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Semaphorin-3A (Semaphorin III) (Sema III) (Semaphorin-D) (Sema D)

 SEM3A_MOUSE             Reviewed;         772 AA.
O08665; E9QK85; Q5BL08; Q62180; Q62215;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
20-JUN-2018, entry version 164.
RecName: Full=Semaphorin-3A;
AltName: Full=Semaphorin III;
Short=Sema III;
AltName: Full=Semaphorin-D;
Short=Sema D;
Flags: Precursor;
Name=Sema3a; Synonyms=Semad, SemD;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=NMRI; TISSUE=Embryo;
PubMed=7748561; DOI=10.1016/0896-6273(95)90332-1;
Pueschel A.W., Adams R.H., Betz H.;
"Murine semaphorin D/collapsin is a member of a diverse gene family
and creates domains inhibitory for axonal extension.";
Neuron 14:941-948(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9331345; DOI=10.1016/S0896-6273(00)80368-2;
Taniguchi M., Yuasa S., Fujisawa H., Naruse I., Saga S., Mishina M.,
Yagi T.;
"Disruption of semaphorin III/D gene causes severe abnormality in
peripheral nerve projection.";
Neuron 19:519-530(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Kimura T., Fishman M.C.;
"cDNA sequence of mouse collapsin/semaphorin III.";
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 107-772.
TISSUE=Fetal brain;
PubMed=7748562; DOI=10.1016/0896-6273(95)90333-X;
Messersmith E.K., Leonardo E.D., Shatz C.J., Tessier-Lavigne M.,
Goodman C.S., Kolodkin A.L.;
"Semaphorin III can function as a selective chemorepellent to pattern
sensory projections in the spinal cord.";
Neuron 14:949-959(1995).
[7]
INTERACTION WITH PLXND1.
PubMed=15239958; DOI=10.1016/j.devcel.2004.06.002;
Gitler A.D., Lu M.M., Epstein J.A.;
"PlexinD1 and semaphorin signaling are required in endothelial cells
for cardiovascular development.";
Dev. Cell 7:107-116(2004).
[8]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 26-520, GLYCOSYLATION AT
ASN-53 AND ASN-125, AND DISULFIDE BONDS.
PubMed=12925274; DOI=10.1016/S0896-6273(03)00502-6;
Antipenko A., Himanen J.P., van Leyen K., Nardi-Dei V., Lesniak J.,
Barton W.A., Rajashankar K.R., Lu M., Hoemme C., Puschel A.W.,
Nikolov D.B.;
"Structure of the semaphorin-3A receptor binding module.";
Neuron 39:589-598(2003).
-!- FUNCTION: Plays a role in growth cones guidance. May function to
pattern sensory projections by selectively repelling axons that
normally terminate dorsally. Involved in the development of the
olfactory system and in neuronal control of puberty (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with PXND1. {ECO:0000269|PubMed:15239958}.
-!- INTERACTION:
P97333:Nrp1; NbExp=3; IntAct=EBI-8586029, EBI-1555129;
-!- SUBCELLULAR LOCATION: Secreted.
-!- DEVELOPMENTAL STAGE: Expressed early in embryonic development
(E11) in distinct regions of the neuroectoderm and mesoderm.
Expression became more extensive at later stages.
-!- DOMAIN: Strong binding to neuropilin is mediated by the carboxy
third of the protein.
-!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
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EMBL; X85993; CAA59985.1; -; mRNA.
EMBL; D85028; BAA19773.1; -; mRNA.
EMBL; L41541; AAL77611.1; -; mRNA.
EMBL; AC022368; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC109165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC121125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC121841; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC159971; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC057588; AAH57588.1; -; mRNA.
EMBL; BC090844; AAH90844.1; -; mRNA.
EMBL; L40484; AAA73934.1; -; mRNA.
CCDS; CCDS19092.1; -.
PIR; I48747; I48747.
PIR; I58169; I58169.
RefSeq; NP_001230001.1; NM_001243072.1.
RefSeq; NP_001230002.1; NM_001243073.1.
RefSeq; NP_033178.2; NM_009152.4.
RefSeq; XP_006503620.1; XM_006503557.3.
RefSeq; XP_006503621.1; XM_006503558.3.
RefSeq; XP_006503622.1; XM_006503559.1.
RefSeq; XP_011238967.1; XM_011240665.2.
UniGene; Mm.372039; -.
UniGene; Mm.483774; -.
PDB; 1Q47; X-ray; 2.80 A; A/B=26-520.
PDB; 4GZ8; X-ray; 3.30 A; A/B=21-569.
PDB; 4GZA; X-ray; 7.00 A; G=21-555.
PDBsum; 1Q47; -.
PDBsum; 4GZ8; -.
PDBsum; 4GZA; -.
