UNC22_CAEEL
ID UNC22_CAEEL Reviewed; 7158 AA.
AC Q23551; A3RMU0; D3YT57; D3YT58; Q23020; Q23550; Q27232; Q7JN85;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 3.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Twitchin {ECO:0000303|PubMed:7190524};
DE EC=2.7.11.1 {ECO:0000269|PubMed:18390597};
DE AltName: Full=Uncoordinated protein 22 {ECO:0000303|PubMed:2812002};
GN Name=unc-22 {ECO:0000312|WormBase:ZK617.1b}; ORFNames=ZK617.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000312|EMBL:CAA33463.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAA33463.1};
RX PubMed=2812002; DOI=10.1038/342045a0;
RA Benian G.M., Kiff J.E., Neckelmann N., Moerman D.G., Waterston R.H.;
RT "Sequence of an unusually large protein implicated in regulation of myosin
RT activity in C. elegans.";
RL Nature 342:45-50(1989).
RN [2] {ECO:0000305}
RP SEQUENCE REVISION TO N-TERMINUS.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:8397135};
RX PubMed=8397135; DOI=10.1093/genetics/134.4.1097;
RA Benian G.M., L'Hernault S.W., Morris M.E.;
RT "Additional sequence complexity in the muscle gene, unc-22, and its encoded
RT protein, twitchin, of Caenorhabditis elegans.";
RL Genetics 134:1097-1104(1993).
RN [3] {ECO:0000305, ECO:0000312|EMBL:CAA98065.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAA98065.2};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [4] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=7190524; DOI=10.1016/0012-1606(80)90475-3;
RA Waterston R.H., Thomson J.N., Brenner S.;
RT "Mutants with altered muscle structure of Caenorhabditis elegans.";
RL Dev. Biol. 77:271-302(1980).
RN [5] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=2833427; DOI=10.1101/gad.2.1.93;
RA Moerman D.G., Benian G.M., Barstead R.J., Schriefer L.A., Waterston R.H.;
RT "Identification and intracellular localization of the unc-22 gene product
RT of Caenorhabditis elegans.";
RL Genes Dev. 2:93-105(1988).
RN [6] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=16765996; DOI=10.1016/j.mrfmmm.2006.05.001;
RA Zhao Y., Lai K., Cheung I., Youds J., Tarailo M., Tarailo S., Rose A.;
RT "A mutational analysis of Caenorhabditis elegans in space.";
RL Mutat. Res. 601:19-29(2006).
RN [7] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND ACTIVITY REGULATION.
RX PubMed=18390597; DOI=10.1529/biophysj.108.130237;
RA Greene D.N., Garcia T., Sutton R.B., Gernert K.M., Benian G.M.,
RA Oberhauser A.F.;
RT "Single-molecule force spectroscopy reveals a stepwise unfolding of
RT Caenorhabditis elegans giant protein kinase domains.";
RL Biophys. J. 95:1360-1370(2008).
RN [8]
RP FUNCTION, INTERACTION WITH MAK-1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP PHOSPHORYLATION, AND DISRUPTION PHENOTYPE.
RX PubMed=25851606; DOI=10.1091/mbc.e14-05-1009;
RA Matsunaga Y., Qadota H., Furukawa M., Choe H.H., Benian G.M.;
RT "Twitchin kinase interacts with MAPKAP kinase 2 in Caenorhabditis elegans
RT striated muscle.";
RL Mol. Biol. Cell 26:2096-2111(2015).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 6211-6699, ACTIVITY REGULATION,
RP AND REGION.
RX PubMed=8202162; DOI=10.1038/369581a0;
RA Hu S.H., Parker M.W., Lei J.Y., Wilce M.C., Benian G.M., Kemp B.E.;
RT "Insights into autoregulation from the crystal structure of twitchin
RT kinase.";
RL Nature 369:581-584(1994).
RN [10]
RP STRUCTURE BY NMR OF 4148-4240.
RX PubMed=8969309; DOI=10.1006/jmbi.1996.0665;
RA Fong S., Hamill S.J., Proctor M., Freund S.M., Benian G.M., Chothia C.,
RA Bycroft M., Clarke J.;
RT "Structure and stability of an immunoglobulin superfamily domain from
RT twitchin, a muscle protein of the nematode Caenorhabditis elegans.";
RL J. Mol. Biol. 264:624-639(1996).
CC -!- FUNCTION: Regulator of muscle contraction and relaxation. Senses
CC mechanical strain that occurs during muscle activity by unfolding in
CC clearly resolvable steps at differing forces (PubMed:18390597,
CC PubMed:7190524). Plays a role in the organization of sarcomeres in body
CC wall muscles (PubMed:25851606). {ECO:0000269|PubMed:18390597,
CC ECO:0000269|PubMed:25851606, ECO:0000269|PubMed:7190524}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:18390597};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:18390597};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:18390597};
CC -!- ACTIVITY REGULATION: Forces generated by the contraction/relaxation
CC cycles of muscle activity separate the regulatory domain from the
CC catalytic core, activating the enzyme. At rest, the kinase domain is in
CC a closed conformation. The active site is occupied by the
CC autoinhibitory region (CDR), which makes extensive contact with the
CC catalytic site, blocking substrate binding. At low forces the
CC regulatory tail will unravel reversibly and expose the active site to
CC its substrates, potentially stabilized by binding of Ca/CALM. At high
CC forces the kinase begins to unfold and the integrity of the active site
CC is disrupted. {ECO:0000269|PubMed:18390597,
CC ECO:0000269|PubMed:8202162}.
