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 27-MAR-2024, entry version 206. 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 (By similarity). Interacts with SCUBE3 (By CC similarity). Interacts with TSC22D1/TSC-22 (By similarity). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 10090-ENSMUSP00000029948; -. DR ProteomicsDB; 273694; -. DR Antibodypedia; 4045; 714 antibodies from 36 providers. DR DNASU; 12167; -. DR Ensembl; ENSMUST00000029948.15; ENSMUSP00000029948.8; ENSMUSG00000052430.16. DR Ensembl; ENSMUST00000098568.8; ENSMUSP00000096167.2; ENSMUSG00000052430.16. DR Ensembl; ENSMUST00000106230.2; ENSMUSP00000101837.2; ENSMUSG00000052430.16. DR Ensembl; ENSMUST00000106232.8; ENSMUSP00000101839.2; ENSMUSG00000052430.16. DR GeneID; 12167; -. DR KEGG; mmu:12167; -. DR UCSC; uc008rog.2; mouse. DR AGR; MGI:107191; -. 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; RRTIACC; -. DR OrthoDB; 3900892at2759; -. 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 80 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 279 other cell types or tissues. DR ExpressionAtlas; P36898; baseline and differential. DR GO; GO:0030425; C:dendrite; ISO:MGI. 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: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:0004888; F:transmembrane signaling receptor activity; ISO:MGI. 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:0016310; P:phosphorylation; IEA:UniProtKB-KW. 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:0010628; P:positive regulation of gene expression; ISO: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: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 CDD; cd14219; STKc_BMPR1b; 1. DR Gene3D; 2.10.60.10; CD59; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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:SF62; BONE MORPHOGENETIC PROTEIN RECEPTOR TYPE-1B; 1. DR PANTHER; PTHR23255; TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE I AND II; 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; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF57302; Snake toxin-like; 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. DR Genevisible; P36898; MM. 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 //