ID BMR1B_HUMAN Reviewed; 502 AA.
AC O00238; B2R953; B4DSV1; P78366;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 01-MAY-2013, entry version 141.
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;
DE AltName: CD_antigen=CDw293;
DE Flags: Precursor;
GN Name=BMPR1B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Prostate;
RX PubMed=9178898; DOI=10.1038/sj.onc.1200964;
RA Ide H., Katoh M., Sasaki H., Yoshida T., Aoki K., Nawa Y., Osada Y.,
RA Sugimura T., Terada M.;
RT "Cloning of human bone morphogenetic protein type IB receptor (BMPR-
RT IB) and its expression in prostate cancer in comparison with other
RT BMPRs.";
RL Oncogene 14:1377-1382(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Ovary;
RX PubMed=10051328; DOI=10.1007/s003359900990;
RA Astroem A.-K., Jin D.F., Imamura T., Roijer E., Rosenzweig B.,
RA Miyazono K., ten Dijke P., Stenman G.;
RT "Chromosomal localization of three human genes encoding bone
RT morphogenetic protein receptors.";
RL Mamm. Genome 10:299-302(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Uterus;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP VARIANTS BDA2 LYS-200 AND TRP-486.
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
RT brachydactyly type A2.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12277-12282(2003).
RN [8]
RP INVOLVEMENT IN AMDGA.
RX PubMed=15805157; DOI=10.1136/jmg.2004.023564;
RA Demirhan O., Tuerkmen S., Schwabe G.C., Soyupak S., Akguel E.,
RA Tastemir D., Karahan D., Mundlos S., Lehmann K.;
RT "A homozygous BMPR1B mutation causes a new subtype of acromesomelic
RT chondrodysplasia with genital anomalies.";
RL J. Med. Genet. 42:314-317(2005).
RN [9]
RP VARIANT BRACHYDACTYLY TYPE C/BDA2 GLN-486.
RX PubMed=16957682; DOI=10.1038/sj.ejhg.5201708;
RA Lehmann K., Seemann P., Boergermann J., Morin G., Reif S., Knaus P.,
RA Mundlos S.;
RT "A novel R486Q mutation in BMPR1B resulting in either a brachydactyly
RT type C/symphalangism-like phenotype or brachydactyly type A2.";
RL Eur. J. Hum. Genet. 14:1248-1254(2006).
RN [10]
RP VARIANTS [LARGE SCALE ANALYSIS] HIS-31; TRP-149; HIS-224; ASN-297 AND
RP GLN-371.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: On ligand binding, forms a receptor complex consisting
CC of two type II and two type I transmembrane serine/threonine
CC kinases. Type II receptors phosphorylate and activate type I
CC receptors which autophosphorylate, then bind and activate SMAD
CC transcriptional regulators. Receptor for BMP7/OP-1 and GDF5.
CC -!- CATALYTIC ACTIVITY: ATP + [receptor-protein] = ADP + [receptor-
CC protein] phosphate.
CC -!- COFACTOR: Magnesium or manganese (By similarity).
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O00238-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O00238-2; Sequence=VSP_045100;
CC -!- DISEASE: Acromesomelic chondrodysplasia, with genital anomalies
CC (AMDGA) [MIM:609441]: A form of chondrodysplasia. Acromesomelic
CC chondrodysplasias are rare hereditary skeletal disorders
CC characterized by short stature, very short limbsand hand/foot
CC malformations. The severity of limb abnormalities increases from
CC proximal to distal with profoundly affected hands and feet showing
CC brachydactyly and/or rudimentary fingers (knob-like fingers).
CC Note=The disease is caused by mutations affecting the gene
CC represented in this entry.
