PLX2_CAEEL
ID PLX2_CAEEL Reviewed; 1766 AA.
AC O45657; Q6BCZ2;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 4.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Plexin-2;
DE Flags: Precursor;
GN Name=plx-2; ORFNames=K04B12.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Nakao F., Kurokawa R., Liu Z., Gengyo-Ando K., Fujii T., Nukazuka A.,
RA Suto F., Shibata Y., Shioi G., Mitani S., Fujisawa H., Takagi S.;
RT "PLX-2, a Caenorhabditis elegans plexin, participates in mediating the
RT signal of a class 2 semaphorin MAB-20.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH MAB-20.
RX PubMed=15030761; DOI=10.1016/s1534-5807(04)00057-7;
RA Ikegami R., Zheng H., Ong S.-H., Culotti J.G.;
RT "Integration of semaphorin-2A/MAB-20, ephrin-4, and UNC-129 TGF-beta
RT signaling pathways regulates sorting of distinct sensory rays in C.
RT elegans.";
RL Dev. Cell 6:383-395(2004).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH MAB-20.
RX PubMed=17507686; DOI=10.1534/genetics.106.067116;
RA Nakao F., Hudson M.L., Suzuki M., Peckler Z., Kurokawa R., Liu Z.,
RA Gengyo-Ando K., Nukazuka A., Fujii T., Suto F., Shibata Y., Shioi G.,
RA Fujisawa H., Mitani S., Chisholm A.D., Takagi S.;
RT "The plexin PLX-2 and the ephrin EFN-4 have distinct roles in MAB-
RT 20/semaphorin 2A signaling in Caenorhabditis elegans morphogenesis.";
RL Genetics 176:1591-1607(2007).
RN [5]
RP FUNCTION.
RX PubMed=25358863; DOI=10.1038/ncomms6325;
RA Nakamura F., Kumeta K., Hida T., Isono T., Nakayama Y.,
RA Kuramata-Matsuoka E., Yamashita N., Uchida Y., Ogura K., Gengyo-Ando K.,
RA Mitani S., Ogino T., Goshima Y.;
RT "Amino- and carboxyl-terminal domains of Filamin-A interact with CRMP1 to
RT mediate Sema3A signalling.";
RL Nat. Commun. 5:5325-5325(2014).
RN [6]
RP FUNCTION.
RX PubMed=26903502; DOI=10.1242/dev.128934;
RA Dong B., Moseley-Alldredge M., Schwieterman A.A., Donelson C.J.,
RA McMurry J.L., Hudson M.L., Chen L.;
RT "EFN-4 functions in LAD-2-mediated axon guidance in Caenorhabditis
RT elegans.";
RL Development 143:1182-1191(2016).
CC -!- FUNCTION: Involved as a receptor for mab-20/sema-2a in the formation or
CC stabilization of cell-cell contacts at several stages of epithelial
CC morphogenesis (PubMed:17507686). In early embryonic development,
CC required for proper ventral closure of the epidermis (PubMed:17507686).
CC During male tail morphogenesis, involved in precursor cell sorting and
CC in the formation of distinct sensory rays (PubMed:15030761). Involved
CC in axon guidance of SDQL neurons during neurogenesis (PubMed:26903502).
CC Probably in response to stimulation by mab-20, regulates fln-1-mediated
CC remodeling of the actin cytoskeleton and thus axon guidance and/or
CC fasciculation of DD/VD neurons (PubMed:25358863).
CC {ECO:0000269|PubMed:15030761, ECO:0000269|PubMed:17507686,
CC ECO:0000269|PubMed:25358863, ECO:0000269|PubMed:26903502}.
CC -!- SUBUNIT: Interacts with mab-20. {ECO:0000269|PubMed:15030761,
CC ECO:0000269|PubMed:17507686}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the central nervous
CC system from embryonic to adult stages. Expressed in early embryos in
CC ventral neuroblasts. Expressed in neurons and in a subset of posterior
CC lateral and ventral epidermal cells following epidermal enclosure.
CC Present in neurons, muscles and weakly expressed in epidermal cells of
CC the larval tail. {ECO:0000269|PubMed:15030761,
CC ECO:0000269|PubMed:17507686}.
