ID SEM3C_MOUSE Reviewed; 751 AA.
AC Q62181; Q6NXW7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 27-MAR-2024, entry version 171.
DE RecName: Full=Semaphorin-3C;
DE AltName: Full=Semaphorin-E;
DE Short=Sema E;
DE Flags: Precursor;
GN Name=Sema3c; Synonyms=Semae, SemE;
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=NMRI; TISSUE=Embryo;
RX PubMed=7748561; DOI=10.1016/0896-6273(95)90332-1;
RA Pueschel A.W., Adams R.H., Betz H.;
RT "Murine semaphorin D/collapsin is a member of a diverse gene family and
RT creates domains inhibitory for axonal extension.";
RL Neuron 14:941-948(1995).
RN [2]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CD-1; TISSUE=Neural stem cell;
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 [4]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=11688556; DOI=10.1242/dev.128.16.3061;
RA Feiner L., Webber A.L., Brown C.B., Lu M.M., Jia L., Feinstein P.,
RA Mombaerts P., Epstein J.A., Raper J.A.;
RT "Targeted disruption of semaphorin 3C leads to persistent truncus
RT arteriosus and aortic arch interruption.";
RL Development 128:3061-3070(2001).
RN [5]
RP FUNCTION, AND INTERACTION WITH PLXND1.
RX PubMed=15239958; DOI=10.1016/j.devcel.2004.06.002;
RA Gitler A.D., Lu M.M., Epstein J.A.;
RT "PlexinD1 and semaphorin signaling are required in endothelial cells for
RT cardiovascular development.";
RL Dev. Cell 7:107-116(2004).
RN [6]
RP FUNCTION.
RX PubMed=17021275; DOI=10.1093/cercor/bhl082;
RA Gonthier B., Nasarre C., Roth L., Perraut M., Thomasset N., Roussel G.,
RA Aunis D., Bagnard D.;
RT "Functional interaction between matrix metalloproteinase-3 and semaphorin-
RT 3C during cortical axonal growth and guidance.";
RL Cereb. Cortex 17:1712-1721(2007).
CC -!- FUNCTION: Binds to plexin family members and plays an important role in
CC the regulation of developmental processes. Required for normal
CC cardiovascular development during embryogenesis. Functions as
CC attractant for growing axons, and thereby plays an important role in
CC axon growth and axon guidance. {ECO:0000269|PubMed:11688556,
CC ECO:0000269|PubMed:15239958, ECO:0000269|PubMed:17021275}.
CC -!- SUBUNIT: Interacts with PLXND1. {ECO:0000269|PubMed:15239958}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed from day 10 in the embryo. Maximum
CC expression between days 10-12 with moderate levels from day 13 until
CC birth.
CC -!- DISRUPTION PHENOTYPE: Perinatal lethality. Mice display severe defects
CC in cardiovascular development, including aortic arch malformations and
CC septation defects in the cardiac outflow tract.
CC {ECO:0000269|PubMed:11688556}.
CC -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
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DR EMBL; X85994; CAA59986.1; -; mRNA.
DR EMBL; CH466586; EDL03234.1; -; Genomic_DNA.
DR EMBL; BC066852; AAH66852.1; -; mRNA.
DR CCDS; CCDS19099.1; -.
DR PIR; I48748; I48748.
DR RefSeq; NP_038685.3; NM_013657.5.
DR AlphaFoldDB; Q62181; -.
DR SMR; Q62181; -.
DR BioGRID; 203163; 3.
DR STRING; 10090.ENSMUSP00000030568; -.
DR GlyCosmos; Q62181; 7 sites, No reported glycans.
DR GlyGen; Q62181; 7 sites.
DR iPTMnet; Q62181; -.
DR PhosphoSitePlus; Q62181; -.
DR MaxQB; Q62181; -.
DR PaxDb; 10090-ENSMUSP00000030568; -.
DR PeptideAtlas; Q62181; -.
DR ProteomicsDB; 261150; -.
DR Antibodypedia; 48987; 306 antibodies from 27 providers.
DR DNASU; 20348; -.
DR Ensembl; ENSMUST00000030568.14; ENSMUSP00000030568.8; ENSMUSG00000028780.14.
DR GeneID; 20348; -.
DR KEGG; mmu:20348; -.
DR UCSC; uc008wnl.1; mouse.
DR AGR; MGI:107557; -.
DR CTD; 10512; -.
DR MGI; MGI:107557; Sema3c.
DR VEuPathDB; HostDB:ENSMUSG00000028780; -.
DR eggNOG; KOG3611; Eukaryota.
DR GeneTree; ENSGT00940000159379; -.
DR HOGENOM; CLU_009051_5_0_1; -.
DR InParanoid; Q62181; -.
DR OMA; TVQYGVK; -.
DR OrthoDB; 5342713at2759; -.
DR PhylomeDB; Q62181; -.
DR TreeFam; TF352628; -.
DR BioGRID-ORCS; 20348; 1 hit in 78 CRISPR screens.
DR ChiTaRS; Sema3c; mouse.
