CNTN2_HUMAN
ID CNTN2_HUMAN Reviewed; 1040 AA.
AC Q02246; P78432; Q5T054;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Contactin-2;
DE AltName: Full=Axonal glycoprotein TAG-1;
DE AltName: Full=Axonin-1;
DE AltName: Full=Transient axonal glycoprotein 1;
DE Short=TAX-1;
DE Flags: Precursor;
GN Name=CNTN2; Synonyms=AXT, TAG1, TAX1;
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].
RC TISSUE=Brain;
RX PubMed=8425542; DOI=10.1111/j.1432-1033.1993.tb19902.x;
RA Hasler T.H., Rader C., Stoeckli E.T., Zuellig R.A., Sonderegger P.;
RT "cDNA cloning, structural features, and eucaryotic expression of human TAG-
RT 1/axonin-1.";
RL Eur. J. Biochem. 211:329-339(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8307567; DOI=10.1016/s0888-7543(05)80357-x;
RA Tsiotra C.P., Karagogeos D., Theodorakis K., Michaelidis M.T., Modi W.S.,
RA Furley J.A., Jessel M.T., Papamatheakis J.;
RT "Isolation of the cDNA and chromosomal localization of the gene (TAX1)
RT encoding the human axonal glycoprotein TAG-1.";
RL Genomics 18:562-567(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RX PubMed=8586412; DOI=10.1006/geno.1995.9892;
RA Kozlov S.V., Giger R.J., Hasler T., Korvatska E., Schorderet D.F.,
RA Sonderegger P.;
RT "The human TAX1 gene encoding the axon-associated cell adhesion molecule
RT TAG-1/axonin-1: genomic structure and basic promoter.";
RL Genomics 30:141-148(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-136.
RC TISSUE=Placenta;
RA Tsiotra C.P., Theodorakis C., Michaelidis M.T., Mamalaki C., Karagogeus D.,
RA Papamatheakis J.;
RT "Molecular structure and functional studies of the TAX-1 promoter.";
RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 31-45.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-904.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [8]
RP INVOLVEMENT IN FAME5, AND FUNCTION.
RX PubMed=23518707; DOI=10.1093/brain/awt068;
RA Stogmann E., Reinthaler E., Eltawil S., El Etribi M.A., Hemeda M.,
RA El Nahhas N., Gaber A.M., Fouad A., Edris S., Benet-Pages A., Eck S.H.,
RA Pataraia E., Mei D., Brice A., Lesage S., Guerrini R., Zimprich F.,
RA Strom T.M., Zimprich A.;
RT "Autosomal recessive cortical myoclonic tremor and epilepsy: association
RT with a mutation in the potassium channel associated gene CNTN2.";
RL Brain 136:1155-1160(2013).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.07 ANGSTROMS) OF 34-414, AND DISULFIDE BONDS.
RX PubMed=17766378; DOI=10.1110/ps.072802707;
RA Mortl M., Sonderegger P., Diederichs K., Welte W.;
RT "The crystal structure of the ligand-binding module of human TAG-1 suggests
RT a new mode of homophilic interaction.";
RL Protein Sci. 16:2174-2183(2007).
CC -!- FUNCTION: In conjunction with another transmembrane protein, CNTNAP2,
CC contributes to the organization of axonal domains at nodes of Ranvier
CC by maintaining voltage-gated potassium channels at the juxtaparanodal
CC region. May be involved in cell adhesion.
CC {ECO:0000269|PubMed:23518707}.
CC -!- INTERACTION:
CC Q02246; P05067: APP; NbExp=3; IntAct=EBI-4397248, EBI-77613;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC Note=Attached to the neuronal membrane by a GPI-anchor and is also
CC released from neurons.
CC -!- DISEASE: Epilepsy, familial adult myoclonic, 5 (FAME5) [MIM:615400]: A
CC form of familial myoclonic epilepsy, a neurologic disorder
CC characterized by cortical hand tremors, myoclonic jerks and occasional
CC generalized or focal seizures with a non-progressive or very slowly
CC progressive disease course. Usually, myoclonic tremor is the presenting
CC symptom, characterized by tremulous finger movements and myoclonic
CC jerks of the limbs increased by action and posture. In a minority of
CC patients, seizures are the presenting symptom. Some patients exhibit
CC mild cognitive impairment. FAME5 is characterized by onset of seizures
CC in adolescence, followed by the development of cortical myoclonic
CC tremor later in life. Inheritance is autosomal recessive.