ProteinModelPortal; O08665; -.
SMR; O08665; -.
BioGrid; 203161; 2.
DIP; DIP-59997N; -.
IntAct; O08665; 2.
MINT; O08665; -.
STRING; 10090.ENSMUSP00000030714; -.
iPTMnet; O08665; -.
PhosphoSitePlus; O08665; -.
MaxQB; O08665; -.
PaxDb; O08665; -.
PeptideAtlas; O08665; -.
PRIDE; O08665; -.
Ensembl; ENSMUST00000030714; ENSMUSP00000030714; ENSMUSG00000028883.
Ensembl; ENSMUST00000095012; ENSMUSP00000092621; ENSMUSG00000028883.
GeneID; 20346; -.
KEGG; mmu:20346; -.
UCSC; uc008wmb.3; mouse.
CTD; 10371; -.
MGI; MGI:107558; Sema3a.
eggNOG; KOG3611; Eukaryota.
eggNOG; ENOG410XQZC; LUCA.
GeneTree; ENSGT00760000118854; -.
HOGENOM; HOG000039964; -.
HOVERGEN; HBG055071; -.
InParanoid; O08665; -.
KO; K06840; -.
OMA; REPTTIS; -.
OrthoDB; EOG091G01W0; -.
TreeFam; TF316102; -.
Reactome; R-MMU-399954; Sema3A PAK dependent Axon repulsion.
Reactome; R-MMU-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
Reactome; R-MMU-399956; CRMPs in Sema3A signaling.
EvolutionaryTrace; O08665; -.
PRO; PR:O08665; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000028883; -.
ExpressionAtlas; O08665; baseline and differential.
Genevisible; O08665; MM.
GO; GO:0030424; C:axon; ISO:MGI.
GO; GO:0030425; C:dendrite; ISO:MGI.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
GO; GO:0045499; F:chemorepellent activity; IDA:MGI.
GO; GO:0038191; F:neuropilin binding; IPI:BHF-UCL.
GO; GO:0030215; F:semaphorin receptor binding; IPI:MGI.
GO; GO:0006915; P:apoptotic process; ISO:MGI.
GO; GO:0048846; P:axon extension involved in axon guidance; IMP:BHF-UCL.
GO; GO:0007411; P:axon guidance; IDA:MGI.
GO; GO:0007413; P:axonal fasciculation; IMP:MGI.
GO; GO:0060385; P:axonogenesis involved in innervation; IMP:BHF-UCL.
GO; GO:0150020; P:basal dendrite arborization; IGI:ARUK-UCL.
GO; GO:0021785; P:branchiomotor neuron axon guidance; IMP:ParkinsonsUK-UCL.
GO; GO:0048813; P:dendrite morphogenesis; IMP:MGI.
GO; GO:0060666; P:dichotomous subdivision of terminal units involved in salivary gland branching; IDA:MGI.
GO; GO:0021612; P:facial nerve structural organization; IMP:ParkinsonsUK-UCL.
GO; GO:1903375; P:facioacoustic ganglion development; IMP:ParkinsonsUK-UCL.
GO; GO:0021828; P:gonadotrophin-releasing hormone neuronal migration to the hypothalamus; IMP:BHF-UCL.
GO; GO:0008045; P:motor neuron axon guidance; IMP:ParkinsonsUK-UCL.
GO; GO:0050919; P:negative chemotaxis; IGI:MGI.
GO; GO:0030517; P:negative regulation of axon extension; IDA:MGI.
GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; IDA:MGI.
GO; GO:0010633; P:negative regulation of epithelial cell migration; IDA:MGI.
GO; GO:0010977; P:negative regulation of neuron projection development; ISO:MGI.
GO; GO:0021675; P:nerve development; IMP:BHF-UCL.
GO; GO:1901166; P:neural crest cell migration involved in autonomic nervous system development; IMP:ParkinsonsUK-UCL.
GO; GO:1903045; P:neural crest cell migration involved in sympathetic nervous system development; IMP:BHF-UCL.
GO; GO:0001764; P:neuron migration; IMP:BHF-UCL.
GO; GO:0021772; P:olfactory bulb development; ISS:UniProtKB.
GO; GO:2000020; P:positive regulation of male gonad development; IMP:BHF-UCL.
GO; GO:2001224; P:positive regulation of neuron migration; IGI:BHF-UCL.
GO; GO:0048841; P:regulation of axon extension involved in axon guidance; IDA:UniProtKB.
GO; GO:0002027; P:regulation of heart rate; IMP:MGI.
GO; GO:0071526; P:semaphorin-plexin signaling pathway; IGI:MGI.
GO; GO:1902287; P:semaphorin-plexin signaling pathway involved in axon guidance; IMP:ParkinsonsUK-UCL.
