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Serine/threonine-protein kinase TNNI3K (EC 2.7.11.1) (Cardiac ankyrin repeat kinase) (Cardiac troponin I-interacting kinase) (TNNI3-interacting kinase)

 TNI3K_HUMAN             Reviewed;         835 AA.
Q59H18; Q17RN0; Q49AR1; Q6MZS9; Q9Y2V6;
22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
13-JUL-2010, sequence version 3.
25-OCT-2017, entry version 143.
RecName: Full=Serine/threonine-protein kinase TNNI3K;
EC=2.7.11.1;
AltName: Full=Cardiac ankyrin repeat kinase;
AltName: Full=Cardiac troponin I-interacting kinase;
AltName: Full=TNNI3-interacting kinase;
Name=TNNI3K {ECO:0000312|EMBL:AAH32865.1}; Synonyms=CARK;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:AAD29632.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY,
SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, INTERACTION WITH TNNI3;
ACTC; ACTA1; MYBPC3; AIP; BABP3 AND HADHB, AND MUTAGENESIS OF LYS-490.
TISSUE=Heart {ECO:0000312|EMBL:AAD29632.1};
PubMed=12721663; DOI=10.1007/s00109-003-0427-x;
Zhao Y., Meng X.-M., Wei Y.-J., Zhao X.-W., Liu D.-Q., Cao H.-Q.,
Liew C.-C., Ding J.-F.;
"Cloning and characterization of a novel cardiac-specific kinase that
interacts specifically with cardiac troponin I.";
J. Mol. Med. 81:297-304(2003).
[2] {ECO:0000305, ECO:0000312|EMBL:AAP72030.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Jeyaseelan R.;
"Cardiac ankyrin repeat kinase (CARK).";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000305, ECO:0000312|EMBL:AAP72030.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain {ECO:0000312|EMBL:BAD92178.1};
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Fetal kidney;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5] {ECO:0000305, ECO:0000312|EMBL:AAP72030.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLY-785 AND TYR-833.
SeattleSNPs variation discovery resource;
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
[6] {ECO:0000312|EMBL:CAI16293.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[7] {ECO:0000305, ECO:0000312|EMBL:AAP72030.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8] {ECO:0000305, ECO:0000312|EMBL:AAH32865.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
TISSUE=Brain {ECO:0000312|EMBL:AAH32865.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
VARIANT [LARGE SCALE ANALYSIS] GLY-629.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[10]
VARIANTS [LARGE SCALE ANALYSIS] HIS-151; LEU-263; LEU-309; LEU-430;
LEU-510; MET-637; THR-686 AND ILE-798.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
[11]
INVOLVEMENT IN CCDD, VARIANT CCDD ASP-526, AND CHARACTERIZATION OF
VARIANT CCDD ASP-526.
PubMed=24925317; DOI=10.1093/hmg/ddu297;
Theis J.L., Zimmermann M.T., Larsen B.T., Rybakova I.N., Long P.A.,
Evans J.M., Middha S., de Andrade M., Moss R.L., Wieben E.D.,
Michels V.V., Olson T.M.;
"TNNI3K mutation in familial syndrome of conduction system disease,
atrial tachyarrhythmia and dilated cardiomyopathy.";
Hum. Mol. Genet. 23:5793-5804(2014).
-!- FUNCTION: May play a role in cardiac physiology.
{ECO:0000303|PubMed:12721663}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:12721663}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:12721663};
-!- SUBUNIT: Interacts with TNNI3, ACTC, ACTA1, MYBPC3, AIP, BABP3 and
HADHB. {ECO:0000269|PubMed:12721663}.
-!- INTERACTION:
P19429:TNNI3; NbExp=2; IntAct=EBI-704142, EBI-704146;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12721663}.
Cytoplasm {ECO:0000269|PubMed:12721663}. Note=Expressed at lower
levels in the cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=2 {ECO:0000269|PubMed:12721663};
IsoId=Q59H18-2; Sequence=Displayed;
Name=1 {ECO:0000305};
IsoId=Q59H18-1; Sequence=VSP_039403;
Note=Based on a naturally occurring readthrough transcript which
produces a FPGT-TNNI3K fusion protein.;
Name=3 {ECO:0000305};
IsoId=Q59H18-3; Sequence=VSP_039403, VSP_051882, VSP_051883;
Note=Based on a naturally occurring readthrough transcript which
produces a FPGT-TNNI3K fusion protein.;
Name=4 {ECO:0000305};
IsoId=Q59H18-4; Sequence=VSP_039403, VSP_051884, VSP_051885;
Note=Based on a naturally occurring readthrough transcript which
produces a FPGT-TNNI3K fusion protein.;
-!- TISSUE SPECIFICITY: Highly expressed in both adult and fetal
heart. {ECO:0000269|PubMed:12721663}.
