UNC5B_MOUSE
ID UNC5B_MOUSE Reviewed; 945 AA.
AC Q8K1S3; Q3U4F2; Q6PFH0; Q80Y85; Q9D398;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Netrin receptor UNC5B;
DE AltName: Full=Protein unc-5 homolog 2;
DE AltName: Full=Protein unc-5 homolog B;
DE Flags: Precursor;
GN Name=Unc5b; Synonyms=Unc5h2;
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), AND TISSUE SPECIFICITY.
RX PubMed=12351186; DOI=10.1016/s0925-4773(02)00248-4;
RA Engelkamp D.;
RT "Cloning of three mouse Unc5 genes and their expression patterns at mid-
RT gestation.";
RL Mech. Dev. 118:191-197(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Medulla oblongata;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=12799072; DOI=10.1016/s1567-133x(03)00047-4;
RA Dalvin S., Anselmo M.A., Prodhan P., Komatsuzaki K., Schnitzer J.J.,
RA Kinane T.B.;
RT "Expression of Netrin-1 and its two receptors DCC and UNC5H2 in the
RT developing mouse lung.";
RL Gene Expr. Patterns 3:279-283(2003).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=15510105; DOI=10.1038/nature03080;
RA Lu X., Le Noble F., Yuan L., Jiang Q., De Lafarge B., Sugiyama D.,
RA Breant C., Claes F., De Smet F., Thomas J.L., Autiero M., Carmeliet P.,
RA Tessier-Lavigne M., Eichmann A.;
RT "The netrin receptor UNC5B mediates guidance events controlling
RT morphogenesis of the vascular system.";
RL Nature 432:179-186(2004).
RN [6]
RP INTERACTION WITH FLRT3, AND SUBCELLULAR LOCATION.
RX PubMed=19492039; DOI=10.1371/journal.pone.0005742;
RA Karaulanov E., Boettcher R.T., Stannek P., Wu W., Rau M., Ogata S.,
RA Cho K.W.Y., Niehrs C.;
RT "Unc5B interacts with FLRT3 and Rnd1 to modulate cell adhesion in Xenopus
RT embryos.";
RL PLoS ONE 4:E5742-E5742(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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 INTERACTION WITH FLRT2 AND FLRT3, AND SUBCELLULAR LOCATION.
RX PubMed=21673655; DOI=10.1038/emboj.2011.189;
RA Yamagishi S., Hampel F., Hata K., Del Toro D., Schwark M., Kvachnina E.,
RA Bastmeyer M., Yamashita T., Tarabykin V., Klein R., Egea J.;
RT "FLRT2 and FLRT3 act as repulsive guidance cues for Unc5-positive
RT neurons.";
RL EMBO J. 30:2920-2933(2011).
RN [9]
RP INTERACTION WITH FLRT3.
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 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 X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 854-943.
RX PubMed=17139086; DOI=10.1107/s0907444906039369;
RA Handa N., Kukimoto-Niino M., Akasaka R., Murayama K., Terada T., Inoue M.,
RA Yabuki T., Aoki M., Seki E., Matsuda T., Nunokawa E., Tanaka A.,
RA Hayashizaki Y., Kigawa T., Shirouzu M., Yokoyama S.;
RT "Structure of the UNC5H2 death domain.";
RL Acta Crystallogr. D 62:1502-1509(2006).
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 (PubMed:15510105). Mediates
CC retraction of tip cell filopodia on endothelial growth cones in
CC response to netrin (PubMed:15510105). It also acts as a dependence
CC receptor required for apoptosis induction when not associated with
CC netrin ligand. Mediates apoptosis by activating DAPK1. In the absence
CC of NTN1, activates DAPK1 by reducing its autoinhibitory phosphorylation
CC at Ser-308 thereby increasing its catalytic activity (By similarity).
CC {ECO:0000250|UniProtKB:O08722, ECO:0000269|PubMed:15510105}.
CC -!- SUBUNIT: Interacts with the cytoplasmic part of DCC (By similarity).
CC Interacts with GNAI2 via its cytoplasmic part. Interacts (via death
CC domain) with DAPK1 (via death domain) (By similarity). Interacts (via
CC extracellular domain) with FLRT2 and FLRT3 (via extracellular domain),
CC but has higher affinity for FLRT3 (PubMed:19492039, PubMed:21673655,
CC PubMed:22405201, PubMed:25374360). Identified in a complex with FLRT3
CC and ADGRL3; does not interact with ADGRL3 by itself (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:O08722,
CC ECO:0000250|UniProtKB:Q8IZJ1, ECO:0000269|PubMed:19492039,
CC ECO:0000269|PubMed:21673655, ECO:0000269|PubMed:22405201,
CC ECO:0000269|PubMed:25374360}.