CC -!- SUBUNIT: May interact (via protein kinase and CRD domains) with mak-1
CC (via protein kinase domain). {ECO:0000269|PubMed:25851606}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere
CC {ECO:0000269|PubMed:25851606, ECO:0000269|PubMed:2833427}. Cytoplasm,
CC myofibril, sarcomere, A band {ECO:0000269|PubMed:25851606,
CC ECO:0000269|PubMed:2833427}. Note=Expressed at the outer edge of A-
CC bands. {ECO:0000269|PubMed:25851606, ECO:0000269|PubMed:2833427}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=b {ECO:0000269|PubMed:9851916};
CC IsoId=Q23551-1; Sequence=Displayed;
CC Name=a {ECO:0000269|PubMed:2812002, ECO:0000269|PubMed:8397135,
CC ECO:0000269|PubMed:9851916};
CC IsoId=Q23551-2; Sequence=VSP_040609, VSP_040611;
CC Name=c {ECO:0000269|PubMed:9851916};
CC IsoId=Q23551-3; Sequence=VSP_040606, VSP_040607;
CC Name=d {ECO:0000269|PubMed:9851916};
CC IsoId=Q23551-4; Sequence=VSP_040608, VSP_040611;
CC Name=e {ECO:0000269|PubMed:9851916};
CC IsoId=Q23551-5; Sequence=VSP_040605, VSP_040611;
CC -!- TISSUE SPECIFICITY: Expressed in body wall, anal, vulval, and
CC pharyngeal muscles (at protein level). {ECO:0000269|PubMed:25851606,
CC ECO:0000269|PubMed:2833427}.
CC -!- PTM: Phosphorylated by mak-1 on the protein kinase domain and/or CDR
CC domain in vitro. {ECO:0000269|PubMed:25851606}.
CC -!- DISRUPTION PHENOTYPE: Body muscles are unable to develop or sustain
CC normal contractions but small regions within the myofilament lattice of
CC individual muscle cells contract transiently in the absence of
CC contraction of the adjacent lattice (PubMed:16765996, PubMed:7190524).
CC This results in a nearly constant body twitching phenotype
CC (PubMed:16765996, PubMed:7190524, PubMed:25851606). Resistant to
CC nicotine-induced paralysis (PubMed:25851606).
CC {ECO:0000269|PubMed:16765996, ECO:0000269|PubMed:25851606,
CC ECO:0000269|PubMed:7190524}.
CC -!- MISCELLANEOUS: Determination of the mutation frequency of the unc-22
CC gene has been used to study the biological effects of short duration
CC spaceflight. {ECO:0000269|PubMed:16765996}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA33463.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X15423; CAA33463.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z73897; CAA98064.2; -; Genomic_DNA.
DR EMBL; Z73899; CAA98064.2; JOINED; Genomic_DNA.
DR EMBL; Z73897; CAA98065.2; -; Genomic_DNA.
DR EMBL; Z73899; CAA98065.2; JOINED; Genomic_DNA.
DR EMBL; Z73897; CAM35838.2; -; Genomic_DNA.
DR EMBL; Z73899; CAM35838.2; JOINED; Genomic_DNA.
DR EMBL; Z73897; CBK19522.1; -; Genomic_DNA.
DR EMBL; Z73899; CBK19522.1; JOINED; Genomic_DNA.
DR EMBL; Z73897; CBK19523.1; -; Genomic_DNA.
DR EMBL; Z73899; CBK19523.1; JOINED; Genomic_DNA.
DR PIR; A88852; A88852.
DR PIR; S57242; S57242.
DR PIR; T27935; T27935.
DR RefSeq; NP_001122835.2; NM_001129363.2. [Q23551-3]
DR RefSeq; NP_001255603.2; NM_001268674.2.
DR RefSeq; NP_001255604.1; NM_001268675.1. [Q23551-5]
DR RefSeq; NP_502273.2; NM_069872.5. [Q23551-2]
DR RefSeq; NP_502274.2; NM_069873.4. [Q23551-1]
DR PDB; 1KOA; X-ray; 3.30 A; A=6209-6699.
DR PDB; 1WIT; NMR; -; A=4148-4240.
DR PDB; 1WIU; NMR; -; A=4148-4240.
DR PDB; 3UTO; X-ray; 2.40 A; A/B=6108-6675.
DR PDBsum; 1KOA; -.
DR PDBsum; 1WIT; -.
DR PDBsum; 1WIU; -.
DR PDBsum; 3UTO; -.
DR SMR; Q23551; -.
DR BioGRID; 43229; 4.
DR STRING; 6239.ZK617.1b.1; -.
DR EPD; Q23551; -.
DR PaxDb; Q23551; -.
DR PeptideAtlas; Q23551; -.
DR PRIDE; Q23551; -.
DR EnsemblMetazoa; ZK617.1a.1; ZK617.1a.1; WBGene00006759. [Q23551-2]
DR EnsemblMetazoa; ZK617.1b.1; ZK617.1b.1; WBGene00006759. [Q23551-1]
DR EnsemblMetazoa; ZK617.1c.1; ZK617.1c.1; WBGene00006759. [Q23551-3]
DR EnsemblMetazoa; ZK617.1d.1; ZK617.1d.1; WBGene00006759.
DR EnsemblMetazoa; ZK617.1e.1; ZK617.1e.1; WBGene00006759. [Q23551-5]
DR GeneID; 178135; -.
DR UCSC; ZK617.1a.2; c. elegans.
DR CTD; 178135; -.