-!- PTM: Autophosphorylated. {ECO:0000269|PubMed:12721663}.
-!- DISEASE: Cardiac conduction disease with or without dilated
cardiomyopathy (CCDD) [MIM:616117]: A cardiac disorder
characterized by atrial tachyarrhythmia and conduction system
disease. Some patients have dilated cardiomyopathy.
{ECO:0000269|PubMed:24925317}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
protein kinase family. MAP kinase kinase kinase subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAD92178.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAE45949.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/tnni3k/";
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EMBL; AF116826; AAD29632.1; -; mRNA.
EMBL; AY303691; AAP72030.1; -; mRNA.
EMBL; AB208941; BAD92178.1; ALT_INIT; Transcribed_RNA.
EMBL; BX640903; CAE45949.1; ALT_INIT; mRNA.
EMBL; DQ822519; ABG46944.1; -; Genomic_DNA.
EMBL; BX470253; CAI16293.1; -; Genomic_DNA.
EMBL; AC093158; CAI16293.1; JOINED; Genomic_DNA.
EMBL; AC098692; CAI16293.1; JOINED; Genomic_DNA.
EMBL; AC105271; CAI16293.1; JOINED; Genomic_DNA.
EMBL; AC119672; CAI16293.1; JOINED; Genomic_DNA.
EMBL; CH471059; EAX06415.1; -; Genomic_DNA.
EMBL; BC032865; AAH32865.1; -; mRNA.
EMBL; BC113539; AAI13540.1; -; mRNA.
EMBL; BC117262; AAI17263.1; -; mRNA.
CCDS; CCDS664.1; -. [Q59H18-2]
RefSeq; NP_001186256.2; NM_001199327.1.
RefSeq; NP_057062.1; NM_015978.2. [Q59H18-2]
UniGene; Hs.480085; -.
PDB; 4YFF; X-ray; 3.07 A; A/B/C/D=420-730.
PDB; 4YFI; X-ray; 2.70 A; A/B/C/D=402-730.
PDBsum; 4YFF; -.
PDBsum; 4YFI; -.
ProteinModelPortal; Q59H18; -.
SMR; Q59H18; -.
BioGrid; 119276; 11.
IntAct; Q59H18; 8.
STRING; 9606.ENSP00000450895; -.
BindingDB; Q59H18; -.
ChEMBL; CHEMBL5260; -.
GuidetoPHARMACOLOGY; 2247; -.
iPTMnet; Q59H18; -.
PhosphoSitePlus; Q59H18; -.
BioMuta; TNNI3K; -.
DMDM; 300669705; -.
PaxDb; Q59H18; -.
PeptideAtlas; Q59H18; -.
PRIDE; Q59H18; -.
DNASU; 51086; -.
Ensembl; ENST00000326637; ENSP00000322251; ENSG00000116783. [Q59H18-2]
GeneID; 100526835; -.
GeneID; 51086; -.
KEGG; hsa:100526835; -.
KEGG; hsa:51086; -.
UCSC; uc001dgf.3; human. [Q59H18-2]
CTD; 100526835; -.
CTD; 51086; -.
DisGeNET; 51086; -.
EuPathDB; HostDB:ENSG00000116783.14; -.
GeneCards; TNNI3K; -.
HGNC; HGNC:19661; TNNI3K.
HPA; HPA072331; -.
MalaCards; TNNI3K; -.
MIM; 613932; gene.
MIM; 616117; phenotype.
neXtProt; NX_Q59H18; -.
OpenTargets; ENSG00000116783; -.
OpenTargets; ENSG00000259030; -.
PharmGKB; PA134976654; -.
eggNOG; ENOG410IT5N; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00900000140790; -.
HOGENOM; HOG000234421; -.
HOVERGEN; HBG079513; -.
InParanoid; Q59H18; -.
KO; K17535; -.
OrthoDB; EOG091G01QL; -.
PhylomeDB; Q59H18; -.
PRO; PR:Q59H18; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000116783; -.
