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Creatine kinase B-type (EC 2.7.3.2) (B-CK) (Creatine kinase B chain)

 KCRB_HUMAN              Reviewed;         381 AA.
P12277; A8K236; B2R5R4; Q2LE07; Q6FG40; Q9UC66;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 1.
25-OCT-2017, entry version 185.
RecName: Full=Creatine kinase B-type;
EC=2.7.3.2;
AltName: Full=B-CK;
AltName: Full=Creatine kinase B chain;
Name=CKB; Synonyms=CKBB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3034271; DOI=10.1016/0006-291X(87)91427-6;
Villarreal-Levy G., Ma T.S., Kerner S.A., Roberts R., Perryman M.B.;
"Human creatine kinase: isolation and sequence analysis of cDNA clones
for the B subunit, development of subunit specific probes and
determination of gene copy number.";
Biochem. Biophys. Res. Commun. 144:1116-1127(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3692484; DOI=10.1016/0888-7543(87)90004-8;
Mariman E.C.M., Broers C.A.M., Claesen C.A.A., Tesser G.I.,
Wieringa B.;
"Structure and expression of the human creatine kinase B gene.";
Genomics 1:126-137(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2883200; DOI=10.1172/JCI112969;
Kaye F.J., McBride O.W., Battey J.F., Gazder A.F., Sausville E.A.;
"Human creatine kinase-B complementary DNA. Nucleotide sequence, gene
expression in lung cancer, and chromosomal assignment to two distinct
loci.";
J. Clin. Invest. 79:1412-1420(1987).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Brain;
PubMed=2771648; DOI=10.1093/nar/17.15.6385;
Mariman E.C.M., Schepens J.T.G., Wieringa B.;
"Complete nucleotide sequence of the human creatine kinase B gene.";
Nucleic Acids Res. 17:6385-6385(1989).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cerebellum, and Subthalamic nucleus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-177 AND LEU-309.
NIEHS SNPs program;
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
[8]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Eye, and Lung;
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).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-97.
PubMed=2828370;
Daouk G.H., Kaddurah-Daouk R., Putney S., Kingston R., Schimmel P.;
"Isolation of a functional human gene for brain creatine kinase.";
J. Biol. Chem. 263:2442-2446(1988).
[11]
PROTEIN SEQUENCE OF 2-22.
TISSUE=Eye;
PubMed=7637327;
Kliffen M., de Jong P.T.V.M., Luider T.M.;
"Protein analysis of human maculae in relation to age-related
maculopathy.";
Lab. Invest. 73:267-272(1995).
[12]
PROTEIN SEQUENCE OF 2-11; 33-43; 157-172; 224-236; 253-265; 308-314
AND 342-366, CLEAVAGE OF INITIATOR METHIONINE, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=Colon carcinoma;
Bienvenut W.V., Heiserich L., Gottlieb E.;
Submitted (MAR-2008) to UniProtKB.
[13]
PROTEIN SEQUENCE OF 33-43; 87-96; 108-130; 157-172; 224-236; 253-265;
320-341 AND 359-381, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[14]
MUTAGENESIS OF CYS-283; ARG-292 AND ASP-340.
PubMed=8186255;
Lin L., Perryman M.B., Friedman D., Roberts R., Ma T.S.;
"Determination of the catalytic site of creatine kinase by site-
directed mutagenesis.";
Biochim. Biophys. Acta 1206:97-104(1994).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-35 AND SER-199, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22905912; DOI=10.1021/pr300539b;
Rosenow A., Noben J.P., Jocken J., Kallendrusch S.,
Fischer-Posovszky P., Mariman E.C., Renes J.;
"Resveratrol-induced changes of the human adipocyte secretion
profile.";
J. Proteome Res. 11:4733-4743(2012).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 AND THR-35, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ADP AND
CREATINE, ATP-BINDING SITES, AND SUBSTRATE-BINDING SITES.
PubMed=18977227; DOI=10.1016/j.febslet.2008.10.039;
Bong S.M., Moon J.H., Nam K.H., Lee K.S., Chi Y.M., Hwang K.Y.;
"Structural studies of human brain-type creatine kinase complexed with
the ADP-Mg2+-NO3- -creatine transition-state analogue complex.";
FEBS Lett. 582:3959-3965(2008).
-!- FUNCTION: Reversibly catalyzes the transfer of phosphate between
ATP and various phosphogens (e.g. creatine phosphate). Creatine
kinase isoenzymes play a central role in energy transduction in
tissues with large, fluctuating energy demands, such as skeletal
muscle, heart, brain and spermatozoa.