CC {ECO:0000269|PubMed:23518707}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. Contactin
CC family. {ECO:0000305}.
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DR EMBL; X68274; CAA48335.1; -; mRNA.
DR EMBL; X67734; CAA47963.1; -; mRNA.
DR EMBL; X84420; CAA59137.1; -; Genomic_DNA.
DR EMBL; AL583832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X92681; CAA63365.1; -; Genomic_DNA.
DR CCDS; CCDS1449.1; -.
DR PIR; S35508; A49356.
DR RefSeq; NP_001333012.1; NM_001346083.1.
DR RefSeq; NP_005067.1; NM_005076.4.
DR PDB; 2OM5; X-ray; 3.07 A; A=34-414.
DR PDBsum; 2OM5; -.
DR AlphaFoldDB; Q02246; -.
DR SMR; Q02246; -.
DR BioGRID; 112763; 15.
DR IntAct; Q02246; 3.
DR MINT; Q02246; -.
DR STRING; 9606.ENSP00000330633; -.
DR TCDB; 8.A.23.1.3; the basigin (basigin) family.
DR GlyGen; Q02246; 11 sites.
DR iPTMnet; Q02246; -.
DR PhosphoSitePlus; Q02246; -.
DR BioMuta; CNTN2; -.
DR DMDM; 399092; -.
DR MassIVE; Q02246; -.
DR PaxDb; Q02246; -.
DR PeptideAtlas; Q02246; -.
DR PRIDE; Q02246; -.
DR ProteomicsDB; 58068; -.
DR Antibodypedia; 670; 273 antibodies from 32 providers.
DR DNASU; 6900; -.
DR Ensembl; ENST00000331830.7; ENSP00000330633.4; ENSG00000184144.12.
DR Ensembl; ENST00000638378.1; ENSP00000492617.1; ENSG00000184144.12.
DR Ensembl; ENST00000639302.1; ENSP00000491671.1; ENSG00000184144.12.
DR Ensembl; ENST00000640326.1; ENSP00000492495.1; ENSG00000184144.12.
DR GeneID; 6900; -.
DR KEGG; hsa:6900; -.
DR MANE-Select; ENST00000331830.7; ENSP00000330633.4; NM_005076.5; NP_005067.1.
DR UCSC; uc001hbr.4; human.
DR CTD; 6900; -.
DR DisGeNET; 6900; -.
DR GeneCards; CNTN2; -.
DR HGNC; HGNC:2172; CNTN2.
DR HPA; ENSG00000184144; Tissue enriched (brain).
DR MalaCards; CNTN2; -.
DR MIM; 190197; gene.
DR MIM; 615400; phenotype.
DR neXtProt; NX_Q02246; -.
DR OpenTargets; ENSG00000184144; -.
DR Orphanet; 86814; Benign adult familial myoclonic epilepsy.
DR PharmGKB; PA26686; -.
DR VEuPathDB; HostDB:ENSG00000184144; -.
DR eggNOG; KOG3513; Eukaryota.
DR GeneTree; ENSGT00940000159193; -.
DR HOGENOM; CLU_005756_0_0_1; -.
DR InParanoid; Q02246; -.
DR OMA; RIIIQAQ; -.
DR OrthoDB; 655902at2759; -.
DR PhylomeDB; Q02246; -.
DR TreeFam; TF351103; -.
DR PathwayCommons; Q02246; -.
DR Reactome; R-HSA-373760; L1CAM interactions.
DR Reactome; R-HSA-419037; NCAM1 interactions.
DR Reactome; R-HSA-447038; NrCAM interactions.
DR SignaLink; Q02246; -.
DR BioGRID-ORCS; 6900; 14 hits in 1062 CRISPR screens.
DR ChiTaRS; CNTN2; human.
DR EvolutionaryTrace; Q02246; -.
DR GeneWiki; CNTN2; -.
DR GenomeRNAi; 6900; -.
DR Pharos; Q02246; Tbio.
DR PRO; PR:Q02246; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q02246; protein.
DR Bgee; ENSG00000184144; Expressed in inferior vagus X ganglion and 146 other tissues.
DR ExpressionAtlas; Q02246; baseline and differential.
DR Genevisible; Q02246; HS.
DR GO; GO:0099025; C:anchored component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0043194; C:axon initial segment; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0044224; C:juxtaparanode region of axon; ISS:BHF-UCL.
