CNTN4_MOUSE
ID CNTN4_MOUSE Reviewed; 1026 AA.
AC Q69Z26; Q14BL8; Q8BRT6; Q8CBD3;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Contactin-4;
DE AltName: Full=Brain-derived immunoglobulin superfamily protein 2;
DE Short=BIG-2;
DE Flags: Precursor;
GN Name=Cntn4; Synonyms=Kiaa3024;
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 [GENOMIC DNA] (ISOFORM 2).
RC TISSUE=Nasal epithelium;
RX PubMed=9221934; DOI=10.1016/s0169-328x(97)00104-6;
RA Mimmack M.L., Saito H., Evans G., Bresler M., Keverne E.B., Emson P.C.;
RT "A novel splice variant of the cell adhesion molecule BIG-2 is expressed in
RT the olfactory and vomeronasal neuroepithelia.";
RL Brain Res. Mol. Brain Res. 47:345-350(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, and Cerebellum;
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).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 129-1026 (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=9733924; DOI=10.1016/s0165-3806(98)00096-0;
RA Saito H., Mimmack M., Kishimoto J., Keverne E.B., Emson P.C.;
RT "Expression of olfactory receptors, G-proteins and AxCAMs during the
RT development and maturation of olfactory sensory neurons in the mouse.";
RL Brain Res. Dev. Brain Res. 110:69-81(1998).
RN [6]
RP IDENTIFICATION BY 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 [7]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 25-404 IN COMPLEX WITH PTPRG,
RP INTERACTION WITH PTPRG, GLYCOSYLATION AT ASN-65; ASN-90; ASN-191 AND
RP ASN-370, AND DISULFIDE BONDS.
RX PubMed=20133774; DOI=10.1073/pnas.0911235107;
RA Bouyain S., Watkins D.J.;
RT "The protein tyrosine phosphatases PTPRZ and PTPRG bind to distinct members
RT of the contactin family of neural recognition molecules.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:2443-2448(2010).
CC -!- FUNCTION: Contactins mediate cell surface interactions during nervous
CC system development. Has some neurite outgrowth-promoting activity. May
CC be involved in synaptogenesis. {ECO:0000269|PubMed:9733924}.
CC -!- SUBUNIT: Interacts with PTPRG. {ECO:0000269|PubMed:20133774}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. Secreted
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q69Z26-1; Sequence=Displayed;
CC Name=2; Synonyms=BIG-2A;
CC IsoId=Q69Z26-2; Sequence=VSP_011965, VSP_011966;
CC Name=3;
CC IsoId=Q69Z26-3; Sequence=VSP_011963, VSP_011964;
CC -!- TISSUE SPECIFICITY: Expressed in the region of developing olfactory
CC neurons. Isoform 2 is expressed in mature sensory cells of the
CC vomeronasal neuroepithelium and at lower level in olfactory
CC neuroepithelium. {ECO:0000269|PubMed:9733924}.
CC -!- DEVELOPMENTAL STAGE: Expressed from 14 dpc at a time when developing
CC axons reach the olfactory bulb. {ECO:0000269|PubMed:9733924}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. Contactin
CC family. {ECO:0000305}.
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DR EMBL; X99043; CAA67504.1; -; Genomic_DNA.
DR EMBL; AK036262; BAC29365.1; -; mRNA.
DR EMBL; AK043507; BAC31563.1; -; mRNA.
DR EMBL; BC115766; AAI15767.1; -; mRNA.
DR EMBL; AK173340; BAD32618.1; -; mRNA.
DR CCDS; CCDS20395.1; -. [Q69Z26-2]
DR CCDS; CCDS51866.1; -. [Q69Z26-1]
DR RefSeq; NP_001103219.1; NM_001109749.1. [Q69Z26-1]
DR RefSeq; NP_001103221.1; NM_001109751.1. [Q69Z26-2]
DR RefSeq; NP_766592.2; NM_173004.3. [Q69Z26-2]
DR RefSeq; XP_006506256.1; XM_006506193.2. [Q69Z26-1]
DR RefSeq; XP_006506257.1; XM_006506194.3.
DR RefSeq; XP_006506258.1; XM_006506195.3. [Q69Z26-1]
DR RefSeq; XP_017177088.1; XM_017321599.1.
DR PDB; 3JXA; X-ray; 2.40 A; A/B=25-404.
DR PDB; 3KLD; X-ray; 2.00 A; A=25-404.
DR PDB; 5E4S; X-ray; 2.50 A; A=596-898.
