FAS2_SCHAM
ID FAS2_SCHAM Reviewed; 898 AA.
AC P22648;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Fasciclin-2;
DE AltName: Full=Fasciclin II;
DE Short=FAS II;
DE Flags: Precursor;
GN Name=FAS2;
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=3187519; DOI=10.1126/science.3187519;
RA Harrelson A.L., Goodman C.S.;
RT "Growth cone guidance in insects: fasciclin II is a member of the
RT immunoglobulin superfamily.";
RL Science 242:700-708(1988).
RN [2]
RP PROTEIN SEQUENCE OF 423-436.
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: Neuronal recognition molecule. Involved in a pathway
CC recognition for axons during the development of nerve fascicles.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
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DR EMBL; J03789; AAA29810.1; -; mRNA.
DR PIR; A40114; A40114.
DR AlphaFoldDB; P22648; -.
DR SMR; P22648; -.
DR PRIDE; P22648; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.40.10; -; 7.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR009138; Neural_cell_adh.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07679; I-set; 2.
DR PRINTS; PR01838; NCAMFAMILY.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF48726; SSF48726; 5.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 1: Evidence at protein level;
KW Cell adhesion; Developmental protein; Differentiation;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Neurogenesis; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..898
FT /note="Fasciclin-2"
FT /id="PRO_0000014759"
FT TOPO_DOM 23..764
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 765..782
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 783..898
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..124
FT /note="Ig-like C2-type 1"
FT DOMAIN 134..219
FT /note="Ig-like C2-type 2"
FT DOMAIN 226..316
FT /note="Ig-like C2-type 3"
FT DOMAIN 321..423
FT /note="Ig-like C2-type 4"
FT DOMAIN 428..525
FT /note="Ig-like C2-type 5"
FT DOMAIN 532..626
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 644..745
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 580
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 48..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 156..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 248..300
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 343..407
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 450..509
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 898 AA; 99065 MW; 07989EA4F39604AC CRC64;
MRTVACAVLL ACFMGCLAGA WAQSAGLEIL PNSENQTKPI GRSMLLTCKP NVTNKNLISQ
LRWTDPSGRE VPFKNPTLLK PHIFVDWLPP PGEKVLTLMI PELREADTGT YTCSALYSNT
KQLSKSVHVR TIMPITWDDA PEEQYPTVNE TFKIRCRVSA NPPAIVNWMR DGHIVETGDR
YVVEQDGLTI LNVTEMDDGT YTCRAIVIAT GEMALRPIRV EVHTPPQMSG ALPPKLEAVE
GTDFTAKCAA SGKPVPRYTW IRVDTARDLT KDGDRVSADV LLGELRIREV RPEDAANYSC
TAKNAAGTAT ATVEVTVVVR PRIGRFDNIS VASGKDSEAV LECHATGSPL PAVTFRKLSN
PNRYINGIQP TEDRITVDGV DSPDGRTRIG KLIISNVLRS DDGLYECIAT NKGGEVKKNG
HLMVEFKPSF ADTPQKEVWG WEQHAVNLTC LAHSIPNATI SWHFNGADLF RGREGQELQQ
TGYTLFGSGP RSTLQVIPFN RKMYGNYKCT ATNKHGTAVH EIMLREARVP SAVLQVKMDV
MTATTVTFKF FGPGNDGGLP TKNYAVQYKQ DSQGWEDALN RTWPVDSPYI LENLKPQTRY
NFRFAAQNEV GFGPWSSQQT HTTPRISAPE EPRLLGLPLS ATSGTENEVV VSPYPNRYEL
RWQVPADNGE PITHYSVKSC PVEKYDTEWR LLPYPCQEHK LEGQATTFQL ESLQPDTHYK
VEVRATNAIG NSVPGQIIVR TVKDPSQMPG VANVEDGSEG QMSSAAIVVL VVAALLLALL
VVDLVCCLVW RGGLIAALCH RCCSAAKTDD SDAKIASLYS WRFPLPYCSN KEDPAMLAPA
KMQQATVKIP VIEEKEPLRD GKEPVPIIKE RVKRETAVDF DVKKSVSRTS FVGKDSAV