DR GO; GO:0043209; C:myelin sheath; ISS:BHF-UCL.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0033268; C:node of Ranvier; ISS:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; ISS:BHF-UCL.
DR GO; GO:0045202; C:synapse; ISS:BHF-UCL.
DR GO; GO:0030246; F:carbohydrate binding; IEA:Ensembl.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; TAS:BHF-UCL.
DR GO; GO:0043621; F:protein self-association; IEA:Ensembl.
DR GO; GO:0007628; P:adult walking behavior; IEA:Ensembl.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0007413; P:axonal fasciculation; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; NAS:ProtInc.
DR GO; GO:0022010; P:central nervous system myelination; IEA:Ensembl.
DR GO; GO:0021853; P:cerebral cortex GABAergic interneuron migration; IEA:Ensembl.
DR GO; GO:0045163; P:clustering of voltage-gated potassium channels; ISS:BHF-UCL.
DR GO; GO:0070593; P:dendrite self-avoidance; IBA:GO_Central.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0071206; P:establishment of protein localization to juxtaparanode region of axon; IEA:Ensembl.
DR GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl.
DR GO; GO:0001973; P:G protein-coupled adenosine receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0007612; P:learning; IEA:Ensembl.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0060168; P:positive regulation of adenosine receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0010954; P:positive regulation of protein processing; IEA:Ensembl.
DR GO; GO:0097090; P:presynaptic membrane organization; IMP:UniProtKB.
DR GO; GO:0071205; P:protein localization to juxtaparanode region of axon; ISS:BHF-UCL.
DR GO; GO:0016485; P:protein processing; IEA:Ensembl.
DR GO; GO:0031623; P:receptor internalization; IEA:Ensembl.
DR GO; GO:0002023; P:reduction of food intake in response to dietary excess; IEA:Ensembl.
DR GO; GO:0048710; P:regulation of astrocyte differentiation; IEA:Ensembl.
DR GO; GO:0031133; P:regulation of axon diameter; IEA:Ensembl.
DR GO; GO:0010769; P:regulation of cell morphogenesis involved in differentiation; IEA:Ensembl.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IEA:Ensembl.
DR CDD; cd00063; FN3; 3.
DR Gene3D; 2.60.40.10; -; 10.
DR InterPro; IPR043204; Basigin-like.
DR InterPro; IPR032991; Contactin-2.
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; PTHR10075; PTHR10075; 1.
DR PANTHER; PTHR10075:SF55; PTHR10075:SF55; 1.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF07679; I-set; 2.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF48726; SSF48726; 6.
DR SUPFAM; SSF49265; SSF49265; 3.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS50835; IG_LIKE; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Epilepsy; Glycoprotein; GPI-anchor; Immunoglobulin domain;
KW Lipoprotein; Membrane; Reference proteome; Repeat; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 31..1012
FT /note="Contactin-2"
FT /id="PRO_0000014695"
FT PROPEP 1013..1040
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014696"
FT DOMAIN 43..128
FT /note="Ig-like C2-type 1"
FT DOMAIN 133..222
FT /note="Ig-like C2-type 2"
FT DOMAIN 239..322
FT /note="Ig-like C2-type 3"
FT DOMAIN 327..411
FT /note="Ig-like C2-type 4"
FT DOMAIN 417..504
FT /note="Ig-like C2-type 5"
FT DOMAIN 509..603
FT /note="Ig-like C2-type 6"
FT DOMAIN 610..708
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 713..810
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 815..910
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 915..1006
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 694..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 794..796
FT /note="Cell attachment site"
FT /evidence="ECO:0000250"
FT LIPID 1012
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 477
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 525
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 830
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 904
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 918
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 940