CC -!- INTERACTION:
CC Q8K1S3; Q7TNP2: Ppp2r1b; NbExp=2; IntAct=EBI-4396886, EBI-4396871;
CC Q8K1S3-1; O09118: Ntn1; NbExp=4; IntAct=EBI-11658250, EBI-1798844;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19492039,
CC ECO:0000269|PubMed:21673655, ECO:0000269|PubMed:25374360}; Single-pass
CC type I membrane protein {ECO:0000250|UniProtKB:O08722}. Membrane raft
CC {ECO:0000250|UniProtKB:O08722}. Note=Associated with lipid rafts.
CC {ECO:0000250|UniProtKB:O08722}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K1S3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K1S3-2; Sequence=VSP_011699;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain. Expressed in lung during
CC late development. Expressed during early blood vessel formation, in the
CC semicircular canal and in a dorsal to ventral gradient in the retina.
CC {ECO:0000269|PubMed:12351186, ECO:0000269|PubMed:12799072,
CC ECO:0000269|PubMed:15510105}.
CC -!- PTM: Phosphorylated on cytoplasmic tyrosine residues. {ECO:0000250}.
CC -!- PTM: Palmitoylation is required for pro-apoptotic activity, but not for
CC location at lipid rafts. {ECO:0000250|UniProtKB:O08722}.
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:O08722}.
CC -!- DISRUPTION PHENOTYPE: Complete embryonic lethality, due to defects in
CC blood vessel development that lead to heart failure. Mutant embryos
CC display increased branching of the internal carotid artery and of blood
CC vessels in the nervous system, including thinner and more highly
CC branched brain capillaries. Endothelial tip cells present an increased
CC number of filopodia. {ECO:0000269|PubMed:15510105}.
CC -!- SIMILARITY: Belongs to the unc-5 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH48162.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ487853; CAD32251.1; -; mRNA.
DR EMBL; AK018177; BAB31108.1; -; mRNA.
DR EMBL; AK154271; BAE32479.1; -; mRNA.
DR EMBL; BC048162; AAH48162.1; ALT_INIT; mRNA.
DR EMBL; BC057560; AAH57560.1; -; mRNA.
DR CCDS; CCDS23872.1; -. [Q8K1S3-1]
DR CCDS; CCDS88011.1; -. [Q8K1S3-2]
DR RefSeq; NP_084046.2; NM_029770.2. [Q8K1S3-1]
DR RefSeq; XP_006513091.1; XM_006513028.3.
DR PDB; 1WMG; X-ray; 2.10 A; A/B/C/D/E/F=854-943.
DR PDB; 6OOL; X-ray; 2.80 A; A=25-374.
DR PDBsum; 1WMG; -.
DR PDBsum; 6OOL; -.
DR AlphaFoldDB; Q8K1S3; -.
DR SMR; Q8K1S3; -.
DR BioGRID; 223296; 9.
DR IntAct; Q8K1S3; 3.
DR STRING; 10090.ENSMUSP00000077080; -.
DR GlyGen; Q8K1S3; 2 sites.
DR iPTMnet; Q8K1S3; -.
DR PhosphoSitePlus; Q8K1S3; -.
DR jPOST; Q8K1S3; -.
DR MaxQB; Q8K1S3; -.
DR PaxDb; Q8K1S3; -.
DR PRIDE; Q8K1S3; -.
DR ProteomicsDB; 275382; -. [Q8K1S3-1]
DR ProteomicsDB; 275383; -. [Q8K1S3-2]
DR ABCD; Q8K1S3; 21 sequenced antibodies.
DR Antibodypedia; 2329; 178 antibodies from 32 providers.
DR DNASU; 107449; -.
DR Ensembl; ENSMUST00000077925; ENSMUSP00000077080; ENSMUSG00000020099. [Q8K1S3-1]
DR Ensembl; ENSMUST00000218637; ENSMUSP00000151251; ENSMUSG00000020099. [Q8K1S3-2]
DR GeneID; 107449; -.
DR KEGG; mmu:107449; -.
DR UCSC; uc007ffd.1; mouse. [Q8K1S3-2]
DR UCSC; uc007ffe.1; mouse. [Q8K1S3-1]
DR CTD; 219699; -.
DR MGI; MGI:894703; Unc5b.
DR VEuPathDB; HostDB:ENSMUSG00000020099; -.
DR eggNOG; KOG1480; Eukaryota.
DR GeneTree; ENSGT00950000182815; -.
DR HOGENOM; CLU_014383_0_0_1; -.
DR InParanoid; Q8K1S3; -.
DR OMA; TIEHNLI; -.
DR OrthoDB; 334938at2759; -.
DR PhylomeDB; Q8K1S3; -.
DR TreeFam; TF316767; -.
DR BioGRID-ORCS; 107449; 0 hits in 76 CRISPR screens.
DR ChiTaRS; Unc5b; mouse.
DR EvolutionaryTrace; Q8K1S3; -.
DR PRO; PR:Q8K1S3; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8K1S3; protein.
DR Bgee; ENSMUSG00000020099; Expressed in dorsal horn of spinal cord and 251 other tissues.
DR Genevisible; Q8K1S3; MM.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005042; F:netrin receptor activity; ISO:MGI.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0033564; P:anterior/posterior axon guidance; IMP:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007411; P:axon guidance; ISO:MGI.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISO:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISO:MGI.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISO:MGI.
