P70275 (SEM3E_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Semaphorin-3E

Alternative name(s):
Semaphorin-H
Short name=Sema H

Gene names

Name:	Sema3e
Synonyms:	Semah, Semh

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	775 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays an important role in signaling via the cell surface receptor PLXND1. Mediates reorganization of the actin cytoskeleton, leading to the retraction of cell projections. Promotes focal adhesion disassembly and inhibits adhesion of endothelial cells to the extracellular matrix. Regulates angiogenesis, both during embryogenesis and after birth. Can down-regulate sprouting angiogenesis. Required for normal vascular patterning during embryogenesis. Plays an important role in ensuring the specificity of synapse formation. Ref.6 Ref.7 Ref.8 Ref.9
Subunit structure	Interacts with PLXND1. Ref.6 Ref.8
Subcellular location	Secreted.
Tissue specificity	Detected in neurons in the thalamus. Detected in embryonic vasculature. Developing lungs, developing skeletal elements and ventral horns of the developing neural tube. Correlates positively with tumor progression. Ref.6 Ref.9
Disruption phenotype	Embryos present defects in the patterning of intersomitic vasculature. Ref.6
Sequence similarities	Belongs to the semaphorin family. Contains 1 Ig-like C2-type (immunoglobulin-like) domain. Contains 1 Sema domain.