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 61..111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:17766378"
FT DISULFID 155..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:17766378"
FT DISULFID 261..306
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:17766378"
FT DISULFID 348..395
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:17766378"
FT VARIANT 145
FT /note="A -> T (in dbSNP:rs2275697)"
FT /id="VAR_021918"
FT VARIANT 366
FT /note="P -> L (in dbSNP:rs2229866)"
FT /id="VAR_029129"
FT VARIANT 657
FT /note="R -> W (in dbSNP:rs2305276)"
FT /id="VAR_021919"
FT VARIANT 1024
FT /note="V -> I (in dbSNP:rs17416074)"
FT /id="VAR_049867"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:2OM5"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:2OM5"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:2OM5"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:2OM5"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:2OM5"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:2OM5"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:2OM5"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:2OM5"
FT STRAND 107..115
FT /evidence="ECO:0007829|PDB:2OM5"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:2OM5"
FT STRAND 125..132
FT /evidence="ECO:0007829|PDB:2OM5"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:2OM5"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:2OM5"
FT STRAND 165..172
FT /evidence="ECO:0007829|PDB:2OM5"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:2OM5"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:2OM5"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:2OM5"
FT STRAND 203..213
FT /evidence="ECO:0007829|PDB:2OM5"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:2OM5"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:2OM5"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:2OM5"
FT STRAND 237..243
FT /evidence="ECO:0007829|PDB:2OM5"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:2OM5"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:2OM5"
FT STRAND 262..267
FT /evidence="ECO:0007829|PDB:2OM5"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:2OM5"
FT STRAND 289..295
FT /evidence="ECO:0007829|PDB:2OM5"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:2OM5"
FT STRAND 302..310
FT /evidence="ECO:0007829|PDB:2OM5"
FT STRAND 313..324
FT /evidence="ECO:0007829|PDB:2OM5"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:2OM5"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:2OM5"
FT STRAND 344..347
FT /evidence="ECO:0007829|PDB:2OM5"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:2OM5"
FT STRAND 357..366
FT /evidence="ECO:0007829|PDB:2OM5"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:2OM5"
FT STRAND 379..384
FT /evidence="ECO:0007829|PDB:2OM5"
FT HELIX 387..389
FT /evidence="ECO:0007829|PDB:2OM5"
FT STRAND 391..398
FT /evidence="ECO:0007829|PDB:2OM5"
FT STRAND 403..413
FT /evidence="ECO:0007829|PDB:2OM5"
SQ SEQUENCE 1040 AA; 113393 MW; 254E78DD3C28EFB6 CRC64;
MGTATRRKPH LLLVAAVALV SSSAWSSALG SQTTFGPVFE DQPLSVLFPE ESTEEQVLLA
CRARASPPAT YRWKMNGTEM KLEPGSRHQL VGGNLVIMNP TKAQDAGVYQ CLASNPVGTV
VSREAILRFG FLQEFSKEER DPVKAHEGWG VMLPCNPPAH YPGLSYRWLL NEFPNFIPTD
GRHFVSQTTG NLYIARTNAS DLGNYSCLAT SHMDFSTKSV FSKFAQLNLA AEDTRLFAPS
IKARFPAETY ALVGQQVTLE CFAFGNPVPR IKWRKVDGSL SPQWTTAEPT LQIPSVSFED
EGTYECEAEN SKGRDTVQGR IIVQAQPEWL KVISDTEADI GSNLRWGCAA AGKPRPTVRW
LRNGEPLASQ NRVEVLAGDL RFSKLSLEDS GMYQCVAENK HGTIYASAEL AVQALAPDFR
LNPVRRLIPA ARGGEILIPC QPRAAPKAVV LWSKGTEILV NSSRVTVTPD GTLIIRNISR
SDEGKYTCFA ENFMGKANST GILSVRDATK ITLAPSSADI NLGDNLTLQC HASHDPTMDL
TFTWTLDDFP IDFDKPGGHY RRTNVKETIG DLTILNAQLR HGGKYTCMAQ TVVDSASKEA
TVLVRGPPGP PGGVVVRDIG DTTIQLSWSR GFDNHSPIAK YTLQARTPPA GKWKQVRTNP
ANIEGNAETA QVLGLTPWMD YEFRVIASNI LGTGEPSGPS SKIRTREAAP SVAPSGLSGG
GGAPGELIVN WTPMSREYQN GDGFGYLLSF RRQGSTHWQT ARVPGADAQY FVYSNESVRP
YTPFEVKIRS YNRRGDGPES LTALVYSAEE EPRVAPTKVW AKGVSSSEMN VTWEPVQQDM
NGILLGYEIR YWKAGDKEAA ADRVRTAGLD TSARVSGLHP NTKYHVTVRA YNRAGTGPAS
PSANATTMKP PPRRPPGNIS WTFSSSSLSI KWDPVVPFRN ESAVTGYKML YQNDLHLTPT
LHLTGKNWIE IPVPEDIGHA LVQIRTTGPG GDGIPAEVHI VRNGGTSMMV ENMAVRPAPH
PGTVISHSVA MLILIGSLEL
