ID   SEM3A_RAT               Reviewed;         772 AA.
AC   Q63548;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 171.
DE   RecName: Full=Semaphorin-3A;
DE   AltName: Full=Semaphorin III;
DE            Short=Sema III;
DE   Flags: Precursor;
GN   Name=Sema3a;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar; TISSUE=Brain;
RX   PubMed=8915837;
RX   DOI=10.1002/(sici)1096-9861(19961118)375:3<378::aid-cne3>3.0.co;2-#;
RA   Giger R.J., Wolfer D.P., De Wit G.M.J., Verhaagen J.;
RT   "Anatomy of rat semaphorin III/collapsin-1 mRNA expression and relationship
RT   to developing nerve tracts during neuroembryogenesis.";
RL   J. Comp. Neurol. 375:378-392(1996).
RN   [2]
RP   TISSUE SPECIFICITY, AND INDUCTION BY INJURY.
RX   PubMed=28270793; DOI=10.3389/fneur.2017.00049;
RA   Lindholm T., Risling M., Carlstedt T., Hammarberg H., Wallquist W.,
RA   Cullheim S., Skoeld M.K.;
RT   "Expression of Semaphorins, Neuropilins, VEGF, and Tenascins in Rat and
RT   Human Primary Sensory Neurons after a Dorsal Root Injury.";
RL   Front. Neurol. 8:49-49(2017).
CC   -!- FUNCTION: May be involved in guiding growing axons towards their
CC       targets by forming a molecular boundary that instructs axons to engage
CC       in the formation of specific nerve tracts. Binds to neuropilin.
CC       Involved in the development of the olfactory system and in neuronal
CC       control of puberty (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with PLXND1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in the dorsal root ganglia.
CC       {ECO:0000269|PubMed:28270793}.
CC   -!- DEVELOPMENTAL STAGE: At 11 dpc, expression was restricted to the
CC       olfactory pit, the basal and rostral surface of the telencephalic
CC       vesicle, the eye anlage, the epithelium of Rathke pouch, and somites.
CC       At later developmental stages, it was widely distributed in neuronal as
CC       well as in mesenchymal and epithelial structures outside the nervous
CC       system. After birth, mesenchymal levels decreased rapidly and
CC       expression became restricted to specific sets of neurons in the CNS. In
CC       the mature CNS, it is detectable in mitral cells, neurons of the
CC       accessory bulb and cerebral cortex, cerebellar Purkinje cells, as well
CC       as a subset of cranial and spinal motoneurons.
CC   -!- INDUCTION: General decrease in dorsal root ganglia in response to
CC       injury from dorsal rhizotomy, with the greatest decrease evident 21
CC       days post-injury, returning to comparable levels 1 year post-injury
CC       (PubMed:28270793). Decreased in dorsal root ganglia in response to
CC       sciatic nerve transection 3 days post-injury, returning to comparable
CC       levels 14 days post-injury (PubMed:28270793).
CC       {ECO:0000269|PubMed:28270793}.
CC   -!- DOMAIN: Strong binding to neuropilin is mediated by the carboxy third
CC       of the protein.
CC   -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
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DR   EMBL; X95286; CAA64607.1; -; mRNA.
DR   RefSeq; NP_059006.1; NM_017310.1.
DR   RefSeq; XP_006236051.1; XM_006235989.3.
DR   RefSeq; XP_006236052.1; XM_006235990.3.
DR   RefSeq; XP_008760924.1; XM_008762702.1.
DR   RefSeq; XP_017448057.1; XM_017592568.1.
DR   AlphaFoldDB; Q63548; -.
DR   SMR; Q63548; -.
DR   IntAct; Q63548; 1.
DR   MINT; Q63548; -.
DR   STRING; 10116.ENSRNOP00000036472; -.
DR   GlyCosmos; Q63548; 3 sites, No reported glycans.
DR   GlyGen; Q63548; 3 sites.
DR   iPTMnet; Q63548; -.
DR   PhosphoSitePlus; Q63548; -.