Ontologies

Keywords
Biological process	Angiogenesis Differentiation Neurogenesis
Cellular component	Secreted
Domain	Immunoglobulin domain Signal
Molecular function	Developmental protein
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of angiogenesis Inferred from mutant phenotype Ref.8. Source: UniProtKB negative regulation of cell-matrix adhesion Inferred from mutant phenotype Ref.8. Source: UniProtKB nervous system development Inferred from electronic annotation. Source: UniProtKB-KW patterning of blood vessels Inferred from mutant phenotype Ref.6. Source: UniProtKB regulation of actin cytoskeleton reorganization Inferred from mutant phenotype Ref.8. Source: UniProtKB regulation of cell shape Inferred from mutant phenotype Ref.6Ref.8. Source: UniProtKB semaphorin-plexin signaling pathway Inferred from mutant phenotype Ref.6. Source: UniProtKB sprouting angiogenesis Inferred from mutant phenotype Ref.8. Source: UniProtKB synapse organization Inferred from mutant phenotype Ref.9. Source: UniProtKB
Cellular_component	extracellular region Non-traceable author statement Ref.9. Source: UniProtKB membrane Inferred from electronic annotation. Source: InterPro
Molecular_function	receptor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 25	25	Potential
	Chain	26 – 775	750	Semaphorin-3E		PRO_0000032318
Regions
	Domain	32 – 516	485	Sema
	Domain	581 – 669	89	Ig-like C2-type
	Compositional bias	737 – 770	34	Arg/Lys-rich (basic)
Amino acid modifications
	Glycosylation	44	1	N-linked (GlcNAc...) Potential
	Glycosylation	126	1	N-linked (GlcNAc...) Potential
	Glycosylation	175	1	N-linked (GlcNAc...) Potential
	Glycosylation	330	1	N-linked (GlcNAc...) Potential
	Glycosylation	596	1	N-linked (GlcNAc...) Potential
	Disulfide bond	105 ↔ 115		By similarity
	Disulfide bond	133 ↔ 142		By similarity
	Disulfide bond	270 ↔ 382		By similarity
	Disulfide bond	294 ↔ 342		By similarity
	Disulfide bond	519 ↔ 537		By similarity
	Disulfide bond	654 ↔ 729		By similarity
Experimental info
	Sequence conflict	407 – 408	2	MH → ID in CAB02590. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P70275 [UniParc]. Last modified July 27, 2011. Version 3. Checksum: 221E766F404098D4	FASTA	775	89,543
	10 20 30 40 50 60 MAPAGHILTL LLWGHLLELW TPGHSANPSY PRLRLSHKEL LELNRTSIFQ SPLGFLDLHT 70 80 90 100 110 120 MLLDEYQERL FVGGRDLVYS LNLERVSDGY REIYWPSTAV KVEECIMKGK DANECANYIR 130 140 150 160 170 180 VLHHYNRTHL LTCATGAFDP HCAFIRVGHH SEEPLFHLES HRSERGRGRC PFDPNSSFVS 190 200 210 220 230 240 TLVGNELFAG LYSDYWGRDS AIFRSMGKLG HIRTEHDDER LLKEPKFVGS YMIPDNEDRD 250 260 270 280 290 300 DNKMYFFFTE KALEAENNAH TIYTRVGRLC VNDMGGQRIL VNKWSTFLKA RLVCSVPGMN 310 320 330 340 350 360 GIDTYFDELE DVFLLPTRDP KNPVIFGLFN TTSNIFRGHA VCVYHMSSIR EAFNGPYAHK 370 380 390 400 410 420 EGPEYHWSLY EGKVPYPRPG SCASKVNGGK YGTTKDYPDD AIRFARMHPL MYQPIKPVHK 430 440 450 460 470 480 KPILVKTDGK YNLRQLAVDR VEAEDGQYDV LFIGTDTGIV LKVITIYNQE TEWMEEVILE 490 500 510 520 530 540 ELQIFKDPAP IISMEISSKR QQLYIGSASA VAQVRFHHCD MYGSACADCC LARDPYCAWD 550 560 570 580 590 600 GISCSRYYPT GAHAKRRFRR QDVRHGNAAQ QCFGQQFVGD ALDRTEERLA YGIESNSTLL 610 620 630 640 650 660 ECTPRSLQAK VIWFVQKGRD VRKEEVKTDD RVVKMDLGLL FLRVRKSDAG TYFCQTVEHN 670 680 690 700 710 720 FVHTVRKITL EVVEEHKVEG MFHKDHEEER HHKMPCPPLS GMSQGTKPWY KEFLQLIGYS 730 740 750 760 770 NFQRVEEYCE KVWCTDKKRK KLKMSPSKWK YANPQEKRLR SKAEHFRLPR HTLLS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Transcription of a novel mouse semaphorin gene, M-semaH, correlates with the metastatic ability of mouse tumor cell lines." Christensen C.R.L., Klingelhoefer J., Tarabykina S., Hulgaard E.F., Kramerov D., Lukanidin E. Cancer Res. 58:1238-1244(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c.
[2]	Christensen C.R.L. Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"Developmental localization of semaphorin H messenger RNA acting as a collapsing factor on sensory axons in the mouse brain." Miyazaki N., Furuyama T., Sakai T., Fujioka S., Mori T., Ohoka Y., Takeda N., Kubo T., Inagaki S. Neuroscience 93:401-408(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57/Black 6.
[4]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Eye.
[6]	"Semaphorin 3E and plexin-D1 control vascular pattern independently of neuropilins." Gu C., Yoshida Y., Livet J., Reimert D.V., Mann F., Merte J., Henderson C.E., Jessell T.M., Kolodkin A.L., Ginty D.D. Science 307:265-268(2005) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION, INTERACTION WITH PLXND1, TISSUE SPECIFICITY.
[7]	"Specificity of sensory-motor connections encoded by Sema3e-Plxnd1 recognition." Pecho-Vrieseling E., Sigrist M., Yoshida Y., Jessell T.M., Arber S. Nature 459:842-846(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Semaphorin 3E initiates antiangiogenic signaling through plexin D1 by regulating Arf6 and R-Ras." Sakurai A., Gavard J., Annas-Linhares Y., Basile J.R., Amornphimoltham P., Palmby T.R., Yagi H., Zhang F., Randazzo P.A., Li X., Weigert R., Gutkind J.S. Mol. Cell. Biol. 30:3086-3098(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PLXND1.
[9]	"Semaphorin 3E-Plexin-D1 signaling controls pathway-specific synapse formation in the striatum." Ding J.B., Oh W.J., Sabatini B.L., Gu C. Nat. Neurosci. 15:215-223(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z80941 mRNA. Translation: CAB02590.1. Z93947 mRNA. Translation: CAB07987.1. Sequence problems. Z93948 mRNA. Translation: CAB07988.1. Sequence problems. AF034744 mRNA. Translation: AAD01996.1. CH466635 Genomic DNA. Translation: EDL38710.1. BC057956 mRNA. Translation: AAH57956.1.
IPI	IPI00785319.
RefSeq	NP_035478.2. NM_011348.2.
UniGene	Mm.134093.
3D structure databases
ProteinModelPortal	P70275.
SMR	P70275. Positions 31-522, 591-658.
ModBase	Search...
PTM databases
PhosphoSite	P70275.
Proteomic databases
PRIDE	P70275.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000073957; ENSMUSP00000073612; ENSMUSG00000063531.
GeneID	20349.
KEGG	mmu:20349.
Organism-specific databases
CTD	9723.
MGI	MGI:1340034. Sema3e.
Phylogenomic databases
eggNOG	NOG324739.
GeneTree	ENSGT00560000076660.
HOGENOM	HOG000039964.
HOVERGEN	HBG055071.
InParanoid	Q9QX23.
KO	K06840.
OMA	MIPDNED.
OrthoDB	EOG4THVSM.
Gene expression databases
ArrayExpress	P70275.
Bgee	P70275.
Genevestigator	P70275.
GermOnline	ENSMUSG00000063531. Mus musculus.
Family and domain databases
Gene3D	2.130.10.10. 1 hit.
InterPro	IPR007110. Ig-like_dom. IPR003599. Ig_sub. IPR013151. Immunoglobulin. IPR003659. Plexin-like. IPR016201. Plexin-like_fold. IPR027231. Semaphorin. IPR001627. Semaphorin/CD100_Ag. IPR015513. Semaphorin_3E. IPR015943. WD40/YVTN_repeat-like_dom. [Graphical view]
PANTHER	PTHR11036. PTHR11036. 1 hit. PTHR11036:SF22. PTHR11036:SF22. 1 hit.
Pfam	PF00047. ig. 1 hit. PF01403. Sema. 1 hit. [Graphical view]
SMART	SM00409. IG. 1 hit. SM00423. PSI. 1 hit. SM00630. Sema. 1 hit. [Graphical view]
SUPFAM	SSF103575. Plexin-like_fold. 1 hit. SSF101912. Sema. 1 hit.
PROSITE	PS50835. IG_LIKE. 1 hit. PS51004. SEMA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	298199.
SOURCE	Search...

Entry information

Entry name

SEM3E_MOUSE

Accession

Primary (citable) accession number: P70275
Secondary accession number(s): O09078, O09079, Q9QX23

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 109 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program