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   27-MAR-2024, entry version 213.
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   PDB; 8K53; EM; 3.80 A; A/B=31-1012.
DR   PDBsum; 2OM5; -.
DR   PDBsum; 8K53; -.
DR   AlphaFoldDB; Q02246; -.
DR   SMR; Q02246; -.
DR   BioGRID; 112763; 16.
DR   IntAct; Q02246; 3.
DR   MINT; Q02246; -.
DR   STRING; 9606.ENSP00000330633; -.
DR   TCDB; 8.A.23.1.3; the basigin (basigin) family.
DR   GlyCosmos; Q02246; 11 sites, No reported glycans.
DR   GlyGen; Q02246; 11 sites.
DR   iPTMnet; Q02246; -.
DR   PhosphoSitePlus; Q02246; -.
DR   BioMuta; CNTN2; -.
DR   DMDM; 399092; -.
DR   MassIVE; Q02246; -.
DR   PaxDb; 9606-ENSP00000330633; -.
DR   PeptideAtlas; Q02246; -.
DR   ProteomicsDB; 58068; -.
DR   Antibodypedia; 670; 308 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   AGR; HGNC:2172; -.
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; 3073820at2759; -.
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 1140 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 148 other cell types or tissues.
DR   ExpressionAtlas; Q02246; baseline and differential.
DR   GO; GO:0030424; C:axon; IBA:GO_Central.
DR   GO; GO:0043194; C:axon initial segment; 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:0033268; C:node of Ranvier; ISS:BHF-UCL.
DR   GO; GO:0005886; C:plasma membrane; ISS:BHF-UCL.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:SynGO.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045202; C:synapse; ISS:BHF-UCL.
DR   GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR   GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR   GO; GO:0007155; P:cell adhesion; NAS:ProtInc.
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: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:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
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:0002023; P:reduction of food intake in response to dietary excess; IEA:Ensembl.
DR   CDD; cd00063; FN3; 3.
DR   CDD; cd05727; Ig2_Contactin-2-like; 1.
DR   CDD; cd05728; Ig4_Contactin-2-like; 1.
DR   CDD; cd04969; Ig5_Contactin; 1.
DR   CDD; cd05854; Ig6_Contactin-2; 1.
DR   CDD; cd05850; IgI_1_Contactin-2; 1.
DR   CDD; cd04968; IgI_3_Contactin; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 10.
DR   InterPro; IPR047102; Contactin-1_2_Ig1.
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; PTHR44170:SF28; CONTACTIN-2; 1.
DR   PANTHER; PTHR44170; PROTEIN SIDEKICK; 1.
DR   Pfam; PF00041; fn3; 3.
DR   Pfam; PF07679; I-set; 2.
DR   Pfam; PF13927; Ig_3; 3.
DR   SMART; SM00060; FN3; 4.
DR   SMART; SM00409; IG; 6.
DR   SMART; SM00408; IGc2; 5.
DR   SUPFAM; SSF49265; Fibronectin type III; 3.
DR   SUPFAM; SSF48726; Immunoglobulin; 6.
DR   PROSITE; PS50853; FN3; 4.
DR   PROSITE; PS50835; IG_LIKE; 6.
DR   Genevisible; Q02246; HS.
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
//