UNC5C_MOUSE
ID UNC5C_MOUSE Reviewed; 931 AA.
AC O08747; Q8CD16;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Netrin receptor UNC5C;
DE AltName: Full=Protein unc-5 homolog 3;
DE AltName: Full=Protein unc-5 homolog C;
DE AltName: Full=Rostral cerebellar malformation protein {ECO:0000303|PubMed:9126743};
DE Flags: Precursor;
GN Name=Unc5c;
GN Synonyms=Rcm {ECO:0000303|PubMed:11533026},
GN Unc5h3 {ECO:0000303|PubMed:12451134};
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), FUNCTION, DISEASE, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57B6/SJL;
RX PubMed=9126743; DOI=10.1038/386838a0;
RA Ackerman S.L., Kozak L.P., Przyborski S.A., Rund L.A., Boyer B.B.,
RA Knowles B.B.;
RT "The mouse rostral cerebellar malformation gene encodes an UNC-5-like
RT protein.";
RL Nature 386:838-842(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [3]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=9389662; DOI=10.1242/dev.125.1.41;
RA Przyborski S.A., Knowles B.B., Ackerman S.L.;
RT "Embryonic phenotype of Unc5h3 mutant mice suggests chemorepulsion during
RT the formation of the rostral cerebellar boundary.";
RL Development 125:41-50(1998).
RN [4]
RP FUNCTION, AND INTERACTION WITH DCC.
RX PubMed=10399920; DOI=10.1016/s0092-8674(00)80804-1;
RA Hong K., Hinck L., Nishiyama M., Poo M.-M., Tessier-Lavigne M., Stein E.;
RT "A ligand-gated association between cytoplasmic domains of UNC5 and DCC
RT family receptors converts netrin-induced growth cone attraction to
RT repulsion.";
RL Cell 97:927-941(1999).
RN [5]
RP PHOSPHORYLATION AT TYR-568, MUTAGENESIS OF TYR-568, AND INTERACTION WITH
RP DCC AND PTPN11.
RX PubMed=11533026; DOI=10.1074/jbc.m103872200;
RA Tong J., Killeen M., Steven R., Binns K.L., Culotti J., Pawson T.;
RT "Netrin stimulates tyrosine phosphorylation of the UNC-5 family of netrin
RT receptors and induces Shp2 binding to the RCM cytodomain.";
RL J. Biol. Chem. 276:40917-40925(2001).
RN [6]
RP FUNCTION.
RX PubMed=12451134; DOI=10.1523/jneurosci.22-23-10346.2002;
RA Finger J.H., Bronson R.T., Harris B., Johnson K., Przyborski S.A.,
RA Ackerman S.L.;
RT "The netrin 1 receptors Unc5h3 and Dcc are necessary at multiple choice
RT points for the guidance of corticospinal tract axons.";
RL J. Neurosci. 22:10346-10356(2002).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502, AND IDENTIFICATION BY
RP 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 [8]
RP FUNCTION, INTERACTION WITH DSCAM, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND PHOSPHORYLATION.
RX PubMed=22685302; DOI=10.1074/jbc.m112.340174;
RA Purohit A.A., Li W., Qu C., Dwyer T., Shao Q., Guan K.L., Liu G.;
RT "Down syndrome cell adhesion molecule (DSCAM) associates with
RT uncoordinated-5C (UNC5C) in netrin-1-mediated growth cone collapse.";
RL J. Biol. Chem. 287:27126-27138(2012).
RN [9]
RP INTERACTION WITH FLRT3, AND SUBCELLULAR LOCATION.
