ID   PLXA3_MOUSE             Reviewed;        1872 AA.
AC   P70208; A5D6Q5; Q684J0; Q8BWZ5;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 160.
DE   RecName: Full=Plexin-A3;
DE   Flags: Precursor;
GN   Name=Plxna3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   TISSUE=Embryonic brain;
RX   PubMed=8806646; DOI=10.1006/bbrc.1996.1367;
RA   Kameyama T., Murakami Y., Suto F., Kawakami A., Takagi S., Hirata T.,
RA   Fujisawa H.;
RT   "Identification of plexin family molecules in mice.";
RL   Biochem. Biophys. Res. Commun. 226:396-402(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1116-1560.
RC   STRAIN=NMRI; TISSUE=Embryo;
RA   Kolb-Kokocinski A.A., Mehrle A., Bechtel S., Wellenreuther R., Simpson J.,
RA   Pepperkok R., Wiemann S., Poustka A.;
RT   "Towards functional annotation of all Xq28 genes: expression and
RT   intracellular localization analyses reveal novel candidates for disease
RT   genes.";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1138-1872.
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=11683995; DOI=10.1016/s0896-6273(01)00478-0;
RA   Cheng H.J., Bagri A., Yaron A., Stein E., Pleasure S.J.,
RA   Tessier-Lavigne M.;
RT   "Plexin-A3 mediates semaphorin signaling and regulates the development of
RT   hippocampal axonal projections.";
RL   Neuron 32:249-263(2001).
RN   [6]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=18262512; DOI=10.1016/j.ydbio.2008.01.002;
RA   Waimey K.E., Huang P.H., Chen M., Cheng H.J.;
RT   "Plexin-A3 and plexin-A4 restrict the migration of sympathetic neurons but
RT   not their neural crest precursors.";
RL   Dev. Biol. 315:448-458(2008).
RN   [7]
RP   DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=18804103; DOI=10.1016/j.ydbio.2008.08.020;
RA   Schwarz Q., Waimey K.E., Golding M., Takamatsu H., Kumanogoh A.,
RA   Fujisawa H., Cheng H.J., Ruhrberg C.;
RT   "Plexin A3 and plexin A4 convey semaphorin signals during facial nerve
RT   development.";
RL   Dev. Biol. 324:1-9(2008).
RN   [8]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=19020035; DOI=10.1523/jneurosci.3573-08.2008;
RA   Ben-Zvi A., Manor O., Schachner M., Yaron A., Tessier-Lavigne M., Behar O.;
RT   "The Semaphorin receptor PlexinA3 mediates neuronal apoptosis during dorsal
RT   root ganglia development.";
RL   J. Neurosci. 28:12427-12432(2008).
RN   [9]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=20010807; DOI=10.1038/nature08628;
RA   Tran T.S., Rubio M.E., Clem R.L., Johnson D., Case L., Tessier-Lavigne M.,
RA   Huganir R.L., Ginty D.D., Kolodkin A.L.;
RT   "Secreted semaphorins control spine distribution and morphogenesis in the
RT   postnatal CNS.";
RL   Nature 462:1065-1069(2009).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 1170-1795, FUNCTION, AND
RP   MUTAGENESIS OF LEU-1279; TYR-1300; PHE-1309; 1407-ARG-ARG-1408; ILE-1453;
RP   LEU-1464; GLN-1506 AND 1631-HIS-HIS-1632.
RX   PubMed=19717441; DOI=10.1073/pnas.0906923106;
RA   He H., Yang T., Terman J.R., Zhang X.;
RT   "Crystal structure of the plexin A3 intracellular region reveals an
RT   autoinhibited conformation through active site sequestration.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:15610-15615(2009).
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. {ECO:0000269|PubMed:11683995,
CC       ECO:0000269|PubMed:18262512, ECO:0000269|PubMed:18804103,
CC       ECO:0000269|PubMed:19020035, ECO:0000269|PubMed:19717441,
CC       ECO:0000269|PubMed:20010807}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P70208-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P70208-2; Sequence=VSP_041609;
CC   -!- TISSUE SPECIFICITY: Detected in embryonic hindbrain, spinal cord,
CC       dorsal root ganglion, trigeminal ganglion and superior cervical
CC       ganglion. In newborns, detected throughout all layers of the
CC       hippocampus. {ECO:0000269|PubMed:11683995, ECO:0000269|PubMed:18804103,
CC       ECO:0000269|PubMed:8806646}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype, but causes subtle changes
CC       in the central nervous system. Mice exhibit altered apical dendrite
CC       spine morphology in pyramidal neurons. Mice exhibit defasciculation of
CC       the facial branchiomotor nerve and of the ophthalmic branch of the
CC       trigeminus, with variable severity. The number of neurons in the dorsal
CC       root ganglion is higher than normal, probably due to reduced neuronal
CC       apoptosis. In mice lacking both Plxna3 and Plxna4, migrating neurons do
CC       not show the normal response to Sema3A and Sema3F and do not migrate
CC       away from these semaphorins (in vitro). {ECO:0000269|PubMed:11683995,
CC       ECO:0000269|PubMed:18262512, ECO:0000269|PubMed:18804103,
CC       ECO:0000269|PubMed:19020035, ECO:0000269|PubMed:20010807}.
