PLXA4_DANRE
ID PLXA4_DANRE Reviewed; 1903 AA.
AC Q6BEA0; Q5RHC7;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Plexin-A4;
DE Flags: Precursor;
GN Name=plxna4;
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 DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=15229183; DOI=10.1242/dev.01228;
RA Miyashita T., Yeo S.-Y., Hirate Y., Segawa H., Wada H., Little M.H.,
RA Yamada T., Takahashi N., Okamoto H.;
RT "PlexinA4 is necessary as a downstream target of Islet2 to mediate Slit
RT signaling for promotion of sensory axon branching.";
RL Development 131:3705-3715(2004).
RN [2]
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).
CC -!- FUNCTION: Involved in the development of primary sensory neurons
CC especially in branching of the peripheral axons. Interacts with the
CC SLIT2 signaling specifically to promote axonal branching of Rohon-Beard
CC neurons and the trigeminal sensory ganglion neurons.
CC {ECO:0000269|PubMed:15229183}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: In the embryonic brain expressed in specific
CC subtypes of neurons. Found in the tectal region, hindbrain, neurons in
CC the nucleus of the anterior commissure, posterior commissure, postoptic
CC commissure, medial lateral fascile and epiphysis. Localized to both
CC central and peripheral axons of the primary sensory neurons.
CC {ECO:0000269|PubMed:15229183}.
CC -!- SIMILARITY: Belongs to the plexin family. {ECO:0000305}.
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DR EMBL; AB103158; BAD35133.1; -; mRNA.
DR EMBL; BX537358; CAI21292.1; -; Genomic_DNA.
DR EMBL; BX649446; CAI21292.1; JOINED; Genomic_DNA.
DR EMBL; BX649446; CAK10809.1; -; Genomic_DNA.
DR EMBL; BX537358; CAK10809.1; JOINED; Genomic_DNA.
DR RefSeq; NP_001004495.1; NM_001004495.1.
DR AlphaFoldDB; Q6BEA0; -.
DR SMR; Q6BEA0; -.
DR STRING; 7955.ENSDARP00000021195; -.
DR PaxDb; Q6BEA0; -.
DR GeneID; 325938; -.
DR KEGG; dre:325938; -.
DR CTD; 91584; -.
DR ZFIN; ZDB-GENE-030131-4663; plxna4.
DR eggNOG; KOG3610; Eukaryota.
DR InParanoid; Q6BEA0; -.
DR OrthoDB; 90434at2759; -.
DR PhylomeDB; Q6BEA0; -.
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:Q6BEA0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; ISS:ZFIN.
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; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IGI:ZFIN.
DR GO; GO:0007414; P:axonal defasciculation; IGI:ZFIN.
DR GO; GO:0001763; P:morphogenesis of a branching structure; 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: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; -; 1.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 4.
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; Developmental protein; Disulfide bond; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..1903
FT /note="Plexin-A4"
FT /id="PRO_0000240285"
FT TOPO_DOM 27..1246
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1247..1267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1268..1903
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..515
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 517..567
FT /note="PSI 1"
FT DOMAIN 663..710
FT /note="PSI 2"
FT DOMAIN 811..864
FT /note="PSI 3"
FT DOMAIN 866..960
FT /note="IPT/TIG 1"
FT DOMAIN 962..1046
FT /note="IPT/TIG 2"
FT DOMAIN 1049..1148
FT /note="IPT/TIG 3"
FT DOMAIN 1151..1246
FT /note="IPT/TIG 4"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 575