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; PS50017; DEATH_DOMAIN; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS50092; TSP1; 2.
DR PROSITE; PS51145; ZU5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 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_0000036072"
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 153..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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
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:0000250|UniProtKB:O08722"
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="NQRTLNDPKSHP -> T (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011699"
FT CONFLICT 238
FT /note="T -> A (in Ref. 2; BAB31108)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="V -> E (in Ref. 2; BAB31108)"
FT /evidence="ECO:0000305"
FT CONFLICT 679
FT /note="T -> S (in Ref. 2; BAB31108)"
FT /evidence="ECO:0000305"
FT CONFLICT 874
FT /note="N -> D (in Ref. 2; BAB31108)"
FT /evidence="ECO:0000305"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:6OOL"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:6OOL"
FT STRAND 65..73
FT /evidence="ECO:0007829|PDB:6OOL"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:6OOL"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:6OOL"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:6OOL"
FT HELIX 114..119
FT /evidence="ECO:0007829|PDB:6OOL"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:6OOL"
FT STRAND 126..133
FT /evidence="ECO:0007829|PDB:6OOL"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:6OOL"
FT STRAND 144..151
FT /evidence="ECO:0007829|PDB:6OOL"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:6OOL"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:6OOL"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:6OOL"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:6OOL"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:6OOL"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:6OOL"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:6OOL"
FT STRAND 221..228
FT /evidence="ECO:0007829|PDB:6OOL"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:6OOL"
FT STRAND 239..245
FT /evidence="ECO:0007829|PDB:6OOL"
FT STRAND 259..270
FT /evidence="ECO:0007829|PDB:6OOL"
FT STRAND 289..297
FT /evidence="ECO:0007829|PDB:6OOL"
FT HELIX 860..871
FT /evidence="ECO:0007829|PDB:1WMG"
FT HELIX 873..875
FT /evidence="ECO:0007829|PDB:1WMG"
FT HELIX 880..886
FT /evidence="ECO:0007829|PDB:1WMG"
FT HELIX 890..892
FT /evidence="ECO:0007829|PDB:1WMG"
FT HELIX 893..897
FT /evidence="ECO:0007829|PDB:1WMG"
FT HELIX 902..913
FT /evidence="ECO:0007829|PDB:1WMG"
FT TURN 917..919
FT /evidence="ECO:0007829|PDB:1WMG"
FT HELIX 920..929
FT /evidence="ECO:0007829|PDB:1WMG"
FT HELIX 933..941
FT /evidence="ECO:0007829|PDB:1WMG"
SQ SEQUENCE 945 AA; 103739 MW; 80E896F0F0E06012 CRC64;
MRARSGVRSA LLLALLLCWD PTPSLAGVDS AGQVLPDSYP SAPAEQLPYF LLEPQDAYIV
KNKPVELHCR AFPATQIYFK CNGEWVSQND HVTQESLDEA TGLRVREVQI EVSRQQVEEL
FGLEDYWCQC VAWSSSGTTK SRRAYIRIAY LRKNFDQEPL AKEVPLDHEV LLQCRPPEGV
PVAEVEWLKN EDVIDPAQDT NFLLTIDHNL IIRQARLSDT ANYTCVAKNI VAKRRSTTAT
VIVYVNGGWS SWAEWSPCSN RCGRGWQKRT RTCTNPAPLN GGAFCEGQAF QKTACTTVCP
VDGAWTEWSK WSACSTECAH WRSRECMAPP PQNGGRDCSG TLLDSKNCTD GLCVLNQRTL
NDPKSHPLET SGDVALYAGL VVAVFVVVAV LMAVGVIVYR RNCRDFDTDI TDSSAALTGG
FHPVNFKTAR PNNPQLLHPS APPDLTASAG IYRGPVYALQ DSADKIPMTN SPLLDPLPSL
KIKVYNSSTI GSGSGLADGA DLLGVLPPGT YPGDFSRDTH FLHLRSASLG SQHLLGLPRD
PSSSVSGTFG CLGGRLSLPG TGVSLLVPNG AIPQGKFYDL YLHINKAEST LPLSEGSQTV
LSPSVTCGPT GLLLCRPVVL TVPHCAEVIA GDWIFQLKTQ AHQGHWEEVV TLDEETLNTP
CYCQLEAKSC HILLDQLGTY VFMGESYSRS AVKRLQLAIF APALCTSLEY SLRVYCLEDT
PVALKEVLEL ERTLGGYLVE EPKPLLFKDS YHNLRLSLHD IPHAHWRSKL LAKYQEIPFY
HVWNGSQRAL HCTFTLERHS LASTEFTCKV CVRQVEGEGQ IFQLHTTLAE TPAGSLDALC
SAPGNAITTQ LGPYAFKIPL SIRQKICSSL DAPNSRGNDW RLLAQKLSMD RYLNYFATKA
SPTGVILDLW EARQQDDGDL NSLASALEEM GKSEMLVAMA TDGDC