-!- CATALYTIC ACTIVITY: ATP + creatine = ADP + phosphocreatine.
{ECO:0000255|PROSITE-ProRule:PRU10029}.
-!- SUBUNIT: Dimer of identical or non-identical chains. With MM being
the major form in skeletal muscle and myocardium, MB existing in
myocardium, and BB existing in many tissues, especially brain.
{ECO:0000269|PubMed:18977227}.
-!- INTERACTION:
Q03463:- (xeno); NbExp=3; IntAct=EBI-357706, EBI-9081620;
Q96DX5:ASB9; NbExp=8; IntAct=EBI-357706, EBI-745641;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
{ECO:0000255|PROSITE-ProRule:PRU00842, ECO:0000255|PROSITE-
ProRule:PRU00843}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/ckb/";
-!- WEB RESOURCE: Name=Wikipedia; Note=Creatine kinase entry;
URL="https://en.wikipedia.org/wiki/Creatine_kinase";
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EMBL; M16451; AAA76851.1; -; mRNA.
EMBL; M21243; AAC31758.1; -; Genomic_DNA.
EMBL; M21237; AAC31758.1; JOINED; Genomic_DNA.
EMBL; M21238; AAC31758.1; JOINED; Genomic_DNA.
EMBL; M21239; AAC31758.1; JOINED; Genomic_DNA.
EMBL; M21240; AAC31758.1; JOINED; Genomic_DNA.
EMBL; M21241; AAC31758.1; JOINED; Genomic_DNA.
EMBL; M21242; AAC31758.1; JOINED; Genomic_DNA.
EMBL; L47647; AAA76852.1; -; mRNA.
EMBL; M16364; AAA76850.1; -; mRNA.
EMBL; X15334; CAA33389.1; -; Genomic_DNA.
EMBL; AK290101; BAF82790.1; -; mRNA.
EMBL; AK312282; BAG35211.1; -; mRNA.
EMBL; CR542268; CAG47064.1; -; mRNA.
EMBL; DQ333313; ABC67465.1; -; Genomic_DNA.
EMBL; CH471061; EAW81822.1; -; Genomic_DNA.
EMBL; BC001190; AAH01190.1; -; mRNA.
EMBL; BC004914; AAH04914.1; -; mRNA.
EMBL; BC008323; AAH08323.1; -; mRNA.
EMBL; BC010002; AAH10002.1; -; mRNA.
EMBL; BC019259; AAH19259.1; -; mRNA.
EMBL; BC019281; AAH19281.1; -; mRNA.
EMBL; M22356; AAA52024.1; -; Genomic_DNA.
EMBL; M22355; AAA52024.1; JOINED; Genomic_DNA.
CCDS; CCDS9981.1; -.
PIR; S15935; KIHUCB.
RefSeq; NP_001814.2; NM_001823.4.
UniGene; Hs.173724; -.
PDB; 3B6R; X-ray; 2.00 A; A/B=1-381.
PDB; 3DRB; X-ray; 2.00 A; A/B=1-381.
PDB; 3DRE; X-ray; 2.20 A; A/B=1-381.
PDBsum; 3B6R; -.
PDBsum; 3DRB; -.
PDBsum; 3DRE; -.
ProteinModelPortal; P12277; -.
SMR; P12277; -.
BioGrid; 107572; 78.
CORUM; P12277; -.
DIP; DIP-52968N; -.
IntAct; P12277; 44.
MINT; MINT-1484821; -.
STRING; 9606.ENSP00000299198; -.
ChEMBL; CHEMBL6049; -.
DrugBank; DB00148; Creatine.
iPTMnet; P12277; -.
PhosphoSitePlus; P12277; -.
BioMuta; CKB; -.
DMDM; 125294; -.
REPRODUCTION-2DPAGE; IPI00022977; -.
REPRODUCTION-2DPAGE; P12277; -.
UCD-2DPAGE; P12277; -.
EPD; P12277; -.
PaxDb; P12277; -.
PeptideAtlas; P12277; -.
PRIDE; P12277; -.
TopDownProteomics; P12277; -.
DNASU; 1152; -.
Ensembl; ENST00000348956; ENSP00000299198; ENSG00000166165.
GeneID; 1152; -.
KEGG; hsa:1152; -.
CTD; 1152; -.
DisGeNET; 1152; -.
EuPathDB; HostDB:ENSG00000166165.12; -.