DR PDBsum; 3JXA; -.
DR PDBsum; 3KLD; -.
DR PDBsum; 5E4S; -.
DR AlphaFoldDB; Q69Z26; -.
DR SMR; Q69Z26; -.
DR BioGRID; 234711; 2.
DR IntAct; Q69Z26; 3.
DR MINT; Q69Z26; -.
DR STRING; 10090.ENSMUSP00000108886; -.
DR GlyConnect; 2227; 5 N-Linked glycans (4 sites).
DR GlyGen; Q69Z26; 13 sites, 5 N-linked glycans (4 sites).
DR iPTMnet; Q69Z26; -.
DR PhosphoSitePlus; Q69Z26; -.
DR CPTAC; non-CPTAC-4027; -.
DR MaxQB; Q69Z26; -.
DR PaxDb; Q69Z26; -.
DR PeptideAtlas; Q69Z26; -.
DR PRIDE; Q69Z26; -.
DR ProteomicsDB; 283661; -. [Q69Z26-1]
DR ProteomicsDB; 283662; -. [Q69Z26-2]
DR ProteomicsDB; 283663; -. [Q69Z26-3]
DR Antibodypedia; 9906; 200 antibodies from 31 providers.
DR DNASU; 269784; -.
DR Ensembl; ENSMUST00000089208; ENSMUSP00000086616; ENSMUSG00000064293. [Q69Z26-1]
DR Ensembl; ENSMUST00000113258; ENSMUSP00000108883; ENSMUSG00000064293. [Q69Z26-3]
DR Ensembl; ENSMUST00000113260; ENSMUSP00000108885; ENSMUSG00000064293. [Q69Z26-2]
DR Ensembl; ENSMUST00000113261; ENSMUSP00000108886; ENSMUSG00000064293. [Q69Z26-2]
DR Ensembl; ENSMUST00000113264; ENSMUSP00000108889; ENSMUSG00000064293. [Q69Z26-1]
DR GeneID; 269784; -.
DR KEGG; mmu:269784; -.
DR UCSC; uc009dcr.2; mouse. [Q69Z26-2]
DR UCSC; uc009dcu.1; mouse. [Q69Z26-3]
DR UCSC; uc009dcv.2; mouse. [Q69Z26-1]
DR CTD; 152330; -.
DR MGI; MGI:1095737; Cntn4.
DR VEuPathDB; HostDB:ENSMUSG00000064293; -.
DR eggNOG; KOG3513; Eukaryota.
DR GeneTree; ENSGT00940000155198; -.
DR HOGENOM; CLU_005756_0_1_1; -.
DR InParanoid; Q69Z26; -.
DR OMA; KICKAYT; -.
DR OrthoDB; 655902at2759; -.
DR PhylomeDB; Q69Z26; -.
DR TreeFam; TF351103; -.
DR BioGRID-ORCS; 269784; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Cntn4; mouse.
DR PRO; PR:Q69Z26; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q69Z26; protein.
DR Bgee; ENSMUSG00000064293; Expressed in olfactory epithelium and 118 other tissues.
DR ExpressionAtlas; Q69Z26; baseline and differential.
DR Genevisible; Q69Z26; MM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007411; P:axon guidance; IEA:InterPro.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR CDD; cd00063; FN3; 4.
DR Gene3D; 2.60.40.10; -; 10.
DR InterPro; IPR043204; Basigin-like.
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 Pfam; PF00041; fn3; 2.
