ID   SEM2A_SCHGR             Reviewed;         697 AA.
AC   Q9XZC8;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Semaphorin-2A;
DE            Short=Sema-2A;
DE   AltName: Full=Sema II;
DE   Flags: Precursor;
GN   Name=SEMA-2A;
OS   Schistocerca gregaria (Desert locust) (Gryllus gregarius).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Orthoptera; Caelifera; Acrididea; Acridomorpha;
OC   Acridoidea; Acrididae; Cyrtacanthacridinae; Schistocerca.
OX   NCBI_TaxID=7010;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Embryo;
RX   PubMed=10101134; DOI=10.1242/dev.126.9.2007;
RA   Isbister C.M., Tsai A., Wong S.T., Kolodkin A.L., O'Connor T.P.;
RT   "Discrete roles for secreted and transmembrane semaphorins in neuronal
RT   growth cone guidance in vivo.";
RL   Development 126:2007-2019(1999).
CC   -!- FUNCTION: Acts as chemorepulsive guidance molecule critical for axon
CC       fasciculation and for determining both the initial direction and
CC       subsequent pathfinding events of the Ti axon projection.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in a gradient in the developing limb bud
CC       epithelium during Ti pioneer axon outgrowth.
CC   -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
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DR   EMBL; AF134904; AAD30114.1; -; mRNA.
DR   AlphaFoldDB; Q9XZC8; -.
DR   SMR; Q9XZC8; -.
DR   PRIDE; Q9XZC8; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030215; F:semaphorin receptor binding; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR001627; Semap_dom.
DR   InterPro; IPR036352; Semap_dom_sf.
DR   InterPro; IPR027231; Semaphorin.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR11036; PTHR11036; 1.
DR   Pfam; PF01403; Sema; 1.
DR   SMART; SM00630; Sema; 1.
DR   SUPFAM; SSF101912; SSF101912; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS51004; SEMA; 1.
PE   2: Evidence at transcript level;
KW   Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Neurogenesis; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..697
FT                   /note="Semaphorin-2A"
FT                   /id="PRO_0000032302"
FT   DOMAIN          21..493
FT                   /note="Sema"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DOMAIN          526..634
FT                   /note="Ig-like C2-type"
FT   REGION          673..697
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        63
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        66
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        132
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        198
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        283
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        369
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        534
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        629
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        679
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        87..98
FT                   /evidence="ECO:0000250"
FT   DISULFID        260..367
FT                   /evidence="ECO:0000250"
FT   DISULFID        284..326
FT                   /evidence="ECO:0000250"
FT   DISULFID        496..512
FT                   /evidence="ECO:0000250"
FT   DISULFID        506..521
FT                   /evidence="ECO:0000250"
FT   DISULFID        618..654
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   697 AA;  78673 MW;  7FE55AB4A965E1E4 CRC64;
     MAAKLWNLLL VAASVHLVGS VEQLHQDLIH EFSCGHKYYR TFHLDEKRES LYVGALDKVY
     KLNLTNISLS DCERDSLTLE PTNIANCVSK GKSADFDCKN HIRVIQPMGD GSRLYICGTN
     AHSPKDWVVY SNLTHLQRHE YVPGIGVGIA KCPFDPEDSS TAVWVENGNP GDLPGLYSGT
     NAEFTKADTV IFRTDLYNLT TGRREYSFKR TLKYDSKWLD NPNFVGSFDV GEYVLFFFRE
     TAVEYINCGK SVYSRVARVC KKDVGGKNIL SQNWATFLKA RLNCSIPGEF PFYFNEIQGV
     YKMPNTDKFF GVFSTSVTGL TGSAICSFTL KDIQEVFSGK FKEQATSSSA WLPVLPSRVP
     DPRPGECVND TELLPDTVLN FIRSHPLMDG AVSHEGGKPV FYKRDVLFTQ LVVDKLKVNL
     VGKNMEYIVY YAGTSTGQVY KVVQWYDSGG LPQSLLVDIF DVTPPEPVQA LHLSKEYKSL
     YAASDNIVRQ IELVMCHHRY SNCLQCARDP YCGWDRDSNS CKSYTPGLLQ DVTNTSANLC
     EHSVMKKKLI VTWGQSIHLG CFLKVPEVLS SQTISWVHYT KDKGRYPIVY RPDKYIETSE
     HGLVLISVTD SDSGRYDCWL GGSLLCSYNI TVDAHRCSAP GRSNDYQKIY SDWCHEFERS
     KIAMKTWERK QAQCSTKQNN SNQKTHPNDI FHSNPVA