KCRU_HUMAN
ID KCRU_HUMAN Reviewed; 417 AA.
AC P12532; B4DIT8; B7ZA09; Q0VAM3; Q32NF6; Q53FC4;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 221.
DE RecName: Full=Creatine kinase U-type, mitochondrial;
DE EC=2.7.3.2;
DE AltName: Full=Acidic-type mitochondrial creatine kinase;
DE Short=Mia-CK;
DE AltName: Full=Ubiquitous mitochondrial creatine kinase;
DE Short=U-MtCK;
DE Flags: Precursor;
GN Name=CKMT1A; Synonyms=CKMT;
GN and
GN Name=CKMT1B; Synonyms=CKMT;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2914937; DOI=10.1016/s0021-9258(19)81696-4;
RA Haas R.C., Korenfeld C., Zhang Z., Perryman B., Roman D., Strauss A.W.;
RT "Isolation and characterization of the gene and cDNA encoding human
RT mitochondrial creatine kinase.";
RL J. Biol. Chem. 264:2890-2897(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Colon, and Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, and PNS;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 39-417, AND SUBUNIT.
RX PubMed=10737943;
RX DOI=10.1002/(sici)1097-0134(20000515)39:3<216::aid-prot40>3.0.co;2-#;
RA Eder M., Fritz-Wolf K., Kabsch W., Wallimann T., Schlattner U.;
RT "Crystal structure of human ubiquitous mitochondrial creatine kinase.";
RL Proteins 39:216-225(2000).
CC -!- FUNCTION: Reversibly catalyzes the transfer of phosphate between ATP
CC and various phosphogens (e.g. creatine phosphate). Creatine kinase
CC isoenzymes play a central role in energy transduction in tissues with
CC large, fluctuating energy demands, such as skeletal muscle, heart,
CC brain and spermatozoa.
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 -!- SUBUNIT: Exists as an octamer composed of four MTCK homodimers.
CC {ECO:0000269|PubMed:10737943}.
CC -!- INTERACTION:
CC P12532; Q96DX5: ASB9; NbExp=3; IntAct=EBI-1050662, EBI-745641;
CC P12532; P06732: CKM; NbExp=3; IntAct=EBI-1050662, EBI-4287089;
CC P12532; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-1050662, EBI-11962928;
CC P12532; P84074: HPCA; NbExp=3; IntAct=EBI-1050662, EBI-12197079;
CC P12532; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-1050662, EBI-1055254;
CC P12532; P61970: NUTF2; NbExp=3; IntAct=EBI-1050662, EBI-591778;
CC P12532; P0CE72: OCM; NbExp=6; IntAct=EBI-1050662, EBI-11955379;
CC P12532; Q96I34: PPP1R16A; NbExp=3; IntAct=EBI-1050662, EBI-710402;
CC P12532; P17980: PSMC3; NbExp=3; IntAct=EBI-1050662, EBI-359720;
CC P12532; P48443: RXRG; NbExp=5; IntAct=EBI-1050662, EBI-712405;
CC P12532; O76024: WFS1; NbExp=3; IntAct=EBI-1050662, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane
CC protein; Intermembrane side.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P12532-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P12532-2; Sequence=VSP_038045;
CC -!- MISCELLANEOUS: Mitochondrial creatine kinase binds cardiolipin.
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; J04469; AAA98744.1; -; Genomic_DNA.
DR EMBL; BT006628; AAP35274.1; -; mRNA.
DR EMBL; AK295776; BAG58600.1; -; mRNA.
DR EMBL; AK223365; BAD97085.1; -; mRNA.
DR EMBL; AK316124; BAH14495.1; -; mRNA.
DR EMBL; AK316319; BAH14690.1; -; mRNA.
DR EMBL; BC001926; AAH01926.1; -; mRNA.
DR EMBL; BC006467; AAH06467.1; -; mRNA.
DR EMBL; BC108652; AAI08653.1; -; mRNA.
DR EMBL; BC121001; AAI21002.1; -; mRNA.
DR EMBL; BC121002; AAI21003.1; -; mRNA.
DR CCDS; CCDS10097.1; -. [P12532-1]
DR CCDS; CCDS32217.1; -. [P12532-1]
DR PIR; A31431; A30789.
DR RefSeq; NP_001015001.1; NM_001015001.2. [P12532-1]
DR RefSeq; NP_001308855.1; NM_001321926.1. [P12532-1]
DR RefSeq; NP_001308856.1; NM_001321927.1. [P12532-2]
DR RefSeq; NP_001308857.1; NM_001321928.1. [P12532-2]
DR RefSeq; NP_066270.1; NM_020990.4. [P12532-1]
DR RefSeq; XP_011519496.1; XM_011521194.1. [P12532-2]
DR RefSeq; XP_011519497.1; XM_011521195.2. [P12532-2]
DR RefSeq; XP_011519498.1; XM_011521196.1. [P12532-2]
DR RefSeq; XP_011519499.1; XM_011521197.2.