DR WormBase; ZK617.1a; CE33017; WBGene00006759; unc-22. [Q23551-2]
DR WormBase; ZK617.1b; CE33018; WBGene00006759; unc-22. [Q23551-1]
DR WormBase; ZK617.1c; CE47057; WBGene00006759; unc-22. [Q23551-3]
DR WormBase; ZK617.1d; CE49926; WBGene00006759; unc-22.
DR WormBase; ZK617.1e; CE44668; WBGene00006759; unc-22. [Q23551-5]
DR eggNOG; KOG0613; Eukaryota.
DR GeneTree; ENSGT00940000169746; -.
DR InParanoid; Q23551; -.
DR OMA; DADEYTC; -.
DR OrthoDB; 184at2759; -.
DR PhylomeDB; Q23551; -.
DR Reactome; R-CEL-114608; Platelet degranulation.
DR EvolutionaryTrace; Q23551; -.
DR PRO; PR:Q23551; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00006759; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; Q23551; baseline and differential.
DR GO; GO:0031672; C:A band; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:WormBase.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:UniProtKB.
DR GO; GO:0035095; P:behavioral response to nicotine; IMP:UniProtKB.
DR GO; GO:0051782; P:negative regulation of cell division; IGI:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:WormBase.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:WormBase.
DR GO; GO:0040017; P:positive regulation of locomotion; IGI:UniProtKB.
DR GO; GO:0060298; P:positive regulation of sarcomere organization; IMP:UniProtKB.
DR GO; GO:0045989; P:positive regulation of striated muscle contraction; IGI:UniProtKB.
DR CDD; cd00063; FN3; 31.
DR Gene3D; 2.60.40.10; -; 61.
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 InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00041; fn3; 31.
DR Pfam; PF07679; I-set; 27.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00060; FN3; 32.
DR SMART; SM00409; IG; 30.
DR SMART; SM00408; IGc2; 24.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48726; SSF48726; 30.
DR SUPFAM; SSF49265; SSF49265; 17.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50853; FN3; 31.
DR PROSITE; PS50835; IG_LIKE; 21.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Calcium;
KW Calmodulin-binding; Cytoplasm; Disulfide bond; Immunoglobulin domain;
KW Kelch repeat; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..7158
FT /note="Twitchin"
FT /id="PRO_0000404604"
FT DOMAIN 5..97
FT /note="Ig-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 111..204
FT /note="Ig-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 377..466
FT /note="Ig-like 3"
FT /evidence="ECO:0000255"
FT REPEAT 718..764
FT /note="Kelch 1"
FT /evidence="ECO:0000255"
FT DOMAIN 980..1072
FT /note="Ig-like 4"
FT /evidence="ECO:0000255"
FT DOMAIN 1122..1213
FT /note="Ig-like 5"
FT /evidence="ECO:0000255"
FT DOMAIN 1217..1306
FT /note="Ig-like 6"
FT /evidence="ECO:0000255"
FT DOMAIN 1312..1398
FT /note="Ig-like 7"
FT /evidence="ECO:0000255"
FT DOMAIN 1598..1690
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1696..1791
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1891..1988
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1994..2087
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REPEAT 2014..2058
FT /note="Kelch 2"
FT /evidence="ECO:0000255"
FT DOMAIN 2086..2181
FT /note="Ig-like 8"
FT /evidence="ECO:0000255"
FT DOMAIN 2189..2282
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REPEAT 2207..2253
FT /note="Kelch 3"
FT /evidence="ECO:0000255"
FT DOMAIN 2288..2383
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2483..2576
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REPEAT 2502..2547
FT /note="Kelch 4"
FT /evidence="ECO:0000255"
FT DOMAIN 2579..2675
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2679..2763
