ID   FAS1_SCHAM              Reviewed;         662 AA.
AC   P10675;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Fasciclin-1;
DE   AltName: Full=Fasciclin I;
DE            Short=FAS I;
DE            Short=FCN;
DE   Flags: Precursor;
GN   Name=FAS1;
OS   Schistocerca americana (American grasshopper).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Orthoptera; Caelifera; Acrididea; Acridomorpha;
OC   Acridoidea; Acrididae; Cyrtacanthacridinae; Schistocerca.
OX   NCBI_TaxID=7009;
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   PROTEIN SEQUENCE OF 25-42.
RX   PubMed=2839842; DOI=10.1073/pnas.85.14.5291;
RA   Snow P.M., Zinn K., Harrelson A.L., McAllister L., Schilling J.,
RA   Bastiani M.J., Makk G., Goodman C.S.;
RT   "Characterization and cloning of fasciclin I and fasciclin II glycoproteins
RT   in the grasshopper.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:5291-5295(1988).
CC   -!- FUNCTION: Neural cell adhesion molecule.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC   -!- TISSUE SPECIFICITY: Expressed on different subsets of axon bundles
CC       (fascicles) in insect embryos.
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DR   EMBL; M20544; AAA29809.1; -; mRNA.
DR   PIR; A29900; A29900.
DR   AlphaFoldDB; P10675; -.
DR   SMR; P10675; -.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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   Cell adhesion; Cell membrane; Direct protein sequencing; Glycoprotein;
KW   GPI-anchor; Lipoprotein; Membrane; Repeat; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:2839842"
FT   CHAIN           25..631
FT                   /note="Fasciclin-1"
FT                   /id="PRO_0000008774"
FT   PROPEP          632..662
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000008775"
FT   DOMAIN          27..155
FT                   /note="FAS1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT   DOMAIN          167..321
FT                   /note="FAS1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT   DOMAIN          329..470
FT                   /note="FAS1 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT   DOMAIN          474..622
FT                   /note="FAS1 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT   LIPID           631
FT                   /note="GPI-anchor amidated glycine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        54
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        175
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        437
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        448
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        488
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        569
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   662 AA;  75282 MW;  1E648D139A16B816 CRC64;
     MEGPRLTALM LLLLLTLAAD RASAKGEKSL EYKIRDDPDL SQFYSWLEHN EVANSTLQLR
     QVTVFAPTNL AFQNYKARDG DENIILYHMT NLAHSLDQLG HKVLSELDGN PPLWITRRRD
     TIFVNNARVL TERSNYEAVN RHGKKQVLHV VDSVLEPVWS TSGQLYNPDA FQFLNQSENL
     DLGLHRVRSF RQRVFQNQKQ NDFKLEGKHT FFIPVDEGFK PLPRPEKIDQ KVIDGHIIPN
     HVLFTSATPL DEEYETLAFT DMLRVVISFT MESDGKAHKP YVKSNTVIGD ANHATGAVLA
     EIVKANIPVK NGVVHLIQRP LMVVDNTVKQ FLEGFEKEDG PLYKFYQVIL DAGGDFINQI
     TEMKDLTLFA PSNAAWSETT ANNLLTDRKK FREILNLHIV AEKLSIESIV EQNVKQVPTM
     ADRKNLYFNV VHGPAGNKTV TVEGGGVNAT IVQPNIAATN GMVHIINKIL GVPYTTVKEK
     LRTDPMLNKT YHLGEMSDFN KMLDEKHTKF TYFVPRDLAW KKMEVRDPSA HRKLFMKEFT
     YQVKQILERH LVISDRVYTM GALKKLASNT SSVLPTMRDH LRLRVRETEK SYYVEWQGEW
     THIFRPDVEC TNGIIHVMDY VFMKEGDIVV GGPDGAGQQV ASFAVVASAH LVVLATVRWL
     LH