ID ROBO3_HUMAN Reviewed; 1386 AA. AC Q96MS0; DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 21-JUN-2004, sequence version 2. DT 02-SEP-2026, entry version 188. DE RecName: Full=Roundabout homolog 3; DE AltName: Full=Roundabout-like protein 3; DE Flags: Precursor; GN Name=ROBO3 {ECO:0000312|HGNC:HGNC:13433}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND VARIANTS HGPPS1 RP PRO-5; LEU-66; LYS-319; GLU-361; PRO-703 AND PRO-705. RX PubMed=15105459; DOI=10.1126/science.1096437; RA Jen J.C., Chan W.-M., Bosley T.M., Wan J.-J., Carr J.R., Rueb U., RA Shattuck D., Salamon G., Kudo L.C., Ou J., Lin D.D.M., Salih M.A.M., RA Kansu T., Al Dhalaan H., Al-Zayed Z., MacDonald D.B., Stigsby B., RA Plaitakis A., Dretakis E.K., Gottlob I., Pieh C., Traboulsi E.I., Wang Q., RA Wang L., Andrews C., Yamada K., Demer J.L., Karim S., Alger J.R., RA Geschwind D.H., Deller T., Sicotte N.L., Nelson S.F., Baloh R.W., RA Engle E.C.; RT "Mutations in a human ROBO gene disrupt hindbrain axon pathway crossing and RT morphogenesis."; RL Science 304:1509-1513(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS MET-423 RP AND LEU-868. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1263, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [4] {ECO:0007744|PDB:6POG, ECO:0007744|PDB:6POK, ECO:0007744|PDB:6POL} RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 664-870 IN COMPLEX WITH NELL2, RP AND MUTAGENESIS OF PHE-594; ASN-600; THR-601; TRP-602; THR-604; ILE-624; RP LEU-626; ARG-630; TRP-635 AND GLU-639. RX PubMed=32198364; DOI=10.1038/s41467-020-15211-1; RA Pak J.S., DeLoughery Z.J., Wang J., Acharya N., Park Y., Jaworski A., RA Ozkan E.; RT "NELL2-Robo3 complex structure reveals mechanisms of receptor activation RT for axon guidance."; RL Nat. Commun. 11:1489-1489(2020). CC -!- FUNCTION: Receptor involved in axon guidance during development CC (PubMed:15105459). Acts as a multifunctional regulator of pathfinding CC that simultaneously mediates NELL2 repulsion, inhibits SLIT repulsion, CC and facilitates Netrin-1/NTN1 attraction. In spinal cord development CC plays a role in guiding commissural axons probably by preventing CC premature sensitivity to Slit proteins thus inhibiting Slit signaling CC through ROBO1/ROBO2. Binding OF NELL2 to the receptor ROBO3 promotes CC oligomerization of ROBO3, resulting in the repulsion of commissural CC axons in the midline. ROBO3 also indirectly boosts axon attraction to CC NTN1 without interacting with NTN1 itself (By similarity). CC {ECO:0000250|UniProtKB:Q9Z2I4, ECO:0000269|PubMed:15105459}. CC -!- SUBUNIT: Monomer (PubMed:32198364). Interacts (via Fibronectin type-III CC 1 domain) with NELL2 (via the EGF domains) with a 3:3 stoichiometry; CC this interaction promotes oligomerization of ROBO3 resulting in the CC repulsion of commissural axons in the midline (PubMed:32198364). CC {ECO:0000269|PubMed:32198364}. CC -!- INTERACTION: CC Q96MS0; Q99435-1: NELL2; NbExp=3; IntAct=EBI-1220465, EBI-16185191; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9Z2I4}; Single- CC pass type I membrane protein {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=Robo3.1 {ECO:0000303|PubMed:32198364}; CC IsoId=Q96MS0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96MS0-2; Sequence=VSP_010650, VSP_010651; CC -!