RX PubMed=22405201; DOI=10.1016/j.neuron.2012.01.018;
RA O'Sullivan M.L., de Wit J., Savas J.N., Comoletti D., Otto-Hitt S.,
RA Yates J.R. III, Ghosh A.;
RT "FLRT proteins are endogenous latrophilin ligands and regulate excitatory
RT synapse development.";
RL Neuron 73:903-910(2012).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=25419706; DOI=10.1038/nm.3736;
RG Alzheimer's Disease Genetics Consortium;
RA Wetzel-Smith M.K., Hunkapiller J., Bhangale T.R., Srinivasan K.,
RA Maloney J.A., Atwal J.K., Sa S.M., Yaylaoglu M.B., Foreman O., Ortmann W.,
RA Rathore N., Hansen D.V., Tessier-Lavigne M., Mayeux R., Pericak-Vance M.,
RA Haines J., Farrer L.A., Schellenberg G.D., Goate A., Behrens T.W.,
RA Cruchaga C., Watts R.J., Graham R.R.;
RT "A rare mutation in UNC5C predisposes to late-onset Alzheimer's disease and
RT increases neuronal cell death.";
RL Nat. Med. 20:1452-1457(2014).
RN [11]
RP FUNCTION, INTERACTION WITH TUBB3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=28483977; DOI=10.1523/jneurosci.2617-16.2017;
RA Shao Q., Yang T., Huang H., Alarmanazi F., Liu G.;
RT "Uncoupling of UNC5C with Polymerized TUBB3 in Microtubules Mediates
RT Netrin-1 Repulsion.";
RL J. Neurosci. 37:5620-5633(2017).
CC -!- FUNCTION: Receptor for netrin required for axon guidance
CC (PubMed:22685302, PubMed:10399920). Mediates axon repulsion of neuronal
CC growth cones in the developing nervous system upon ligand binding
CC (PubMed:10399920, PubMed:22685302). NTN1/Netrin-1 binding might cause
CC dissociation of UNC5C from polymerized TUBB3 in microtubules and
CC thereby lead to increased microtubule dynamics and axon repulsion
CC (PubMed:28483977). Axon repulsion in growth cones may also be caused by
CC its association with DCC that may trigger signaling for repulsion
CC (PubMed:10399920). Might also collaborate with DSCAM in NTN1-mediated
CC axon repulsion independently of DCC (PubMed:22685302). Also involved in
CC corticospinal tract axon guidance independently of DCC (PubMed:9126743,
CC PubMed:9389662, PubMed:12451134). Involved in dorsal root ganglion axon
CC projection towards the spinal cord (By similarity). It also acts as a
CC dependence receptor required for apoptosis induction when not
CC associated with netrin ligand (By similarity).
CC {ECO:0000250|UniProtKB:O95185, ECO:0000250|UniProtKB:Q761X5,
CC ECO:0000269|PubMed:10399920, ECO:0000269|PubMed:12451134,
CC ECO:0000269|PubMed:22685302, ECO:0000269|PubMed:28483977,
CC ECO:0000269|PubMed:9126743, ECO:0000269|PubMed:9389662}.
CC -!- SUBUNIT: Interacts with DCC (via cytoplasmic domain) (PubMed:10399920,
CC PubMed:11533026). Interacts (tyrosine phosphorylated form) with PTPN11
CC (PubMed:11533026). Interacts (via extracellular domain) with FLRT3 (via
CC extracellular domain) (PubMed:22405201). Interacts (via Ig-like C2-type
CC domain) with DSCAM (via extracellular domain) (PubMed:22685302).
CC Interacts (via death domain) with DAPK1 (By similarity). Interacts (via
CC cytoplasmic domain) with TUBB3; this interaction is decreased by
CC NTN1/Netrin-1 (PubMed:28483977). {ECO:0000250|UniProtKB:O95185,
CC ECO:0000269|PubMed:10399920, ECO:0000269|PubMed:11533026,
CC ECO:0000269|PubMed:22405201, ECO:0000269|PubMed:22685302,
CC ECO:0000269|PubMed:28483977}.