FT /note="Ig-like 9"
FT /evidence="ECO:0000255"
FT DOMAIN 2775..2868
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REPEAT 2793..2839
FT /note="Kelch 5"
FT /evidence="ECO:0000255"
FT DOMAIN 2874..2968
FT /note="Fibronectin type-III 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2972..3062
FT /note="Ig-like 10"
FT /evidence="ECO:0000255"
FT DOMAIN 3070..3165
FT /note="Fibronectin type-III 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REPEAT 3089..3134
FT /note="Kelch 6"
FT /evidence="ECO:0000255"
FT DOMAIN 3171..3265
FT /note="Fibronectin type-III 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 3268..3358
FT /note="Ig-like 11"
FT /evidence="ECO:0000255"
FT DOMAIN 3365..3459
FT /note="Fibronectin type-III 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REPEAT 3384..3430
FT /note="Kelch 7"
FT /evidence="ECO:0000255"
FT DOMAIN 3465..3559
FT /note="Fibronectin type-III 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 3563..3653
FT /note="Ig-like 12"
FT /evidence="ECO:0000255"
FT DOMAIN 3661..3753
FT /note="Fibronectin type-III 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 3759..3853
FT /note="Fibronectin type-III 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 3954..4047
FT /note="Fibronectin type-III 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REPEAT 3972..4018
FT /note="Kelch 8"
FT /evidence="ECO:0000255"
FT DOMAIN 4053..4146
FT /note="Fibronectin type-III 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 4246..4340
FT /note="Fibronectin type-III 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REPEAT 4265..4310
FT /note="Kelch 9"
FT /evidence="ECO:0000255"
FT DOMAIN 4346..4440
FT /note="Fibronectin type-III 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REPEAT 4365..4410
FT /note="Kelch 10"
FT /evidence="ECO:0000255"
FT DOMAIN 4445..4531
FT /note="Ig-like 13"
FT /evidence="ECO:0000255"
FT DOMAIN 4538..4631
FT /note="Fibronectin type-III 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REPEAT 4557..4602
FT /note="Kelch 11"
FT /evidence="ECO:0000255"
FT DOMAIN 4637..4733
FT /note="Fibronectin type-III 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 4739..4834
FT /note="Fibronectin type-III 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 4936..5028
FT /note="Fibronectin type-III 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 5034..5129
FT /note="Fibronectin type-III 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 5231..5326
FT /note="Fibronectin type-III 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REPEAT 5287..5335
FT /note="Kelch 12"
FT /evidence="ECO:0000255"
FT DOMAIN 5333..5427
FT /note="Fibronectin type-III 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 5430..5528
FT /note="Fibronectin type-III 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 5533..5621
FT /note="Ig-like 14"
FT /evidence="ECO:0000255"
FT DOMAIN 5723..5817
FT /note="Fibronectin type-III 29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REPEAT 5742..5787
FT /note="Kelch 13"
FT /evidence="ECO:0000255"
FT DOMAIN 5823..5919
FT /note="Fibronectin type-III 30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 5923..6011
FT /note="Ig-like 15"
FT /evidence="ECO:0000255"
FT DOMAIN 6016..6107
FT /note="Ig-like 16"
FT /evidence="ECO:0000255"
FT DOMAIN 6114..6207
FT /note="Fibronectin type-III 31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 6261..6516
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 6585..6673
FT /note="Ig-like 17"
FT /evidence="ECO:0000255"