DR RefSeq; XP_016877858.1; XM_017022369.1. [P12532-2]
DR RefSeq; XP_016877859.1; XM_017022370.1. [P12532-2]
DR PDB; 1QK1; X-ray; 2.70 A; A/B/C/D/E/F/G/H=39-417.
DR PDBsum; 1QK1; -.
DR AlphaFoldDB; P12532; -.
DR SMR; P12532; -.
DR BioGRID; 107579; 61.
DR BioGRID; 139227; 56.
DR IntAct; P12532; 44.
DR MINT; P12532; -.
DR STRING; 9606.ENSP00000300283; -.
DR DrugBank; DB00787; Acyclovir.
DR DrugBank; DB00148; Creatine.
DR DrugBank; DB13191; Phosphocreatine.
DR DrugBank; DB00300; Tenofovir disoproxil.
DR iPTMnet; P12532; -.
DR PhosphoSitePlus; P12532; -.
DR SwissPalm; P12532; -.
DR BioMuta; CKMT1B; -.
DR DMDM; 125315; -.
DR UCD-2DPAGE; P12532; -.
DR EPD; P12532; -.
DR jPOST; P12532; -.
DR MassIVE; P12532; -.
DR MaxQB; P12532; -.
DR PaxDb; P12532; -.
DR PeptideAtlas; P12532; -.
DR PRIDE; P12532; -.
DR ProteomicsDB; 52856; -. [P12532-1]
DR ProteomicsDB; 52857; -. [P12532-2]
DR Antibodypedia; 23991; 285 antibodies from 32 providers.
DR Antibodypedia; 65061; 153 antibodies from 13 providers.
DR DNASU; 1159; -.
DR Ensembl; ENST00000300283.10; ENSP00000300283.6; ENSG00000237289.10. [P12532-1]
DR Ensembl; ENST00000413453.7; ENSP00000406577.3; ENSG00000223572.10. [P12532-1]
DR Ensembl; ENST00000434505.5; ENSP00000413165.1; ENSG00000223572.10. [P12532-1]
DR Ensembl; ENST00000441322.6; ENSP00000413255.2; ENSG00000237289.10. [P12532-1]
DR GeneID; 1159; -.
DR GeneID; 548596; -.
DR KEGG; hsa:1159; -.
DR KEGG; hsa:548596; -.
DR MANE-Select; ENST00000413453.7; ENSP00000406577.3; NM_001321926.2; NP_001308855.1.
DR MANE-Select; ENST00000441322.6; ENSP00000413255.2; NM_001375484.1; NP_001362413.1.
DR UCSC; uc001zsc.3; human. [P12532-1]
DR CTD; 1159; -.
DR CTD; 548596; -.
DR DisGeNET; 1159; -.
DR DisGeNET; 548596; -.
DR GeneCards; CKMT1A; -.
DR GeneCards; CKMT1B; -.
DR HGNC; HGNC:31736; CKMT1A.
DR HGNC; HGNC:1995; CKMT1B.
DR HPA; ENSG00000223572; Tissue enhanced (esophagus, intestine).
DR HPA; ENSG00000237289; Tissue enhanced (brain, esophagus, intestine).
DR MIM; 123290; gene.
DR MIM; 613415; gene.
DR neXtProt; NX_P12532; -.
DR OpenTargets; ENSG00000223572; -.
DR OpenTargets; ENSG00000237289; -.
DR PharmGKB; PA142672108; -.
DR VEuPathDB; HostDB:ENSG00000223572; -.
DR VEuPathDB; HostDB:ENSG00000237289; -.
DR eggNOG; KOG3581; Eukaryota.
DR GeneTree; ENSGT00950000182772; -.
DR HOGENOM; CLU_019868_4_2_1; -.
DR InParanoid; P12532; -.
DR OMA; KIRGGMF; -.
DR OrthoDB; 825025at2759; -.
DR PhylomeDB; P12532; -.
DR TreeFam; TF314214; -.
DR BioCyc; MetaCyc:HS09820-MON; -.
DR BRENDA; 2.7.3.2; 2681.
DR PathwayCommons; P12532; -.
DR Reactome; R-HSA-71288; Creatine metabolism.
DR SignaLink; P12532; -.
DR SIGNOR; P12532; -.
DR BioGRID-ORCS; 1159; 13 hits in 616 CRISPR screens.
