PLXA3_RAT
ID PLXA3_RAT Reviewed; 1872 AA.
AC D3ZPX4;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Plexin-A3;
DE Flags: Precursor;
GN Name=Plxna3;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
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.
CC -!- FUNCTION: Coreceptor for SEMA3A and SEMA3F. Necessary for signaling by
CC class 3 semaphorins and subsequent remodeling of the cytoskeleton.
CC Plays a role in axon guidance in the developing nervous system.
CC Regulates the migration of sympathetic neurons, but not of neural crest
CC precursors. Required for normal dendrite spine morphology in pyramidal
CC neurons. May play a role in regulating semaphorin-mediated programmed
CC cell death in the developing nervous system. Class 3 semaphorins bind
CC to a complex composed of a neuropilin and a plexin. The plexin
CC modulates the affinity of the complex for specific semaphorins, and its
CC cytoplasmic domain is required for the activation of down-stream
CC signaling events in the cytoplasm (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the plexin family. {ECO:0000305}.
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DR EMBL; AC094668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH474099; EDL84973.1; -; Genomic_DNA.
DR RefSeq; NP_001101051.2; NM_001107581.2.
DR RefSeq; XP_006229639.1; XM_006229577.3.
DR RefSeq; XP_017457512.1; XM_017602023.1.
DR AlphaFoldDB; D3ZPX4; -.
DR SMR; D3ZPX4; -.
DR STRING; 10116.ENSRNOP00000053147; -.
DR GlyGen; D3ZPX4; 3 sites.
DR iPTMnet; D3ZPX4; -.
DR PhosphoSitePlus; D3ZPX4; -.
DR PaxDb; D3ZPX4; -.
DR PeptideAtlas; D3ZPX4; -.
DR PRIDE; D3ZPX4; -.
DR Ensembl; ENSRNOT00000083148; ENSRNOP00000068735; ENSRNOG00000060464.
DR GeneID; 309280; -.
DR KEGG; rno:309280; -.
DR CTD; 55558; -.
DR RGD; 1584973; Plxna3.
DR eggNOG; KOG3610; Eukaryota.
DR GeneTree; ENSGT01050000244850; -.
DR HOGENOM; CLU_001436_2_0_1; -.
DR InParanoid; D3ZPX4; -.
DR OMA; VYYNCSV; -.
DR OrthoDB; 90434at2759; -.
DR PhylomeDB; D3ZPX4; -.
DR TreeFam; TF312962; -.
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:D3ZPX4; -.
DR Proteomes; UP000002494; Chromosome X.
DR Proteomes; UP000234681; Chromosome 1.
DR Bgee; ENSRNOG00000060464; Expressed in frontal cortex and 19 other tissues.
DR Genevisible; D3ZPX4; RN.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0002116; C:semaphorin receptor complex; IBA:GO_Central.
DR GO; GO:0017154; F:semaphorin receptor activity; ISO:RGD.
DR GO; GO:0048846; P:axon extension involved in axon guidance; IEA:Ensembl.
DR GO; GO:0007411; P:axon guidance; ISO:RGD.
DR GO; GO:0021785; P:branchiomotor neuron axon guidance; ISO:RGD.
DR GO; GO:0021612; P:facial nerve structural organization; ISO:RGD.
DR GO; GO:0021828; P:gonadotrophin-releasing hormone neuronal migration to the hypothalamus; IEA:Ensembl.
DR GO; GO:0021766; P:hippocampus development; ISO:RGD.
DR GO; GO:0050919; P:negative chemotaxis; ISO:RGD.
DR GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; ISO:RGD.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IBA:GO_Central.
DR GO; GO:1990138; P:neuron projection extension; ISO:RGD.
DR GO; GO:0097485; P:neuron projection guidance; ISO:RGD.
DR GO; GO:0021628; P:olfactory nerve formation; IEA:Ensembl.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IBA:GO_Central.
DR GO; GO:0051495; P:positive regulation of cytoskeleton organization; ISO:RGD.
DR GO; GO:0021860; P:pyramidal neuron development; ISO:RGD.
DR GO; GO:0030334; P:regulation of cell migration; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:0043087; P:regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:1902287; P:semaphorin-plexin signaling pathway involved in axon guidance; ISO:RGD.
DR GO; GO:0021637; P:trigeminal nerve structural organization; ISO:RGD.
DR Gene3D; 1.10.506.10; -; 2.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR031148; Plexin.
DR InterPro; IPR013548; Plexin_cytoplasmic_RasGAP_dom.
DR InterPro; IPR002165; Plexin_repeat.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR001627; Semap_dom.
DR InterPro; IPR036352; Semap_dom_sf.
DR InterPro; IPR041019; TIG1_plexin.
DR InterPro; IPR041362; TIG2_plexin.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR22625; PTHR22625; 1.
DR Pfam; PF08337; Plexin_cytopl; 1.
DR Pfam; PF01437; PSI; 2.
DR Pfam; PF01403; Sema; 1.
DR Pfam; PF01833; TIG; 4.
DR Pfam; PF18020; TIG_2; 1.
DR Pfam; PF17960; TIG_plexin; 1.
DR SMART; SM00429; IPT; 4.
DR SMART; SM00423; PSI; 3.
DR SMART; SM00630; Sema; 1.
DR SUPFAM; SSF101912; SSF101912; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF81296; SSF81296; 4.
DR PROSITE; PS51004; SEMA; 1.
