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Protein

Fasciclin-1

Gene

Fas1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Neural cell adhesion molecule.

GO - Molecular functioni

  • cell adhesion molecule binding Source: FlyBase

GO - Biological processi

  • axon guidance Source: FlyBase
  • calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules Source: FlyBase
  • homophilic cell adhesion via plasma membrane adhesion molecules Source: FlyBase
  • neuron cell-cell adhesion Source: FlyBase
  • neuron recognition Source: FlyBase
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Names & Taxonomyi

Protein namesi
Recommended name:
Fasciclin-1
Alternative name(s):
Fasciclin I
Short name:
FAS I
Short name:
FCN
Gene namesi
Name:Fas1
ORF Names:CG6588
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0262742. Fas1.

Subcellular locationi

GO - Cellular componenti

  • anchored component of membrane Source: UniProtKB-KW
  • plasma membrane Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Chaini22 – 625604Fasciclin-1PRO_0000008772Add
BLAST
Propeptidei626 – 65227Removed in mature formSequence analysisPRO_0000008773Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi47 – 471N-linked (GlcNAc...)Sequence analysis
Glycosylationi368 – 3681N-linked (GlcNAc...)Sequence analysis
Glycosylationi416 – 4161N-linked (GlcNAc...)Sequence analysis
Glycosylationi441 – 4411N-linked (GlcNAc...)1 Publication
Glycosylationi493 – 4931N-linked (GlcNAc...); atypical1 Publication
Glycosylationi497 – 4971N-linked (GlcNAc...)2 Publications
Lipidationi625 – 6251GPI-anchor amidated alanineSequence analysis

Keywords - PTMi

Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiP10674.
PRIDEiP10674.

Expressioni

Tissue specificityi

Expressed on different subsets of axon bundles (fascicles) in insect embryos.

Gene expression databases

BgeeiP10674.
ExpressionAtlasiP10674. differential.
GenevisibleiP10674. DM.

Interactioni

GO - Molecular functioni

  • cell adhesion molecule binding Source: FlyBase

Protein-protein interaction databases

BioGridi67070. 7 interactions.
IntActiP10674. 1 interaction.
STRINGi7227.FBpp0111715.

Structurei

Secondary structure

1
652
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi330 – 34213Combined sources
Helixi346 – 3527Combined sources
Beta strandi355 – 3628Combined sources
Helixi364 – 3696Combined sources
Helixi373 – 3764Combined sources
Helixi379 – 38810Combined sources
Beta strandi390 – 3934Combined sources
Helixi397 – 4037Combined sources
Beta strandi405 – 4073Combined sources
Beta strandi411 – 4155Combined sources
Beta strandi419 – 4268Combined sources
Helixi428 – 4303Combined sources
Beta strandi432 – 4376Combined sources
Beta strandi440 – 45011Combined sources
Beta strandi452 – 46110Combined sources
Helixi470 – 4767Combined sources
Helixi478 – 4803Combined sources
Helixi481 – 4866Combined sources
Turni487 – 4915Combined sources
Helixi494 – 4974Combined sources
Beta strandi499 – 50810Combined sources
Helixi510 – 51910Combined sources
Helixi521 – 5277Combined sources
Helixi530 – 5323Combined sources
Helixi533 – 5419Combined sources
Beta strandi544 – 5496Combined sources
Helixi553 – 56210Combined sources
Beta strandi563 – 5697Combined sources
Beta strandi571 – 58212Combined sources
Beta strandi585 – 5906Combined sources
Beta strandi593 – 60412Combined sources
Beta strandi607 – 6148Combined sources
Turni619 – 6224Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1O70X-ray2.60A314-628[»]
ProteinModelPortaliP10674.
SMRiP10674. Positions 328-623.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10674.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 144123FAS1 1PROSITE-ProRule annotationAdd
BLAST
Domaini166 – 310145FAS1 2PROSITE-ProRule annotationAdd
BLAST
Domaini317 – 463147FAS1 3PROSITE-ProRule annotationAdd
BLAST
Domaini467 – 616150FAS1 4PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 4 FAS1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG1437. Eukaryota.
COG2335. LUCA.
GeneTreeiENSGT00530000063860.
InParanoidiP10674.
OrthoDBiEOG79CXXZ.
PhylomeDBiP10674.

Family and domain databases

Gene3Di2.30.180.10. 4 hits.
InterProiIPR000782. FAS1_domain.
[Graphical view]
PfamiPF02469. Fasciclin. 4 hits.
[Graphical view]
SMARTiSM00554. FAS1. 4 hits.
[Graphical view]
SUPFAMiSSF82153. SSF82153. 4 hits.
PROSITEiPS50213. FAS1. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: Many isoforms are produced by alternative splicing.1 Publication

