PLXA3_DANRE
ID PLXA3_DANRE Reviewed; 1892 AA.
AC B0S5N4; A5JJU2; A8IYK6; B3DKK4;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Plexin A3;
DE Flags: Precursor;
GN Name=plxna3; ORFNames=si:dkey-7i23.3;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17475806; DOI=10.1523/jneurosci.1132-07.2007;
RA Feldner J., Reimer M.M., Schweitzer J., Wendik B., Meyer D., Becker T.,
RA Becker C.G.;
RT "PlexinA3 restricts spinal exit points and branching of trunk motor nerves
RT in embryonic zebrafish.";
RL J. Neurosci. 27:4978-4983(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=AB; TISSUE=Brain;
RX PubMed=17897628; DOI=10.1016/j.bbrc.2007.09.038;
RA Kimura M., Taniguchi M., Mikami Y., Masuda T., Yoshida T., Mishina M.,
RA Shimizu T.;
RT "Identification and characterization of zebrafish semaphorin 6D.";
RL Biochem. Biophys. Res. Commun. 363:762-768(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=17699603; DOI=10.1242/dev.007112;
RA Palaisa K.A., Granato M.;
RT "Analysis of zebrafish sidetracked mutants reveals a novel role for Plexin
RT A3 in intraspinal motor axon guidance.";
RL Development 134:3251-3257(2007).
CC -!- FUNCTION: Coreceptor for class 3 semaphorins. Necessary for signaling
CC by class 3 semaphorins and subsequent remodeling of the cytoskeleton.
CC Plays a role in axon guidance in the developing nervous system. Class 3
CC semaphorins bind to a complex composed of a neuropilin and a plexin.
CC The plexin modulates the affinity of the complex for specific
CC semaphorins, and its cytoplasmic domain is required for the activation
CC of down-stream signaling events in the cytoplasm.
CC {ECO:0000269|PubMed:17475806, ECO:0000269|PubMed:17699603}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in primary motor neurons in the embryonic
CC nervous system. {ECO:0000269|PubMed:17475806}.
CC -!- SIMILARITY: Belongs to the plexin family. {ECO:0000305}.
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DR EMBL; EF538743; ABQ45399.1; -; mRNA.
DR EMBL; AB262187; BAF81998.1; -; mRNA.
DR EMBL; BX284684; CAQ14174.1; -; Genomic_DNA.
DR EMBL; BX284664; CAQ14174.1; JOINED; Genomic_DNA.
DR EMBL; CR847854; CAQ14174.1; JOINED; Genomic_DNA.
DR EMBL; BX284664; CAQ15628.1; -; Genomic_DNA.
DR EMBL; BX284684; CAQ15628.1; JOINED; Genomic_DNA.
DR EMBL; CR847854; CAQ15628.1; JOINED; Genomic_DNA.
DR EMBL; BC163880; AAI63880.1; -; mRNA.
DR RefSeq; NP_001091959.1; NM_001098489.1.
DR AlphaFoldDB; B0S5N4; -.
DR SMR; B0S5N4; -.
DR STRING; 7955.ENSDARP00000074151; -.
DR PaxDb; B0S5N4; -.
DR PeptideAtlas; B0S5N4; -.
DR PRIDE; B0S5N4; -.
DR GeneID; 567422; -.
DR KEGG; dre:567422; -.
DR CTD; 55558; -.
DR ZFIN; ZDB-GENE-070613-1; plxna3.
DR eggNOG; KOG3610; Eukaryota.
DR InParanoid; B0S5N4; -.
DR OrthoDB; 90434at2759; -.
DR PhylomeDB; B0S5N4; -.
DR TreeFam; TF312962; -.
DR Reactome; R-DRE-399954; Sema3A PAK dependent Axon repulsion.
DR Reactome; R-DRE-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
DR Reactome; R-DRE-399956; CRMPs in Sema3A signaling.
DR PRO; PR:B0S5N4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:ZFIN.
DR GO; GO:0002116; C:semaphorin receptor complex; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:ZFIN.
DR GO; GO:0017154; F:semaphorin receptor activity; IBA:GO_Central.
DR GO; GO:0048675; P:axon extension; IMP:ZFIN.
DR GO; GO:0048755; P:branching morphogenesis of a nerve; IMP:ZFIN.
DR GO; GO:0060272; P:embryonic skeletal joint morphogenesis; IMP:ZFIN.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:ZFIN.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IBA:GO_Central.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IBA:GO_Central.
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:0048696; P:regulation of collateral sprouting in absence of injury; IMP:ZFIN.