CC   -!- SIMILARITY: Belongs to the plexin family. {ECO:0000305}.
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DR   EMBL; D86950; BAA13190.1; -; mRNA.
DR   EMBL; BC093482; AAH93482.1; -; mRNA.
DR   EMBL; AJ748653; CAG38687.1; -; mRNA.
DR   EMBL; AK049319; BAC33681.1; -; mRNA.
DR   CCDS; CCDS30228.1; -. [P70208-1]
DR   PIR; JC4976; JC4976.
DR   RefSeq; NP_032909.2; NM_008883.2. [P70208-1]
DR   RefSeq; XP_006527963.1; XM_006527900.2.
DR   PDB; 3IG3; X-ray; 1.99 A; A=1247-1872.
DR   PDBsum; 3IG3; -.
DR   AlphaFoldDB; P70208; -.
DR   SMR; P70208; -.
DR   BioGRID; 202263; 4.
DR   DIP; DIP-48959N; -.
DR   STRING; 10090.ENSMUSP00000004326; -.
DR   GlyConnect; 2591; 1 N-Linked glycan (1 site).
DR   GlyCosmos; P70208; 4 sites, 1 glycan.
DR   GlyGen; P70208; 5 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; P70208; -.
DR   PhosphoSitePlus; P70208; -.
DR   MaxQB; P70208; -.
DR   PaxDb; 10090-ENSMUSP00000004326; -.
DR   PeptideAtlas; P70208; -.
DR   ProteomicsDB; 289630; -. [P70208-1]
DR   ProteomicsDB; 289631; -. [P70208-2]
DR   Pumba; P70208; -.
DR   Antibodypedia; 31267; 90 antibodies from 18 providers.
DR   DNASU; 18846; -.
DR   Ensembl; ENSMUST00000004326.4; ENSMUSP00000004326.4; ENSMUSG00000031398.14. [P70208-1]
DR   GeneID; 18846; -.
DR   KEGG; mmu:18846; -.
DR   UCSC; uc009too.1; mouse. [P70208-1]
DR   UCSC; uc012hku.1; mouse. [P70208-2]
DR   AGR; MGI:107683; -.
DR   CTD; 55558; -.
DR   MGI; MGI:107683; Plxna3.
DR   VEuPathDB; HostDB:ENSMUSG00000031398; -.
DR   eggNOG; KOG3610; Eukaryota.
DR   GeneTree; ENSGT01050000244850; -.
DR   HOGENOM; CLU_001436_2_0_1; -.
DR   InParanoid; P70208; -.
DR   OMA; CTHRLAP; -.
DR   OrthoDB; 1387371at2759; -.
DR   PhylomeDB; P70208; -.
DR   TreeFam; TF312962; -.
DR   Reactome; R-MMU-399954; Sema3A PAK dependent Axon repulsion.
DR   Reactome; R-MMU-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
DR   Reactome; R-MMU-399956; CRMPs in Sema3A signaling.
DR   BioGRID-ORCS; 18846; 2 hits in 77 CRISPR screens.
DR   ChiTaRS; Plxna3; mouse.
DR   EvolutionaryTrace; P70208; -.
DR   PRO; PR:P70208; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; P70208; Protein.
DR   Bgee; ENSMUSG00000031398; Expressed in cortical plate and 270 other cell types or tissues.
DR   ExpressionAtlas; P70208; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0002116; C:semaphorin receptor complex; IBA:GO_Central.
DR   GO; GO:0017154; F:semaphorin receptor activity; IMP:UniProtKB.
DR   GO; GO:0048846; P:axon extension involved in axon guidance; IGI:MGI.
DR   GO; GO:0007411; P:axon guidance; IMP:MGI.
DR   GO; GO:0021785; P:branchiomotor neuron axon guidance; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0021612; P:facial nerve structural organization; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0021828; P:gonadotrophin-releasing hormone neuronal migration to the hypothalamus; IGI:ARUK-UCL.
