BMR1B_MOUSE
ID BMR1B_MOUSE Reviewed; 502 AA.
AC P36898; Q3TRF2;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Bone morphogenetic protein receptor type-1B;
DE Short=BMP type-1B receptor;
DE Short=BMPR-1B;
DE EC=2.7.11.30 {ECO:0000305|PubMed:14523231};
DE AltName: Full=Activin receptor-like kinase 6;
DE Short=ALK-6;
DE AltName: Full=Serine/threonine-protein kinase receptor R6;
DE Short=SKR6;
DE AltName: CD_antigen=CDw293;
DE Flags: Precursor;
GN Name=Bmpr1b; Synonyms=Acvrlk6;
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 [MRNA].
RX PubMed=8140412; DOI=10.1126/science.8140412;
RA ten Dijke P., Yamashita H., Ichijo H., Franzen P., Laiho M., Miyazono K.,
RA Heldin C.-H.;
RT "Characterization of type I receptors for transforming growth factor-beta
RT and activin.";
RL Science 264:101-104(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, and Hypothalamus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Retina;
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 [4]
RP CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, MUTAGENESIS OF ILE-200 AND
RP ARG-486, AND SUBCELLULAR LOCATION.
RX PubMed=14523231; DOI=10.1073/pnas.2133476100;
RA Lehmann K., Seemann P., Stricker S., Sammar M., Meyer B., Suering K.,
RA Majewski F., Tinschert S., Grzeschik K.-H., Mueller D., Knaus P.,
RA Nuernberg P., Mundlos S.;
RT "Mutations in bone morphogenetic protein receptor 1B cause brachydactyly
RT type A2.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12277-12282(2003).
RN [5]
RP FUNCTION.
RX PubMed=24098149; DOI=10.1371/journal.pgen.1003846;
RA Degenkolbe E., Konig J., Zimmer J., Walther M., Reissner C., Nickel J.,
RA Ploger F., Raspopovic J., Sharpe J., Dathe K., Hecht J.T., Mundlos S.,
RA Doelken S.C., Seemann P.;
RT "A GDF5 point mutation strikes twice--causing BDA1 and SYNS2.";
RL PLoS Genet. 9:E1003846-E1003846(2013).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24129431; DOI=10.1038/ejhg.2013.222;
RA Graul-Neumann L.M., Deichsel A., Wille U., Kakar N., Koll R., Bassir C.,
RA Ahmad J., Cormier-Daire V., Mundlos S., Kubisch C., Borck G., Klopocki E.,
RA Mueller T.D., Doelken S.C., Seemann P.;
RT "Homozygous missense and nonsense mutations in BMPR1B cause acromesomelic
RT chondrodysplasia-type Grebe.";
RL Eur. J. Hum. Genet. 22:726-733(2014).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26105076; DOI=10.1186/s13023-015-0299-5;
RA Stange K., Desir J., Kakar N., Mueller T.D., Budde B.S., Gordon C.T.,
RA Horn D., Seemann P., Borck G.;
RT "A hypomorphic BMPR1B mutation causes du Pan acromesomelic dysplasia.";
RL Orphanet J. Rare Dis. 10:84-84(2015).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 14-126 IN COMPLEX WITH HUMAN GDF5,
RP AND DISULFIDE BONDS.
RX PubMed=19229295; DOI=10.1038/emboj.2009.37;
RA Kotzsch A., Nickel J., Seher A., Sebald W., Muller T.D.;
RT "Crystal structure analysis reveals a spring-loaded latch as molecular
RT mechanism for GDF-5-type I receptor specificity.";
RL EMBO J. 28:937-947(2009).
CC -!- FUNCTION: On ligand binding, forms a receptor complex consisting of two
CC type II and two type I transmembrane serine/threonine kinases. Type II
CC receptors phosphorylate and activate type I receptors which
CC autophosphorylate, then bind and activate SMAD transcriptional
CC regulators. Receptor for BMP7/OP-1. Receptor for GDF5 (PubMed:26105076,
CC PubMed:19229295). Positively regulates chondrocyte differentiation
CC through GDF5 interaction (PubMed:24098149).
CC {ECO:0000269|PubMed:19229295, ECO:0000269|PubMed:24098149,
CC ECO:0000269|PubMed:26105076}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-
CC L-threonyl-[receptor-protein]; Xref=Rhea:RHEA:44880, Rhea:RHEA-
CC COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
CC ChEBI:CHEBI:456216; EC=2.7.11.30;
CC Evidence={ECO:0000305|PubMed:14523231};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44881;
CC Evidence={ECO:0000305|PubMed:14523231};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[receptor-protein] = ADP + H(+) + O-phospho-L-
CC seryl-[receptor-protein]; Xref=Rhea:RHEA:18673, Rhea:RHEA-COMP:11022,
CC Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC EC=2.7.11.30; Evidence={ECO:0000305|PubMed:14523231};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18674;
CC Evidence={ECO:0000305|PubMed:14523231};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Interacts with high affinity with GDF5; positively regulates
CC chondrocyte differentiation. Interacts with SCUBE3.