CleanEx; HS_TNNI3K; -.
ExpressionAtlas; Q59H18; baseline and differential.
Genevisible; Q59H18; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0004871; F:signal transducer activity; IBA:GO_Central.
GO; GO:0031013; F:troponin I binding; IPI:UniProtKB.
GO; GO:0086069; P:bundle of His cell to Purkinje myocyte communication; IMP:BHF-UCL.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:1903779; P:regulation of cardiac conduction; IGI:BHF-UCL.
GO; GO:0055117; P:regulation of cardiac muscle contraction; IMP:BHF-UCL.
GO; GO:0002027; P:regulation of heart rate; IMP:BHF-UCL.
CDD; cd00204; ANK; 5.
Gene3D; 1.25.40.20; -; 4.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
Pfam; PF12796; Ank_2; 3.
Pfam; PF07714; Pkinase_Tyr; 1.
PRINTS; PR01415; ANKYRIN.
SMART; SM00248; ANK; 10.
SUPFAM; SSF48403; SSF48403; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 6.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ANK repeat; ATP-binding;
Cardiomyopathy; Coiled coil; Complete proteome; Cytoplasm;
Disease mutation; Kinase; Magnesium; Metal-binding;
Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Serine/threonine-protein kinase;
Transferase.
CHAIN 1 835 Serine/threonine-protein kinase TNNI3K.
/FTId=PRO_0000086757.
REPEAT 66 96 ANK 1.
REPEAT 100 129 ANK 2.
REPEAT 133 162 ANK 3.
REPEAT 166 195 ANK 4.
REPEAT 199 228 ANK 5.
REPEAT 234 263 ANK 6.
REPEAT 269 298 ANK 7.
REPEAT 304 335 ANK 8.
REPEAT 339 368 ANK 9.
REPEAT 381 410 ANK 10.
DOMAIN 463 723 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 469 477 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COILED 21 51 {ECO:0000255}.
COMPBIAS 733 746 Poly-Ser.
ACT_SITE 588 588 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 490 490 ATP.
VAR_SEQ 1 13 MGNYKSRPTQTCT -> MAAARDPPEVSLREATQRKLRRFS
ELRGKLVARGEFWDIVAITAADEKQELAYNQQLSEKLKRKE
LPLGVQYHVFVDPAGAKIGNGGSTLCALQCLEKLYGDKWNS
FTILLIHS (in isoform 1, isoform 3 and
isoform 4). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005,
ECO:0000303|Ref.3}.
/FTId=VSP_039403.
VAR_SEQ 591 596 SHNILL -> RYFFPK (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_051882.
VAR_SEQ 597 835 Missing (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_051883.
VAR_SEQ 708 742 GRPEFSEVVMKLEECLCNIELMSPASSNSSGSLSP -> AK
SRPSHYPVSSVYTETLKKKNEDRFGMWIEYLRR (in
isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_051884.
VAR_SEQ 743 835 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_051885.
VARIANT 151 151 D -> H (in dbSNP:rs34874695).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041223.
VARIANT 263 263 P -> L (in dbSNP:rs34521608).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041224.
VARIANT 309 309 F -> L. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_041225.
VARIANT 430 430 S -> L (in a colorectal adenocarcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041226.
VARIANT 510 510 V -> L (in dbSNP:rs34335537).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041227.
VARIANT 526 526 G -> D (in CCDD; the mutation results in
decreased protein solubility; causes
abnormal aggregation; markedly reduced
protein expression is observed in the
sarcoplasm and nuclei of patient
cardiomyocytes; dbSNP:rs606231469).
{ECO:0000269|PubMed:24925317}.
/FTId=VAR_072650.
VARIANT 629 629 R -> G (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035639.
VARIANT 637 637 T -> M (in dbSNP:rs2274260).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041228.
VARIANT 686 686 I -> T (in dbSNP:rs3737564).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041229.
VARIANT 785 785 A -> G (in dbSNP:rs45578635).
{ECO:0000269|Ref.5}.
/FTId=VAR_038821.
VARIANT 798 798 M -> I (in a head & Neck squamous cell
carcinoma sample; somatic mutation;
dbSNP:rs201613442).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041230.
VARIANT 833 833 D -> Y (in dbSNP:rs45614933).
{ECO:0000269|Ref.5}.
/FTId=VAR_038822.
MUTAGEN 490 490 K->R: Loss of autophosphorylation
activity. {ECO:0000269|PubMed:12721663}.