DR Pfam; PF07679; I-set; 3.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF48726; SSF48726; 6.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS50835; IG_LIKE; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Disulfide bond; Glycoprotein; GPI-anchor; Immunoglobulin domain;
KW Lipoprotein; Membrane; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1000
FT /note="Contactin-4"
FT /id="PRO_0000014713"
FT PROPEP 1001..1026
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014714"
FT DOMAIN 32..117
FT /note="Ig-like C2-type 1"
FT DOMAIN 122..207
FT /note="Ig-like C2-type 2"
FT DOMAIN 225..311
FT /note="Ig-like C2-type 3"
FT DOMAIN 316..400
FT /note="Ig-like C2-type 4"
FT DOMAIN 406..493
FT /note="Ig-like C2-type 5"
FT DOMAIN 497..586
FT /note="Ig-like C2-type 6"
FT DOMAIN 599..697
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 702..799
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 804..899
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 900..995
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 685..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 886..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1000
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20133774"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20133774"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20133774"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20133774"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 705
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 764
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 858
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 893
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 911
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 929
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 954
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 50..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:20133774"
FT DISULFID 144..194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:20133774"
FT DISULFID 247..295
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:20133774"
FT DISULFID 337..384
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:20133774"
FT DISULFID 429..477
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 519..576
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 496..498
FT /note="DPT -> GNG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011963"
FT VAR_SEQ 499..1026
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011964"
FT VAR_SEQ 698..705
FT /note="LPEVTPAN -> QNTGDQRG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_011965"
FT VAR_SEQ 706..1026
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_011966"
FT CONFLICT 64
FT /note="I -> L (in Ref. 1; CAA67504 and 3; AAI15767)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="T -> S (in Ref. 1; CAA67504)"
FT /evidence="ECO:0000305"
FT CONFLICT 202..203
FT /note="NH -> HP (in Ref. 1; CAA67504)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="E -> D (in Ref. 1; CAA67504)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="A -> V (in Ref. 2; BAC29365)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="A -> G (in Ref. 1; CAA67504)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="P -> A (in Ref. 1; CAA67504)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="L -> V (in Ref. 1; CAA67504)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="N -> T (in Ref. 1; CAA67504)"
FT /evidence="ECO:0000305"
FT CONFLICT 373..374
FT /note="IV -> KG (in Ref. 1; CAA67504)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="S -> Q (in Ref. 1; CAA67504)"
FT /evidence="ECO:0000305"
FT CONFLICT 382..386
FT /note="YQCVA -> SQRVG (in Ref. 1; CAA67504)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="I -> V (in Ref. 1; CAA67504 and 3; AAI15767)"
FT /evidence="ECO:0000305"
FT CONFLICT 686
FT /note="S -> G (in Ref. 2; BAC29365)"
FT /evidence="ECO:0000305"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:3KLD"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:3KLD"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:3KLD"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:3KLD"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:3KLD"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:3KLD"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:3KLD"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:3KLD"
FT STRAND 96..104