CC -!- SIMILARITY: Belongs to the plexin family. {ECO:0000305}.
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DR EMBL; AB162421; BAD36749.1; -; mRNA.
DR EMBL; BX284602; CAB05755.4; -; Genomic_DNA.
DR PIR; T23298; T23298.
DR RefSeq; NP_497001.4; NM_064600.5.
DR AlphaFoldDB; O45657; -.
DR SMR; O45657; -.
DR BioGRID; 40382; 3.
DR STRING; 6239.K04B12.1; -.
DR EPD; O45657; -.
DR PaxDb; O45657; -.
DR EnsemblMetazoa; K04B12.1.1; K04B12.1.1; WBGene00004048.
DR UCSC; K04B12.1; c. elegans.
DR WormBase; K04B12.1; CE41510; WBGene00004048; plx-2.
DR eggNOG; KOG3610; Eukaryota.
DR GeneTree; ENSGT01020000230394; -.
DR HOGENOM; CLU_001436_1_1_1; -.
DR InParanoid; O45657; -.
DR OMA; NFSYCTE; -.
DR OrthoDB; 90434at2759; -.
DR PhylomeDB; O45657; -.
DR Reactome; R-CEL-399954; Sema3A PAK dependent Axon repulsion.
DR Reactome; R-CEL-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
DR Reactome; R-CEL-399956; CRMPs in Sema3A signaling.
DR Reactome; R-CEL-416482; G alpha (12/13) signalling events.
DR Reactome; R-CEL-416550; Sema4D mediated inhibition of cell attachment and migration.
DR Reactome; R-CEL-416572; Sema4D induced cell migration and growth-cone collapse.
DR Reactome; R-CEL-416700; Other semaphorin interactions.
DR Reactome; R-CEL-9013405; RHOD GTPase cycle.
DR PRO; PR:O45657; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00004048; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0031252; C:cell leading edge; IDA:WormBase.
DR GO; GO:0009986; C:cell surface; IDA:WormBase.
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; IPI:WormBase.
DR GO; GO:0007413; P:axonal fasciculation; IMP:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IGI:WormBase.
DR GO; GO:0008045; P:motor neuron axon guidance; IBA:GO_Central.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IBA:GO_Central.
DR GO; GO:0002119; P:nematode larval development; IGI:WormBase.
DR GO; GO:0045138; P:nematode male tail tip morphogenesis; IGI:WormBase.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IBA:GO_Central.
DR GO; GO:1902667; P:regulation of axon guidance; IMP:UniProtKB.
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:0071526; P:semaphorin-plexin signaling pathway; IC:WormBase.
DR GO; GO:1902287; P:semaphorin-plexin signaling pathway involved in axon guidance; IBA:GO_Central.
DR GO; GO:0097374; P:sensory neuron 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; -; 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; 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; 3.
DR SMART; SM00429; IPT; 3.
DR SMART; SM00423; PSI; 3.
DR SMART; SM00630; Sema; 1.
DR SUPFAM; SSF101912; SSF101912; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF81296; SSF81296; 3.