FT DOMAIN 6696..6795
FT /note="Ig-like 18"
FT /evidence="ECO:0000255"
FT DOMAIN 6863..6952
FT /note="Ig-like 19"
FT /evidence="ECO:0000255"
FT DOMAIN 6958..7059
FT /note="Ig-like 20"
FT /evidence="ECO:0000255"
FT DOMAIN 7067..7149
FT /note="Ig-like 21"
FT /evidence="ECO:0000255"
FT REGION 204..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1088..1118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2266..2295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2849..2901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 6517..6581
FT /note="C-terminal regulatory domain (CDR)"
FT /evidence="ECO:0000303|PubMed:8202162"
FT COMPBIAS 208..222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..577
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..815
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..849
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..955
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2269..2283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2864..2893
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 6382
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 6267..6275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 6290
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT DISULFID 25..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 132..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1150..1201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 5944..5995
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..610
FT /note="Missing (in isoform e)"
FT /evidence="ECO:0000303|PubMed:8397135"
FT /id="VSP_040605"
FT VAR_SEQ 1..539
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000303|PubMed:8397135"
FT /id="VSP_040606"
FT VAR_SEQ 540..550
FT /note="RSSSVRPDPDE -> MGQDFDSDSDS (in isoform c)"
FT /evidence="ECO:0000303|PubMed:8397135"
FT /id="VSP_040607"
FT VAR_SEQ 551..809
FT /note="ESQLDEIPSSGLTIPEERRRELLGQVGESDDEVSESISELPSFAGGKPRRKT
FT DSPPKQDDMFSRDTLLRKTTTSTKNESSTVEEKTKLRKTVKKVDGELDFKAMVKLKKVK
FT KEEGGTTEKSGFPLDHADSTSSVLSQESRSRRGSNAPFAKDGLPEQPANPFAQLKKVKS
FT GAGGLEKSDSMASLKKLDLKKGKIDDNSDGAFKVQLKKVVKKEVKESTISVKEKNGTES
FT GIKTEFKMEKRERTTLQKYEKTDSDGSKKE -> NLLKKSASNDGSDHGASPSSSTSSS
FT SRRLPPRPPLESSHSASSPSSSNGGPRRMFNLRSASDRQGASRPTGGQTPNPLNMRSAN
FT SSGQDLHKISQIHAFILSKMPEGEAKERFLRSILDLEGPDSRRGSRDDVGSPNMLKKTN
FT SKSSVNSSSNESQLDEIPSSGLTIPEERRRELLGQVGESDDEVSESISELPSFAGGKPR
FT RKTD (in isoform d)"
FT /evidence="ECO:0000303|PubMed:8397135"
FT /id="VSP_040608"
FT VAR_SEQ 604..809
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000303|PubMed:2812002,
FT ECO:0000303|PubMed:8397135"
FT /id="VSP_040609"
FT VAR_SEQ 835..947
FT /note="Missing (in isoform a, isoform d and isoform e)"
FT /evidence="ECO:0000303|PubMed:2812002,
FT ECO:0000303|PubMed:8397135"
FT /id="VSP_040611"
FT STRAND 4158..4161
FT /evidence="ECO:0007829|PDB:1WIT"
FT STRAND 4163..4165
FT /evidence="ECO:0007829|PDB:1WIU"
FT STRAND 4168..4174
FT /evidence="ECO:0007829|PDB:1WIT"
FT STRAND 4180..4184
FT /evidence="ECO:0007829|PDB:1WIT"
FT TURN 4187..4189
FT /evidence="ECO:0007829|PDB:1WIT"
FT STRAND 4196..4201
FT /evidence="ECO:0007829|PDB:1WIT"
FT STRAND 4204..4208
FT /evidence="ECO:0007829|PDB:1WIT"
FT HELIX 4214..4216
FT /evidence="ECO:0007829|PDB:1WIT"
FT STRAND 4218..4226
FT /evidence="ECO:0007829|PDB:1WIT"
FT STRAND 4229..4239
FT /evidence="ECO:0007829|PDB:1WIT"
FT STRAND 6116..6123
FT /evidence="ECO:0007829|PDB:3UTO"
FT STRAND 6128..6133
FT /evidence="ECO:0007829|PDB:3UTO"
FT STRAND 6139..6141
FT /evidence="ECO:0007829|PDB:3UTO"
FT STRAND 6145..6155
