KCRB_MOUSE
ID KCRB_MOUSE Reviewed; 381 AA.
AC Q04447; Q3KQP4; Q3TKI3; Q3U5P5; Q3UF71; Q9CXK6;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Creatine kinase B-type {ECO:0000303|PubMed:33597756};
DE EC=2.7.3.2 {ECO:0000269|PubMed:33597756};
DE AltName: Full=B-CK;
DE AltName: Full=Creatine kinase B chain;
DE AltName: Full=Creatine phosphokinase B-type;
DE Short=CPK-B;
GN Name=Ckb {ECO:0000303|PubMed:33597756, ECO:0000312|MGI:MGI:88407};
GN Synonyms=Ckbb;
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].
RX PubMed=1740343; DOI=10.1016/0888-7543(92)90383-4;
RA van Deursen J., Schepens J., Peters W., Meijer D., Grosveld G.,
RA Hendriks W., Wieringa B.;
RT "Genetic variability of the murine creatine kinase B gene locus and related
RT pseudogenes in different inbred strains of mice.";
RL Genomics 12:340-349(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Pentecost B.T.;
RL Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Embryonic head, Kidney, Sympathetic ganglion, and Wolffian duct;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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 [5]
RP PROTEIN SEQUENCE OF 12-43; 87-96; 108-130; 139-148; 157-172; 178-209;
RP 224-236; 253-265; 268-292 AND 320-381, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 354-381.
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=3641191; DOI=10.1093/nar/14.21.8690;
RA Papenbrock T., Wille W.;
RT "The 3' non-coding region of the mouse brain B creatine kinase mRNA: a
RT sequence with exceptional homology among species.";
RL Nucleic Acids Res. 14:8690-8690(1986).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15648052; DOI=10.1002/pmic.200401066;
RA Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,
RA Hart G.W., Burlingame A.L.;
RT "Quantitative analysis of both protein expression and serine / threonine
RT post-translational modifications through stable isotope labeling with
RT dithiothreitol.";
RL Proteomics 5:388-398(2005).
RN [8]
RP NITRATION [LARGE SCALE ANALYSIS] AT TYR-269, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16800626; DOI=10.1021/bi060474w;
RA Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H., Lacan G.,
RA Melega W.P., Camp D.G. II, Smith R.D., Smith D.J., Squier T.C.,
RA Bigelow D.J.;
RT "Endogenously nitrated proteins in mouse brain: links to neurodegenerative
RT disease.";
RL Biochemistry 45:8009-8022(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-125, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-35; SER-199 AND THR-322, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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 [12]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DOMAIN, INDUCTION,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 130-ARG--ARG-138 AND CYS-283.
RX PubMed=33597756; DOI=10.1038/s41586-021-03221-y;
RA Rahbani J.F., Roesler A., Hussain M.F., Samborska B., Dykstra C.B.,
RA Tsai L., Jedrychowski M.P., Vergnes L., Reue K., Spiegelman B.M., Kazak L.;
RT "Creatine kinase B controls futile creatine cycling in thermogenic fat.";
RL Nature 590:480-485(2021).
CC -!- FUNCTION: Reversibly catalyzes the transfer of phosphate between ATP
CC and various phosphogens (e.g. creatine phosphate) (PubMed:33597756).
CC Creatine kinase isoenzymes play a central role in energy transduction
CC in tissues with large, fluctuating energy demands, such as skeletal
CC muscle, heart, brain and spermatozoa (Probable). Acts as a key
CC regulator of adaptive thermogenesis as part of the futile creatine
CC cycle: localizes to the mitochondria of thermogenic fat cells and acts
CC by mediating phosphorylation of creatine to initiate a futile cycle of
CC creatine phosphorylation and dephosphorylation (PubMed:33597756).
