SEM1A_DROME
ID SEM1A_DROME Reviewed; 899 AA.
AC Q24322; Q8MYZ9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 3.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Semaphorin-1A;
DE AltName: Full=Semaphorin-I;
DE Short=Sema I;
GN Name=Sema1a {ECO:0000312|FlyBase:FBgn0011259};
GN Synonyms=Dsema-I {ECO:0000312|FlyBase:FBgn0011259},
GN Sema-1a {ECO:0000312|FlyBase:FBgn0011259};
GN ORFNames=CG18405 {ECO:0000312|FlyBase:FBgn0011259};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC TISSUE=Embryo;
RX PubMed=8269517; DOI=10.1016/0092-8674(93)90625-z;
RA Kolodkin A.L., Matthes D.J., Goodman C.S.;
RT "The semaphorin genes encode a family of transmembrane and secreted growth
RT cone guidance molecules.";
RL Cell 75:1389-1399(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-213.
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM29460.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAM29460.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP FUNCTION.
RX PubMed=15282266; DOI=10.1523/jneurosci.1104-04.2004;
RA Ayoob J.C., Yu H.H., Terman J.R., Kolodkin A.L.;
RT "The Drosophila receptor guanylyl cyclase Gyc76C is required for
RT semaphorin-1a-plexin A-mediated axonal repulsion.";
RL J. Neurosci. 24:6639-6649(2004).
CC -!- FUNCTION: Involved in growth cone guidance through its role in axonal
CC repulsion. {ECO:0000269|PubMed:15282266, ECO:0000269|PubMed:8269517}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15282266,
CC ECO:0000269|PubMed:8269517}; Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed by subsets of neurons and muscles.
CC {ECO:0000269|PubMed:8269517}.
CC -!- DEVELOPMENTAL STAGE: Expression begins around stage 10, primarily in
CC the developing CNS. In stage 16 embryos, it is expressed at highest
CC levels throughout the CNS, and weak expression is seen in portions of
CC the peripheral nervous system, most clearly in the lateral sensory
CC clusters. {ECO:0000269|PubMed:8269517}.
CC -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA88789.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA88789.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=AAM29460.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; L26082; AAA88789.1; ALT_FRAME; mRNA.
DR EMBL; AE014134; AAF52696.2; -; Genomic_DNA.
DR EMBL; AY113455; AAM29460.1; ALT_SEQ; mRNA.
DR RefSeq; NP_723407.2; NM_164830.5.
DR PDB; 6QP9; X-ray; 3.60 A; A/B=80-603.
DR PDBsum; 6QP9; -.
DR AlphaFoldDB; Q24322; -.
DR SMR; Q24322; -.
DR BioGRID; 60311; 151.
DR IntAct; Q24322; 121.
DR STRING; 7227.FBpp0292880; -.
DR GlyGen; Q24322; 7 sites.
DR PaxDb; Q24322; -.
DR PRIDE; Q24322; -.
DR EnsemblMetazoa; FBtr0079691; FBpp0079302; FBgn0011259.
DR GeneID; 34192; -.
DR KEGG; dme:Dmel_CG18405; -.
DR CTD; 34192; -.
DR FlyBase; FBgn0011259; Sema1a.
DR VEuPathDB; VectorBase:FBgn0011259; -.
DR eggNOG; KOG3611; Eukaryota.
DR GeneTree; ENSGT00940000167882; -.
DR InParanoid; Q24322; -.
DR PhylomeDB; Q24322; -.
DR Reactome; R-DME-399954; Sema3A PAK dependent Axon repulsion.
DR Reactome; R-DME-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
DR Reactome; R-DME-399956; CRMPs in Sema3A signaling.
DR Reactome; R-DME-416572; Sema4D induced cell migration and growth-cone collapse.
DR Reactome; R-DME-416700; Other semaphorin interactions.
DR SignaLink; Q24322; -.
DR BioGRID-ORCS; 34192; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Sema-1a; fly.
DR GenomeRNAi; 34192; -.
