ID   LACH_SCHAM              Reviewed;         349 AA.
AC   Q26474;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Lachesin;
DE   Flags: Precursor;
GN   Name=LAC;
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], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=8223276; DOI=10.1242/dev.118.2.509;
RA   Karlstrom R.O., Wilder L.P., Bastiani M.J.;
RT   "Lachesin: an immunoglobulin superfamily protein whose expression
RT   correlates with neurogenesis in grasshopper embryos.";
RL   Development 118:509-522(1993).
CC   -!- FUNCTION: May play a role in early neuronal differentiation and axon
CC       outgrowth.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC   -!- TISSUE SPECIFICITY: Expressed by all neurogenic cells early, but only
CC       those cells that become neuroblasts continue to express it. Expressed
CC       by neuroblasts, ganglion mother cells and neurons early in their lives,
CC       but expression becomes restricted to a subset of neurons as development
CC       progresses. Expressed by sensory neurons as they delaminate from the
CC       body wall ectoderm. It is also present on growing axons of the CNS and
CC       PNS and becomes restricted to a subset of axons later in development.
CC   -!- DEVELOPMENTAL STAGE: Expressed on differentiating neuronal cells from
CC       the onset of neurogenesis in both the central and peripheral nervous
CC       systems.
CC   -!- PTM: The N-terminus is blocked.
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DR   EMBL; L13256; AAC37185.1; -; mRNA.
DR   AlphaFoldDB; Q26474; -.
DR   SMR; Q26474; -.
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; 2.60.40.10; -; 3.
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   Pfam; PF07679; I-set; 2.
DR   SMART; SM00409; IG; 3.
DR   SMART; SM00408; IGc2; 3.
DR   SUPFAM; SSF48726; SSF48726; 3.
DR   PROSITE; PS50835; IG_LIKE; 3.
PE   1: Evidence at protein level;
KW   Cell adhesion; Cell membrane; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; GPI-anchor; Immunoglobulin domain; Lipoprotein; Membrane;
KW   Repeat; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..332
FT                   /note="Lachesin"
FT                   /id="PRO_0000014812"
FT   PROPEP          333..349
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000014813"
FT   DOMAIN          22..127
FT                   /note="Ig-like V-type"
FT   DOMAIN          132..218
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          222..315
FT                   /note="Ig-like C2-type 2"
FT   LIPID           332
FT                   /note="GPI-anchor amidated glycine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        137
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        43..110
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        154..201
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        244..299
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   349 AA;  38974 MW;  5F139A44BF849689 CRC64;
     MDLRLYTIFV GFFSVVYAQR TPTISYISQE QIKDIGGTVE LECSVQYAQD YPVLWMKVDR
     NRQVDPLPIS TGSSLIIRDS RFALRYDTAS STYTLQIKDI QETDAGFYQC QVIIGLNNKI
     TAEVDLQVRR PPVISDNSTR SLVVSEGQAV RLECYAGGYP APRVSWRREN NAILPTGGSI
     YRGNVLKISR IGKEDRGTYY CVAENGVGKG ARRNIAVEVE FPPVITVPRP RLGQALQYDM
     DLECHVEAYP PPAITWLKDE TVLSNNQHYS ISHFATADEF TDTTRVITIE KRQYGKYQCK
     AANKLGEARE EVELFETIIP VCPPACGQAY GGDAAEISTS MALILISTI