UNC5B_HUMAN
ID UNC5B_HUMAN Reviewed; 945 AA.
AC Q8IZJ1; Q5T3R9; Q5T3S0; Q86SN3; Q8N1Y2; Q9H9F3;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Netrin receptor UNC5B;
DE AltName: Full=Protein unc-5 homolog 2;
DE AltName: Full=Protein unc-5 homolog B;
DE AltName: Full=p53-regulated receptor for death and life protein 1 {ECO:0000303|PubMed:12598906};
DE Short=p53RDL1 {ECO:0000303|PubMed:12598906};
DE Flags: Precursor;
GN Name=UNC5B;
GN Synonyms=P53RDL1 {ECO:0000303|PubMed:12598906},
GN UNC5H2 {ECO:0000303|PubMed:12359238}; ORFNames=UNQ1883/PRO4326;
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 2), TISSUE SPECIFICITY, AND INTERACTION
RP WITH GNAI2.
RC TISSUE=Lung;
RX PubMed=12359238; DOI=10.1016/s0006-291x(02)02277-5;
RA Komatsuzaki K., Dalvin S., Kinane T.B.;
RT "Modulation of G(ialpha(2)) signaling by the axonal guidance molecule
RT UNC5H2.";
RL Biochem. Biophys. Res. Commun. 297:898-905(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND MUTAGENESIS OF
RP ASP-412.
RX PubMed=12598906; DOI=10.1038/ncb943;
RA Tanikawa C., Matsuda K., Fukuda S., Nakamura Y., Arakawa H.;
RT "p53RDL1 regulates of p53-dependent apoptosis.";
RL Nat. Cell Biol. 5:216-223(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala, Teratocarcinoma, and Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP DOWN-REGULATION IN CANCER.
RX PubMed=12655055; DOI=10.1073/pnas.0738063100;
RA Thiebault K., Mazelin L., Pays L., Llambi F., Joly M.-O., Scoazec J.-Y.,
RA Saurin J.-C., Romeo G., Mehlen P.;
RT "The netrin-1 receptors UNC5H are putative tumor suppressors controlling
RT cell death commitment.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:4173-4178(2003).
RN [8]
RP INTERACTION WITH DAPK1.
RX PubMed=15729359; DOI=10.1038/sj.emboj.7600584;
RA Llambi F., Lourenco F.C., Gozuacik D., Guix C., Pays L., Del Rio G.,
RA Kimchi A., Mehlen P.;
RT "The dependence receptor UNC5H2 mediates apoptosis through DAP-kinase.";
RL EMBO J. 24:1192-1201(2005).
RN [9]
RP INTERACTION WITH DAPK1.
RX PubMed=18582460; DOI=10.1016/j.yexcr.2008.06.001;
RA Maisse C., Rossin A., Cahuzac N., Paradisi A., Klein C., Haillot M.L.,
RA Herincs Z., Mehlen P., Hueber A.O.;
RT "Lipid raft localization and palmitoylation: identification of two
RT requirements for cell death induction by the tumor suppressors UNC5H.";
RL Exp. Cell Res. 314:2544-2552(2008).
RN [10]
RP INTERACTION WITH FLRT2 AND FLRT3, AND SUBCELLULAR LOCATION.
RX PubMed=25374360; DOI=10.1016/j.neuron.2014.10.008;
RA Seiradake E., del Toro D., Nagel D., Cop F., Haertl R., Ruff T.,
RA Seyit-Bremer G., Harlos K., Border E.C., Acker-Palmer A., Jones E.Y.,
RA Klein R.;
RT "FLRT structure: balancing repulsion and cell adhesion in cortical and
RT vascular development.";
RL Neuron 84:370-385(2014).
RN [11]
RP INTERACTION WITH FLRT3, AND SUBUNIT.
RX PubMed=26235030; DOI=10.1016/j.str.2015.06.024;
RA Lu Y.C., Nazarko O.V., Sando R. III, Salzman G.S., Suedhof T.C., Arac D.;
RT "Structural basis of latrophilin-FLRT-UNC5 interaction in cell adhesion.";
RL Structure 23:1678-1691(2015).