GO; GO:1902285; P:semaphorin-plexin signaling pathway involved in neuron projection guidance; IMP:BHF-UCL.
GO; GO:0061549; P:sympathetic ganglion development; IMP:BHF-UCL.
GO; GO:0097490; P:sympathetic neuron projection extension; IMP:BHF-UCL.
GO; GO:0097491; P:sympathetic neuron projection guidance; IMP:BHF-UCL.
GO; GO:0061551; P:trigeminal ganglion development; IMP:ParkinsonsUK-UCL.
GO; GO:0021637; P:trigeminal nerve structural organization; IMP:ParkinsonsUK-UCL.
GO; GO:0036486; P:ventral trunk neural crest cell migration; IMP:ParkinsonsUK-UCL.
Gene3D; 2.130.10.10; -; 1.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR016201; PSI.
InterPro; IPR001627; Semap_dom.
InterPro; IPR036352; Semap_dom_sf.
InterPro; IPR027231; Semaphorin.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
PANTHER; PTHR11036; PTHR11036; 1.
Pfam; PF01403; Sema; 1.
SMART; SM00409; IG; 1.
SMART; SM00423; PSI; 1.
SMART; SM00630; Sema; 1.
SUPFAM; SSF101912; SSF101912; 1.
SUPFAM; SSF48726; SSF48726; 1.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS51004; SEMA; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Developmental protein;
Differentiation; Disulfide bond; Glycoprotein; Immunoglobulin domain;
Neurogenesis; Reference proteome; Secreted; Signal.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 772 Semaphorin-3A.
/FTId=PRO_0000032304.
DOMAIN 31 514 Sema. {ECO:0000255|PROSITE-
ProRule:PRU00352}.
DOMAIN 579 665 Ig-like C2-type.
COMPBIAS 728 770 Arg/Lys-rich (basic).
CARBOHYD 53 53 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12925274}.
CARBOHYD 125 125 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12925274}.
CARBOHYD 591 591 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 103 114 {ECO:0000269|PubMed:12925274}.
DISULFID 132 141 {ECO:0000269|PubMed:12925274}.
DISULFID 269 381 {ECO:0000269|PubMed:12925274}.
DISULFID 293 341 {ECO:0000269|PubMed:12925274}.
DISULFID 517 535 {ECO:0000250}.
DISULFID 650 723 {ECO:0000250}.
CONFLICT 193 193 D -> N (in Ref. 6; AAA73934).
{ECO:0000305}.
CONFLICT 207 207 H -> D (in Ref. 1; CAA59985).
{ECO:0000305}.
CONFLICT 253 253 D -> G (in Ref. 1; CAA59985).
{ECO:0000305}.
CONFLICT 352 352 F -> L (in Ref. 6; AAA73934).
{ECO:0000305}.
CONFLICT 403 403 A -> G (in Ref. 1; CAA59985).
{ECO:0000305}.
CONFLICT 475 475 I -> V (in Ref. 1; CAA59985, 2; BAA19773,
3; AAL77611, 5; AAH57588/AAH90844 and 6;
AAA73934). {ECO:0000305}.
CONFLICT 571 572 QH -> ED (in Ref. 1; CAA59985).
{ECO:0000305}.
CONFLICT 616 620 EDRKE -> RRSKR (in Ref. 1; CAA59985).
{ECO:0000305}.
CONFLICT 623 623 R -> K (in Ref. 6; AAA73934).
{ECO:0000305}.
STRAND 31 34 {ECO:0000244|PDB:4GZ8}.
HELIX 36 40 {ECO:0000244|PDB:1Q47}.
TURN 41 43 {ECO:0000244|PDB:1Q47}.
STRAND 46 48 {ECO:0000244|PDB:1Q47}.
STRAND 59 63 {ECO:0000244|PDB:1Q47}.
TURN 64 67 {ECO:0000244|PDB:1Q47}.
STRAND 68 74 {ECO:0000244|PDB:1Q47}.
STRAND 76 83 {ECO:0000244|PDB:1Q47}.
STRAND 87 92 {ECO:0000244|PDB:1Q47}.
HELIX 97 105 {ECO:0000244|PDB:1Q47}.
TURN 110 113 {ECO:0000244|PDB:1Q47}.
STRAND 117 123 {ECO:0000244|PDB:1Q47}.
STRAND 125 133 {ECO:0000244|PDB:1Q47}.
STRAND 136 138 {ECO:0000244|PDB:1Q47}.
STRAND 140 145 {ECO:0000244|PDB:1Q47}.
STRAND 148 151 {ECO:0000244|PDB:4GZ8}.
STRAND 156 164 {ECO:0000244|PDB:1Q47}.
TURN 166 168 {ECO:0000244|PDB:1Q47}.
