362
FT /evidence="ECO:0007829|PDB:1O70"
FT HELIX 364..369
FT /evidence="ECO:0007829|PDB:1O70"
FT HELIX 373..376
FT /evidence="ECO:0007829|PDB:1O70"
FT HELIX 379..388
FT /evidence="ECO:0007829|PDB:1O70"
FT STRAND 390..393
FT /evidence="ECO:0007829|PDB:1O70"
FT HELIX 397..403
FT /evidence="ECO:0007829|PDB:1O70"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:1O70"
FT STRAND 411..415
FT /evidence="ECO:0007829|PDB:1O70"
FT STRAND 419..426
FT /evidence="ECO:0007829|PDB:1O70"
FT HELIX 428..430
FT /evidence="ECO:0007829|PDB:1O70"
FT STRAND 432..437
FT /evidence="ECO:0007829|PDB:1O70"
FT STRAND 440..450
FT /evidence="ECO:0007829|PDB:1O70"
FT STRAND 452..461
FT /evidence="ECO:0007829|PDB:1O70"
FT HELIX 470..476
FT /evidence="ECO:0007829|PDB:1O70"
FT HELIX 478..480
FT /evidence="ECO:0007829|PDB:1O70"
FT HELIX 481..486
FT /evidence="ECO:0007829|PDB:1O70"
FT TURN 487..491
FT /evidence="ECO:0007829|PDB:1O70"
FT HELIX 494..497
FT /evidence="ECO:0007829|PDB:1O70"
FT STRAND 499..508
FT /evidence="ECO:0007829|PDB:1O70"
FT HELIX 510..519
FT /evidence="ECO:0007829|PDB:1O70"
FT HELIX 521..527
FT /evidence="ECO:0007829|PDB:1O70"
FT HELIX 530..532
FT /evidence="ECO:0007829|PDB:1O70"
FT HELIX 533..541
FT /evidence="ECO:0007829|PDB:1O70"
FT STRAND 544..549
FT /evidence="ECO:0007829|PDB:1O70"
FT HELIX 553..562
FT /evidence="ECO:0007829|PDB:1O70"
FT STRAND 563..569
FT /evidence="ECO:0007829|PDB:1O70"
FT STRAND 571..582
FT /evidence="ECO:0007829|PDB:1O70"
FT STRAND 585..590
FT /evidence="ECO:0007829|PDB:1O70"
FT STRAND 593..604
FT /evidence="ECO:0007829|PDB:1O70"
FT STRAND 607..614
FT /evidence="ECO:0007829|PDB:1O70"
FT TURN 619..622
FT /evidence="ECO:0007829|PDB:1O70"
SQ SEQUENCE 652 AA; 72599 MW; 4D846358A47DBFD6 CRC64;
MLNAAALLLA LLCAANAAAA ADLADKLRDD SELSQFYSLL ESNQIANSTL SLRSCTIFVP
TNEAFQRYKS KTAHVLYHIT TEAYTQKRLP NTVSSDMAGN PPLYITKNSN GDIFVNNARI
IPSLSVETNS DGKRQIMHII DEVLEPLTVK AGHSDTPNNP NALKFLKNAE EFNVDNIGVR
TYRSQVTMAK KESVYDAAGQ HTFLVPVDEG FKLSARSSLV DGKVIDGHVI PNTVIFTAAA
QHDDPKASAA FEDLLKVTVS FFKQKNGKMY VKSNTIVGDA KHRVGVVLAE IVKANIPVSN
GVVHLIHRPL MIIDTTVTQF LQSFKENAEN GALRKFYEVI MDNGGAVLDD INSLTEVTIL
APSNEAWNSS NINNVLRDRN KMRQILNMHI IKDRLNVDKI RQKNANLIAQ VPTVNNNTFL
YFNVRGEGSD TVITVEGGGV NATVIQADVA QTNGYVHIID HVLGVPYTTV LGKLESDPMM
SDTYKMGKFS HFNDQLNNTQ RRFTYFVPRD KGWQKTELDY PSAHKKLFMA DFSYHSKSIL
ERHLAISDKE YTMKDLVKFS QESGSVILPT FRDSLSIRVE EEAGRYVIIW NYKKINVYRP
DVECTNGIIH VIDYPLLEEK DVVVAGGSYL PESSICIILA NLIMITVAKF LN