FT /evidence="ECO:0007829|PDB:3UTO"
FT STRAND 6159..6171
FT /evidence="ECO:0007829|PDB:3UTO"
FT STRAND 6179..6188
FT /evidence="ECO:0007829|PDB:3UTO"
FT HELIX 6206..6208
FT /evidence="ECO:0007829|PDB:3UTO"
FT STRAND 6219..6221
FT /evidence="ECO:0007829|PDB:3UTO"
FT HELIX 6234..6237
FT /evidence="ECO:0007829|PDB:3UTO"
FT HELIX 6241..6244
FT /evidence="ECO:0007829|PDB:3UTO"
FT STRAND 6253..6255
FT /evidence="ECO:0007829|PDB:3UTO"
FT HELIX 6257..6259
FT /evidence="ECO:0007829|PDB:3UTO"
FT STRAND 6261..6270
FT /evidence="ECO:0007829|PDB:3UTO"
FT STRAND 6273..6280
FT /evidence="ECO:0007829|PDB:3UTO"
FT TURN 6281..6283
FT /evidence="ECO:0007829|PDB:3UTO"
FT STRAND 6286..6293
FT /evidence="ECO:0007829|PDB:3UTO"
FT HELIX 6297..6312
FT /evidence="ECO:0007829|PDB:3UTO"
FT STRAND 6321..6326
FT /evidence="ECO:0007829|PDB:3UTO"
FT STRAND 6328..6336
FT /evidence="ECO:0007829|PDB:3UTO"
FT HELIX 6343..6347
FT /evidence="ECO:0007829|PDB:3UTO"
FT HELIX 6356..6375
FT /evidence="ECO:0007829|PDB:3UTO"
FT HELIX 6385..6387
FT /evidence="ECO:0007829|PDB:3UTO"
FT STRAND 6388..6394
FT /evidence="ECO:0007829|PDB:3UTO"
FT STRAND 6398..6400
FT /evidence="ECO:0007829|PDB:3UTO"
FT STRAND 6413..6418
FT /evidence="ECO:0007829|PDB:3UTO"
FT HELIX 6422..6424
FT /evidence="ECO:0007829|PDB:3UTO"
FT HELIX 6427..6430
FT /evidence="ECO:0007829|PDB:3UTO"
FT HELIX 6437..6453
FT /evidence="ECO:0007829|PDB:3UTO"
FT HELIX 6463..6471
FT /evidence="ECO:0007829|PDB:3UTO"
FT HELIX 6480..6482
FT /evidence="ECO:0007829|PDB:3UTO"
FT HELIX 6487..6494
FT /evidence="ECO:0007829|PDB:3UTO"
FT HELIX 6501..6503
FT /evidence="ECO:0007829|PDB:3UTO"
FT HELIX 6507..6512
FT /evidence="ECO:0007829|PDB:3UTO"
FT TURN 6514..6516
FT /evidence="ECO:0007829|PDB:3UTO"
FT TURN 6522..6525
FT /evidence="ECO:0007829|PDB:3UTO"
FT HELIX 6530..6533
FT /evidence="ECO:0007829|PDB:3UTO"
FT HELIX 6534..6543
FT /evidence="ECO:0007829|PDB:3UTO"
FT TURN 6544..6546
FT /evidence="ECO:0007829|PDB:3UTO"
FT HELIX 6553..6559
FT /evidence="ECO:0007829|PDB:3UTO"
FT HELIX 6562..6566
FT /evidence="ECO:0007829|PDB:3UTO"
FT TURN 6568..6572
FT /evidence="ECO:0007829|PDB:3UTO"
FT STRAND 6573..6578
FT /evidence="ECO:0007829|PDB:3UTO"
FT HELIX 6580..6583
FT /evidence="ECO:0007829|PDB:3UTO"
FT STRAND 6586..6589
FT /evidence="ECO:0007829|PDB:3UTO"
FT STRAND 6594..6597
FT /evidence="ECO:0007829|PDB:3UTO"
FT STRAND 6602..6609
FT /evidence="ECO:0007829|PDB:3UTO"
FT STRAND 6615..6620
FT /evidence="ECO:0007829|PDB:3UTO"
FT STRAND 6627..6636
FT /evidence="ECO:0007829|PDB:3UTO"
FT STRAND 6639..6644
FT /evidence="ECO:0007829|PDB:3UTO"
FT HELIX 6649..6651
FT /evidence="ECO:0007829|PDB:3UTO"
FT STRAND 6653..6661
FT /evidence="ECO:0007829|PDB:3UTO"
FT STRAND 6664..6675
FT /evidence="ECO:0007829|PDB:3UTO"
SQ SEQUENCE 7158 AA; 788953 MW; 561EF9DB13387505 CRC64;
MVGAPRFTQK PSIQQTPTGD LLMECHLEAD PQPTIAWQHS GNLLEPSGRV VQTLTPLGGS
LYKATLVIKE PNAGDGGAYK CTARNQLGES NANINLNFAG AGGDEAKSRG PSFVGKPRII
PKDGGALIVM ECKVKSASTP VAKWMKDGVP LSMGGLYHAI FSDLGDQTYL CQLEIRGPSS
SDAGQYRCNI RNDQGETNAN LALNFEEPDP SERQERKRST ASPRPSSRGP GSRPSSPKKS
MKSREGTPKR TLKPREGSPS KKLRSRTSTP VNEEVSQSES RRSSRTDKME VDQVSGASKR
KPDGLPPPGG DEKKLRAGSP STRKSPSRKS ASPTPSRKGS SAGGAASGTT GASASATSAT
SGGSASSDAS RDKYTRPPIV LEASRSQTGR IGGSVVLEVQ WQCHSSTIIE WYRDGTLVRN
SSEYSQSFNG SIAKLQVNKL TEEKSGLYKC HAKCDYGEGQ SSAMVKIEQS DVEEELMKHR
KDAEDEYQKE EQKSQTLQAE TKKRVARRSK SKSKSPAPQA KKSTTSESGR QEASEVEHKR
SSSVRPDPDE ESQLDEIPSS GLTIPEERRR ELLGQVGESD DEVSESISEL PSFAGGKPRR
KTDSPPKQDD MFSRDTLLRK TTTSTKNESS TVEEKTKLRK TVKKVDGELD FKAMVKLKKV
KKEEGGTTEK SGFPLDHADS TSSVLSQESR SRRGSNAPFA KDGLPEQPAN PFAQLKKVKS