CC {ECO:0000250|UniProtKB:O00238}.
CC -!- INTERACTION:
CC P36898; O35182: Smad6; NbExp=2; IntAct=EBI-7107883, EBI-4321242;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14523231,
CC ECO:0000269|PubMed:24129431, ECO:0000269|PubMed:26105076}; Single-pass
CC type I membrane protein {ECO:0000255}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:14523231}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
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DR EMBL; Z23143; CAA80674.1; -; mRNA.
DR EMBL; AK086130; BAC39617.1; -; mRNA.
DR EMBL; AK162844; BAE37078.1; -; mRNA.
DR EMBL; BC065106; AAH65106.1; -; mRNA.
DR EMBL; BC065143; AAH65143.1; -; mRNA.
DR CCDS; CCDS17874.1; -.
DR PIR; A53444; A53444.
DR RefSeq; NP_001264145.1; NM_001277216.1.
DR RefSeq; NP_001264146.1; NM_001277217.1.
DR RefSeq; NP_001264147.1; NM_001277218.1.
DR RefSeq; NP_001264149.1; NM_001277220.1.
DR RefSeq; NP_031586.1; NM_007560.4.
DR RefSeq; XP_006501002.1; XM_006500939.3.
DR RefSeq; XP_006501003.1; XM_006500940.3.
DR RefSeq; XP_006501005.1; XM_006500942.1.
DR RefSeq; XP_006501006.1; XM_006500943.3.
DR RefSeq; XP_006501007.1; XM_006500944.2.
DR RefSeq; XP_011238303.1; XM_011240001.1.
DR RefSeq; XP_011238304.1; XM_011240002.2.
DR PDB; 3EVS; X-ray; 2.10 A; C=14-126.
DR PDBsum; 3EVS; -.
DR AlphaFoldDB; P36898; -.
DR SMR; P36898; -.
DR DIP; DIP-252N; -.
DR IntAct; P36898; 1.
DR MINT; P36898; -.
DR STRING; 10090.ENSMUSP00000029948; -.
DR BindingDB; P36898; -.
DR PhosphoSitePlus; P36898; -.
DR PaxDb; P36898; -.
DR PRIDE; P36898; -.
DR ProteomicsDB; 273694; -.
DR Antibodypedia; 4045; 659 antibodies from 36 providers.
DR DNASU; 12167; -.
DR Ensembl; ENSMUST00000029948; ENSMUSP00000029948; ENSMUSG00000052430.
DR Ensembl; ENSMUST00000098568; ENSMUSP00000096167; ENSMUSG00000052430.
DR Ensembl; ENSMUST00000106230; ENSMUSP00000101837; ENSMUSG00000052430.
DR Ensembl; ENSMUST00000106232; ENSMUSP00000101839; ENSMUSG00000052430.
DR GeneID; 12167; -.
DR KEGG; mmu:12167; -.
DR UCSC; uc008rog.2; mouse.
DR CTD; 658; -.
DR MGI; MGI:107191; Bmpr1b.
DR VEuPathDB; HostDB:ENSMUSG00000052430; -.
DR eggNOG; KOG2052; Eukaryota.
DR GeneTree; ENSGT00940000155919; -.
DR HOGENOM; CLU_000288_8_1_1; -.
DR InParanoid; P36898; -.
DR OMA; SWNNERE; -.
DR OrthoDB; 776697at2759; -.
DR PhylomeDB; P36898; -.
DR TreeFam; TF314724; -.
DR BRENDA; 2.7.10.2; 3474.
DR Reactome; R-MMU-201451; Signaling by BMP.
DR BioGRID-ORCS; 12167; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Bmpr1b; mouse.
DR EvolutionaryTrace; P36898; -.
DR PRO; PR:P36898; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P36898; protein.
DR Bgee; ENSMUSG00000052430; Expressed in cumulus cell and 277 other tissues.
DR ExpressionAtlas; P36898; baseline and differential.
DR Genevisible; P36898; MM.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IC:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0036122; F:BMP binding; IDA:MGI.
DR GO; GO:0098821; F:BMP receptor activity; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019211; F:phosphatase activator activity; IDA:MGI.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IDA:MGI.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0046332; F:SMAD binding; ISO:MGI.
DR GO; GO:0005024; F:transforming growth factor beta receptor activity; TAS:MGI.
DR GO; GO:0005025; F:transforming growth factor beta receptor activity, type I; IMP:MGI.
DR GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IMP:UniProtKB.
DR GO; GO:0030509; P:BMP signaling pathway; IDA:UniProtKB.
DR GO; GO:0060348; P:bone development; IMP:MGI.
DR GO; GO:0043010; P:camera-type eye development; IGI:MGI.
DR GO; GO:0001502; P:cartilage condensation; IMP:MGI.
DR GO; GO:0030154; P:cell differentiation; IMP:MGI.
DR GO; GO:0071773; P:cellular response to BMP stimulus; ISO:MGI.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:UniProtKB.
