ID   SEM3E_MOUSE             Reviewed;         775 AA.
AC   P70275; O09078; O09079; Q9QX23;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   27-MAR-2024, entry version 180.
DE   RecName: Full=Semaphorin-3E;
DE   AltName: Full=Semaphorin-H;
DE            Short=Sema H;
DE   Flags: Precursor;
GN   Name=Sema3e; Synonyms=Semah, Semh;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ;
RX   PubMed=9515811;
RA   Christensen C.R.L., Klingelhoefer J., Tarabykina S., Hulgaard E.F.,
RA   Kramerov D., Lukanidin E.;
RT   "Transcription of a novel mouse semaphorin gene, M-semaH, correlates with
RT   the metastatic ability of mouse tumor cell lines.";
RL   Cancer Res. 58:1238-1244(1998).
RN   [2]
RP   SEQUENCE REVISION.
RA   Christensen C.R.L.;
RL   Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57/Black 6;
RX   PubMed=10430503; DOI=10.1016/s0306-4522(99)00134-7;
RA   Miyazaki N., Furuyama T., Sakai T., Fujioka S., Mori T., Ohoka Y.,
RA   Takeda N., Kubo T., Inagaki S.;
RT   "Developmental localization of semaphorin H messenger RNA acting as a
RT   collapsing factor on sensory axons in the mouse brain.";
RL   Neuroscience 93:401-408(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   DISRUPTION PHENOTYPE, FUNCTION, INTERACTION WITH PLXND1, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=15550623; DOI=10.1126/science.1105416;
RA   Gu C., Yoshida Y., Livet J., Reimert D.V., Mann F., Merte J.,
RA   Henderson C.E., Jessell T.M., Kolodkin A.L., Ginty D.D.;
RT   "Semaphorin 3E and plexin-D1 control vascular pattern independently of
RT   neuropilins.";
RL   Science 307:265-268(2005).
RN   [7]
RP   FUNCTION.
RX   PubMed=19421194; DOI=10.1038/nature08000;
RA   Pecho-Vrieseling E., Sigrist M., Yoshida Y., Jessell T.M., Arber S.;
RT   "Specificity of sensory-motor connections encoded by Sema3e-Plxnd1
RT   recognition.";
RL   Nature 459:842-846(2009).
RN   [8]
RP   FUNCTION, AND INTERACTION WITH PLXND1.
RX   PubMed=20385769; DOI=10.1128/mcb.01652-09;
RA   Sakurai A., Gavard J., Annas-Linhares Y., Basile J.R., Amornphimoltham P.,
RA   Palmby T.R., Yagi H., Zhang F., Randazzo P.A., Li X., Weigert R.,
RA   Gutkind J.S.;
RT   "Semaphorin 3E initiates antiangiogenic signaling through plexin D1 by
RT   regulating Arf6 and R-Ras.";
RL   Mol. Cell. Biol. 30:3086-3098(2010).
RN   [9]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=22179111; DOI=10.1038/nn.3003;
RA   Ding J.B., Oh W.J., Sabatini B.L., Gu C.;
RT   "Semaphorin 3E-Plexin-D1 signaling controls pathway-specific synapse
RT   formation in the striatum.";
RL   Nat. Neurosci. 15:215-223(2012).
CC   -!- FUNCTION: Plays an important role in signaling via the cell surface
CC       receptor PLXND1. Mediates reorganization of the actin cytoskeleton,
CC       leading to the retraction of cell projections. Promotes focal adhesion
CC       disassembly and inhibits adhesion of endothelial cells to the
CC       extracellular matrix. Regulates angiogenesis, both during embryogenesis
CC       and after birth. Can down-regulate sprouting angiogenesis. Required for
CC       normal vascular patterning during embryogenesis. Plays an important
CC       role in ensuring the specificity of synapse formation.
CC       {ECO:0000269|PubMed:15550623, ECO:0000269|PubMed:19421194,
CC       ECO:0000269|PubMed:20385769, ECO:0000269|PubMed:22179111}.
CC   -!- SUBUNIT: Interacts with PLXND1. {ECO:0000269|PubMed:15550623,
CC       ECO:0000269|PubMed:20385769}.