DR PRO; PR:Q24322; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0011259; Expressed in brain and 31 other tissues.
DR ExpressionAtlas; Q24322; baseline and differential.
DR Genevisible; Q24322; DM.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; ISS:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045499; F:chemorepellent activity; IBA:GO_Central.
DR GO; GO:0008201; F:heparin binding; IDA:FlyBase.
DR GO; GO:0030215; F:semaphorin receptor binding; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IDA:FlyBase.
DR GO; GO:0016199; P:axon midline choice point recognition; IMP:FlyBase.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:FlyBase.
DR GO; GO:0050919; P:negative chemotaxis; IBA:GO_Central.
DR GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; IBA:GO_Central.
DR GO; GO:0045792; P:negative regulation of cell size; IMP:FlyBase.
DR GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; IBA:GO_Central.
DR GO; GO:2000305; P:semaphorin-plexin signaling pathway involved in regulation of photoreceptor cell axon guidance; IGI:FlyBase.
DR GO; GO:0007416; P:synapse assembly; IMP:FlyBase.
DR GO; GO:0008039; P:synaptic target recognition; IMP:FlyBase.
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 3D-structure; Cell membrane; Developmental protein; Differentiation;
KW Disulfide bond; Glycoprotein; Membrane; Neurogenesis; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..899
FT /note="Semaphorin-1A"
FT /id="PRO_0000032297"
FT TOPO_DOM 1..40
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..657
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 658..678
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 679..899
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 74..543
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..830
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..878
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 141..151
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 169..178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 288..402
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 312..361
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT CONFLICT 14
FT /note="A -> V (in Ref. 1; AAA88789)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 899 AA; 101057 MW; 3F9653A2D735F64C CRC64;
MLNSHNTNHN NNSASNSNYN KGHKMHLKSA TAKATIMKHK LSKFYGYGWM QVFLLLTVLV
IGNQSAWQEN IRPKLYVELG PEDVLKFVGN ESVVDHFKLV TKDGNSLLIG ARNTVFNLSI
HDLVEQQRLV WTSPEDDTKM CLVKGKDEEA CQNYIRIMVV PSPGRLFVCG TNSFRPMCNT
YIISDSNYTL EATKNGQAVC PYDPRHNSTS VLADNELYSG TVADFSGSDP IIYREPLQTE
QYDSLSLNAP NFVSSFTQGD FVYFFFRETA VEFINCGKAI YSRVARVCKW DKGGPHRFRN
RWTSFLKSRL NCSIPGDYPF YFNEIQSASN LVEGQYGSMS SKLIYGVFNT PSNSIPGSAV
CAFALQDIAD TFEGQFKEQT GINSNWLPVN NAKVPDPRPG SCHNDSRALP DPTLNFIKTH
SLMDENVPAF FSQPILVRTS TIYRFTQIAV DAQIKTPGGK TYDVIFVGTD HGKIIKSVNA
ESADSADKVT SVVIEEIDVL TKSEPIRNLE IVRTMQYDQP KDGSYDDGKL IIVTDSQVVA
IQLHRCHNDK ITSCSECVAL QDPYCAWDKI AGKCRSHGAP RWLEENYFYQ NVATGQHAAC
PSGKINSKDA NAGEQKGFRN DMDLLDSRRQ SKDQEIIDNI DKNFEDIINA QYTVETLVMA
VLAGSIFSLL VGFFTGYFCG RRCHKDEDDN LPYPDTEYEY FEQRQNVNSF PSSCRIQQEP
KLLPQVEEVT YAEPVLLPQP PPPNKMHSPK NTLRKPPMHQ MHQGPNSETL FQFQPDGYNT
QQSYRGRDNF GTLRSHQVMG DNYRRGDGFS TTRSVKKAVN NTNTRNRSLG RARRQPPRHG
IVTQHRSNSP QQQQQQSQQP HSSSGSSPVM SNSSSSPAPP SSSPSPQESP KNCSYIYRD