Isoform 1 (identifier: P10674-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLNAAALLLA LLCAANAAAA ADLADKLRDD SELSQFYSLL ESNQIANSTL
60 70 80 90 100
SLRSCTIFVP TNEAFQRYKS KTAHVLYHIT TEAYTQKRLP NTVSSDMAGN
110 120 130 140 150
PPLYITKNSN GDIFVNNARI IPSLSVETNS DGKRQIMHII DEVLEPLTVK
160 170 180 190 200
AGHSDTPNNP NALKFLKNAE EFNVDNIGVR TYRSQVTMAK KESVYDAAGQ
210 220 230 240 250
HTFLVPVDEG FKLSARSSLV DGKVIDGHVI PNTVIFTAAA QHDDPKASAA
260 270 280 290 300
FEDLLKVTVS FFKQKNGKMY VKSNTIVGDA KHRVGVVLAE IVKANIPVSN
310 320 330 340 350
GVVHLIHRPL MIIDTTVTQF LQSFKENAEN GALRKFYEVI MDNGGAVLDD
360 370 380 390 400
INSLTEVTIL APSNEAWNSS NINNVLRDRN KMRQILNMHI IKDRLNVDKI
410 420 430 440 450
RQKNANLIAQ VPTVNNNTFL YFNVRGEGSD TVITVEGGGV NATVIQADVA
460 470 480 490 500
QTNGYVHIID HVLGVPYTTV LGKLESDPMM SDTYKMGKFS HFNDQLNNTQ
510 520 530 540 550
RRFTYFVPRD KGWQKTELDY PSAHKKLFMA DFSYHSKSIL ERHLAISDKE
560 570 580 590 600
YTMKDLVKFS QESGSVILPT FRDSLSIRVE EEAGRYVIIW NYKKINVYRP
610 620 630 640 650
DVECTNGIIH VIDYPLLEEK DVVVAGGSYL PESSICIILA NLIMITVAKF

LN
Length:652
Mass (Da):72,599
Last modified:July 1, 1989 - v1
Checksum:i4D846358A47DBFD6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20545 mRNA. Translation: AAA28531.1.
M32311 Genomic DNA. Translation: AAA28529.1.
AE014297 Genomic DNA. Translation: AAN13715.1.
PIRiB29900.
RefSeqiNP_732165.1. NM_169725.2. [P10674-1]
UniGeneiDm.7092.

Genome annotation databases

EnsemblMetazoaiFBtr0083333; FBpp0082783; FBgn0262742. [P10674-1]
GeneIDi42025.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20545 mRNA. Translation: AAA28531.1.
M32311 Genomic DNA. Translation: AAA28529.1.
AE014297 Genomic DNA. Translation: AAN13715.1.
PIRiB29900.
RefSeqiNP_732165.1. NM_169725.2. [P10674-1]
UniGeneiDm.7092.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1O70X-ray2.60A314-628[»]
ProteinModelPortaliP10674.
SMRiP10674. Positions 328-623.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi67070. 7 interactions.
IntActiP10674. 1 interaction.
STRINGi7227.FBpp0111715.

Proteomic databases

PaxDbiP10674.
PRIDEiP10674.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0083333; FBpp0082783; FBgn0262742. [P10674-1]
GeneIDi42025.

Organism-specific databases

CTDi42025.
FlyBaseiFBgn0262742. Fas1.

Phylogenomic databases

eggNOGiKOG1437. Eukaryota.
COG2335. LUCA.
GeneTreeiENSGT00530000063860.
InParanoidiP10674.
OrthoDBiEOG79CXXZ.
PhylomeDBiP10674.

Miscellaneous databases

ChiTaRSiFas1. fly.
EvolutionaryTraceiP10674.
GenomeRNAii42025.
NextBioi826799.
PROiP10674.

Gene expression databases

BgeeiP10674.
ExpressionAtlasiP10674. differential.
GenevisibleiP10674. DM.

Family and domain databases

Gene3Di2.30.180.10. 4 hits.
InterProiIPR000782. FAS1_domain.
[Graphical view]
PfamiPF02469. Fasciclin. 4 hits.
[Graphical view]
SMARTiSM00554. FAS1. 4 hits.
[Graphical view]
SUPFAMiSSF82153. SSF82153. 4 hits.
PROSITEiPS50213. FAS1. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis and neuronal expression of fasciclin I in grasshopper and Drosophila."
    Zinn K., McAllister L., Goodman C.
    Cell 53:577-587(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Alternative splicing of micro-exons creates multiple forms of the insect cell adhesion molecule fasciclin I."
    McAllister L., Rehm E.J., Goodman G.S., Zinn K.
    J. Neurosci. 12:895-905(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. "Drosophila fasciclin I, a neural cell adhesion molecule, has a phosphatidylinositol lipid membrane anchor that is developmentally regulated."
    Hortsch M., Goodman C.S.
    J. Biol. Chem. 265:15104-15109(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: GPI-ANCHOR.
  6. "Identification of N-glycosylated proteins from the central nervous system of Drosophila melanogaster."
    Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L., Panin V.
    Glycobiology 17:1388-1403(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-497, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Oregon-R.
    Tissue: Head.
  7. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-493 AND ASN-497, IDENTIFICATION BY MASS SPECTROMETRY.
  8. "Novel fold revealed by the structure of a FAS1 domain pair from the insect cell adhesion molecule fasciclin I."
    Clout N.J., Tisi D., Hohenester E.
    Structure 11:197-203(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 314-628, GLYCOSYLATION AT ASN-441.

Entry informationi

Entry nameiFAS1_DROME
AccessioniPrimary (citable) accession number: P10674
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: May 11, 2016
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.