CC -!- INTERACTION:
CC O08747; Q9ERD7: Tubb3; NbExp=3; IntAct=EBI-21004500, EBI-2255594;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22405201};
CC Single-pass type I membrane protein {ECO:0000255}. Cell surface
CC {ECO:0000250|UniProtKB:O95185}. Synapse, synaptosome
CC {ECO:0000250|UniProtKB:Q761X5}. Cell projection, dendrite
CC {ECO:0000269|PubMed:22685302}. Cell projection, axon
CC {ECO:0000269|PubMed:22685302}. Cell projection, growth cone
CC {ECO:0000269|PubMed:22685302, ECO:0000269|PubMed:28483977}. Cell
CC projection, lamellipodium {ECO:0000269|PubMed:28483977}. Cell
CC projection, filopodium {ECO:0000269|PubMed:28483977}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O08747-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O08747-2; Sequence=VSP_011702;
CC -!- TISSUE SPECIFICITY: Expressed in cortical and cerebellar neurons,
CC including cells of the external and internal granular layer and of the
CC Purkinje cell layer (at protein level) (PubMed:22685302,
CC PubMed:28483977). Mainly expressed in regions of differentiating
CC neurons (PubMed:9126743). Highly expressed in brain and lung
CC (PubMed:9126743, PubMed:9389662). Expressed in the cerebellum and the
CC neurons of the hippocampus, with enrichment in neurons of the CA3
CC hippocampal pyramidal layer (PubMed:25419706). Weakly expressed in
CC testis, ovary, spleen, thymus and bladder (PubMed:9126743). Expressed
CC at very low level in kidney, intestine and salivary gland
CC (PubMed:9126743). {ECO:0000269|PubMed:22685302,
CC ECO:0000269|PubMed:25419706, ECO:0000269|PubMed:28483977,
CC ECO:0000269|PubMed:9126743, ECO:0000269|PubMed:9389662}.
CC -!- DEVELOPMENTAL STAGE: Detected at 15 dpc in the cortex and cerebellum
CC and at postnatal day 2 and 4 in the cerebellum (at protein level).
CC {ECO:0000269|PubMed:22685302, ECO:0000269|PubMed:28483977}.
CC -!- PTM: Phosphorylated on different cytoplasmic tyrosine residues
CC (PubMed:11533026). Phosphorylation of Tyr-568 leads to an interaction
CC with PTPN11 phosphatase, suggesting that its activity is regulated by
CC phosphorylation/dephosphorylation (PubMed:11533026). Tyrosine
CC phosphorylation is netrin-dependent (PubMed:11533026, PubMed:22685302).
CC {ECO:0000269|PubMed:11533026, ECO:0000269|PubMed:22685302}.
CC -!- PTM: Proteolytically cleaved by caspases during apoptosis. The cleavage
CC does not take place when the receptor is associated with netrin ligand.
CC Its cleavage by caspases is required to induce apoptosis.
CC {ECO:0000250|UniProtKB:Q761X5}.
CC -!- DISEASE: Note=Defects in Unc5c are the cause of rostral cerebellar
CC malformation (Rcm). Rcm is characterized by cerebellar and midbrain
CC defects, apparently as a result of abnormal neuronal migration.
CC {ECO:0000269|PubMed:9126743}.
CC -!- SIMILARITY: Belongs to the unc-5 family. {ECO:0000305}.
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DR EMBL; U72634; AAB54103.1; -; mRNA.
DR EMBL; AK031655; BAC27495.1; -; mRNA.
DR CCDS; CCDS17873.1; -. [O08747-1]
DR CCDS; CCDS80034.1; -. [O08747-2]
DR RefSeq; NP_033498.1; NM_009472.4. [O08747-1]
DR AlphaFoldDB; O08747; -.
DR SMR; O08747; -.
DR BioGRID; 204445; 6.
DR IntAct; O08747; 1.
DR STRING; 10090.ENSMUSP00000101843; -.
DR GlyGen; O08747; 2 sites.
DR iPTMnet; O08747; -.
DR PhosphoSitePlus; O08747; -.
DR MaxQB; O08747; -.
DR PaxDb; O08747; -.
DR PRIDE; O08747; -.
DR ProteomicsDB; 300199; -. [O08747-1]
DR ProteomicsDB; 300200; -. [O08747-2]
DR Antibodypedia; 2665; 273 antibodies from 34 providers.
DR DNASU; 22253; -.