CC   -!- INTERACTION:
CC       P70275; Q9Y4D7: PLXND1; Xeno; NbExp=2; IntAct=EBI-8876322, EBI-310731;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Detected in neurons in the thalamus. Detected in
CC       embryonic vasculature. Developing lungs, developing skeletal elements
CC       and ventral horns of the developing neural tube. Correlates positively
CC       with tumor progression. {ECO:0000269|PubMed:15550623,
CC       ECO:0000269|PubMed:22179111}.
CC   -!- DISRUPTION PHENOTYPE: Embryos present defects in the patterning of
CC       intersomitic vasculature. {ECO:0000269|PubMed:15550623}.
CC   -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z80941; CAB02590.1; -; mRNA.
DR   EMBL; Z93947; CAB07987.1; ALT_SEQ; mRNA.
DR   EMBL; Z93948; CAB07988.1; ALT_SEQ; mRNA.
DR   EMBL; AF034744; AAD01996.1; -; mRNA.
DR   EMBL; CH466635; EDL38710.1; -; Genomic_DNA.
DR   EMBL; BC057956; AAH57956.1; -; mRNA.
DR   CCDS; CCDS19093.1; -.
DR   RefSeq; NP_035478.2; NM_011348.2.
DR   AlphaFoldDB; P70275; -.
DR   SMR; P70275; -.
DR   BioGRID; 203164; 4.
DR   CORUM; P70275; -.
DR   IntAct; P70275; 1.
DR   STRING; 10090.ENSMUSP00000073612; -.
DR   GlyConnect; 2694; 6 N-Linked glycans (2 sites).
DR   GlyCosmos; P70275; 5 sites, 6 glycans.
DR   GlyGen; P70275; 5 sites, 6 N-linked glycans (2 sites).
DR   iPTMnet; P70275; -.
DR   PhosphoSitePlus; P70275; -.
DR   MaxQB; P70275; -.
DR   PaxDb; 10090-ENSMUSP00000073612; -.
DR   PeptideAtlas; P70275; -.
DR   ProteomicsDB; 256612; -.
DR   Antibodypedia; 29599; 306 antibodies from 31 providers.
DR   DNASU; 20349; -.
DR   Ensembl; ENSMUST00000073957.8; ENSMUSP00000073612.7; ENSMUSG00000063531.8.
DR   GeneID; 20349; -.
DR   KEGG; mmu:20349; -.
DR   UCSC; uc008wme.1; mouse.
DR   AGR; MGI:1340034; -.
DR   CTD; 9723; -.
DR   MGI; MGI:1340034; Sema3e.
DR   VEuPathDB; HostDB:ENSMUSG00000063531; -.
DR   eggNOG; KOG3611; Eukaryota.
DR   GeneTree; ENSGT00940000158437; -.
DR   HOGENOM; CLU_009051_5_0_1; -.
DR   InParanoid; P70275; -.
DR   OMA; ASECANF; -.
DR   OrthoDB; 5342713at2759; -.
DR   PhylomeDB; P70275; -.
DR   TreeFam; TF352628; -.
DR   Reactome; R-MMU-416700; Other semaphorin interactions.
DR   BioGRID-ORCS; 20349; 2 hits in 78 CRISPR screens.
DR   ChiTaRS; Sema3e; mouse.
DR   PRO; PR:P70275; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; P70275; Protein.
DR   Bgee; ENSMUSG00000063531; Expressed in lumbar dorsal root ganglion and 181 other cell types or tissues.
DR   GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR   GO; GO:0045499; F:chemorepellent activity; IBA:GO_Central.
DR   GO; GO:0048018; F:receptor ligand activity; ISO:MGI.
DR   GO; GO:0030215; F:semaphorin receptor binding; IPI:UniProtKB.
DR   GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR   GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IMP:UniProtKB.
DR   GO; GO:0021828; P:gonadotrophin-releasing hormone neuronal migration to the hypothalamus; ISO:MGI.
DR   GO; GO:0050919; P:negative chemotaxis; IBA:GO_Central.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; IMP:UniProtKB.
DR   GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; IBA:GO_Central.
DR   GO; GO:0001953; P:negative regulation of cell-matrix adhesion; IMP:UniProtKB.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
DR   GO; GO:0001755; P:neural crest cell migration; IBA:GO_Central.
DR   GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISO:MGI.
DR   GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR   GO; GO:0071526; P:semaphorin-plexin signaling pathway; IMP:UniProtKB.