GeneCards; CKB; -.
HGNC; HGNC:1991; CKB.
HPA; CAB047313; -.
HPA; HPA001254; -.
MIM; 123280; gene.
neXtProt; NX_P12277; -.
OpenTargets; ENSG00000166165; -.
PharmGKB; PA26528; -.
eggNOG; KOG3581; Eukaryota.
eggNOG; COG3869; LUCA.
GeneTree; ENSGT00550000074561; -.
HOGENOM; HOG000232165; -.
HOVERGEN; HBG001339; -.
InParanoid; P12277; -.
KO; K00933; -.
OMA; RGHEFMW; -.
OrthoDB; EOG091G0HZ0; -.
PhylomeDB; P12277; -.
TreeFam; TF314214; -.
BioCyc; MetaCyc:HS09344-MONOMER; -.
BRENDA; 2.7.3.2; 2681.
Reactome; R-HSA-71288; Creatine metabolism.
SABIO-RK; P12277; -.
ChiTaRS; CKB; human.
EvolutionaryTrace; P12277; -.
GeneWiki; CKB_(gene); -.
GenomeRNAi; 1152; -.
PRO; PR:P12277; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000166165; -.
CleanEx; HS_CKB; -.
ExpressionAtlas; P12277; baseline and differential.
Genevisible; P12277; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; ISS:AgBase.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004111; F:creatine kinase activity; ISS:AgBase.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0030644; P:cellular chloride ion homeostasis; IEA:Ensembl.
GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
GO; GO:0006600; P:creatine metabolic process; TAS:Reactome.
GO; GO:0021762; P:substantia nigra development; IEP:UniProtKB.
Gene3D; 1.10.135.10; -; 1.
Gene3D; 3.30.590.10; -; 1.
InterPro; IPR000749; ATP-guanido_PTrfase.
InterPro; IPR022415; ATP-guanido_PTrfase_AS.
InterPro; IPR022414; ATP-guanido_PTrfase_cat.
InterPro; IPR022413; ATP-guanido_PTrfase_N.
InterPro; IPR036802; ATP-guanido_PTrfase_N_sf.
InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
PANTHER; PTHR11547; PTHR11547; 1.
Pfam; PF00217; ATP-gua_Ptrans; 1.
Pfam; PF02807; ATP-gua_PtransN; 1.
SUPFAM; SSF48034; SSF48034; 1.
SUPFAM; SSF55931; SSF55931; 1.
PROSITE; PS00112; PHOSPHAGEN_KINASE; 1.
PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1.
PROSITE; PS51509; PHOSPHAGEN_KINASE_N; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome; Cytoplasm;
Direct protein sequencing; Kinase; Nitration; Nucleotide-binding;
Phosphoprotein; Polymorphism; Reference proteome; Transferase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:7637327,
ECO:0000269|Ref.12}.
CHAIN 2 381 Creatine kinase B-type.
/FTId=PRO_0000211966.
DOMAIN 11 98 Phosphagen kinase N-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00842}.
DOMAIN 125 367 Phosphagen kinase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00843}.
NP_BIND 128 132 ATP.
NP_BIND 320 325 ATP.
BINDING 72 72 Substrate; via amide nitrogen.
BINDING 130 130 ATP.
BINDING 132 132 ATP.
BINDING 191 191 ATP.
BINDING 232 232 Substrate.
BINDING 236 236 ATP.
BINDING 285 285 Substrate.
BINDING 292 292 ATP.
BINDING 320 320 ATP.
BINDING 335 335 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00843}.
MOD_RES 4 4 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 35 35 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 125 125 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q04447}.
MOD_RES 199 199 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 269 269 Nitrated tyrosine.
{ECO:0000250|UniProtKB:Q04447}.
MOD_RES 309 309 Phosphoserine.
{ECO:0000250|UniProtKB:P07335}.
MOD_RES 322 322 Phosphothreonine.
{ECO:0000250|UniProtKB:Q04447}.
VARIANT 177 177 K -> R (in dbSNP:rs36002620).
{ECO:0000269|Ref.7}.
/FTId=VAR_025838.
VARIANT 309 309 S -> L (in dbSNP:rs35156510).
{ECO:0000269|Ref.7}.
/FTId=VAR_025839.
VARIANT 360 360 L -> F (in dbSNP:rs12505).
/FTId=VAR_049674.
MUTAGEN 283 283 C->S,Y: Complete loss of activity.