DR Ensembl; ENSMUST00000075282; ENSMUSP00000074758; ENSMUSG00000059921. [O08747-2]
DR Ensembl; ENSMUST00000106236; ENSMUSP00000101843; ENSMUSG00000059921. [O08747-1]
DR Ensembl; ENSMUST00000142762; ENSMUSP00000118212; ENSMUSG00000059921. [O08747-2]
DR GeneID; 22253; -.
DR KEGG; mmu:22253; -.
DR UCSC; uc008roe.2; mouse. [O08747-1]
DR CTD; 8633; -.
DR MGI; MGI:1095412; Unc5c.
DR VEuPathDB; HostDB:ENSMUSG00000059921; -.
DR eggNOG; KOG1480; Eukaryota.
DR GeneTree; ENSGT00950000182815; -.
DR HOGENOM; CLU_014383_0_0_1; -.
DR InParanoid; O08747; -.
DR OMA; CECQAWS; -.
DR TreeFam; TF316767; -.
DR BioGRID-ORCS; 22253; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Unc5c; mouse.
DR PRO; PR:O08747; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; O08747; protein.
DR Bgee; ENSMUSG00000059921; Expressed in ureter smooth muscle and 248 other tissues.
DR ExpressionAtlas; O08747; baseline and differential.
DR Genevisible; O08747; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0030175; C:filopodium; IDA:UniProtKB.
DR GO; GO:0030426; C:growth cone; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0005042; F:netrin receptor activity; IDA:MGI.
DR GO; GO:0005043; F:netrin receptor activity involved in chemorepulsion; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0015631; F:tubulin binding; IPI:UniProtKB.
DR GO; GO:0033564; P:anterior/posterior axon guidance; IMP:MGI.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0007411; P:axon guidance; IDA:UniProtKB.
DR GO; GO:0007420; P:brain development; IMP:MGI.
DR GO; GO:0061643; P:chemorepulsion of axon; IMP:UniProtKB.
DR GO; GO:1990791; P:dorsal root ganglion development; ISS:UniProtKB.
DR GO; GO:0035234; P:ectopic germ cell programmed cell death; IMP:MGI.
DR GO; GO:0038007; P:netrin-activated signaling pathway; IGI:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:MGI.
DR GO; GO:0051094; P:positive regulation of developmental process; IMP:MGI.
DR GO; GO:2000243; P:positive regulation of reproductive process; IMP:MGI.
DR GO; GO:0030334; P:regulation of cell migration; IMP:MGI.
DR GO; GO:2001222; P:regulation of neuron migration; IMP:MGI.
DR CDD; cd08799; Death_UNC5C; 1.
DR Gene3D; 1.10.533.10; -; 1.
DR Gene3D; 2.20.100.10; -; 2.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR InterPro; IPR042154; Death_UNC5C.
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; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR InterPro; IPR037936; UNC5.
DR InterPro; IPR033772; UPA.
DR InterPro; IPR000906; ZU5_dom.
DR PANTHER; PTHR12582; PTHR12582; 1.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00090; TSP_1; 1.
DR Pfam; PF17217; UPA; 1.
DR Pfam; PF00791; ZU5; 1.
DR SMART; SM00005; DEATH; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00209; TSP1; 2.
DR SMART; SM00218; ZU5; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR SUPFAM; SSF82895; SSF82895; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS50092; TSP1; 2.
DR PROSITE; PS51145; ZU5; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Cell membrane; Cell projection;
KW Developmental protein; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Synapse; Synaptosome; Transmembrane; Transmembrane helix.