STRAND 171 175 {ECO:0000244|PDB:4GZ8}.
STRAND 178 182 {ECO:0000244|PDB:1Q47}.
STRAND 185 191 {ECO:0000244|PDB:1Q47}.
STRAND 199 208 {ECO:0000244|PDB:1Q47}.
TURN 218 220 {ECO:0000244|PDB:1Q47}.
STRAND 225 232 {ECO:0000244|PDB:1Q47}.
STRAND 235 237 {ECO:0000244|PDB:1Q47}.
HELIX 238 240 {ECO:0000244|PDB:1Q47}.
STRAND 242 250 {ECO:0000244|PDB:1Q47}.
STRAND 261 269 {ECO:0000244|PDB:1Q47}.
STRAND 275 280 {ECO:0000244|PDB:1Q47}.
STRAND 287 291 {ECO:0000244|PDB:1Q47}.
STRAND 307 314 {ECO:0000244|PDB:1Q47}.
STRAND 323 329 {ECO:0000244|PDB:1Q47}.
STRAND 333 335 {ECO:0000244|PDB:1Q47}.
STRAND 338 343 {ECO:0000244|PDB:1Q47}.
HELIX 345 352 {ECO:0000244|PDB:1Q47}.
STRAND 356 358 {ECO:0000244|PDB:1Q47}.
STRAND 384 387 {ECO:0000244|PDB:4GZ8}.
HELIX 392 394 {ECO:0000244|PDB:1Q47}.
HELIX 397 404 {ECO:0000244|PDB:1Q47}.
STRAND 408 411 {ECO:0000244|PDB:1Q47}.
HELIX 416 418 {ECO:0000244|PDB:1Q47}.
STRAND 421 429 {ECO:0000244|PDB:1Q47}.
STRAND 431 440 {ECO:0000244|PDB:1Q47}.
STRAND 445 453 {ECO:0000244|PDB:1Q47}.
STRAND 458 462 {ECO:0000244|PDB:1Q47}.
STRAND 466 468 {ECO:0000244|PDB:1Q47}.
STRAND 478 480 {ECO:0000244|PDB:1Q47}.
STRAND 483 485 {ECO:0000244|PDB:1Q47}.
STRAND 491 495 {ECO:0000244|PDB:1Q47}.
TURN 496 499 {ECO:0000244|PDB:1Q47}.
STRAND 500 507 {ECO:0000244|PDB:1Q47}.
STRAND 509 514 {ECO:0000244|PDB:1Q47}.
HELIX 517 519 {ECO:0000244|PDB:4GZ8}.
HELIX 524 529 {ECO:0000244|PDB:4GZ8}.
STRAND 539 541 {ECO:0000244|PDB:4GZ8}.
TURN 564 566 {ECO:0000244|PDB:4GZ8}.
SEQUENCE 772 AA; 88813 MW; C6533FF007018D0C CRC64;
MGWFTGIACL FWGVLLTARA NYANGKNNVP RLKLSYKEML ESNNVITFNG LANSSSYHTF
LLDEERSRLY VGAKDHIFSF NLVNIKDFQK IVWPVSYTRR DECKWAGKDI LKECANFIKV
LEAYNQTHLY ACGTGAFHPI CTYIEVGHHP EDNIFKLQDS HFENGRGKSP YDPKLLTASL
LIDGELYSGT AADFMGRDFA IFRTLGHHHP IRTEQHDSRW LNDPRFISAH LIPESDNPED
DKVYFFFREN AIDGEHSGKA THARIGQICK NDFGGHRSLV NKWTTFLKAR LICSVPGPNG
IDTHFDELQD VFLMNSKDPK NPIVYGVFTT SSNIFKGSAV CMYSMSDVRR VFLGPYAHRD
GPNYQWVPYQ GRVPYPRPGT CPSKTFGGFD STKDLPDDVI TFARSHPAMY NPVFPINNRP
IMIKTDVNYQ FTQIVVDRVD AEDGQYDVMF IGTDVGTVLK VVSVPKETWH DLEEILLEEM
TVFREPTTIS AMELSTKQQQ LYIGSTAGVA QLPLHRCDIY GKACAECCLA RDPYCAWDGS
SCSRYFPTAK RRTRRQDIRN GDPLTHCSDL QHHDNHHGPS LEERIIYGVE NSSTFLECSP
KSQRALVYWQ FQRRNEDRKE EIRMGDHIIR TEQGLLLRSL QKKDSGNYLC HAVEHGFMQT
LLKVTLEVID TEHLEELLHK DDDGDGSKIK EMSSSMTPSQ KVWYRDFMQL INHPNLNTMD
EFCEQVWKRD RKQRRQRPGH SQGSSNKWKH MQESKKGRNR RTHEFERAPR SV


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