GAGGLEKSDS MASLKKLDLK KGKIDDNSDG AFKVQLKKVV KKEVKESTIS VKEKNGTESG
IKTEFKMEKR ERTTLQKYEK TDSDGSKKED KPKKVSIAPV STNKSSDDEP STPRHHKEVE
EKSTSEELKA KVAGRQVGQK RNGAQKPEEP KNLLSQIQLK KVTKKAHDDT NELEGIKLKK
VTTVPKHVAD DDSQSESESR RGSVFGELRR GSRAPRDSAD NSRRDSIRRS SIDMRRESVQ
EILEKTSTPL VPSGASGSAP KIVEVPENVT VVENETAILT CKVSGSPAPT FRWFKGSREV
ISGGRFKHIT DGKEHTVALA LLKCRSQDEG PYTLTIENVH GTDSADVKLL VTSDNGLDFR
AMLKHRESQA GFQKDGEGGG AGGGGGEKKP MTEAERRQSL FPGKKVEKWD IPLPEKTVQQ
QVDKICEWKC TYSRPNAKIR WYKDRKEIFS GGLKYKIVIE KNVCTLIINN PEVDDTGKYT
CEANGVPTHA QLTVLEPPMK YSFLNPLPNT QEIYRTKQAV LTCKVNTPRA PLVWYRGSKA
IQEGDPRFII EKDAVGRCTL TIKEVEEDDQ AEWTARITQD VFSKVQVYVE EPRHTFVVPM
KSQKVNESDL ATLETDVNDK DAEVVWWHDG KRIDIDGVKF KVESSNRKRR LIINGARIED
HGEYKCTTKD DRTMAQLIVD AKNKFIVALK DTEVIEKDDV TLMCQTKDTK TPGIWFRNGK
QISSMPGGKF ETQSRNGTHT LKIGKIEMNE ADVYEIDQAG LRGSCNVTVL EAEKRPILNW
KPKKIEAKAG EPCVVKVPFQ IKGTRRGDPK AQILKNGKPI DEEMRKLVEV IIKDDVAEIV
FKNPQLADTG KWALELGNSA GTALAPFELF VKDKPKPPKG PLETKNVTAE GLDLVWGTPD
PDEGAPVKAY IIEMQEGRSG NWAKVGETKG TDFKVKDLKE HGEYKFRVKA LNECGLSDPL
TGESVLAKNP YGVPGKPKNM DAIDVDKDHC TLAWEPPEED GGAPITGYII ERREKSEKDW
HQVGQTKPDC CELTDKKVVE DKEYLYRVKA VNKAGPGDPC DHGKPIKMKA KKASPEFTGG
GIKDLRLKVG ETIKYDVPIS GEPLPECLWV VNGKPLKAVG RVKMSSERGK HIMKIENAVR
ADSGKFTITL KNSSGSCDST ATVTVVGRPT PPKGPLDIAD VCADGATLSW NPPDDDGGDP
LTGYIVEAQD MDNKGKYIEV GKVDPNTTTL KVNGLRNKGN YKFRVKAVNN EGESEPLSAD
QYTQIKDPWD EPGKPGRPEI TDFDADRIDI AWEPPHKDGG APIEEYIVEV RDPDTKEWKE
VKRVPDTNAS ISGLKEGKEY QFRVRAVNKA GPGQPSEPSE KQLAKPKFIP AWLKHDNLKS
ITVKAGATVR WEVKIGGEPI PEVKWFKGNQ QLENGIQLTI DTRKNEHTIL CIPSAMRSDV
GEYRLTVKNS HGADEEKANL TVLDRPSKPN GPLEVSDVFE DNLNLSWKPP DDDGGEPIEY
YEVEKLDTAT GRWVPCAKVK DTKAHIDGLK KGQTYQFRVK AVNKEGASDA LSTDKDTKAK
NPYDEPGKTG TPDVVDWDAD RVSLEWEPPK SDGGAPITQY VIEKKGKHGR DWQECGKVSG
DQTNAEILGL KEGEEYQFRV KAVNKAGPGE ASDPSRKVVA KPRNLKPWID REAMKTITIK
VGNDVEFDVP VRGEPPPKKE WIFNEKPVDD QKIRIESEDY KTRFVLRGAT RKHAGLYTLT
ATNASGSDKH SVEVIVLGKP SSPLGPLEVS NVYEDRADLE WKVPEDDGGA PIDHYEIEKM
DLATGRWVPC GRSETTKTTV PNLQPGHEYK FRVRAVNKEG ESDPLTTNTA ILAKNPYEVP
GKVDKPELVD WDKDHVDLAW NAPDDGGAPI EAFVIEKKDK NGRWEEALVV PGDQKTATVP
NLKEGEEYQF RISARNKAGT GDPSDPSDRV VAKPRNLAPR IHREDLSDTT VKVGATLKFI
VHIDGEPAPD VTWSFNGKGI GESKAQIENE PYISRFALPK ALRKQSGKYT ITATNINGTD
SVTINIKVKS KPTKPKGPIE VTDVFEDRAT LDWKPPEDDG GEPIEFYEIE KMNTKDGIWV
PCGRSGDTHF TVDSLNKGDH YKFRVKAVNS EGPSDPLETE TDILAKNPFD RPDRPGRPEP
TDWDSDHVDL KWDPPLSDGG APIEEYQIEK RTKYGRWEPA ITVPGGQTTA TVPDLTPNEE
YEFRVVAVNK GGPSDPSDAS KAVIAKPRNL KPHIDRDALK NLTIKAGQSI SFDVPVSGEP
APTVTWHWPD NREIRNGGRV KLDNPEYQSK LVVKQMERGD SGTFTIKAVN ANGEDEATVK
INVIDKPTSP NGPLDVSDVH GDHVTLNWRA PDDDGGIPIE NYVIEKYDTA SGRWVPAAKV
AGDKTTAVVD GLIPGHEYKF RVAAVNAEGE SDPLETFGTT LAKDPFDKPG KTNAPEITDW
DKDHVDLEWK PPANDGGAPI EEYVVEMKDE FSPFWNDVAH VPAGQTNATV GNLKEGSKYE
FRIRAKNKAG LGDPSDSASA VAKARNVPPV IDRNSIQEIK VKAGQDFSLN IPVSGEPTPT
ITWTFEGTPV ESDDRMKLNN EDGKTKFHVK RALRSDTGTY IIKAENENGT DTAEVKVTVL
DHPSSPRGPL DVTNIVKDGC DLAWKEPEDD GGAEISHYVI EKQDAATGRW TACGESKDTN
FHVDDLTQGH EYKFRVKAVN RHGDSDPLEA REAIIAKDPF DRADKPGTPE IVDWDKDHAD
LKWTPPADDG GAPIEGYLVE MRTPSGDWVP AVTVGAGELT ATVDGLKPGQ TYQFRVKALN
KAGESTPSDP SRTMVAKPRH LAPKINRDMF VAQRVKAGQT LNFDVNVEGE PAPKIEWFLN
GSPLSSGGNT HIDNNTDNNT KLTTKSTARA DSGKYKIVAT NESGKDEHEV DVNILDIPGA
PEGPLRHKDI TKESVVLKWD EPLDDGGSPI TNYVVEKQED GGRWVPCGET SDTSLKVNKL
SEGHEYKFRV KAVNRQGTSA PLTSDHAIVA KNPFDEPDAP TDVTPVDWDK DHVDLEWKPP
ANDGGAPIDA YIVEKKDKFG DWVECARVDG KTTKATADNL TPGETYQFRV KAVNKAGPGK
PSDPTGNVVA KPRRMAPKLN LAGLLDLRIK AGTPIKLDIA FEGEPAPVAK WKANDATIDT