- DISEASE: Gaze palsy, familial horizontal, with progressive scoliosis, 1 CC (HGPPS1) [MIM:607313]: An autosomal recessive neurologic disorder CC characterized by eye movement abnormalities apparent from birth, CC childhood-onset progressive scoliosis, distinctive brainstem CC malformation and defective crossing of some brainstem neuronal CC pathways. {ECO:0000269|PubMed:15105459}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. ROBO family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY509035; AAS91662.1; -; mRNA. DR EMBL; AK056544; BAB71212.1; -; mRNA. DR CCDS; CCDS44755.1; -. [Q96MS0-1] DR RefSeq; NP_071765.2; NM_022370.4. [Q96MS0-1] DR PDB; 6POG; X-ray; 2.75 A; A=551-663. DR PDB; 6POK; X-ray; 1.80 A; A=664-870. DR PDB; 6POL; X-ray; 1.80 A; A/C/E=549-652. DR AlphaFoldDB; Q96MS0; -. DR SMR; Q96MS0; -. DR BioGRID; 122111; 17. DR DIP; DIP-38410N; -. DR FunCoup; Q96MS0; 446. DR IntAct; Q96MS0; 6. DR NDEx; IQUERY-CP-ROBO3; 2 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000380903; -. DR GlyCosmos; Q96MS0; 11 sites, No reported glycans. DR GlyGen; Q96MS0; 13 sites, 1 O-linked glycan (1 site). DR iPTMnet; Q96MS0; -. DR PhosphoSitePlus; Q96MS0; -. DR BioMuta; ROBO3; -. DR DMDM; 49036492; -. DR jPOST; Q96MS0; -. DR MassIVE; Q96MS0; -. DR PaxDb; 9606-ENSP00000380903; -. DR PeptideAtlas; Q96MS0; -. DR ProteomicsDB; 77392; -. [Q96MS0-1] DR ProteomicsDB; 77393; -. [Q96MS0-2] DR Antibodypedia; 2550; 195 antibodies from 34 providers. DR DNASU; 64221; -. DR Ensembl; ENST00000397801.6; ENSP00000380903.1; ENSG00000154134.15. [Q96MS0-1] DR GeneID; 64221; -. DR KEGG; hsa:64221; -. DR MANE-Select; ENST00000397801.6; ENSP00000380903.1; NM_022370.4; NP_071765.2. DR UCSC; uc001qbc.4; human. [Q96MS0-1] DR AGR; HGNC:13433; -. DR ClinPGx; PA134896648; -. DR CTD; 64221; -. DR DisGeNET; 64221; -. DR GeneCards; ROBO3; -. DR HGNC; HGNC:13433; ROBO3. DR HPA; ENSG00000154134; Tissue enhanced (ovary). DR MalaCards; ROBO3; -. DR MIM; 607313; phenotype. DR MIM; 608630; gene. DR OpenTargets; ENSG00000154134; -. DR Orphanet; 2744; Horizontal gaze palsy with progressive scoliosis. DR VEuPathDB; HostDB:ENSG00000154134; -. DR eggNOG; KOG4222; Eukaryota. DR GeneTree; ENSGT00940000155457; -. DR HOGENOM; CLU_003227_5_1_1; -. DR InParanoid; Q96MS0; -. DR OMA; LMMSHTH; -. DR OrthoDB; 428111at2759; -. DR PAN-GO; Q96MS0; 6 GO annotations based on evolutionary models. DR PhylomeDB; Q96MS0; -. DR PathwayCommons; Q96MS0; -. DR Reactome; R-HSA-428542; Regulation of commissural axon pathfinding by SLIT and ROBO. [Q96MS0-1] DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs. [Q96MS0-1] DR Reactome; R-HSA-9010642; ROBO receptors bind AKAP5. [Q96MS0-1] DR SignaLink; Q96MS0; -. DR SIGNOR; Q96MS0; -. DR Agora; ENSG00000154134; -. DR BioGRID-ORCS; 64221; 6 hits in 1147 CRISPR screens. DR ChiTaRS; ROBO3; human. DR GeneWiki; ROBO3; -. DR GenomeRNAi; 64221; -. DR Pharos; Q96MS0; Tbio. DR PRO; PR:Q96MS0; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q96MS0; protein. DR Bgee; ENSG00000154134; Expressed in right uterine tube and 167 other cell types or tissues. DR ExpressionAtlas; Q96MS0; baseline and differential. DR GO; GO:0030424; C:axon; IBA:GO_Central. DR GO; GO:0016020; C:membrane; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central. DR GO; GO:0007411; P:axon guidance; ISS:UniProtKB. DR GO; GO:0016199; P:axon midline choice point recognition; ISS:UniProtKB. DR GO; GO:0007420; P:brain development; IEA:UniProtKB-ARBA. DR GO; GO:0071679; P:commissural neuron axon guidance; IEA:Ensembl. DR GO; GO:0070593; P:dendrite self-avoidance; IBA:GO_Central. DR GO; GO:0007156; P:homophilic cell-cell adhesion; IBA:GO_Central. DR GO; GO:0050925; P:negative regulation of negative chemotaxis; IEA:UniProtKB-ARBA. DR GO; GO:1902669; P:positive regulation of axon guidance; IEA:Ensembl. DR GO; GO:0050772; P:positive regulation of