FT SIGNAL 1..40
FT /evidence="ECO:0000255"
FT CHAIN 41..931
FT /note="Netrin receptor UNC5C"
FT /id="PRO_0000036076"
FT TOPO_DOM 41..380
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 402..931
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 62..159
FT /note="Ig-like"
FT DOMAIN 161..256
FT /note="Ig-like C2-type"
FT DOMAIN 260..314
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 316..368
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 530..673
FT /note="ZU5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00485"
FT DOMAIN 850..929
FT /note="Death"
FT REGION 402..931
FT /note="Required for netrin-mediated axon repulsion of
FT neuronal growth cones"
FT /evidence="ECO:0000269|PubMed:22685302"
FT REGION 694..712
FT /note="Interaction with DCC"
FT /evidence="ECO:0000269|PubMed:10399920"
FT SITE 415..416
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250|UniProtKB:Q761X5"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 568
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:11533026"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 83..144
FT /evidence="ECO:0000250|UniProtKB:Q6ZN44"
FT DISULFID 95..142
FT /evidence="ECO:0000250|UniProtKB:Q6ZN44"
FT DISULFID 188..239
FT /evidence="ECO:0000250|UniProtKB:Q6ZN44"
FT DISULFID 272..309
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 276..313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 287..299
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 328..362
FT /evidence="ECO:0000250|UniProtKB:Q6ZN44"
FT DISULFID 332..367
FT /evidence="ECO:0000250|UniProtKB:Q6ZN44"
FT DISULFID 340..352
FT /evidence="ECO:0000250|UniProtKB:Q6ZN44"
FT VAR_SEQ 370
FT /note="A -> GFIYPISTEHRPQNEYGFSS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011702"
FT MUTAGEN 568
FT /note="Y->F: Abolishes interaction with PTPN11, leading to
FT an increased level of phosphorylation."
FT /evidence="ECO:0000269|PubMed:11533026"
FT CONFLICT 16
FT /note="L -> I (in Ref. 2; BAC27495)"
FT /evidence="ECO:0000305"
FT CONFLICT 733
FT /note="H -> R (in Ref. 2; BAC27495)"
FT /evidence="ECO:0000305"
FT CONFLICT 924
FT /note="S -> Y (in Ref. 2; BAC27495)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 931 AA; 103063 MW; 8A5D951A4EECA179 CRC64;
MRKGLRATAA RCGLGLGYLL QMLVLPALAL LSASGTGSAA QDDEFFHELP ETFPSDPPEP
LPHFLIEPEE AYIVKNKPVN LYCKASPATQ IYFKCNSEWV HQKDHVVDER VDETSGLIVR
EVSIEISRQQ VEELFGPEDY WCQCVAWSSA GTTKSRKAYV RIAYLRKTFE QEPLGKEVSL
EQEVLLQCRP PEGIPVAEVE WLKNEDIIDP AEDRNFYITI DHNLIIKQAR LSDTANYTCV
AKNIVAKRKS TTATVIVYVN GGWSTWTEWS VCNSRCGRGY QKRTRTCTNP APLNGGAFCE
GQSVQKIACT TLCPVDGRWT SWSKWSTCGT ECTHWRRREC TAPAPKNGGK DCDGLVLQSK
NCTDGLCMQA APDSDDVALY VGIVIAVTVC LAITVVVALF VYRKNHRDFE SDIIDSSALN
GGFQPVNIKA ARQDLLAVPP DLTSAAAMYR GPVYALHDVS DKIPMTNSPI LDPLPNLKIK
VYNSSGAVTP QDDLAEFSSK LSPQMTQSLL ENEALNLKNQ SLARQTDPSC TAFGTFNSLG
GHLIIPNSGV SLLIPAGAIP QGRVYEMYVT VHRKENMRPP MEDSQTLLTP VVSCGPPGAL
LTRPVILTLH HCADPSTEDW KIQLKNQAVQ GQWEDVVVVG EENFTTPCYI QLDAEACHIL
TENLSTYALV GQSTTKAAAK RLKLAIFGPL CCSSLEYSIR VYCLDDTQDA LKEVLQLERQ
MGGQLLEEPK ALHFKGSIHN LRLSIHDIAH SLWKSKLLAK YQEIPFYHIW SGSQRNLHCT
FTLERLSLNT VELVCKLCVR QVEGEGQIFQ LNCTVSEEPT GIDLPLLDPA STITTVTGPS
AFSIPLPIRQ KLCSSLDAPQ TRGHDWRMLA HKLNLDRYLN YFATKSSPTG VILDLWEAQN
FPDGNLSMLA AVLEEMGRHE TVVSLAAEGQ Y
