##gff-version 3 Q61220 UniProtKB Signal peptide 1 24 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Chain 25 819 . . . ID=PRO_0000007667;Note=Protein kinase C-binding protein NELL2 Q61220 UniProtKB Domain 67 231 . . . Note=Laminin G-like Q61220 UniProtKB Domain 275 334 . . . Note=VWFC 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00220 Q61220 UniProtKB Domain 400 442 . . . Note=EGF-like 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00076 Q61220 UniProtKB Domain 443 484 . . . Note=EGF-like 2%3B calcium-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00076 Q61220 UniProtKB Domain 485 525 . . . Note=EGF-like 3%3B calcium-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00076 Q61220 UniProtKB Domain 526 556 . . . Note=EGF-like 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00076 Q61220 UniProtKB Domain 558 604 . . . Note=EGF-like 5%3B calcium-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00076 Q61220 UniProtKB Domain 605 640 . . . Note=EGF-like 6%3B calcium-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00076 Q61220 UniProtKB Domain 701 759 . . . Note=VWFC 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00220 Q61220 UniProtKB Binding site 443 443 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Binding site 444 444 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Binding site 446 446 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Binding site 462 462 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Binding site 463 463 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Binding site 466 466 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Binding site 558 558 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Binding site 559 559 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Binding site 561 561 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Binding site 577 577 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Binding site 578 578 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Binding site 581 581 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Binding site 605 605 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Binding site 606 606 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Binding site 608 608 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Binding site 624 624 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Binding site 625 625 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Binding site 628 628 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Glycosylation 56 56 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q61220 UniProtKB Glycosylation 228 228 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q61220 UniProtKB Glycosylation 296 296 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q61220 UniProtKB Glycosylation 301 301 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q61220 UniProtKB Glycosylation 520 520 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Glycosylation 551 551 . . . Note=O-linked (GlcNAc...) threonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Glycosylation 618 618 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q61220 UniProtKB Glycosylation 638 638 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q61220 UniProtKB Disulfide bond 404 416 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Disulfide bond 410 425 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Disulfide bond 427 441 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Disulfide bond 447 460 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Disulfide bond 454 469 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Disulfide bond 471 483 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Disulfide bond 489 502 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Disulfide bond 496 511 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Disulfide bond 513 524 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Disulfide bond 528 538 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Disulfide bond 532 544 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Disulfide bond 546 555 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Disulfide bond 562 575 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Disulfide bond 569 584 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Disulfide bond 586 603 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Disulfide bond 609 622 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Disulfide bond 616 631 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Disulfide bond 633 639 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99435 Q61220 UniProtKB Mutagenesis 451 451 . . . Note=Strong (120-fold) reduction of affinity towards ROBO3%3B when associated with A-453. Reduced axon repulsive activity%3B when associated with A-453. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32198364;Dbxref=PMID:32198364 Q61220 UniProtKB Mutagenesis 453 453 . . . Note=Strong (120-fold) reduction of affinity towards ROBO3%3B when associated with A-451. Reduced axon repulsive activity%3B when associated with A-453. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32198364;Dbxref=PMID:32198364 Q61220 UniProtKB Mutagenesis 455 455 . . . Note=Mildly (2.4-fold) reduction of affinity towards ROBO3. Does not affect axon repulsive activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32198364;Dbxref=PMID:32198364 Q61220 UniProtKB Mutagenesis 480 480 . . . Note=Strong (120-fold) reduction of affinity towards ROBO3%3B when associated with A-481. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32198364;Dbxref=PMID:32198364 Q61220 UniProtKB Mutagenesis 481 481 . . . Note=Strong (120-fold) reduction of affinity towards ROBO3%3B when associated with A-480. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32198364;Dbxref=PMID:32198364 Q61220 UniProtKB Mutagenesis 501 501 . . . Note=Abolishes binding to ROBO3%3B when associated with A-503. Abolishes axon repulsive activity%3B when associated with A-503. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32198364;Dbxref=PMID:32198364 Q61220 UniProtKB Mutagenesis 503 503 . . . Note=Abolishes binding to ROBO3%3B when associated with A-503. Abolishes axon repulsive activity%3B when associated with A-503. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32198364;Dbxref=PMID:32198364 Q61220 UniProtKB Mutagenesis 512 512 . . . Note=Mildly (2.4-fold) reduced affinity for ROBO3. Does not affect axon repulsive activity. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32198364;Dbxref=PMID:32198364 Q61220 UniProtKB Sequence conflict 81 81 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q61220 UniProtKB Sequence conflict 183 183 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q61220 UniProtKB Sequence conflict 187 187 . . . Note=P->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q61220 UniProtKB Sequence conflict 352 352 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q61220 UniProtKB Sequence conflict 423 423 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q61220 UniProtKB Sequence conflict 470 470 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q61220 UniProtKB Sequence conflict 492 492 . . . Note=N->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q61220 UniProtKB Sequence conflict 668 668 . . . Note=C->W;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q61220 UniProtKB Sequence conflict 687 687 . . . Note=V->D;Ontology_term=ECO:0000305;evidence=ECO:0000305