CC -!- FUNCTION: Receptor for netrin required for axon guidance. Mediates axon
CC repulsion of neuronal growth cones in the developing nervous system
CC upon ligand binding. Axon repulsion in growth cones may be caused by
CC its association with DCC that may trigger signaling for repulsion (By
CC similarity). Functions as netrin receptor that negatively regulates
CC vascular branching during angiogenesis. Mediates retraction of tip cell
CC filopodia on endothelial growth cones in response to netrin (By
CC similarity). It also acts as a dependence receptor required for
CC apoptosis induction when not associated with netrin ligand
CC (PubMed:12598906). Mediates apoptosis by activating DAPK1. In the
CC absence of NTN1, activates DAPK1 by reducing its autoinhibitory
CC phosphorylation at Ser-308 thereby increasing its catalytic activity
CC (By similarity). {ECO:0000250|UniProtKB:O08722,
CC ECO:0000250|UniProtKB:Q8K1S3, ECO:0000269|PubMed:12598906}.
CC -!- SUBUNIT: Interacts with the cytoplasmic part of DCC (By similarity).
CC Interacts with GNAI2 via its cytoplasmic part (PubMed:12359238).
CC Interacts (via death domain) with DAPK1 (via death domain)
CC (PubMed:15729359, PubMed:18582460). Interacts (via extracellular
CC domain) with FLRT3 (via extracellular domain); the interaction is
CC direct (PubMed:26235030). Interacts (via extracellular domain) with
CC FLRT2 and FLRT3 (via extracellular domain), but has higher affinity for
CC FLRT3 (PubMed:25374360). Identified in a complex with FLRT3 and ADGRL3;
CC does not interact with ADGRL3 by itself (PubMed:26235030).
CC {ECO:0000250|UniProtKB:O08722, ECO:0000269|PubMed:12359238,
CC ECO:0000269|PubMed:15729359, ECO:0000269|PubMed:18582460,
CC ECO:0000269|PubMed:25374360}.
CC -!- INTERACTION:
CC Q8IZJ1; Q8CGU4: Agap2; Xeno; NbExp=9; IntAct=EBI-4409075, EBI-4409108;
CC Q8IZJ1-2; O95631: NTN1; NbExp=2; IntAct=EBI-10832046, EBI-2678626;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25374360};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:O08722}.
CC Membrane raft {ECO:0000250|UniProtKB:O08722}. Note=Associated with
CC lipid rafts. {ECO:0000250|UniProtKB:O08722}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8IZJ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IZJ1-2; Sequence=VSP_011698;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain. Also expressed at lower
CC level in developing lung, cartilage, kidney and hematopoietic and
CC immune tissues. {ECO:0000269|PubMed:12359238}.
CC -!- INDUCTION: By p53/TP53.
CC -!- PTM: Phosphorylated on cytoplasmic tyrosine residues. {ECO:0000250}.
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:0000269|PubMed:12598906}.
CC -!- PTM: Palmitoylation is required for pro-apoptotic activity, but not for
CC location at lipid rafts. {ECO:0000250|UniProtKB:O08722}.
CC -!- MISCELLANEOUS: Down-regulated in multiple cancers including colorectal,
CC breast, ovary, uterus, stomach, lung, or kidney cancers.
CC -!- SIMILARITY: Belongs to the unc-5 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14276.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC04382.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY126437; AAM95701.1; -; mRNA.
DR EMBL; AB096256; BAC57998.1; -; mRNA.
DR EMBL; AY358351; AAQ88717.1; -; mRNA.
DR EMBL; AK022859; BAB14276.1; ALT_INIT; mRNA.
DR EMBL; AK094595; BAC04382.1; ALT_INIT; mRNA.
DR EMBL; AK128132; BAG54634.1; -; mRNA.
DR EMBL; AL359384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471083; EAW54420.1; -; Genomic_DNA.
DR EMBL; CH471083; EAW54421.1; -; Genomic_DNA.
DR CCDS; CCDS58083.1; -. [Q8IZJ1-2]
DR CCDS; CCDS7309.1; -. [Q8IZJ1-1]
DR RefSeq; NP_001231818.1; NM_001244889.1. [Q8IZJ1-2]
DR RefSeq; NP_734465.2; NM_170744.4. [Q8IZJ1-1]
DR AlphaFoldDB; Q8IZJ1; -.
DR SMR; Q8IZJ1; -.
DR BioGRID; 128567; 72.
DR CORUM; Q8IZJ1; -.
DR DIP; DIP-46275N; -.
DR IntAct; Q8IZJ1; 15.