DR GO; GO:0021953; P:central nervous system neuron differentiation; IGI:MGI.
DR GO; GO:0002063; P:chondrocyte development; ISS:AgBase.
DR GO; GO:0002062; P:chondrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IGI:MGI.
DR GO; GO:0060350; P:endochondral bone morphogenesis; ISS:AgBase.
DR GO; GO:0006703; P:estrogen biosynthetic process; NAS:UniProtKB.
DR GO; GO:0001654; P:eye development; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; IEP:UniProtKB.
DR GO; GO:1902731; P:negative regulation of chondrocyte proliferation; ISS:AgBase.
DR GO; GO:0001649; P:osteoblast differentiation; IDA:MGI.
DR GO; GO:0001550; P:ovarian cumulus expansion; IMP:UniProtKB.
DR GO; GO:0042698; P:ovulation cycle; IMP:UniProtKB.
DR GO; GO:0030501; P:positive regulation of bone mineralization; ISO:MGI.
DR GO; GO:0061036; P:positive regulation of cartilage development; ISS:AgBase.
DR GO; GO:0032332; P:positive regulation of chondrocyte differentiation; ISS:UniProtKB.
DR GO; GO:1902043; P:positive regulation of extrinsic apoptotic signaling pathway via death domain receptors; IGI:MGI.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR GO; GO:0030166; P:proteoglycan biosynthetic process; ISS:AgBase.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; IMP:MGI.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:MGI.
DR GO; GO:0007178; P:transmembrane receptor protein serine/threonine kinase signaling pathway; IGI:MGI.
DR Gene3D; 2.10.60.10; -; 1.
DR InterPro; IPR000472; Activin_recp.
DR InterPro; IPR003605; GS_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR InterPro; IPR000333; TGFB_receptor.
DR PANTHER; PTHR23255; PTHR23255; 1.
DR Pfam; PF01064; Activin_recp; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF08515; TGF_beta_GS; 1.
DR SMART; SM00467; GS; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57302; SSF57302; 1.
DR PROSITE; PS51256; GS; 1.
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; ATP-binding; Cell membrane; Chondrogenesis; Disulfide bond;
KW Kinase; Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding;
KW Receptor; Reference proteome; Serine/threonine-protein kinase; Signal;
KW Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..13
FT /evidence="ECO:0000255"
FT CHAIN 14..502
FT /note="Bone morphogenetic protein receptor type-1B"
FT /id="PRO_0000024413"
FT TOPO_DOM 14..126
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 149..502
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 174..203
FT /note="GS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00585"
FT DOMAIN 204..494
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 332
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 210..218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DISULFID 32..53
FT /evidence="ECO:0000269|PubMed:19229295"
FT DISULFID 34..38
FT /evidence="ECO:0000269|PubMed:19229295"
FT DISULFID 47..71
FT /evidence="ECO:0000269|PubMed:19229295"
FT DISULFID 81..95
FT /evidence="ECO:0000269|PubMed:19229295"
FT DISULFID 96..102
FT /evidence="ECO:0000269|PubMed:19229295"
FT MUTAGEN 200
FT /note="I->K: Loss of kinase activity. No effect on cell
FT membrane location."
FT /evidence="ECO:0000269|PubMed:14523231"
FT MUTAGEN 486
FT /note="R->W: No effect on kinase activity. No effect on
FT cell membrane location."
FT /evidence="ECO:0000269|PubMed:14523231"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:3EVS"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:3EVS"
FT STRAND 46..59
FT /evidence="ECO:0007829|PDB:3EVS"
FT STRAND 64..72
FT /evidence="ECO:0007829|PDB:3EVS"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:3EVS"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:3EVS"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:3EVS"
SQ SEQUENCE 502 AA; 56944 MW; AB29681F3FF5A361 CRC64;
MLLRSSGKLN VGTKKEDGES TAPTPRPKIL RCKCHHHCPE DSVNNICSTD GYCFTMIEED
DSGMPVVTSG CLGLEGSDFQ CRDTPIPHQR RSIECCTERN ECNKDLHPTL PPLKDRDFVD
GPIHHKALLI SVTVCSLLLV LIILFCYFRY KRQEARPRYS IGLEQDETYI PPGESLRDLI
EQSQSSGSGS GLPLLVQRTI AKQIQMVKQI GKGRYGEVWM GKWRGEKVAV KVFFTTEEAS
WFRETEIYQT VLMRHENILG FIAADIKGTG SWTQLYLITD YHENGSLYDY LKSTTLDAKS
MLKLAYSSVS GLCHLHTEIF STQGKPAIAH RDLKSKNILV KKNGTCCIAD LGLAVKFISD
TNEVDIPPNT RVGTKRYMPP EVLDESLNRN HFQSYIMADM YSFGLILWEI ARRCVSGGIV
EEYQLPYHDL VPSDPSYEDM REIVCMKKLR PSFPNRWSSD ECLRQMGKLM TECWAQNPAS
RLTALRVKKT LAKMSESQDI KL