DR PROSITE; PS51004; SEMA; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Developmental protein; Differentiation;
KW Disulfide bond; Glycoprotein; Membrane; Neurogenesis; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1766
FT /note="Plexin-2"
FT /id="PRO_0000248553"
FT TOPO_DOM 20..1120
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1121..1141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1142..1766
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 21..444
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 446..488
FT /note="PSI 1"
FT DOMAIN 577..617
FT /note="PSI 2"
FT DOMAIN 707..748
FT /note="PSI 3"
FT DOMAIN 750..837
FT /note="IPT/TIG 1"
FT DOMAIN 840..924
FT /note="IPT/TIG 2"
FT DOMAIN 928..1021
FT /note="IPT/TIG 3"
FT COILED 1140..1178
FT /evidence="ECO:0000255"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 502
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 572
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 679
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 702
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 864
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 886
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 984
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 84..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 118..126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 247..349
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 263..300
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 318..336
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 447..464
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 453..487
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 456..473
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 467..479
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 524..544
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
SQ SEQUENCE 1766 AA; 195780 MW; 0B2CDD3EE9EA589C CRC64;
MLPESVFLLL ISHFLRAVTQ PPFETEGVKQ KLFHFSGHID DFIVSRDQQT IYVASLNRLT
SLSISNFSIQ HEVSLGPVQD SPWCSADGKS CLKDNRPFPT DVRTKILQIL PTNQILQCGS
VKLGSCSTFN SKLSLITEST IAVAANSPDA STVSKIIDNR LIVAASATKE SPYRDPFPAV
AIRNLPGLNV ENAGDLEGEA AVFLRAAYKN AFKFLYTFTH QHFVFVVAMV TPRESRLPMT
TRLIRFCRND TKFESYSEIE LQCRGEDNTN YPFLNAIIQS YDKLIASFST SSTSPKSSIC
VFSMQKVKLT FWYNVDRCRS GTDSIRLPHI GRDTKCVNKA HIPLDEDSCE LGVGGSIELV
EMSTKDIMGK VTSLMAVDQK AIFAGTTTSQ IVMFKWDEHH SNQLEEYGRK EVGDGRTGSE
VSKMVKFGDF VIVQMPYGII LEELSTCSHH SSCTECLVSV DPLCQWCHPT QSCTTSARCT
SPVTSQCPIV DGDPIPSIVS VNSSTPISFN IHHLPPPVGF TYRCQFGTST SSIKANWTTT
GVSCPSEIFT SPNTFEILLL TSISNNPISR HNFTVYDCSG YGTCSSCMSS EYNCAWCSGL
HKCSNSCGAL EKSKACVKIQ PMRLPIAIGS QQEIVLEASN LDTLDRRHEH FCKVNEQVSL
AKIASDSIRC GKIQLTLSNT TSANMVVPLS LITRDSVIDI ANVSLYSCTN LASDCSSCLA
LSPSLSCGWC NRQCSHECHE SKATAVCDPP RIDKFEPTSG PIEGGTIIKI YGNDLGMSVE
DVRGKIYVAG SRCNIVEYHV SNMIACQVDK GVSSGPIRIS VGRATVAVAE SSELYSFVRT
SIFSAYPLYG PISGGTRITL YGQNLSSGSQ TSVTVGGMPC PIERVNSSTV LTCLTPSGTR
IGKSARVVVH VDHSQTQLDQ PFEYRSDPSI SSIFPMTSFK AGGRIVYVQG NSLNTVQTAK
LFLISSPTPP FYIISDLAPC HIINSTLMTC MTPKILETIT RRVEYTRQPM GIYPNPTLSP
FKGVRYHQGE QSLILEGHNL NLAAEPNDFK IFIGNERCYV TLVDVRQLVC SGPVRQPKAT
DERGIPINGD NPLVTVIVGS LRMELGLIEY SDHALPSRLS LLILGLLLFI VVTLTVMCLV
FKRRRQEREK EYRKIQLQME NLENNVRKEC KQAFAELQTN LVLSPKSANS VNLGPELINF
PHFVENLLWS DNNLTSAPSL ARTLPVTLAQ FHALLSFKGF IFTIVEAAES DVSISTSEKS
MLASLLISVL LRNFSYCTEV VVDLLRAHIA RSVQNKRAEL LFRNSDSVVE KMFSKWMSIC
LYSHLTPQMN SYFYLYKALQ YQTDKGPVDA VTGDARYTIN EAKLLRESVD TKTLKIRVIP
FEKCDESIDL EVHACDAICQ VKQKVASAVY RETPYSQRPR ITQFELKYKC PKRGDVKLTD
VLPIETLSQK KLPVKLFTLA DYGISDGCTL EMSPAVYTAE SYRNSLADSG QSSWSSLDRC
SPIYSSSKYY HLTNPSSGTM TFKKKSSNDS NLLPKSIPEV YLTRLLTSKG TVETYVEDFL
ESVLYMHDSS YPPILKFFFD ILDREASVNG VSENICQQWK ANGYVLRVWA NFVRNPQLVF
DVPHSISMDA NLSTVAQTMM DCFSFSEPVL GAHSPSSRLL FAKDVARLRP LSVDLFKRVK
NSPPLGMDEL RTELVNMAND VSTCKGSSLA LSELLSWVRG NGIRISQLLS SNEQFSQQRL
PQKLSQVLHV CLETDNHIYS TISDYE
