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 24-JAN-2024, entry version 178.
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}.
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DR EMBL; AY509035; AAS91662.1; -; mRNA.
DR EMBL; AK056544; BAB71212.1; -; mRNA.
DR CCDS; CCDS44755.1; -. [Q96MS0-1]
DR RefSeq; NP_071765.2; NM_022370.3. [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 PDBsum; 6POG; -.
DR PDBsum; 6POK; -.
DR PDBsum; 6POL; -.
DR AlphaFoldDB; Q96MS0; -.
DR SMR; Q96MS0; -.
DR BioGRID; 122111; 16.
DR DIP; DIP-38410N; -.
DR IntAct; Q96MS0; 2.
DR STRING; 9606.ENSP00000380903; -.
DR GlyCosmos; Q96MS0; 11 sites, No reported glycans.
DR GlyGen; Q96MS0; 12 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q96MS0; -.
DR PhosphoSitePlus; Q96MS0; -.
DR BioMuta; ROBO3; -.
DR DMDM; 49036492; -.
DR EPD; Q96MS0; -.
DR jPOST; Q96MS0; -.
DR MassIVE; Q96MS0; -.
DR MaxQB; Q96MS0; -.
DR PaxDb; 9606-ENSP00000380903; -.
DR PeptideAtlas; Q96MS0; -.
DR ProteomicsDB; 77392; -. [Q96MS0-1]
DR ProteomicsDB; 77393; -. [Q96MS0-2]
DR Antibodypedia; 2550; 223 antibodies from 33 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 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 neXtProt; NX_Q96MS0; -.
DR OpenTargets; ENSG00000154134; -.
DR Orphanet; 2744; Horizontal gaze palsy with progressive scoliosis.
DR PharmGKB; PA134896648; -.
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; 5396194at2759; -.
DR PhylomeDB; Q96MS0; -.
DR TreeFam; TF351053; -.
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 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 Genevisible; Q96MS0; HS.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; NAS: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:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0070593; P:dendrite self-avoidance; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:1902669; P:positive regulation of axon guidance; IEA:Ensembl.
DR CDD; cd00063; FN3; 3.
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 PANTHER; PTHR44170; PROTEIN SIDEKICK; 1.
DR PANTHER; PTHR44170:SF37; ROUNDABOUT GUIDANCE RECEPTOR 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.
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; Receptor;
KW Reference proteome; Repeat; Signal; 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 967..981
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1094
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1122..1156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1157..1171
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1217..1238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1263..1277
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1331..1375
FT /note="Polar residues"
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 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 STRAND 672..675
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 STRAND 759..762
FT /evidence="ECO:0007829|PDB:6POK"
FT STRAND 773..779
FT /evidence="ECO:0007829|PDB:6POK"
FT STRAND 782..785
FT /evidence="ECO:0007829|PDB:6POK"
FT STRAND 787..792
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 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
//