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 600
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 656
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 663
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 764
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 772
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 981
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 992
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1025
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 97..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 132..140
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 291..413
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 307..364
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 382..401
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 518..535
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 524..566
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 527..544
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 538..550
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 601..620
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT CONFLICT 974
FT /note="I -> V (in Ref. 2; CAI21292/CAK10809)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1903 AA; 213792 MW; 2345B10968071612 CRC64;
MAFHNRRWNF TFSCCVVVLL LPLVAARPQQ PSAATRVHEE YSTFRVENTE WTFNHLAVDH
RNGNVYLGAV NRIYKLSPGL DIQVSHQTGP DEDNRNCYPP RIVQPCSEPL TLTNNVNKML
LMDYRENRLL ACGSLYQGIC KLLRLDDLFK LGEPFHKKEH YLSGVNESGS VFGVIVSYGD
ASPDKLFVAT AVDGRPEYFP TISSRKLTRN SEEDGMFAYV FHDEFVASMI KIPSDTFTVV
PDFDIYYVYG FSSGNFVYFL TLQPEMGGGP TTGSSSAGRE QVYTSKLVRL CKDDTAFNSY
VEVPLGCVKG GVEYRLLQAA YLSKAGTILA RSLGIGPDDD ILYAVFSKGQ KRRPKESSQE
SALCVFTLKE INERIKDRLQ SCYKGEGTLD LAWLKVKDIS CSSALLTIDD NFCGLDMNAP
LGVSEMVRGI PLFSESKDKM TSVIAYVYKN HSLAFVGTRG GRLKKIRVDG PTYGALQYET
IQVVDNGPIL RDMAFSSDQH FLYVMSESQL TRVPVEACEQ YSSCNECLGS GDPHCGWCVL
HSMCTRKEKC ERSSEPRRFA SNIKQCVRLS VHPNNISVSQ YSVMLVLEAH NVPELSAGVN
CTFEDLAEMD GLVEGNRITC SSPAEKEVPR IIVDQGDHQI VQLYLKSKET GLAFANTSFV
FYNCSVHKSC LSCVGSPYQC HWCKYRHTCT HDPSSCSFQE GRVKQPEECP QLLPADRILV
PVNVVKPITL RAKNLPQPQS GQRGYECVLT IQGVEQRVPA LRFNSSSVQC QNTSYMYDGM
EMSSLPVDLT VIWNGDFSID NPAQNKVHLY KCDARRESCG LCLKADPLFG CVWCKGENRC
SLKQHCSYPQ SMWLEHNGIN SKCTHPRITK ITPLRGPREG GTLVTIRGEN LGLEFSEIKD
HVKVADVECT PVPEGYIPAE QIVCEMGKAE RSQFAGNVQV CVGECRPEFM AKSSKYYYFV
IPQLLSLKPS RGPISGGTIV NITGGNLDAG SNVSIMFKDQ KCTYQRRGGQ WITCRSHASM
QGYGNVSVSV YVDKAHIHKD LKFEYVEDPT ITKLEPEWSI FSGNTPLTVS GTNLDIIHTP
LIRAKYKNLE TINICQVLSP TTMQCMAPEL PYSISKHKDV PERPDEFGFI LDNVQSVLAL
NNTNFVYYPN PVFEPLSVSG VQELKPGSPI ILKGRNFLPP TPGGNGKLNY TVLIGDKPCA
LTVSDTQLLC ESPNLTGRHK VLARVGGIEF SPGVVHITSD SPLSSTAVIS IAGAGGLLIF
FIVIVLIAYK RKSRESDLTL KRLQMQMDNL ESRVALECKE AFAELQTDIH ELTSDLDGAG
IPFLDYRTYT MRVLFPGIEE HPVLRDLEVP GYRQEQVEKG LKLFGQLINN KVFLLSFIRT
LESQRGFSMR DRGNVASLIM TVLQSKLEYA TDVLKHLLSD LIDKNLESKN HPKLLLRRTE
SVAEKMLTNW FTFLLYKFLK ECAGEPLFSL FCAIKQQMEK GPIDSITGEA RYSLSEDKLI
RQQIDYKTLV VNCMHPDNEK SPEVQVKVLN CDTVSQVKEK ILDAIYKNVP YSHRPKASDM
DLEWRQGRVV RVILQDEDVT TKIEADWKRL NMLSHYQVTD NAVVALVPKQ VTAYNSVNNS
TVSRTSASKY ENMIKYTGSP DSLRSRTPMI TPDLESGVKV WHLVKNHEHG DQKEGDRGSK
MVSEIYLTRL LATKGTLQKF VDDLFETIFS TAHRGSALPL AIKYMFDFLD EQADKHNIHD
PHVRHTWKSN CLPLRFWVNV IKNPQFVFDI HKSSITDACL SVVAQTFMDS CSTSEHRLGK
DSPSNKLLYA KDIPSYKSWV ERYYSDISKM PAISDQDMNA YLAEQSRMHM NEFNTMSSLS
EIYSYIGKYT EEIVSALEQD DGARKQRLAY KLEQVVAFMS LES