CONFLICT 127 127 I -> V (in Ref. 8; AAH32865).
{ECO:0000305}.
CONFLICT 250 250 I -> M (in Ref. 4; CAE45949).
{ECO:0000305}.
CONFLICT 367 367 N -> S (in Ref. 4; CAE45949).
{ECO:0000305}.
CONFLICT 629 629 R -> L (in Ref. 8; AAH32865).
{ECO:0000305}.
HELIX 442 451 {ECO:0000244|PDB:4YFI}.
HELIX 454 456 {ECO:0000244|PDB:4YFI}.
HELIX 460 462 {ECO:0000244|PDB:4YFI}.
STRAND 463 470 {ECO:0000244|PDB:4YFI}.
STRAND 473 482 {ECO:0000244|PDB:4YFI}.
STRAND 485 492 {ECO:0000244|PDB:4YFI}.
HELIX 502 515 {ECO:0000244|PDB:4YFI}.
STRAND 524 528 {ECO:0000244|PDB:4YFI}.
HELIX 532 534 {ECO:0000244|PDB:4YFI}.
STRAND 536 540 {ECO:0000244|PDB:4YFI}.
HELIX 547 552 {ECO:0000244|PDB:4YFI}.
HELIX 560 578 {ECO:0000244|PDB:4YFI}.
STRAND 580 582 {ECO:0000244|PDB:4YFI}.
HELIX 591 593 {ECO:0000244|PDB:4YFI}.
STRAND 594 596 {ECO:0000244|PDB:4YFI}.
STRAND 602 604 {ECO:0000244|PDB:4YFI}.
HELIX 628 630 {ECO:0000244|PDB:4YFI}.
HELIX 633 636 {ECO:0000244|PDB:4YFI}.
HELIX 637 639 {ECO:0000244|PDB:4YFI}.
HELIX 645 660 {ECO:0000244|PDB:4YFI}.
TURN 664 667 {ECO:0000244|PDB:4YFI}.
HELIX 670 678 {ECO:0000244|PDB:4YFI}.
HELIX 692 701 {ECO:0000244|PDB:4YFI}.
HELIX 706 708 {ECO:0000244|PDB:4YFI}.
HELIX 712 725 {ECO:0000244|PDB:4YFI}.
SEQUENCE 835 AA; 92851 MW; 3B21484B434F46E8 CRC64;
MGNYKSRPTQ TCTDEWKKKV SESYVITIER LEDDLQIKEK ELTELRNIFG SDEAFSKVNL
NYRTENGLSL LHLCCICGGK KSHIRTLMLK GLRPSRLTRN GFTALHLAVY KDNAELITSL
LHSGADIQQV GYGGLTALHI ATIAGHLEAA DVLLQHGANV NIQDAVFFTP LHIAAYYGHE
QVTRLLLKFG ADVNVSGEVG DRPLHLASAK GFLNIAKLLM EEGSKADVNA QDNEDHVPLH
FCSRFGHHDI VKYLLQSDLE VQPHVVNIYG DTPLHLACYN GKFEVAKEII QISGTESLTK
ENIFSETAFH SACTYGKSID LVKFLLDQNV ININHQGRDG HTGLHSACYH GHIRLVQFLL
DNGADMNLVA CDPSRSSGEK DEQTCLMWAY EKGHDAIVTL LKHYKRPQDE LPCNEYSQPG
GDGSYVSVPS PLGKIKSMTK EKADILLLRA GLPSHFHLQL SEIEFHEIIG SGSFGKVYKG
RCRNKIVAIK RYRANTYCSK SDVDMFCREV SILCQLNHPC VIQFVGACLN DPSQFAIVTQ
YISGGSLFSL LHEQKRILDL QSKLIIAVDV AKGMEYLHNL TQPIIHRDLN SHNILLYEDG
HAVVADFGES RFLQSLDEDN MTKQPGNLRW MAPEVFTQCT RYTIKADVFS YALCLWEILT
GEIPFAHLKP AAAAADMAYH HIRPPIGYSI PKPISSLLIR GWNACPEGRP EFSEVVMKLE
ECLCNIELMS PASSNSSGSL SPSSSSDCLV NRGGPGRSHV AALRSRFELE YALNARSYAA
LSQSAGQYSS QGLSLEEMKR SLQYTPIDKY GYVSDPMSSM HFHSCRNSSS FEDSS


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