DR   GO; GO:0021766; P:hippocampus development; IMP:MGI.
DR   GO; GO:0050919; P:negative chemotaxis; IGI:MGI.
DR   GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; IGI:MGI.
DR   GO; GO:0007162; P:negative regulation of cell adhesion; IBA:GO_Central.
DR   GO; GO:1990138; P:neuron projection extension; IGI:MGI.
DR   GO; GO:0097485; P:neuron projection guidance; IMP:MGI.
DR   GO; GO:0021628; P:olfactory nerve formation; IGI:ARUK-UCL.
DR   GO; GO:0050772; P:positive regulation of axonogenesis; IBA:GO_Central.
DR   GO; GO:0051495; P:positive regulation of cytoskeleton organization; IMP:UniProtKB.
DR   GO; GO:0021860; P:pyramidal neuron development; IMP:MGI.
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:0071526; P:semaphorin-plexin signaling pathway; IMP:ParkinsonsUK-UCL.
DR   GO; GO:1902287; P:semaphorin-plexin signaling pathway involved in axon guidance; IBA:GO_Central.
DR   GO; GO:0021637; P:trigeminal nerve structural organization; IMP:ParkinsonsUK-UCL.
DR   CDD; cd00603; IPT_PCSR; 1.
DR   CDD; cd01180; IPT_plexin_repeat1; 1.
DR   CDD; cd01179; IPT_plexin_repeat2; 1.
DR   CDD; cd01181; IPT_plexin_repeat3; 1.
DR   CDD; cd12790; RasGAP_plexin_A; 1.
DR   CDD; cd11273; Sema_plexin_A3; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 5.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
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; IPR046800; Plexin_RBD.
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; PLEXIN; 1.
DR   PANTHER; PTHR22625:SF32; PLEXIN-A3; 1.
DR   Pfam; PF08337; Plexin_cytopl; 1.
DR   Pfam; PF20170; Plexin_RBD; 1.
DR   Pfam; PF01437; PSI; 3.
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; SSF81296; E set domains; 4.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF103575; Plexin repeat; 1.
DR   SUPFAM; SSF101912; Sema domain; 1.
DR   PROSITE; PS51004; SEMA; 1.
DR   Genevisible; P70208; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; Coiled coil;
KW   Disulfide bond; Glycoprotein; Membrane; Phosphoprotein; Receptor;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..1872
FT                   /note="Plexin-A3"
FT                   /id="PRO_0000411104"
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"
FT   VAR_SEQ         1072..1148
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_041609"
FT   MUTAGEN         1279
FT                   /note="L->R: Strongly reduced response to semaphorin."
FT                   /evidence="ECO:0000269|PubMed:19717441"
FT   MUTAGEN         1300
FT                   /note="Y->A: Almost abolishes response to semaphorin."
FT                   /evidence="ECO:0000269|PubMed:19717441"
FT   MUTAGEN         1309
FT                   /note="F->A: Almost abolishes response to semaphorin."
FT                   /evidence="ECO:0000269|PubMed:19717441"
FT   MUTAGEN         1407..1408
FT                   /note="RR->AA: Abolishes response to semaphorin."
FT                   /evidence="ECO:0000269|PubMed:19717441"
FT   MUTAGEN         1453
FT                   /note="I->R: Abolishes response to semaphorin."
FT                   /evidence="ECO:0000269|PubMed:19717441"
FT   MUTAGEN         1464
FT                   /note="L->G: Almost abolishes response to semaphorin."
FT                   /evidence="ECO:0000269|PubMed:19717441"
FT   MUTAGEN         1506
FT                   /note="Q->A: Abolishes response to semaphorin."
FT                   /evidence="ECO:0000269|PubMed:19717441"
FT   MUTAGEN         1631..1632
FT                   /note="HL->AA: Abolishes response to semaphorin."