axonogenesis; IEA:UniProtKB-ARBA. DR GO; GO:0035295; P:tube development; IEA:UniProtKB-ARBA. DR CDD; cd00063; FN3; 3. DR DisProt; DP03308; -. DR FunFam; 2.60.40.10:FF:000053; Roundabout guidance receptor 1; 1. DR FunFam; 2.60.40.10:FF:000888; Roundabout guidance receptor 3; 1. DR FunFam; 2.60.40.10:FF:001028; Roundabout guidance receptor 3; 1. DR FunFam; 2.60.40.10:FF:000055; roundabout homolog 1 isoform X2; 1. DR FunFam; 2.60.40.10:FF:000026; roundabout homolog 2 isoform X1; 1. DR FunFam; 2.60.40.10:FF:000008; roundabout homolog 2 isoform X2; 2. DR FunFam; 2.60.40.10:FF:000043; roundabout homolog 2 isoform X2; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 8. DR InterPro; IPR003961; FN3_dom. DR InterPro; IPR036116; FN3_sf. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR013098; Ig_I-set. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR003598; Ig_sub2. DR InterPro; IPR051170; Neural/epithelial_adhesion. DR PANTHER; PTHR12231; CTX-RELATED TYPE I TRANSMEMBRANE PROTEIN; 1. DR PANTHER; PTHR12231:SF236; ROUNDABOUT HOMOLOG 3; 1. DR Pfam; PF00041; fn3; 3. DR Pfam; PF07679; I-set; 3. DR Pfam; PF13927; Ig_3; 2. DR SMART; SM00060; FN3; 3. DR SMART; SM00409; IG; 5. DR SMART; SM00408; IGc2; 5. DR SUPFAM; SSF49265; Fibronectin type III; 2. DR SUPFAM; SSF48726; Immunoglobulin; 5. DR PROSITE; PS50853; FN3; 3. DR PROSITE; PS50835; IG_LIKE; 5. DR PDBsum; 6POG; -. DR PDBsum; 6POK; -. DR PDBsum; 6POL; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Chemotaxis; Developmental protein; KW Differentiation; Disease variant; Disulfide bond; Glycoprotein; KW Immunoglobulin domain; Membrane; Neurogenesis; Phosphoprotein; KW Proteomics identification; Receptor; Reference proteome; Repeat; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1..20 FT /evidence="ECO:0000255" FT CHAIN 21..1386 FT /note="Roundabout homolog 3" FT /id="PRO_0000031038" FT TOPO_DOM 21..891 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 892..912 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 913..1386 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 64..160 FT /note="Ig-like C2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DOMAIN 166..253 FT /note="Ig-like C2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DOMAIN 258..342 FT /note="Ig-like C2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DOMAIN 347..440 FT /note="Ig-like C2-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DOMAIN 450..531 FT /note="Ig-like C2-type 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DOMAIN 558..652 FT /note="Fibronectin type-III 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 671..766 FT /note="Fibronectin type-III 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 771..869 FT /note="Fibronectin type-III 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT REGION 541..563 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 639..662 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 965..989 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1028..1310 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1327..1386 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 546..559 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1067..1083 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1099..1112 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1158..1169 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1178..1191 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1202..1229 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1294..1304 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1333..1344 