SEM3E_MOUSE
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 03-AUG-2022, entry version 171.
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}.
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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 GlyGen; P70275; 5 sites, 6 N-linked glycans (2 sites).
DR PhosphoSitePlus; P70275; -.
DR MaxQB; P70275; -.
DR PaxDb; P70275; -.
DR PeptideAtlas; P70275; -.
DR PRIDE; P70275; -.
DR ProteomicsDB; 256612; -.
DR Antibodypedia; 29599; 289 antibodies from 31 providers.
DR DNASU; 20349; -.
DR Ensembl; ENSMUST00000073957; ENSMUSP00000073612; ENSMUSG00000063531.
DR GeneID; 20349; -.
DR KEGG; mmu:20349; -.
DR UCSC; uc008wme.1; mouse.
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; GPHKMPC; -.
DR OrthoDB; 158418at2759; -.
DR PhylomeDB; P70275; -.
DR TreeFam; TF352628; -.
DR Reactome; R-MMU-416700; Other semaphorin interactions.
DR BioGRID-ORCS; 20349; 2 hits in 73 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 179 other tissues.
DR Genevisible; P70275; MM.
DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0045499; F:chemorepellent activity; IBA:GO_Central.
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; IEA:Ensembl.
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; IEA:Ensembl.
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:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
DR GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; IMP:UniProtKB.
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 Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 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.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR11036; PTHR11036; 1.
DR PANTHER; PTHR11036:SF22; PTHR11036:SF22; 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; SSF101912; SSF101912; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51004; SEMA; 1.
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