PE 3: Inferred from homology;
KW Cell membrane; Coiled coil; Disulfide bond; Glycoprotein; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1872
FT /note="Plexin-A3"
FT /id="PRO_0000411105"
FT TOPO_DOM 20..1220
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1221..1241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1242..1872
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..489
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 841..934
FT /note="IPT/TIG 1"
FT DOMAIN 936..1021
FT /note="IPT/TIG 2"
FT DOMAIN 1024..1123
FT /note="IPT/TIG 3"
FT DOMAIN 1126..1212
FT /note="IPT/TIG 4"
FT COILED 1240..1294
FT /evidence="ECO:0000255"
FT MOD_RES 1597
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51805"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 549
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 78..87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 113..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 267..388
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 283..339
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 357..376
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 492..509
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 498..540
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 501..518
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 512..524
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 575..595
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
SQ SEQUENCE 1872 AA; 207982 MW; D8DACA874717E870 CRC64;
MHTVCLLPLL FFTIGGCLGS SRPFRTFVVT DTTLTHLAVH RVTGEVFVGA VNRVFKLASN
LTELRAHVTG PIEDNARCYP PPSMRVCSHR LVPVDNVNKL LLIDYAARRL VACGSIWQGI
CQFLRLDDLF KLGEPHHRKE HYLSGAQEPD SMAGVIVEQG QGPSKLFVGT AVDGKSEYFP
TLSSRKLIDD EDSGDMFSLV YQDEFVSSQI KIPSDTLSLY PAFDIYYIYG FVSASFVYFL
TLQLDTQQTL LDTAGEKFFT SKIVRMCAGD SEFYSYVEFP IGCSWRGVEY RLVQSAHLAK
PGLLLAQALG VPADEDVLFT IFSQGQKNRA NPPRQTILCL FTLSSINAHI RRRIQSCYRG
EGTLALPWLL NKELPCINTP MQINGNFCGL VLNQPLGGLH VIEGLPLLAD STDGMASVAA
YTYHQHSVVF IGTRSGNLKK VRVDGSQDAQ LYETVSVVQG TPILRDLLFS PDHRHIYLLS
EKQVSQLPVE TCEQYLSCAA CLGSGDPHCG WCVLQHRCCR EGACPGASAP HGFAEELNKC
IQVRVRPNNV SVTSSGVQLT VAMRNVPDLS LGVSCSFEEV TESEAILLPS GELRCPSPSL
QELQTLTRGH GATHTVRLQL LSMETGVRFA GVDFVFYNCS ALQSCMSCVG SPYPCHWCKY
RHVCTSHPHE CSFQEGRVHS PEGCPEILPR GDLLIPVGVM QPLTLRAKNL PQPQSGQKNY
ECVVRVQGRQ HRVPAVRFNS SSVQCQNASY FYEGDEFGDT ELDFSVVWDG DFPIDKPPSF
RALLYKCWAQ RPSCGLCLKA DPRFNCGWCI SEHRCQLRVH CPAPKSNWMH PSQKGARCSH
PRITQIHPLT GPKEGGTRVT IVGENLGLTS REVGLRVAGV RCNSIPTEYV SAERIVCEME
ESLVPSPPPG PAELCVGDCS ADFRTQSQQL YSFVTPTLDR VSPTRGPASG GTRLTISGTS
LDAGSRVTVI IRDGECQFVR RDAEAIVCIS PISTLGPSQA PIILAIDHAN ISSTGVIYTY
TQDPTVTHLE PTWSIINGST SITVSGTHLL TVQEPRVRAK YRGIETTNTC QVINDTAMLC
KAPGIFLGHP QPRAQGEHPD EFGFLLDHVQ AARSLNRSSF TYYPDPSFEP LGPSGVLDVK
PGSHVVLKGK NLIPAAAGSS RLNYTVLIGG QPCALTVSDT QLLCDSPSQT GRQPVMVLVG
GLEFWLGTLH ITADRALTLP AMVGLAAGGG LLLLAITVVL VAYKRKTQDA DRTLKRLQLQ
MDNLESRVAL ECKEAFAELQ TDINELTNHM DGVQIPFLDY RTYAVRVLFP GIEAHPVLKE
LDTPPNVEKA LRLFGQLLHS RAFLLTFIHT LEAQSSFSMR DRGTVASLTM VALQSRLDYA
TGLLKQLLAD LIEKNLESKN HPKLLLRRTE SVAEKMLTNW FTFLLHKFLK ECAGEPLFLL
YCAIKQQMEK GPIDAITGEA RYSLSEDKLI RQQIDYKTLT LHCVCPESEG SAQVPVKVLN
CDSITQAKDK LLDTVYKGIP YSQRPKAEDM DLEWRQGRMA RIILQDEDIT TKIECDWKRI
NSLAHYQVTD GSLVALVPKQ VSAYNMANSF TFTRSLSRYE SLLRAASSPD SLRSRAPMLT
PDQEAGTKLW HLVKNHDHAD HREGDRGSKM VSEIYLTRLL ATKGTLQKFV DDLFETVFST
AHRGSALPLA IKYMFDFLDE QADQRQISDP DVRHTWKSNC LPLRFWVNVI KNPQFVFDIH
KNSITDACLS VVAQTFMDSC STSEHRLGKD SPSNKLLYAK DIPNYKSWVE RYYRDIAKMA
SISDQDMDAY LVEQSRLHAN DFNVLSALSE LYFYVTKYRQ EILTSLDRDA SCRKHKLRQK
LEQIITLVSS SS