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1345..1361 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1263 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT CARBOHYD 25 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 34 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 41 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 53 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 156 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 410 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 459 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 503 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 784 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 813 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 820 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 85..143 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 187..236 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 279..326 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 368..424 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 472..521 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT VAR_SEQ 1025..1034 FT /note="AGEELQTFHG -> LTTPLLILTT (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_010650" FT VAR_SEQ 1035..1386 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_010651" FT VARIANT 5 FT /note="L -> P (in HGPPS1; dbSNP:rs121918275)" FT /evidence="ECO:0000269|PubMed:15105459" FT /id="VAR_019119" FT VARIANT 66 FT /note="I -> L (in HGPPS1; dbSNP:rs121918276)" FT /evidence="ECO:0000269|PubMed:15105459" FT /id="VAR_019120" FT VARIANT 319 FT /note="E -> K (in HGPPS1; dbSNP:rs121918274)" FT /evidence="ECO:0000269|PubMed:15105459" FT /id="VAR_019073" FT VARIANT 361 FT /note="G -> E (in HGPPS1; dbSNP:rs121918270)" FT /evidence="ECO:0000269|PubMed:15105459" FT /id="VAR_019121" FT VARIANT 416 FT /note="R -> H (in dbSNP:rs3862618)" FT /id="VAR_053642" FT VARIANT 423 FT /note="V -> M (in dbSNP:rs4935898)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_034474" FT VARIANT 703 FT /note="R -> P (in HGPPS1; dbSNP:rs121918271)" FT /evidence="ECO:0000269|PubMed:15105459" FT /id="VAR_019074" FT VARIANT 705 FT /note="S -> P (in HGPPS1; dbSNP:rs121918272)" FT /evidence="ECO:0000269|PubMed:15105459" FT /id="VAR_019075" FT VARIANT 868 FT /note="P -> L (in dbSNP:rs55706177)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_062145" FT VARIANT 1369 FT /note="Q -> R (in dbSNP:rs35723495)" FT /id="VAR_034475" FT MUTAGEN 594 FT /note="F->A: Abolishes binding to NELL2; when associated FT with A-602." FT /evidence="ECO:0000269|PubMed:32198364" FT MUTAGEN 600 FT /note="N->A: Does not affect binding to NELL2; when FT associated with A-601." FT /evidence="ECO:0000269|PubMed:32198364" FT MUTAGEN 601 FT /note="T->A: Does not affect binding to NELL2; when FT associated with A-600." FT /evidence="ECO:0000269|PubMed:32198364" FT MUTAGEN 602 FT /note="W->A: Abolishes binding to NELL2; when associated FT with A-594." FT /evidence="ECO:0000269|PubMed:32198364" FT MUTAGEN 604 FT /note="T->A: Decreases binding to NELL2." FT /evidence="ECO:0000269|PubMed:32198364" FT MUTAGEN 624 FT /note="I->A: Decreases binding to NELL2; when associated FT with A-626." FT /evidence="ECO:0000269|PubMed:32198364" FT MUTAGEN 626 FT /note="L->A: Decreases binding to NELL2; when associated FT with A-624." FT /evidence="ECO:0000269|PubMed:32198364" FT MUTAGEN 630 FT /note="R->A: Abolishes binding to NELL2." FT /evidence="ECO:0000269|PubMed:32198364" FT MUTAGEN 635 FT /note="W->A: Does not affect binding to NELL2." FT /evidence="ECO:0000269|PubMed:32198364" FT MUTAGEN 639 FT /note="E->A: Does not affect binding to NELL2." FT /evidence="ECO:0000269|PubMed:32198364" FT HELIX 555..562 FT /evidence="ECO:0007829|PDB:6POL" FT STRAND 563..567 FT /evidence="ECO:0007829|PDB:6POL" FT STRAND 572..575 FT /evidence="ECO:0007829|PDB:6POL" FT STRAND 588..594 FT /evidence="ECO:0007829|PDB:6POL" FT TURN 596..598 FT /evidence="ECO:0007829|PDB:6POG" FT STRAND 603..609 FT /evidence="ECO:0007829|PDB:6POL" FT STRAND 611..616 FT /evidence="ECO:0007829|PDB:6POL" FT STRAND 624..633 FT /evidence="ECO:0007829|PDB:6POL" FT HELIX 638..646 FT /evidence="ECO:0007829|PDB:6POL" FT HELIX 649..651 FT /evidence="ECO:0007829|PDB:6POL" FT STRAND 672..675 FT /evidence="ECO:0007829|PDB:6POK" FT HELIX 676..678 FT /evidence="ECO:0007829|PDB:6POK" FT STRAND 686..694 FT /evidence="ECO:0007829|PDB:6POK" FT HELIX 696..698 FT /evidence="ECO:0007829|PDB:6POK" FT STRAND 701..708 FT /evidence="ECO:0007829|PDB:6POK" FT STRAND 717..721 FT /evidence="ECO:0007829|PDB:6POK" FT STRAND 728..731 FT /evidence="ECO:0007829|PDB:6POK" FT STRAND 738..747 FT /evidence="ECO:0007829|PDB:6POK" FT HELIX 754..758 FT /evidence="ECO:0007829|PDB:6POK" FT STRAND 759..762 FT /evidence="ECO:0007829|PDB:6POK" FT HELIX 763..765 FT /evidence="ECO:0007829|PDB:6POK" FT STRAND 773..779 FT /evidence="ECO:0007829|PDB:6POK" FT STRAND 781..785 FT /evidence="ECO:0007829|PDB:6POK" FT STRAND 787..792 FT /evidence="ECO:0007829|PDB:6POK" FT HELIX 793..795 FT /evidence="ECO:0007829|PDB:6POK" FT HELIX 796..799 FT /evidence="ECO:0007829|PDB:6POK" FT STRAND 805..811 FT /evidence="ECO:0007829|PDB:6POK" FT HELIX 815..817 FT /evidence="ECO:0007829|PDB:6POK" FT STRAND 819..824 FT /evidence="ECO:0007829|PDB:6POK" FT STRAND 829..832 FT /evidence="ECO:0007829|PDB:6POK" FT STRAND 840..849 FT /evidence="ECO:0007829|PDB:6POK" FT STRAND 852..856 FT /evidence="ECO:0007829|PDB:6POK" FT HELIX 857..859 FT /evidence="ECO:0007829|PDB:6POK" FT STRAND 860..863 FT /evidence="ECO:0007829|PDB:6POK" SQ SEQUENCE 1386 AA; 148209 MW; 955A7300A2BDA27F CRC64; MLRYLLKTLL QMNLFADSLA GDISNSSELL LGFNSSLAAL NHTLLPPGDP SLNGSRVGPE DAMPRIVEQP PDLLVSRGEP ATLPCRAEGR PRPNIEWYKN GARVATVRED PRAHRLLLPS GALFFPRIVH GRRARPDEGV YTCVARNYLG AAASRNASLE VAVLRDDFRQ SPGNVVVAVG EPAVLECVPP RGHPEPSVSW RKDGARLKEE EGRITIRGGK LMMSHTLKSD AGMYVCVASN MAGERESAAA EVMVLERPSF LRRPVNQVVL ADAPVTFLCE VKGDPPPRLR WRKEDGELPT GRYEIRSDHS LWIGHVSAED EGTYTCVAEN SVGRAEASGS LSVHVPPQLV TQPQDQMAAP GESVAFQCET KGNPPPAIFW QKEGSQVLLF PSQSLQPTGR FSVSPRGQLN ITAVQRGDAG YYVCQAVSVA GSILAKALLE IKGASLDGLP PVILQGPANQ TLVLGSSVWL PCRVTGNPQP SVRWKKDGQW LQGDDLQFKT MANGTLYIAN VQEMDMGFYS CVAKSSTGEA TWSGWLKMRE DWGVSPDPPT EPSSPPGAPS QPVVTEITKN SITLTWKPNP QTGAAVTSYV IEAFSPAAGN TWRTVADGVQ LETHTVSGLQ PNTIYLFLVR AVGAWGLSEP SPVSEPVRTQ DSSPSRPVED PWRGQQGLAE VAVRLQEPIV LGPRTLQVSW TVDGPVQLVQ GFRVSWRVAG PEGGSWTMLD LQSPSQQSTV LRGLPPGTQI QIKVQAQGQE GLGAESLSVT RSIPEEAPSG PPQGVAVALG GDGNSSITVS WEPPLPSQQN GVITEYQIWC LGNESRFHLN RSAAGWARSA MLRGLVPGLL YRTLVAAATS AGVGVPSAPV LVQLPSPPDL EPGLEVGAGL AVRLARVLRE PAFLAGSGAA CGALLLGLCA ALYWRRKQRK ELSHYTASFA YTPAVSFPHS EGLSGASSRP PMGLGPAPYS WLADSWPHPS RSPSAQEPRG SCCPSNPDPD DRYYNEAGIS LYLAQTARGT AAPGEGPVYS TIDPAGEELQ TFHGGFPQHP SGDLGPWSQY APPEWSQGDS GAKGGKVKLL GKPVQMPSLN WPEALPPPPP SCELSCLEGP EEELEGSSEP EEWCPPMPER SHLTEPSSSG GCLVTPSRRE TPSPTPSYGQ QSTATLTPSP PDPPQPPTDM PHLHQMPRRV PLGPSSPLSV SQPMLGIREA RPAGLGAGPA ASPHLSPSPA PSTASSAPGR TWQGNGEMTP PLQGPRARFR KKPKALPYRR ENSPGDLPPP PLPPPEEEAS WALELRAAGS MSSLERERSG ERKAVQAVPL AAQRVLHPDE EAWLPYSRPS FLSRGQGTST CSTAGSNSSR GSSSSRGSRG PGRSRSRSQS RSQSQRPGQK RREEPR //