FT /evidence="ECO:0007829|PDB:3KLD"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:3KLD"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:3KLD"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:3KLD"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:3KLD"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:3KLD"
FT STRAND 153..159
FT /evidence="ECO:0007829|PDB:3KLD"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:3KLD"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:3KLD"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:3KLD"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:3KLD"
FT STRAND 190..198
FT /evidence="ECO:0007829|PDB:3KLD"
FT TURN 199..202
FT /evidence="ECO:0007829|PDB:3KLD"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:3KLD"
FT STRAND 210..219
FT /evidence="ECO:0007829|PDB:3KLD"
FT STRAND 223..230
FT /evidence="ECO:0007829|PDB:3KLD"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:3KLD"
FT STRAND 243..253
FT /evidence="ECO:0007829|PDB:3KLD"
FT STRAND 256..261
FT /evidence="ECO:0007829|PDB:3KLD"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:3JXA"
FT TURN 275..278
FT /evidence="ECO:0007829|PDB:3JXA"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:3KLD"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:3KLD"
FT STRAND 291..299
FT /evidence="ECO:0007829|PDB:3KLD"
FT STRAND 302..320
FT /evidence="ECO:0007829|PDB:3KLD"
FT STRAND 325..328
FT /evidence="ECO:0007829|PDB:3KLD"
FT STRAND 333..336
FT /evidence="ECO:0007829|PDB:3KLD"
FT STRAND 338..343
FT /evidence="ECO:0007829|PDB:3KLD"
FT STRAND 346..351
FT /evidence="ECO:0007829|PDB:3KLD"
FT STRAND 362..365
FT /evidence="ECO:0007829|PDB:3KLD"
FT STRAND 368..373
FT /evidence="ECO:0007829|PDB:3KLD"
FT HELIX 376..378
FT /evidence="ECO:0007829|PDB:3KLD"
FT STRAND 380..388
FT /evidence="ECO:0007829|PDB:3KLD"
FT STRAND 391..402
FT /evidence="ECO:0007829|PDB:3KLD"
FT STRAND 601..608
FT /evidence="ECO:0007829|PDB:5E4S"
FT STRAND 613..618
FT /evidence="ECO:0007829|PDB:5E4S"
FT STRAND 629..635
FT /evidence="ECO:0007829|PDB:5E4S"
FT STRAND 637..641
FT /evidence="ECO:0007829|PDB:5E4S"
FT STRAND 646..652
FT /evidence="ECO:0007829|PDB:5E4S"
FT STRAND 658..663
FT /evidence="ECO:0007829|PDB:5E4S"
FT STRAND 669..677
FT /evidence="ECO:0007829|PDB:5E4S"
FT STRAND 715..719
FT /evidence="ECO:0007829|PDB:5E4S"
FT HELIX 725..727
FT /evidence="ECO:0007829|PDB:5E4S"
FT STRAND 730..732
FT /evidence="ECO:0007829|PDB:5E4S"
FT STRAND 734..741
FT /evidence="ECO:0007829|PDB:5E4S"
FT STRAND 748..752
FT /evidence="ECO:0007829|PDB:5E4S"
FT STRAND 759..763
FT /evidence="ECO:0007829|PDB:5E4S"
FT STRAND 772..781
FT /evidence="ECO:0007829|PDB:5E4S"
FT STRAND 784..788
FT /evidence="ECO:0007829|PDB:5E4S"
FT STRAND 792..795
FT /evidence="ECO:0007829|PDB:5E4S"
FT STRAND 806..812
FT /evidence="ECO:0007829|PDB:5E4S"
FT STRAND 814..816
FT /evidence="ECO:0007829|PDB:5E4S"
FT STRAND 818..823
FT /evidence="ECO:0007829|PDB:5E4S"
FT STRAND 835..842
FT /evidence="ECO:0007829|PDB:5E4S"
FT HELIX 847..849
FT /evidence="ECO:0007829|PDB:5E4S"
FT STRAND 851..854
FT /evidence="ECO:0007829|PDB:5E4S"
FT STRAND 861..864
FT /evidence="ECO:0007829|PDB:5E4S"
FT STRAND 872..881
FT /evidence="ECO:0007829|PDB:5E4S"
FT STRAND 884..888
FT /evidence="ECO:0007829|PDB:5E4S"
FT STRAND 892..895
FT /evidence="ECO:0007829|PDB:5E4S"
SQ SEQUENCE 1026 AA; 113490 MW; 34AC35CE432F03AC CRC64;
MRLPWELLVL QSFMLCLADD YTLHGPVFVQ EPSHVMFPLD SEEKKVKLSC EVKGNPKPHI
RWKINGTDVD IGMDFRYSVV DGSLLINNPN KTQDAGTYQC IATNSFGTIV SREAKLQFAY
LENFKTRTRS TVSVRRGQGM VLLCGPPPHS GELSYAWIFN EYPSYQDNRR FVSQETGNLY
IAKVEKSDVG NYTCVVTNTV TNHKVLGPPT PLILRNDGVM GEYEPKIEVQ FPETVPAEKG
TTVKLECFAL GNPVPTILWR RADGKPIARK ARRHKSNGIL EIPNFQQEDA GSYECVAENS
RGKNVAKGQL TFYAQPNWVQ IINDIHVAME ESVFWECKAN GRPKPTYRWL KNGDPLLTRD
RIQIEQGTLN ITIVNLSDAG MYQCVAENKH GVIFSSAELS VIAESPDFSR TLLKRVTLVK
VGGEVVIECK PKASPRPVYT WRKGREILRE NERITISEDG NLRIINVTKS DAGSYTCIAT
NHFGTASSTG NVIVKDPTKV MVPPSSMDVT VGESIVLPCQ VTHDHSLDIV FTWTFNGHLI
DFDKDGDHFE RVGGQDSAGD LMIRNIQLKH AGKYVCMVQT SVDKLSVAAD LIVRGPPGPP
EAVTIDEITD TTAQLSWRPG PDNHSPITMY VIQARTPFSV GWQAVNTVPD LVDGKTFTAT
VVGLNPWVEY EFRTVAANVI GIGEPSRPSE KRRTEEALPE VTPANVSGGG GSKSELVITW
ETVPEELQNG RGFGYVVAFR PHGKMIWMLT VLASADASRY VFRNESVRPF SPFEVKVGVF
NNKGEGPFSP TTLVYSAEEE PTKPPASIFA RSLSATDIEV FWASPIGKNR GRIQGYEVKY
WRHDDKEENA KKIRTVGNQT STKITNLKGS ALYHLSVKAY NSAGTGPSSA TVNVTTRKPP
PSQPPGNIIW NSSDSKIILN WDQVKALDNE SEVKGYKVLY RWNRQSSTSV IETNKTSVEL
SLPFDEDYII EIKPFSDGGD GSSSEQIRIP KISNSYARGS GASTSNACTL SAISTIMISL
TARSSL