{ECO:0000269|PubMed:8186255}.
MUTAGEN 292 292 R->H,L,Q: Complete loss of activity.
{ECO:0000269|PubMed:8186255}.
MUTAGEN 292 292 R->K: 42% of wild-type activity.
{ECO:0000269|PubMed:8186255}.
MUTAGEN 340 340 D->E: No change in activity.
{ECO:0000269|PubMed:8186255}.
CONFLICT 41 42 EL -> DV (in Ref. 1; AAA76851).
{ECO:0000305}.
CONFLICT 78 78 D -> G (in Ref. 3; AAA76850 and 10;
AAA52024). {ECO:0000305}.
CONFLICT 98 99 GG -> RR (in Ref. 1; AAA76851).
{ECO:0000305}.
CONFLICT 105 106 EH -> DD (in Ref. 1; AAA76851).
{ECO:0000305}.
CONFLICT 130 130 R -> G (in Ref. 3; AAA76850).
{ECO:0000305}.
CONFLICT 132 132 R -> A (in Ref. 1; AAA76851).
{ECO:0000305}.
CONFLICT 144 144 P -> Q (in Ref. 6; CAG47064).
{ECO:0000305}.
CONFLICT 203 203 L -> S (in Ref. 2; AAC31758).
{ECO:0000305}.
CONFLICT 215 216 RG -> AR (in Ref. 1; AAA76851).
{ECO:0000305}.
CONFLICT 296 296 H -> D (in Ref. 1; AAA76851).
{ECO:0000305}.
CONFLICT 358 358 K -> R (in Ref. 5; BAG35211).
{ECO:0000305}.
HELIX 7 11 {ECO:0000244|PDB:3B6R}.
HELIX 16 19 {ECO:0000244|PDB:3B6R}.
HELIX 29 33 {ECO:0000244|PDB:3B6R}.
HELIX 36 42 {ECO:0000244|PDB:3B6R}.
HELIX 53 62 {ECO:0000244|PDB:3B6R}.
STRAND 67 69 {ECO:0000244|PDB:3B6R}.
HELIX 81 84 {ECO:0000244|PDB:3B6R}.
HELIX 86 96 {ECO:0000244|PDB:3B6R}.
HELIX 112 114 {ECO:0000244|PDB:3B6R}.
TURN 123 125 {ECO:0000244|PDB:3B6R}.
STRAND 126 135 {ECO:0000244|PDB:3B6R}.
TURN 143 145 {ECO:0000244|PDB:3B6R}.
HELIX 148 162 {ECO:0000244|PDB:3B6R}.
HELIX 167 169 {ECO:0000244|PDB:3B6R}.
STRAND 171 176 {ECO:0000244|PDB:3B6R}.
HELIX 181 189 {ECO:0000244|PDB:3B6R}.
HELIX 200 203 {ECO:0000244|PDB:3B6R}.
TURN 204 214 {ECO:0000244|PDB:3B6R}.
STRAND 216 220 {ECO:0000244|PDB:3B6R}.
STRAND 223 244 {ECO:0000244|PDB:3B6R}.
HELIX 246 266 {ECO:0000244|PDB:3B6R}.
TURN 275 277 {ECO:0000244|PDB:3B6R}.
HELIX 284 286 {ECO:0000244|PDB:3B6R}.
STRAND 292 298 {ECO:0000244|PDB:3B6R}.
HELIX 300 303 {ECO:0000244|PDB:3B6R}.
HELIX 308 314 {ECO:0000244|PDB:3B6R}.
STRAND 317 321 {ECO:0000244|PDB:3B6R}.
HELIX 325 330 {ECO:0000244|PDB:3B6R}.
STRAND 333 338 {ECO:0000244|PDB:3B6R}.
STRAND 342 344 {ECO:0000244|PDB:3B6R}.
HELIX 346 368 {ECO:0000244|PDB:3B6R}.
HELIX 374 376 {ECO:0000244|PDB:3B6R}.
SEQUENCE 381 AA; 42644 MW; 637AA67A86AE3059 CRC64;
MPFSNSHNAL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG FTLDDVIQTG
VDNPGHPYIM TVGCVAGDEE SYEVFKDLFD PIIEDRHGGY KPSDEHKTDL NPDNLQGGDD
LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE ALSSLDGDLA GRYYALKSMT
EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM
QKGGNMKEVF TRFCTGLTQI ETLFKSKDYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP
NLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL
IEMEQRLEQG QAIDDLMPAQ K


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