CC During the futile creatine cycle, creatine and N-phosphocreatine are in
CC a futile cycle, which dissipates the high energy charge of N-
CC phosphocreatine as heat without performing any mechanical or chemical
CC work (PubMed:33597756). {ECO:0000269|PubMed:33597756, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + creatine = ADP + H(+) + N-phosphocreatine;
CC Xref=Rhea:RHEA:17157, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57947, ChEBI:CHEBI:58092, ChEBI:CHEBI:456216; EC=2.7.3.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10029,
CC ECO:0000269|PubMed:33597756};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17158;
CC Evidence={ECO:0000269|PubMed:33597756};
CC -!- SUBUNIT: Dimer of identical or non-identical chains, which can be
CC either B (brain type) or M (muscle type). With MM being the major form
CC in skeletal muscle and myocardium, MB existing in myocardium, and BB
CC existing in many tissues, especially brain.
CC {ECO:0000250|UniProtKB:P12277}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:33597756}.
CC Mitochondrion {ECO:0000269|PubMed:33597756}. Note=Localizes to the
CC mitochondria of thermogenic fat cells via the internal MTS-like signal
CC (iMTS-L) region. {ECO:0000269|PubMed:33597756}.
CC -!- INDUCTION: Strongly up-regulated in response to cold in fat cells;
CC expression is dependent on cAMP. {ECO:0000269|PubMed:33597756}.
CC -!- DOMAIN: The internal MTS-like signal (iMTS-L) mediates targeting to
CC mitochondria thermogenic fat cells. {ECO:0000269|PubMed:33597756}.
CC -!- DISRUPTION PHENOTYPE: Conditional deletion in adipocytes leads to
CC defective adaptive thermogenesis: defects are caused by abolition of
CC the futile creatine cycle, thereby reducing whole-body energy
CC expenditure and leading to predisposition to obesity.
CC {ECO:0000269|PubMed:33597756}.
CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00842, ECO:0000255|PROSITE-
CC ProRule:PRU00843}.
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DR EMBL; M74149; AAA37462.1; -; Genomic_DNA.
DR EMBL; L09069; AAA37455.1; -; Genomic_DNA.
DR EMBL; AK002467; BAB22121.1; -; mRNA.
DR EMBL; AK014299; BAB29254.1; -; mRNA.
DR EMBL; AK148885; BAE28690.1; -; mRNA.
DR EMBL; AK152388; BAE31176.1; -; mRNA.
DR EMBL; AK153484; BAE32032.1; -; mRNA.
DR EMBL; AK166980; BAE39162.1; -; mRNA.
DR EMBL; AK161990; BAE36669.1; -; mRNA.
DR EMBL; AK167034; BAE39205.1; -; mRNA.
DR EMBL; BC015271; AAH15271.1; -; mRNA.
DR EMBL; BC106109; AAI06110.2; -; mRNA.
DR EMBL; X04591; CAA28259.1; -; mRNA.
DR CCDS; CCDS26183.1; -.
DR PIR; A42078; A42078.
DR RefSeq; NP_067248.1; NM_021273.4.
DR AlphaFoldDB; Q04447; -.
DR SMR; Q04447; -.
DR BioGRID; 198725; 33.
DR CORUM; Q04447; -.
DR IntAct; Q04447; 9.
DR MINT; Q04447; -.
DR STRING; 10090.ENSMUSP00000001304; -.
DR iPTMnet; Q04447; -.
DR PhosphoSitePlus; Q04447; -.
DR SwissPalm; Q04447; -.
DR REPRODUCTION-2DPAGE; Q04447; -.
DR UCD-2DPAGE; Q04447; -.
DR CPTAC; non-CPTAC-3977; -.
DR EPD; Q04447; -.
DR jPOST; Q04447; -.
DR MaxQB; Q04447; -.
DR PaxDb; Q04447; -.
DR PeptideAtlas; Q04447; -.
DR PRIDE; Q04447; -.
DR ProteomicsDB; 263509; -.
DR Antibodypedia; 28; 840 antibodies from 39 providers.
DR DNASU; 12709; -.
DR Ensembl; ENSMUST00000001304; ENSMUSP00000001304; ENSMUSG00000001270.
DR GeneID; 12709; -.
DR KEGG; mmu:12709; -.
DR UCSC; uc007pdn.2; mouse.
DR CTD; 1152; -.
DR MGI; MGI:88407; Ckb.
DR VEuPathDB; HostDB:ENSMUSG00000001270; -.
DR eggNOG; KOG3581; Eukaryota.
DR GeneTree; ENSGT00950000182772; -.