DR PRO; PR:Q62181; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q62181; Protein.
DR Bgee; ENSMUSG00000028780; Expressed in ureter smooth muscle and 276 other cell types or tissues.
DR ExpressionAtlas; Q62181; baseline and differential.
DR Genevisible; Q62181; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0045499; F:chemorepellent activity; IBA:GO_Central.
DR GO; GO:0030215; F:semaphorin receptor binding; IPI:MGI.
DR GO; GO:0007411; P:axon guidance; IDA:UniProtKB.
DR GO; GO:0001974; P:blood vessel remodeling; IMP:MGI.
DR GO; GO:0140074; P:cardiac endothelial to mesenchymal transition; IDA:BHF-UCL.
DR GO; GO:0003215; P:cardiac right ventricle morphogenesis; IEP:BHF-UCL.
DR GO; GO:0060666; P:dichotomous subdivision of terminal units involved in salivary gland branching; IDA:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0060174; P:limb bud formation; IEP:BHF-UCL.
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:0001755; P:neural crest cell migration; IMP:MGI.
DR GO; GO:0021915; P:neural tube development; IEP:BHF-UCL.
DR GO; GO:0003151; P:outflow tract morphogenesis; IEP:BHF-UCL.
DR GO; GO:0003148; P:outflow tract septum morphogenesis; IMP:BHF-UCL.
DR GO; GO:1905312; P:positive regulation of cardiac neural crest cell migration involved in outflow tract morphogenesis; IDA:BHF-UCL.
DR GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:0003350; P:pulmonary myocardium development; IEP:BHF-UCL.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; IMP:BHF-UCL.
DR GO; GO:0001756; P:somitogenesis; IEP:BHF-UCL.
DR CDD; cd05871; Ig_Sema3; 1.
DR CDD; cd11251; Sema_3C; 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; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR016201; PSI.
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; SEMAPHORIN; 1.
DR PANTHER; PTHR11036:SF25; SEMAPHORIN-3C; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF01403; Sema; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 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.
PE 1: Evidence at protein level;
KW Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Neurogenesis; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..751
FT /note="Semaphorin-3C"
FT /id="PRO_0000032312"
FT DOMAIN 28..511
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 571..655
FT /note="Ig-like C2-type"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 585
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 586
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 101..112
FT /evidence="ECO:0000250"
FT DISULFID 130..139
FT /evidence="ECO:0000250"
FT DISULFID 266..378
FT /evidence="ECO:0000250"
FT DISULFID 290..338
FT /evidence="ECO:0000250"
FT DISULFID 514..532
FT /evidence="ECO:0000250"
FT DISULFID 643..709
FT /evidence="ECO:0000250"
FT CONFLICT 206..208
FT /note="NAV -> MQL (in Ref. 1; CAA59986)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="Y -> S (in Ref. 1; CAA59986)"
FT /evidence="ECO:0000305"
FT CONFLICT 490
FT /note="K -> E (in Ref. 1; CAA59986)"
FT /evidence="ECO:0000305"
FT CONFLICT 615
FT /note="V -> G (in Ref. 1; CAA59986)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 751 AA; 85289 MW; 32537E9D664123EE CRC64;
MAFRAICVLV GVFICSICVR GSSQPQARVY LTFDELRETK TSEYFSLSHQ QLDYRILLMD
EDQDRIYVGS KDHILSLNIN NISQEPLSVF WPASTIKVEE CKMAGKDPTH GCGNFVRVIQ
TFNRTHLYVC GSGAFSPVCT YLNRGRRSED QVFMIDSKCE SGKGRCSFNP NVNTVSVMIN
EELFSGMYID FMGTDAAIFR SLTKRNAVRT DQHNSKWLSE PMFVDAHVIP DGTDPNDAKV
YFFFKERLTD NNRSTKQIHS MIARICPNDT GGQRSLVNKW TTFLKARLVC SVTDEDGPET
HFDELEDVFL LETDNPRTTL VYGIFTTSSS VFKGSAVCVY HLSDIQTVFN GPFAHKEGPN
HQLISYQGRI PYPRPGTCPG GAFTPNMRTT KDFPDDVVTF IRNHPLMYNS IYPIHRRPLI
VRIGTDYKYT KIAVDRVNAA DGRYHVLFLG TDRGTVQKVV VLPTNSSASG ELILEELEVF
KNHVPITTMK ISSKKQQLYV SSNEGVSQVS LHRCHIYGTA CADCCLARDP YCAWDGHSCS
RFYPTGKRRS RRQDVRHGNP LTQCRGFNLK AYRNAAEIVQ YGVRNNSTFL ECAPKSPQAS
IKWLLQKDKD RRKEVKLNER IIATSQGLLI RSVQDSDQGL YHCIATENSF KQTIAKINFK
VLDSEMVAVV TDKWSPWTWA GSVRALPFHP KDILGAFSHS EMQLINQYCK DTRQQQQLGE
EPQKMRGDYG KLKALINSRK SRNRRNQLPE S
//