GARADVTNTP TSSAIHIFSA VRGDTGVYKI IVENEHGKDT AQCNVTVLDV PGTPEGPLKI
DEIHKEGCTL NWKPPTDNGG TDVLHYIVEK MDTSRGTWQE VGTFPDCTAK VNKLVPGKEY
AFRVKAVNLQ GESKPLEAEE PIIAKNQFDV PDPVDKPEVT DWDKDRIDIK WNPTANNGGA
PVTGYIVEKK EKGSAIWTEA GKTPGTTFSA DNLKPGVEYE FRVIAVNAAG PSDPSDPTDP
QITKARYLKP KILTASRKIK IKAGFTHNLE VDFIGAPDPT ATWTVGDSGA ALAPELLVDA
KSSTTSIFFP SAKRADSGNY KLKVKNELGE DEAIFEVIVQ DRPSAPEGPL EVSDVTKDSC
VLNWKPPKDD GGAEISNYVV EKRDTKTNTW VPVSAFVTGT SITVPKLTEG HEYEFRVMAE
NTFGRSDSLN TDEPVLAKDP FGTPGKPGRP EIVDTDNDHI DIKWDPPRDN GGSPVDHYDI
ERKDAKTGRW IKVNTSPVQG TAFSDTRVQK GHTYEYRVVA VNKAGPGQPS DSSAAATAKP
MHEAPKFDLD LDGKEFRVKA GEPLVITIPF TASPQPDISW TKEGGKPLAG VETTDSQTKL
VIPSTRRSDS GPVKIKAVNP YGEAEANIKI TVIDKPGAPE NITYPAVSRH TCTLNWDAPK
DDGGAEIAGY KIEYQEVGSQ IWDKVPGLIS GTAYTVRGLE HGQQYRFRIR AENAVGLSDY
CQGVPVVIKD PFDPPGAPST PEITGYDTNQ VSLAWNPPRD DGGSPILGYV VERFEKRGGG
DWAPVKMPMV KGTECIVPGL HENETYQFRV RAVNAAGHGE PSNGSEPVTC RPYVEKPGAP
DAPRVGKITK NSAELTWNRP LRDGGAPIDG YIVEKKKLGD NDWTRCNDKP VRDTAFEVKN
LGEKEEYEFR VIAVNSAGEG EPSKPSDLVL IEEQPGRPIF DINNLKDITV RAGETIQIRI
PYAGGNPKPI IDLFNGNSPI FENERTVVDV NPGEIVITTT GSKRSDAGPY KISATNKYGK
DTCKLNVFVL DAPGKPTGPI RATDIQADAM TLSWRPPKDN GGDAITNYVV EKRTPGGDWV
TVGHPVGTTL RVRNLDANTP YEFRVRAENQ YGVGEPLETD DAIVAKNPFD TPGAPGQPEA
VETSEEAITL QWTRPTSDGG APIQGYVIEK REVGSTEWTK AAFGNILDTK HRVTGLTPKK
TYEFRVAAYN AAGQGEYSVN SVPITADNAP TRPKINMGML TRDILAYAGE RAKILVPFAA
SPAPKVTFSK GENKISPTDP RVKVEYSDFL ATLTIEKSEL TDGGLYFVEL ENSQGSDSAS
IRLKVVDKPA SPQHIRVEDI APDCCTLYWM PPSSDGGSPI TNYIVEKLDL RHSDGKWEKV
SSFVRNLNYT VGGLIKDNRY RFRVRAETQY GVSEPCELAD VVVAKYQFEV PNQPEAPTVR
DKDSTWAELE WDPPRDGGSK IIGYQVQYRD TSSGRWINAK MDLSEQCHAR VTGLRQNGEF
EFRIIAKNAA GFSKPSPPSE RCQLKSRFGP PGPPIHVGAK SIGRNHCTIT WMAPLEDGGS
KITGYNVEIR EYGSTLWTVA SDYNVREPEF TVDKLREFND YEFRVVAINA AGKGIPSLPS
GPIKIQESGG SRPQIVVKPE DTAQPYNRRA VFTCEAVGRP EPTARWLRNG RELPESSRYR
FEASDGVYKF TIKEVWDIDA GEYTVEVSNP YGSDTATANL VVQAPPVIEK DVPNTILPSG
DLVRLKIYFS GTAPFRHSLV LNREEIDMDH PTIRIVEFDD HILITIPALS VREAGRYEYT
VSNDSGEATT GFWLNVTGLP EAPQGPLHIS NIGPSTATLS WRPPVTDGGS KITSYVVEKR
DLSKDEWVTV TSNVKDMNYI VTGLFENHEY EFRVSAQNEN GIGAPLVSEH PIIARLPFDP
PTSPLNLEIV QVGGDYVTLS WQRPLSDGGG RLRGYIVEKQ EEEHDEWFRC NQNPSPPNNY
NVPNLIDGRK YRYRVFAVND AGLSDLAELD QTLFQASGSG EGPKIVSPLS DLNEEVGRCV
TFECEISGSP RPEYRWFKGC KELVDTSKYT LINKGDKQVL IINDLTSDDA DEYTCRATNS
SGTRSTRANL RIKTKPRVFI PPKYHGGYEA QKGETIELKI PYKAYPQGEA RWTKDGEKIE
NNSKFSITTD DKFATLRISN ASREDYGEYR VVVENSVGSD SGTVNVTVAD VPEPPRFPII
ENILDEAVIL SWKPPALDGG SLVTNYTIEK REAMGGSWSP CAKSRYTYTT IEGLRAGKQY
EFRIIAENKH GQSKPCEPTA PVLIPGDERK RRRGYDVDEQ GKIVRGKGTV SSNYDNYVFD
IWKQYYPQPV EIKHDHVLDH YDIHEELGTG AFGVVHRVTE RATGNNFAAK FVMTPHESDK
ETVRKEIQTM SVLRHPTLVN LHDAFEDDNE MVMIYEFMSG GELFEKVADE HNKMSEDEAV
EYMRQVCKGL CHMHENNYVH LDLKPENIMF TTKRSNELKL IDFGLTAHLD PKQSVKVTTG
TAEFAAPEVA EGKPVGYYTD MWSVGVLSYI LLSGLSPFGG ENDDETLRNV KSCDWNMDDS
AFSGISEDGK DFIRKLLLAD PNTRMTIHQA LEHPWLTPGN APGRDSQIPS SRYTKIRDSI
KTKYDAWPEP LPPLGRISNY SSLRKHRPQE YSIRDAFWDR SEAQPRFIVK PYGTEVGEGQ
SANFYCRVIA SSPPVVTWHK DDRELKQSVK YMKRYNGNDY GLTINRVKGD DKGEYTVRAK
NSYGTKEEIV FLNVTRHSEP LKFEPLEPMK KAPSPPRVEE FKERRSAPFF TFHLRNRLIQ
KNHQCKLTCS LQGNPNPTIE WMKDGHPVDE DRVQVSFRSG VCSLEIFNAR VDDAGTYTVT
ATNDLGVDVS ECVLTVQTKG GEPIPRVSSF RPRRAYDTLS TGTDVERSHS YADMRRRSLI
RDVSPDVRSA ADDLKTKITN ELPSFTAQLS DSETEVGGSA EFSAAVSGQP EPLIEWLHNG
ERISESDSRF RASYVAGKAT LRISDAKKSD EGQYLCRASN SAGQEQTRAT LTVKGDQPLL
NGHAGQAVES ELRVTKHLGG EIVNNGESVT FEARVQGTPE EVLWMRNGQE LTNGDKTSIS
QDGETLSFTI NSADASDAGH YQLEVRSKGT NLVSVASLVV VGEKADPPVT RLPSSVSAPL
GGSTAFTIEF ENVEGLTVQW FRGSEKIEKN ERVKSVKTGN TFKLDIKNVE QDDDGIYVAK
VVKEKKAIAK YAAALLLV