DR HOGENOM; CLU_019868_4_2_1; -.
DR InParanoid; Q04447; -.
DR OMA; NRGHEFM; -.
DR OrthoDB; 825025at2759; -.
DR PhylomeDB; Q04447; -.
DR TreeFam; TF314214; -.
DR BRENDA; 2.7.3.2; 3474.
DR Reactome; R-MMU-71288; Creatine metabolism.
DR Reactome; R-MMU-9696264; RND3 GTPase cycle.
DR BioGRID-ORCS; 12709; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Ckb; mouse.
DR PRO; PR:Q04447; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q04447; protein.
DR Bgee; ENSMUSG00000001270; Expressed in cerebellar cortex and 132 other tissues.
DR Genevisible; Q04447; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004111; F:creatine kinase activity; IDA:UniProtKB.
DR GO; GO:0016301; F:kinase activity; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0030644; P:cellular chloride ion homeostasis; ISO:MGI.
DR GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
DR GO; GO:0046314; P:phosphocreatine biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.135.10; -; 1.
DR InterPro; IPR000749; ATP-guanido_PTrfase.
DR InterPro; IPR022415; ATP-guanido_PTrfase_AS.
DR InterPro; IPR022414; ATP-guanido_PTrfase_cat.
DR InterPro; IPR022413; ATP-guanido_PTrfase_N.
DR InterPro; IPR036802; ATP-guanido_PTrfase_N_sf.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR PANTHER; PTHR11547; PTHR11547; 2.
DR Pfam; PF00217; ATP-gua_Ptrans; 1.
DR Pfam; PF02807; ATP-gua_PtransN; 1.
DR SUPFAM; SSF48034; SSF48034; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR PROSITE; PS00112; PHOSPHAGEN_KINASE; 1.
DR PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1.
DR PROSITE; PS51509; PHOSPHAGEN_KINASE_N; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Direct protein sequencing; Kinase; Mitochondrion;
KW Nitration; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..381
FT /note="Creatine kinase B-type"
FT /id="PRO_0000211967"
FT DOMAIN 11..98
FT /note="Phosphagen kinase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00842"
FT DOMAIN 125..367
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT REGION 96..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..138
FT /note="Internal MTS-like signal"
FT /evidence="ECO:0000269|PubMed:33597756"
FT COMPBIAS 96..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 72
FT /ligand="creatine"
FT /ligand_id="ChEBI:CHEBI:57947"
FT /evidence="ECO:0000250|UniProtKB:P12277"
FT BINDING 128..132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 191
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 232
FT /ligand="creatine"
FT /ligand_id="ChEBI:CHEBI:57947"
FT /evidence="ECO:0000250|UniProtKB:P12277"
FT BINDING 236
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 285
FT /ligand="creatine"
FT /ligand_id="ChEBI:CHEBI:57947"
FT /evidence="ECO:0000250|UniProtKB:P12277"
FT BINDING 292
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 320..325
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 320
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 335
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12277"
FT MOD_RES 35
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 125
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 269
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0007744|PubMed:16800626"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07335"
FT MOD_RES 322
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 130..138
FT /note="RVRTGRSIR->AVATGASIA: Abolishes localization to
FT mitochondria in fat cells."
FT /evidence="ECO:0000269|PubMed:33597756"
FT MUTAGEN 283
FT /note="C->S: Abolished creatine kinase activity."
FT /evidence="ECO:0000269|PubMed:33597756"
FT CONFLICT 143
FT /note="P -> H (in Ref. 3; BAE28690)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="I -> M (in Ref. 3; BAE39162)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 381 AA; 42713 MW; D901C5653054A490 CRC64;
MPFSNSHNTQ KLRFPAEDEF PDLSSHNNHM AKVLTPELYA ELRAKCTPSG FTLDDAIQTG
VDNPGHPYIM TVGAVAGDEE SYDVFKDLFD PIIEERHGGY QPSDEHKTDL NPDNLQGGDD
LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE ALSSLDGDLS GRYYALKSMT
EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWIN EEDHLRVISM
QKGGNMKEVF TRFCTGLTQI ETLFKSKNYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP
HLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL
IEMEQRLEQG QAIDDLMPAQ K