DR   GO; GO:0002040; P:sprouting angiogenesis; IMP:UniProtKB.
DR   GO; GO:0050808; P:synapse organization; IMP:UniProtKB.
DR   CDD; cd05871; Ig_Sema3; 1.
DR   CDD; cd11253; Sema_3E; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 3.30.1680.10; ligand-binding face of the semaphorins, domain 2; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR013151; Immunoglobulin.
DR   InterPro; IPR016201; PSI.
DR   InterPro; IPR001627; Semap_dom.
DR   InterPro; IPR036352; Semap_dom_sf.
DR   InterPro; IPR027231; Semaphorin.
DR   InterPro; IPR015513; Semaphorin_3E_Sema.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR11036; SEMAPHORIN; 1.
DR   PANTHER; PTHR11036:SF22; SEMAPHORIN-3E; 1.
DR   Pfam; PF00047; ig; 1.
DR   Pfam; PF01403; Sema; 1.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00423; PSI; 1.
DR   SMART; SM00630; Sema; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   SUPFAM; SSF103575; Plexin repeat; 1.
DR   SUPFAM; SSF101912; Sema domain; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS51004; SEMA; 1.
DR   Genevisible; P70275; MM.
PE   1: Evidence at protein level;
KW   Angiogenesis; Developmental protein; Differentiation; Disulfide bond;
KW   Glycoprotein; Immunoglobulin domain; Neurogenesis; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..775
FT                   /note="Semaphorin-3E"
FT                   /id="PRO_0000032318"
FT   DOMAIN          32..516
FT                   /note="Sema"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DOMAIN          581..669
FT                   /note="Ig-like C2-type"
FT   CARBOHYD        44
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        126
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        175
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        330
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        596
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        105..115
FT                   /evidence="ECO:0000250"
FT   DISULFID        133..142
FT                   /evidence="ECO:0000250"
FT   DISULFID        270..382
FT                   /evidence="ECO:0000250"
FT   DISULFID        294..342
FT                   /evidence="ECO:0000250"
FT   DISULFID        519..537
FT                   /evidence="ECO:0000250"
FT   DISULFID        654..729
FT                   /evidence="ECO:0000250"
FT   CONFLICT        407..408
FT                   /note="MH -> ID (in Ref. 1; CAB02590)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   775 AA;  89543 MW;  221E766F404098D4 CRC64;
     MAPAGHILTL LLWGHLLELW TPGHSANPSY PRLRLSHKEL LELNRTSIFQ SPLGFLDLHT
     MLLDEYQERL FVGGRDLVYS LNLERVSDGY REIYWPSTAV KVEECIMKGK DANECANYIR
     VLHHYNRTHL LTCATGAFDP HCAFIRVGHH SEEPLFHLES HRSERGRGRC PFDPNSSFVS
     TLVGNELFAG LYSDYWGRDS AIFRSMGKLG HIRTEHDDER LLKEPKFVGS YMIPDNEDRD
     DNKMYFFFTE KALEAENNAH TIYTRVGRLC VNDMGGQRIL VNKWSTFLKA RLVCSVPGMN
     GIDTYFDELE DVFLLPTRDP KNPVIFGLFN TTSNIFRGHA VCVYHMSSIR EAFNGPYAHK
     EGPEYHWSLY EGKVPYPRPG SCASKVNGGK YGTTKDYPDD AIRFARMHPL MYQPIKPVHK
     KPILVKTDGK YNLRQLAVDR VEAEDGQYDV LFIGTDTGIV LKVITIYNQE TEWMEEVILE
     ELQIFKDPAP IISMEISSKR QQLYIGSASA VAQVRFHHCD MYGSACADCC LARDPYCAWD
     GISCSRYYPT GAHAKRRFRR QDVRHGNAAQ QCFGQQFVGD ALDRTEERLA YGIESNSTLL
     ECTPRSLQAK VIWFVQKGRD VRKEEVKTDD RVVKMDLGLL FLRVRKSDAG TYFCQTVEHN
     FVHTVRKITL EVVEEHKVEG MFHKDHEEER HHKMPCPPLS GMSQGTKPWY KEFLQLIGYS
     NFQRVEEYCE KVWCTDKKRK KLKMSPSKWK YANPQEKRLR SKAEHFRLPR HTLLS
//