DR   PaxDb; 10116-ENSRNOP00000036472; -.
DR   DNASU; 29751; -.
DR   Ensembl; ENSRNOT00000096965.1; ENSRNOP00000085581.1; ENSRNOG00000023337.3.
DR   Ensembl; ENSRNOT00055033733; ENSRNOP00055027381; ENSRNOG00055019757.
DR   Ensembl; ENSRNOT00060021471; ENSRNOP00060016970; ENSRNOG00060012639.
DR   Ensembl; ENSRNOT00065030307; ENSRNOP00065024087; ENSRNOG00065018091.
DR   GeneID; 29751; -.
DR   KEGG; rno:29751; -.
DR   AGR; RGD:3657; -.
DR   CTD; 10371; -.
DR   RGD; 3657; Sema3a.
DR   eggNOG; KOG3611; Eukaryota.
DR   GeneTree; ENSGT00940000158203; -.
DR   HOGENOM; CLU_009051_5_0_1; -.
DR   InParanoid; Q63548; -.
DR   OMA; TYLCHAV; -.
DR   OrthoDB; 5342713at2759; -.
DR   PhylomeDB; Q63548; -.
DR   TreeFam; TF316102; -.
DR   Reactome; R-RNO-399954; Sema3A PAK dependent Axon repulsion.
DR   Reactome; R-RNO-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
DR   Reactome; R-RNO-399956; CRMPs in Sema3A signaling.
DR   PRO; PR:Q63548; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Bgee; ENSRNOG00000023337; Expressed in cerebellum and 17 other cell types or tissues.
DR   GO; GO:0030424; C:axon; IDA:RGD.
DR   GO; GO:0150053; C:cerebellar climbing fiber to Purkinje cell synapse; ISO:RGD.
DR   GO; GO:0030425; C:dendrite; IDA:RGD.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR   GO; GO:0045499; F:chemorepellent activity; ISO:RGD.
DR   GO; GO:0038191; F:neuropilin binding; ISO:RGD.
DR   GO; GO:0030215; F:semaphorin receptor binding; ISO:RGD.
DR   GO; GO:0048675; P:axon extension; ISO:RGD.
DR   GO; GO:0048846; P:axon extension involved in axon guidance; ISO:RGD.
DR   GO; GO:0007411; P:axon guidance; IGI:MGI.
DR   GO; GO:0007413; P:axonal fasciculation; ISO:RGD.
DR   GO; GO:0060385; P:axonogenesis involved in innervation; ISO:RGD.
DR   GO; GO:0150020; P:basal dendrite arborization; ISO:RGD.
DR   GO; GO:0021785; P:branchiomotor neuron axon guidance; ISO:RGD.
DR   GO; GO:0048813; P:dendrite morphogenesis; ISO:RGD.
DR   GO; GO:0060666; P:dichotomous subdivision of terminal units involved in salivary gland branching; ISO:RGD.
DR   GO; GO:0010631; P:epithelial cell migration; ISO:RGD.
DR   GO; GO:0021612; P:facial nerve structural organization; ISO:RGD.
DR   GO; GO:1903375; P:facioacoustic ganglion development; ISO:RGD.
DR   GO; GO:0021828; P:gonadotrophin-releasing hormone neuronal migration to the hypothalamus; ISO:RGD.
DR   GO; GO:0099558; P:maintenance of synapse structure; ISO:RGD.
DR   GO; GO:0008045; P:motor neuron axon guidance; ISO:RGD.
DR   GO; GO:0050919; P:negative chemotaxis; ISO:RGD.
DR   GO; GO:0030517; P:negative regulation of axon extension; IDA:RGD.
DR   GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; ISO:RGD.
DR   GO; GO:0010633; P:negative regulation of epithelial cell migration; ISO:RGD.
DR   GO; GO:0010977; P:negative regulation of neuron projection development; ISO:RGD.
DR   GO; GO:0021675; P:nerve development; ISO:RGD.
