ID   PLX2_CAEBR              Reviewed;        1773 AA.
AC   Q626H5; A8WP68;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Plexin-2;
DE   Flags: Precursor;
GN   Name=plx-2; ORFNames=CBG00979;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
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. In early embryonic development, required for proper
CC       ventral closure of the epidermis. During male tail morphogenesis,
CC       involved in precursor cell sorting and in the formation of distinct
CC       sensory rays. Involved in axon guidance of SDQL neurons during
CC       neurogenesis. {ECO:0000250|UniProtKB:O45657}.
CC   -!- SUBUNIT: Interacts with mab-20. {ECO:0000250|UniProtKB:O45657}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the plexin family. {ECO:0000305}.
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DR   EMBL; HE600951; CAP22274.4; -; Genomic_DNA.
DR   RefSeq; XP_002629745.1; XM_002629699.1.
DR   AlphaFoldDB; Q626H5; -.
DR   SMR; Q626H5; -.
DR   STRING; 6238.CBG00979; -.
DR   GeneID; 8572989; -.
DR   KEGG; cbr:CBG_00979; -.
DR   CTD; 8572989; -.
DR   WormBase; CBG00979; CBP41590; WBGene00024280; Cbr-plx-2.
DR   eggNOG; KOG3610; Eukaryota.
DR   HOGENOM; CLU_001436_1_1_1; -.
DR   InParanoid; Q626H5; -.
DR   OMA; NFSYCTE; -.
DR   OrthoDB; 90434at2759; -.
DR   Proteomes; UP000008549; Chromosome II.
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: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: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   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; -; 3.
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; 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; 2.
DR   Pfam; PF08337; Plexin_cytopl; 1.
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   3: Inferred from homology;
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..1773
FT                   /note="Plexin-2"
FT                   /id="PRO_0000248552"
FT   TOPO_DOM        20..1130
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1131..1151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1152..1764
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          20..436
FT                   /note="Sema"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DOMAIN          438..480
FT                   /note="PSI 1"
FT   DOMAIN          571..608
FT                   /note="PSI 2"
FT   DOMAIN          698..739
FT                   /note="PSI 3"
FT   DOMAIN          741..829
FT                   /note="IPT/TIG 1"
FT   DOMAIN          831..916
FT                   /note="IPT/TIG 2"
FT   DOMAIN          919..1006
FT                   /note="IPT/TIG 3"
FT   COILED          1150..1188
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        65
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        241
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        494
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        566
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        670
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        693
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        855
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        877
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        975
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1007
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        83..90
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        117..125
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        239..341
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        255..292
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        310..328
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        439..456
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        445..479
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        448..465
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        459..471
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        516..538
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
SQ   SEQUENCE   1773 AA;  194786 MW;  D7A4E239194DA8E8 CRC64;
     MLFIESAFLV LTSLSAAEAA TPFEGGVKQK VFHSAGHIDD FIVSRDQQTI YIASINRITS
     LHSSNLSIQN EVSIGPVQDS PWCSADGKSC LKDNRPFSTD VHTKILQILP SGQLLQCGSV
     KLGSCSTFNS KLSLITEAST PVAANSPDAS TVSQIIDNRL VVAASPTKES PGCNPNLPGL
     NVENAGDLEG EAAVYLRAAY RSSFRFVTTF SHQHFIFVVA TVTPRETRLP VTTRLIRFCK
     NDTKFVSYSE IELQCRGEDN TNYPFLTAVV QTGDKLIASF SASPTSSKNS ICVFSMQKVK
     LTFWYNVDRC RSGTDSIKLS HIGRDTKCVN KAHIPLDEDS CELGVGGSIE LVEMSTIDVL
     AKVTSLMAVD QKALFAGTSS SQIVMLKWDE QNSNKLEEYG RKEIGDGRTG SEVVKMTRFG
     DFILVQMPYG IVMEELSTCA HHESCTDCQV SVDPLCQWCH PTQSCTTSSR CSGPLTTQCP
     IVDGDPIPSM VSVNSSTSIS FNIHHLPPPV GFVYKCYFGS KSHSKSTKAT WTASGISCPS
     EMFGSPKTFE ISLMTSISKN PISRHNFTVF DCAGYSTCST CMSSEFGCQW CSHKCSSSCG
     SASAKACVKI QPMKVPIAIG SQQEIVLEAL NLDTLDRKTE HFCKVNGQVA PAKIASDSIR
     CGKIQLAGSN ETNANMVVPL SLMANDVVVD IANVSLYSCS NLAADCSSCL ALSPSLSCGW
     CNRKCSHECH ESKATAVCDP PKIDRFEPSS GPVEGGTVIK VYGNDLGMSV EDVRGKIYVA
     GSRCNIVEYQ VSNMIACQVD KGVSSGPIKI SVGRATMAVA ESSDLFSFVR VSIFSAYPLY
     GPISGGTRIT LYGQNLSSGS RISVTVGGLP CPIERINSST VLTCLTPSGS SIGKSAKVVV
     HVDHSQIQLD QPFEYRSDPS VNSIFPLSSF KAGGRIVSVQ GSSFNTVQSA RMFLISSPTP
     PFEIISDLAP CHIINSTLMT CMTPKILETI TRRVEYTRQP VGFLMDNVTA VANLGRRIQM
     SVYPNPSLSP FKGIRYHQGE QSLILEGHNL NLAAEPNDFK IFVGSERCYV TLVDVRQLVC
     SGPLKQPKPT DERGVPINGD NPLVTVIVGS LRMELGLIEY SDHALPSRLS FLILGLLLFT
     VITLIVMCLI FKRRRQEREK EYRKIQLQME NLENNVRKEC KQAFAELQTN LVLSPKSTGT
     ITSPELIHFP HFVENLLWAD QNLTSAPSLA RTLPVTLAQF HALLSFKGFI FTIVEAAESD
     VSISTSEKST LASLLISVLL RNFSYCTEIV VDLLKAHIAR SVQAKRAELL FRNSDSVVEK
     MFSKWMSICL YSHLTPQMNS YFYLYKALQY QTDKGPVDAV TGDARYTINE AKLLRESVET
     KTLKIHIVPF EKCDETTHLE VHACDAICQL KQKVASAVYK ETPYSQRPRI TQFELKLKCA
     KRGDIKLTDV SAVETLSQKK LPVKLLTLAD YGIQDGATLE MTSAVYTAES YRNSLADSGQ
     SSWSSLDRCS PIYSSSKYYH LTNPSSGTMT FKKRTSPSEI PKSIPEVYLT RLLTSKGTVE
     TYVEDFLESV LYMHDSSYPP ILKFFFDILD REASINGVSE NICQQWKANG YVLRMWTNFV
     KNPQLVFDVP HSVSMDANLS TVAQTMMDCF SFSEPVLGAH SPSSRLLFAK DVARLRPLSV
     DLFKRVKNSP PLGMEELRTE LVNMANDVST CKGSSLALSE LLSWVRGNGI RISQLLSSNQ
     ETSQQRLPQK LSQVLHVCLE TDNHIYSTIS DYD