FT                   /evidence="ECO:0000269|PubMed:19717441"
FT   CONFLICT        1627
FT                   /note="T -> A (in Ref. 4; BAC33681)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1861
FT                   /note="L -> P (in Ref. 1; BAA13190)"
FT                   /evidence="ECO:0000305"
FT   HELIX           1248..1286
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   HELIX           1300..1308
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   HELIX           1316..1318
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   HELIX           1325..1337
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   HELIX           1341..1352
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   HELIX           1359..1372
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   HELIX           1374..1376
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   HELIX           1377..1397
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   TURN            1403..1407
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   HELIX           1412..1424
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   HELIX           1426..1431
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   HELIX           1434..1448
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   TURN            1455..1457
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   HELIX           1466..1468
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   STRAND          1478..1484
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   TURN            1486..1488
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   STRAND          1493..1499
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   HELIX           1504..1515
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   TURN            1516..1518
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   HELIX           1521..1523
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   HELIX           1527..1529
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   STRAND          1530..1536
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   STRAND          1541..1544
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   STRAND          1546..1548
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   STRAND          1557..1559
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   TURN            1563..1567
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   STRAND          1573..1578
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   STRAND          1628..1632
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   HELIX           1653..1677
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   HELIX           1682..1684
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   HELIX           1689..1703
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   TURN            1704..1706
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   HELIX           1710..1720
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   TURN            1721..1724
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   HELIX           1725..1731
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   HELIX           1733..1735
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   HELIX           1743..1759
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   HELIX           1773..1777
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   TURN            1778..1781
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   HELIX           1782..1798
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   HELIX           1804..1817
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   TURN            1818..1820
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   HELIX           1824..1837
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   HELIX           1839..1848
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   HELIX           1850..1854
FT                   /evidence="ECO:0007829|PDB:3IG3"
FT   HELIX           1857..1869
FT                   /evidence="ECO:0007829|PDB:3IG3"
SQ   SEQUENCE   1872 AA;  207958 MW;  39D57886A0C4830A CRC64;
     MPTVCLLPLL FFTIGGCLGS SRPFRTFVVT DTTLTHLAVH RVTGEVFVGA VNRVFKLAPN
     LTELRAHVTG PIEDNARCYP PPSMRVCSHR LVPVDNVNKL LLIDYAARRL VACGSIWQGI
     CQFLRLDDLF KLGEPHHRKE HYLSGAQEPD SMAGVIVEQV QGPSKLFVGT AVDGKSEYFP
     TLSSRKLIDD EDSGDMFSLV YQDEFVSSQI KIPSDTLSLY PAFDIYYIYG FVSASFVYFL
     TLQLDTQQTL LDTAGEKFFT SKIVRMCAGD SEFYSYVEFP IGCSWRGVEY RLVQSAHLAK
     PGLLLAQALG VPADEDVLFT IFSQGQKNRA NPPRQTILCL FTLSSINAHI RRRIQSCYRG
     EGTLALPWLL NKELPCINTP LQINGNFCGL VLNQPLGGLH VIEGLPLLAD STDGMASVAA
     YTYHQHSVVF IGTRSGNLKK VRVDGSQDAQ LYETVSVVQG SPILRDLLFS PDHRHIYLLS
     EKQVSQLPVE TCEQYLSCAA CLGSGDPHCG WCVLQHRCCR EGACPGASAP HGFAEELSKC
     IQVRVRPNNV SVTSSGVQLT VAMRNVPDLS VGVSCSFEEV TESEAILLPS GELRCPSPSL
     QELQTLTRGH GATHTVRLQL LSMETGVRFA GVDFVFYNCS ALQSCMSCVG SPYPCHWCKY
     RHVCTSHPHE CSFQEGRVHS PEGCPEILPQ GDLLIPVGVM QPLTLRAKNL PQPQSGQKNY
     ECVVRVQGRQ HRVPAVRFNS SSVQCQNASY FYEGDEFGDT ELDFSVVWDG DFPIDKPPSF
     RALLYKCWAQ RPSCGLCLKA DPRFNCGWCI SEHRCQLRAH CPAPKSNWMH PSQKGARCSH
     PRITQIHPLT GPKEGGTRVT IVGENLGLTS REVGLRVAGV RCNSIPTEYV SAERIVCEME
     ESLVPSPPPG PAELCVGDCS ADFRTQSQQL YSFVTPTFDR VSPSRGPASG GTRLTISGIS
     LDAGSRVTVI IRDGECQFVR RDAEAIVCIS PVSTLGPSQS PITLAIDHAN ISNTGVIYTY
     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 TKIECDWKRV
     NSLAHYQVTD GSLVALVPKQ VSAYNMANSF TFTRSLSRYE SLLRAASSPD SLRSRAPMLT
     PDQEAGTKLW HLVRNHDHTD HREGDRGSKM VSEIYLTRLL ATKGTLQKFV DDLFETVFST
     AHRGSALPLA IKYMFDFLDE QADQRQISDP DVRHTWKSNC LPLRFWVNVI KNPQFVFDIH
     KNSITDACLS VVAQTFMDSC STSEHRLGKD SPSNKLLYAK DIPNYKSWVE RYYRDIAKMA
     SISDQDMDAY LVEQSRLHAN DFNVLSALSE LYFYVTKYRQ EILTSLDRDA SCRKHKLRQK
     LEQIITLVSS SS
//