SEM1A_SCHAM
ID SEM1A_SCHAM Reviewed; 730 AA.
AC Q26473;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Semaphorin-1A;
DE AltName: Full=Fasciclin IV;
DE AltName: Full=Fasciclin-4;
DE AltName: Full=Semaphorin-I;
DE Short=Sema I;
DE Flags: Precursor;
GN Name=SEMA-1A; Synonyms=FAS4;
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=1418998; DOI=10.1016/0896-6273(92)90237-8;
RA Kolodkin A.L., Matthes D.J., O'Connor T.P., Patel N.H., Admon A.,
RA Bentley D., Goodman C.S.;
RT "Fasciclin IV: sequence, expression, and function during growth cone
RT guidance in the grasshopper embryo.";
RL Neuron 9:831-845(1992).
CC -!- FUNCTION: Plays a role in growth cones guidance.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Dynamically expressed on a subset of axon pathways
CC in the developing CNS and on circumferential bands of epithelial cells
CC in developing limb buds.
CC -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
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DR EMBL; L00709; AAA29808.1; -; mRNA.
DR PIR; JH0798; JH0798.
DR AlphaFoldDB; Q26473; -.
DR SMR; Q26473; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 CDD; cd11237; Sema_1A; 1.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR002165; Plexin_repeat.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR042068; SEM1A_sema_dom.
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; PF01437; PSI; 1.
DR Pfam; PF01403; Sema; 1.
DR SMART; SM00423; PSI; 1.
DR SMART; SM00630; Sema; 1.
DR SUPFAM; SSF101912; SSF101912; 1.
DR PROSITE; PS51004; SEMA; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Differentiation; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Membrane; Neurogenesis; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..730
FT /note="Semaphorin-1A"
FT /id="PRO_0000032298"
FT TOPO_DOM 21..630
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 631..651
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 652..730
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..490
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT REGION 708..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 539
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 97..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 125..134
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 244..358
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 268..317
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 493..512
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 504..521
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
SQ SEQUENCE 730 AA; 81215 MW; 6D625946E7F8E57F CRC64;
MRAALVAVAA LLWVALHAAA WVNDVSPKMY VQFGEERVQR FLGNESHKDH FKLLEKDHNS
LLVGARNIVY NISLRDLTEF TEQRIEWHSS GAHRELCYLK GKSEDDCQNY IRVLAKIDDD
RVLICGTNAY KPLCRHYALK DGDYVVEKEY EGRGLCPFDP DHNSTAIYSE GQLYSATVAD
FSGTDPLIYR GPLRTERSDL KQLNAPNFVN TMEYNDFIFF FFRETAVEYI NCGKAIYSRV
ARVCKHDKGG PHQFGDRWTS FLKSRLNCSV PGDYPFYFNE IQSTSDIIEG NYGGQVEKLI
YGVFTTPVNS IGGSAVCAFS MKSILESFDG PFKEQETMNS NWLAVPSLKV PEPRPGQCVN
DSRTLPDVSV NFVKSHTLMD EAVPAFFTRP ILIRISLQYR FTKIAVDQQV RTPDGKAYDV
LFIGTDDGKV IKALNSASFD SSDTVDSVVI EELQVLPPGV PVKNLYVVRM DGDDSKLVVV
SDDEILAIKL HRCGSDKITN CRECVSLQDP YCAWDNVELK CTAVGSPDWS AGKRRFIQNI
SLGEHKACGG RPQTEIVASP VPTQPTTKSS GDPVHSIHQA EFEPEIDNEI VIGVDDSNVI
PNTLAEINHA GSKLPSSQEK LPIYTAETLT IAIVTSCLGA LVVGFISGFL FSRRCRGEDY
TDMPFPDQRH QLNRLTEAGL NADSPYLPPC ANNKAAINLV LNVPPKNANG KNANSSAENK
PIQKVKKTYI