DR BioGRID-ORCS; 548596; 8 hits in 301 CRISPR screens.
DR ChiTaRS; CKMT1A; human.
DR ChiTaRS; CKMT1B; human.
DR EvolutionaryTrace; P12532; -.
DR GeneWiki; CKMT1B; -.
DR Pharos; P12532; Tbio.
DR PRO; PR:P12532; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; P12532; protein.
DR Bgee; ENSG00000223572; Expressed in right hemisphere of cerebellum and 91 other tissues.
DR ExpressionAtlas; P12532; baseline and differential.
DR Genevisible; P12532; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004111; F:creatine kinase activity; IBA:GO_Central.
DR GO; GO:0016301; F:kinase activity; IBA:GO_Central.
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; 1.
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 3D-structure; Alternative splicing; ATP-binding; Kinase; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..39
FT /note="Mitochondrion"
FT CHAIN 40..417
FT /note="Creatine kinase U-type, mitochondrial"
FT /id="PRO_0000016590"
FT DOMAIN 45..131
FT /note="Phosphagen kinase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00842"
FT DOMAIN 158..400
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT REGION 40..64
FT /note="Cardiolipin-binding"
FT /evidence="ECO:0000250"
FT BINDING 161..165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 224
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 269
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 325
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 353..358
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 368
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25809"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25809"
FT MOD_RES 213
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P00564"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30275"
FT MOD_RES 355
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07310"
FT VAR_SEQ 50
FT /note="S -> SQTWPTGQLPGNCTRSRRLCPPSMVTGYPLPS (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038045"
FT CONFLICT 176
FT /note="P -> L (in Ref. 3; BAG58600)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="E -> G (in Ref. 4; BAD97085)"
FT /evidence="ECO:0000305"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:1QK1"
FT HELIX 62..66
FT /evidence="ECO:0007829|PDB:1QK1"
FT HELIX 69..75
FT /evidence="ECO:0007829|PDB:1QK1"
FT HELIX 86..95
FT /evidence="ECO:0007829|PDB:1QK1"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:1QK1"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:1QK1"
FT HELIX 119..129
FT /evidence="ECO:0007829|PDB:1QK1"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:1QK1"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:1QK1"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:1QK1"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:1QK1"
FT STRAND 159..168
FT /evidence="ECO:0007829|PDB:1QK1"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:1QK1"
FT HELIX 181..195
FT /evidence="ECO:0007829|PDB:1QK1"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:1QK1"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:1QK1"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:1QK1"
FT HELIX 214..222
FT /evidence="ECO:0007829|PDB:1QK1"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:1QK1"
FT TURN 237..247
FT /evidence="ECO:0007829|PDB:1QK1"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:1QK1"
FT STRAND 258..277
FT /evidence="ECO:0007829|PDB:1QK1"
FT HELIX 279..298
FT /evidence="ECO:0007829|PDB:1QK1"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:1QK1"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:1QK1"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:1QK1"
FT STRAND 325..331
FT /evidence="ECO:0007829|PDB:1QK1"
FT HELIX 333..337
FT /evidence="ECO:0007829|PDB:1QK1"
FT HELIX 341..348
FT /evidence="ECO:0007829|PDB:1QK1"
FT STRAND 350..353
FT /evidence="ECO:0007829|PDB:1QK1"
FT TURN 359..361
FT /evidence="ECO:0007829|PDB:1QK1"
FT STRAND 364..372
FT /evidence="ECO:0007829|PDB:1QK1"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:1QK1"
FT HELIX 379..400
FT /evidence="ECO:0007829|PDB:1QK1"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:1QK1"
SQ SEQUENCE 417 AA; 47037 MW; 274DAC2E9A8AD882 CRC64;
MAGPFSRLLS ARPGLRLLAL AGAGSLAAGF LLRPEPVRAA SERRRLYPPS AEYPDLRKHN
NCMASHLTPA VYARLCDKTT PTGWTLDQCI QTGVDNPGHP FIKTVGMVAG DEETYEVFAD
LFDPVIQERH NGYDPRTMKH TTDLDASKIR SGYFDERYVL SSRVRTGRSI RGLSLPPACT
RAERREVERV VVDALSGLKG DLAGRYYRLS EMTEAEQQQL IDDHFLFDKP VSPLLTAAGM
ARDWPDARGI WHNNEKSFLI WVNEEDHTRV ISMEKGGNMK RVFERFCRGL KEVERLIQER
GWEFMWNERL GYILTCPSNL GTGLRAGVHI KLPLLSKDSR FPKILENLRL QKRGTGGVDT
AATGGVFDIS NLDRLGKSEV ELVQLVIDGV NYLIDCERRL ERGQDIRIPT PVIHTKH