DR MINT; Q8IZJ1; -.
DR STRING; 9606.ENSP00000334329; -.
DR GlyGen; Q8IZJ1; 3 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q8IZJ1; -.
DR PhosphoSitePlus; Q8IZJ1; -.
DR SwissPalm; Q8IZJ1; -.
DR BioMuta; UNC5B; -.
DR DMDM; 54036589; -.
DR EPD; Q8IZJ1; -.
DR jPOST; Q8IZJ1; -.
DR MassIVE; Q8IZJ1; -.
DR MaxQB; Q8IZJ1; -.
DR PaxDb; Q8IZJ1; -.
DR PeptideAtlas; Q8IZJ1; -.
DR PRIDE; Q8IZJ1; -.
DR ProteomicsDB; 71355; -. [Q8IZJ1-1]
DR ProteomicsDB; 71356; -. [Q8IZJ1-2]
DR Antibodypedia; 2329; 178 antibodies from 32 providers.
DR DNASU; 219699; -.
DR Ensembl; ENST00000335350.10; ENSP00000334329.6; ENSG00000107731.12. [Q8IZJ1-1]
DR Ensembl; ENST00000373192.4; ENSP00000362288.4; ENSG00000107731.12. [Q8IZJ1-2]
DR GeneID; 219699; -.
DR KEGG; hsa:219699; -.
DR MANE-Select; ENST00000335350.10; ENSP00000334329.6; NM_170744.5; NP_734465.2.
DR UCSC; uc001jro.4; human. [Q8IZJ1-1]
DR CTD; 219699; -.
DR DisGeNET; 219699; -.
DR GeneCards; UNC5B; -.
DR HGNC; HGNC:12568; UNC5B.
DR HPA; ENSG00000107731; Tissue enhanced (brain).
DR MIM; 607870; gene.
DR neXtProt; NX_Q8IZJ1; -.
DR OpenTargets; ENSG00000107731; -.
DR PharmGKB; PA37205; -.
DR VEuPathDB; HostDB:ENSG00000107731; -.
DR eggNOG; KOG1480; Eukaryota.
DR GeneTree; ENSGT00950000182815; -.
DR HOGENOM; CLU_014383_0_0_1; -.
DR InParanoid; Q8IZJ1; -.
DR OMA; TIEHNLI; -.
DR OrthoDB; 334938at2759; -.
DR PhylomeDB; Q8IZJ1; -.
DR TreeFam; TF316767; -.
DR PathwayCommons; Q8IZJ1; -.
DR Reactome; R-HSA-373752; Netrin-1 signaling.
DR Reactome; R-HSA-418886; Netrin mediated repulsion signals.
DR Reactome; R-HSA-418889; Caspase activation via Dependence Receptors in the absence of ligand.
DR SignaLink; Q8IZJ1; -.
DR SIGNOR; Q8IZJ1; -.
DR BioGRID-ORCS; 219699; 10 hits in 1078 CRISPR screens.
DR ChiTaRS; UNC5B; human.
DR GenomeRNAi; 219699; -.
DR Pharos; Q8IZJ1; Tbio.
DR PRO; PR:Q8IZJ1; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q8IZJ1; protein.
DR Bgee; ENSG00000107731; Expressed in inferior vagus X ganglion and 187 other tissues.
DR Genevisible; Q8IZJ1; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005042; F:netrin receptor activity; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0033564; P:anterior/posterior axon guidance; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IMP:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:UniProtKB.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IMP:UniProtKB.
DR CDD; cd08802; Death_UNC5B; 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; IPR042156; Death_UNC5B.
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; 2.
DR Pfam; PF17217; UPA; 1.
DR Pfam; PF00791; ZU5; 1.
DR SMART; SM00005; DEATH; 1.
DR SMART; SM00409; IG; 2.