DR   GO; GO:0007399; P:nervous system development; ISO:RGD.
DR   GO; GO:0001755; P:neural crest cell migration; IBA:GO_Central.
DR   GO; GO:1901166; P:neural crest cell migration involved in autonomic nervous system development; ISO:RGD.
DR   GO; GO:1903045; P:neural crest cell migration involved in sympathetic nervous system development; ISO:RGD.
DR   GO; GO:0001764; P:neuron migration; ISO:RGD.
DR   GO; GO:0021772; P:olfactory bulb development; ISS:UniProtKB.
DR   GO; GO:2000020; P:positive regulation of male gonad development; ISO:RGD.
DR   GO; GO:2001224; P:positive regulation of neuron migration; ISO:RGD.
DR   GO; GO:0048841; P:regulation of axon extension involved in axon guidance; ISO:RGD.
DR   GO; GO:0002027; P:regulation of heart rate; ISO:RGD.
DR   GO; GO:0071526; P:semaphorin-plexin signaling pathway; ISO:RGD.
DR   GO; GO:0061549; P:sympathetic ganglion development; ISO:RGD.
DR   GO; GO:0097490; P:sympathetic neuron projection extension; ISO:RGD.
DR   GO; GO:0097491; P:sympathetic neuron projection guidance; ISO:RGD.
DR   GO; GO:0008039; P:synaptic target recognition; ISO:RGD.
DR   GO; GO:0061551; P:trigeminal ganglion development; ISO:RGD.
DR   GO; GO:0021637; P:trigeminal nerve structural organization; ISO:RGD.
DR   GO; GO:0036486; P:ventral trunk neural crest cell migration; ISO:RGD.
DR   CDD; cd05871; Ig_Sema3; 1.
DR   CDD; cd11249; Sema_3A; 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; IPR041416; IL-1RAcP-like_ig.
DR   InterPro; IPR016201; PSI.
DR   InterPro; IPR042820; Sema3A_sema.
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:SF23; SEMAPHORIN-3A; 1.
DR   Pfam; PF18452; Ig_6; 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; Q63548; RN.
PE   2: Evidence at transcript 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..772
FT                   /note="Semaphorin-3A"
FT                   /id="PRO_0000032305"
FT   DOMAIN          31..514
FT                   /note="Sema"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DOMAIN          577..665
FT                   /note="Ig-like C2-type"
FT   REGION          677..698
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          729..772
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        749..772
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        53
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        125
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        591
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        103..114
FT                   /evidence="ECO:0000250"
FT   DISULFID        132..141
FT                   /evidence="ECO:0000250"
FT   DISULFID        269..381
FT                   /evidence="ECO:0000250"
FT   DISULFID        293..341
FT                   /evidence="ECO:0000250"
FT   DISULFID        517..535
FT                   /evidence="ECO:0000250"
FT   DISULFID        650..723
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   772 AA;  88808 MW;  240907812FF9F2D2 CRC64;
     MGWFTGIACL FWGILLTARA NYANGKNNVP RLKLSYKEML ESNNVITFNG LANSSSYHTF
     LLDEERSRLY VGAKDHIFSF NLVNIKDFQK IVWPVSYTRR DECKWAGKDI LKECANFIKV
     LKAYNQTHLY 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 DLEEVLLEEM
     TVFREPTTIS AMELSTKQQQ LYIGSTAGVA QLPLHRCDIY GKACAECCLA RDPYCAWDGS
     SCSRYFPTAK RRTRRQDIRN GDPLTHCSDL QHHDNHHGHS LEERIIYGVE NSSTFLECSP
     KSQRALVYWQ FQRRNEDRKE EIRVGDHIIR TEQGLLLRSL QKKDSGNYLC HAVEHGFMQT
     LLKVTLEVID TEHLEELLHK DDDGDGSKTK EMSSSMTPSQ KVWYRDFMQL INHPNLNTMD
     EFCEQVWKRD RKQRRQRPGH SQGSSNKWKH MQESKKGRNR RTHEFERAPR SV
//