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; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Cell membrane; Coiled coil; Disulfide bond; Glycoprotein; Membrane;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1892
FT /note="Plexin A3"
FT /id="PRO_0000411106"
FT TOPO_DOM 21..1240
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1241..1261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1262..1892
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 21..509
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 861..955
FT /note="IPT/TIG 1"
FT DOMAIN 957..1041
FT /note="IPT/TIG 2"
FT DOMAIN 1044..1143
FT /note="IPT/TIG 3"
FT DOMAIN 1146..1232
FT /note="IPT/TIG 4"
FT COILED 1262..1315
FT /evidence="ECO:0000255"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 569
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 86..95
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 121..129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 283..404
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 299..355
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 373..392
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 512..529
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 518..560
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 521..538
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 532..544
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 595..615
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT CONFLICT 62
FT /note="V -> I (in Ref. 2; BAF81998)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="V -> A (in Ref. 1; ABQ45399)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="D -> E (in Ref. 2; BAF81998)"
FT /evidence="ECO:0000305"
FT CONFLICT 610
FT /note="E -> K (in Ref. 2; BAF81998 and 4; AAI63880)"
FT /evidence="ECO:0000305"
FT CONFLICT 672
FT /note="P -> S (in Ref. 1; ABQ45399 and 3; CAQ14174/
FT CAQ15628)"
FT /evidence="ECO:0000305"
FT CONFLICT 1176
FT /note="A -> V (in Ref. 4; AAI63880)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1892 AA; 211677 MW; D5B8CA0F386E723A CRC64;
MRSLWLLVFS FSVLTGTNMA FPMILSERPE VTGSFKVKDT SLTHLTVHRK TGEVFVGAIN
RVYKLSANLT ETRSHQTGPV EDNAKCYPPP SVRACTQKLE STDNVNKLLL VDYAGNRLVA
CGSIWQGVCQ FLRLEDLFKL GEPHHRKEHY LSGAKESDGM AGVVVGDDDG DLKKKKKGGS
RLFIGAAIDG KSEYFPTLSS RKLVADEESV NMFSLVYQDE FVSSQIKIPS DTLSQYPAFD
IYYVYGFSSR TYIYFLTLQL DTQLTQVDVT GEKFFTSKIV RMCSNDTEFY SYVEFPLGCT
KDGVEYRLVQ AAYKHRPGKI LAQALGLSED EDVLFVIFSQ GQKNRANPPR ETVLCLFTLH
QINLAMRERI KSCYRGEGKL SLPWLLNKEL PCINTPKQIG DDFCGLVLNQ PLGGLMVIEG
IPLFDDRTDG MASVAAYTYG DHSVVFVGTR SGHLKKIRVN GVPPPSENAL LYETVTVVEG
SPILRDMVFS PDYQYIYLLS DKQVSRLPVE SCSQYSSCKT CLGSGDPHCG WCVLHNKCSR
KEACEKWAEP LHFSTELKQC VDITVTPDNM SVTSVSTQLS VKVANVPNLS AGVTCVFEEL
TESPGEVLAE GQILCMSPSL RDVPSVTQGY GDKRVVKLSL KSKETGLKFI TTDFVFYNCS
VLQSCSSCVS SPFPCNWCKY RHICTNNVAE CSFQEGRVSS AEGCPQILPS SDILVPAGIV
RPITLRARNL PQPQSGQKNY ECVFNIQGKV QRIPAVRFNS SCIQCQNTSY WYEGNEMGDL
PVDFSIVWDG DFPIDKPSSM RALLYKCEAQ RDSCGLCLKA DSTFECGWCL ADKKCLLKQH
CPSAEHNWMH QGRRNIRCSH PRITKIRPLT GPKEGGTRVT IEGENLGLQV REITHVRVAG
VRCNPAAAEY ISAERIVCDM EESLMSSPPG GPVELCIGDC SAEYRTQSTQ TYSFVMPSFS
RVRPEKGPVS GGTRLTISGR HLDAGSAVTV FLAQEECLFV RRTVREIVCV TPPSASGSGP
SSVKLFIDKA EITSDTRYIY TEDPNISTIE PNWSIINGST SLTVTGTNLL TIQEPKVRAK
YGGVETTNIC SLVNDSVMTC LAPGIIYTKR EAPESGVHPD EFGFILDHVS ALLILNGTPF
TYYPNPTFEP LGNAGILEVK PGSPIILKGK NLIPPAPGNI RLNYSVTIGE TPCLLTVSES
QLLCDSPDLT GEQRVMILVG GLEYSPGMLH IYSDSTLTLP AIIGIGAGGG VLLIAIIAVL
IAYKRKTRDA DRTLKRLQLQ MDNLESRVAL ECKEAFAELQ TDIQELTNDM DGVKIPFLEY
RTYTMRVMFP GIEEHPVLKE LDSPANVEKA LRLFSQLLHN KMFLLTFIHT LEAQRSFSMR
DRGNVASLLM AALQGRMEYA TVVLKQLLAD LIEKNLENRN HPKLLLRRTE SVAEKMLTNW
FTFLLHRFLK ECAGEPLFML YCAIKQQMEK GPIDAITGEA RYSLSEDKLI RQQIDYKQLT
LMCIPPEGEA GTEIPVKVLN CDTITQVKDK LLDAVYKGIP YSQRPQADDM DLEWRQGRLT
RIILQDEDVT TKIESDWKRL NTLAHYQVTD GSLVALVQKQ VSAYNIANSF TFTRSLSRYE
SLLRTSSSPD SLRSRAPMIT PDQETGTKLW HLVKNHEHAD QREGDRGSKM VSEIYLTRLL
ATKGTLQKFV DDLFETVFST AHRGSALPLA IKYMFDFLDE QADKRQITDP DVRHTWKSNC
LPLRFWVNVI KNPQFVFDIH KNSITDACLS VVAQTFMDSC STSEHRLGKD SPSNKLLYAK
DIPNYKSWVE RYYRDISKMP SISDQDMDAY LVEQSRLHGN EFNTLSALSE LYFYINKYKE
EILTALDRDG YCRKHKLRHK LEQAINLMSG SS