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; Angiogenesis; Apoptosis; Cell membrane;
KW Developmental protein; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..945
FT /note="Netrin receptor UNC5B"
FT /id="PRO_0000036071"
FT TOPO_DOM 27..377
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 399..945
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 48..145
FT /note="Ig-like"
FT DOMAIN 147..242
FT /note="Ig-like C2-type"
FT DOMAIN 246..300
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 302..354
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 543..686
FT /note="ZU5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00485"
FT DOMAIN 865..943
FT /note="Death"
FT REGION 689..838
FT /note="UPA domain"
FT /evidence="ECO:0000250"
FT REGION 707..725
FT /note="Interaction with DCC"
FT /evidence="ECO:0000250|UniProtKB:O08722"
FT SITE 412..413
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000305|PubMed:12598906"
FT MOD_RES 581
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O08747"
FT LIPID 403
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:O08722"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 69..130
FT /evidence="ECO:0000250|UniProtKB:Q6ZN44"
FT DISULFID 81..128
FT /evidence="ECO:0000250|UniProtKB:Q6ZN44"
FT DISULFID 174..225
FT /evidence="ECO:0000250|UniProtKB:Q6ZN44"
FT DISULFID 258..295
FT /evidence="ECO:0000250"
FT DISULFID 262..299
FT /evidence="ECO:0000250"
FT DISULFID 273..285
FT /evidence="ECO:0000250"
FT DISULFID 314..348
FT /evidence="ECO:0000250|UniProtKB:Q6ZN44"
FT DISULFID 318..353
FT /evidence="ECO:0000250|UniProtKB:Q6ZN44"
FT DISULFID 326..338
FT /evidence="ECO:0000250|UniProtKB:Q6ZN44"
FT VAR_SEQ 356..367
FT /note="NKKTLSDPNSHL -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12359238"
FT /id="VSP_011698"
FT VARIANT 242
FT /note="I -> V (in dbSNP:rs34957097)"
FT /id="VAR_052472"
FT VARIANT 516
FT /note="A -> T (in dbSNP:rs10509332)"
FT /id="VAR_019730"
FT MUTAGEN 412
FT /note="D->N: Abolishes cleavage by caspase-3 and subsequent
FT induction of apoptosis."
FT /evidence="ECO:0000269|PubMed:12598906"
FT CONFLICT 483
FT /note="K -> E (in Ref. 3; BAC04382)"
FT /evidence="ECO:0000305"
FT CONFLICT 851
FT /note="L -> P (in Ref. 3; BAB14276)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 945 AA; 103638 MW; 56064E335F323447 CRC64;
MGARSGARGA LLLALLLCWD PRLSQAGTDS GSEVLPDSFP SAPAEPLPYF LQEPQDAYIV
KNKPVELRCR AFPATQIYFK CNGEWVSQND HVTQEGLDEA TGLRVREVQI EVSRQQVEEL
FGLEDYWCQC VAWSSAGTTK SRRAYVRIAY LRKNFDQEPL GKEVPLDHEV LLQCRPPEGV
PVAEVEWLKN EDVIDPTQDT NFLLTIDHNL IIRQARLSDT ANYTCVAKNI VAKRRSTTAT
VIVYVNGGWS SWAEWSPCSN RCGRGWQKRT RTCTNPAPLN GGAFCEGQAF QKTACTTICP
VDGAWTEWSK WSACSTECAH WRSRECMAPP PQNGGRDCSG TLLDSKNCTD GLCMQNKKTL
SDPNSHLLEA SGDAALYAGL VVAIFVVVAI LMAVGVVVYR RNCRDFDTDI TDSSAALTGG
FHPVNFKTAR PSNPQLLHPS VPPDLTASAG IYRGPVYALQ DSTDKIPMTN SPLLDPLPSL
KVKVYSSSTT GSGPGLADGA DLLGVLPPGT YPSDFARDTH FLHLRSASLG SQQLLGLPRD
PGSSVSGTFG CLGGRLSIPG TGVSLLVPNG AIPQGKFYEM YLLINKAEST LPLSEGTQTV
LSPSVTCGPT GLLLCRPVIL TMPHCAEVSA RDWIFQLKTQ AHQGHWEEVV TLDEETLNTP
CYCQLEPRAC HILLDQLGTY VFTGESYSRS AVKRLQLAVF APALCTSLEY SLRVYCLEDT
PVALKEVLEL ERTLGGYLVE EPKPLMFKDS YHNLRLSLHD LPHAHWRSKL LAKYQEIPFY
HIWSGSQKAL HCTFTLERHS LASTELTCKI CVRQVEGEGQ IFQLHTTLAE TPAGSLDTLC
SAPGSTVTTQ LGPYAFKIPL SIRQKICNSL DAPNSRGNDW RMLAQKLSMD RYLNYFATKA
SPTGVILDLW EALQQDDGDL NSLASALEEM GKSEMLVAVA TDGDC