CC -!- DISEASE: Brachydactyly A2 (BDA2) [MIM:112600]: A form of
CC brachydactyly. Brachydactyly defines a group of inherited
CC malformations characterized by shortening of the digits due to
CC abnormal development of the phalanges and/or the metacarpals. In
CC brachydactyly type A2 shortening of the middle phalanges is
CC confined to the index finger and the second toe, all other digits
CC being more or less normal. Because of a rhomboid or triangular
CC shape of the affected middle phalanx, the end of the second finger
CC usually deviates radially. Note=The disease is caused by mutations
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. TGFB receptor subfamily.
CC -!- SIMILARITY: Contains 1 GS domain.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
CC -!- WEB RESOURCE: Name=GeneReviews;
CC URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/BMPR1B";
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DR EMBL; D89675; BAA19765.1; -; mRNA.
DR EMBL; U89326; AAC28131.1; -; mRNA.
DR EMBL; AK299930; BAG61763.1; -; mRNA.
DR EMBL; AK313642; BAG36400.1; -; mRNA.
DR EMBL; AC004061; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092609; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093634; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC105395; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471057; EAX06060.1; -; Genomic_DNA.
DR EMBL; BC047773; AAH47773.1; -; mRNA.
DR EMBL; BC069796; AAH69796.1; -; mRNA.
DR EMBL; BC069803; AAH69803.1; -; mRNA.
DR IPI; IPI00939250; -.
DR RefSeq; NP_001194.1; NM_001203.2.
DR RefSeq; NP_001243721.1; NM_001256792.1.
DR RefSeq; NP_001243722.1; NM_001256793.1.
DR RefSeq; NP_001243723.1; NM_001256794.1.
DR UniGene; Hs.598475; -.
DR PDB; 3MDY; X-ray; 2.05 A; A/C=168-502.
DR PDBsum; 3MDY; -.
DR ProteinModelPortal; O00238; -.
DR MINT; MINT-1340235; -.
DR STRING; 9606.ENSP00000264568; -.
DR PhosphoSite; O00238; -.
DR PaxDb; O00238; -.
DR PRIDE; O00238; -.
DR DNASU; 658; -.
DR Ensembl; ENST00000264568; ENSP00000264568; ENSG00000138696.
DR Ensembl; ENST00000394931; ENSP00000378389; ENSG00000138696.
DR Ensembl; ENST00000440890; ENSP00000401907; ENSG00000138696.
DR Ensembl; ENST00000509540; ENSP00000421671; ENSG00000138696.
DR Ensembl; ENST00000512312; ENSP00000425444; ENSG00000138696.
DR Ensembl; ENST00000515059; ENSP00000426617; ENSG00000138696.
DR GeneID; 658; -.
DR KEGG; hsa:658; -.
DR UCSC; uc003htm.4; human.
DR CTD; 658; -.
DR GeneCards; GC04P095679; -.
DR HGNC; HGNC:1077; BMPR1B.
DR HPA; CAB009634; -.
DR MIM; 112600; phenotype.
DR MIM; 603248; gene.
DR MIM; 609441; phenotype.
DR neXtProt; NX_O00238; -.
DR Orphanet; 93396; Brachydactyly type A2.
DR Orphanet; 93384; Brachydactyly type C.
DR PharmGKB; PA25387; -.
DR eggNOG; COG0515; -.
DR HOGENOM; HOG000230587; -.
DR HOVERGEN; HBG054502; -.
DR InParanoid; O00238; -.
DR KO; K13578; -.
DR OMA; DGPIHHK; -.
DR PhylomeDB; O00238; -.
DR BRENDA; 2.7.10.2; 2681.
DR Pathway_Interaction_DB; bmppathway; BMP receptor signaling.
DR Reactome; REACT_111102; Signal Transduction.
DR BindingDB; O00238; -.
DR ChEMBL; CHEMBL5476; -.
DR ChiTaRS; BMPR1B; human.
DR EvolutionaryTrace; O00238; -.
DR GenomeRNAi; 658; -.
DR NextBio; 2676; -.
DR ArrayExpress; O00238; -.
DR Bgee; O00238; -.
DR CleanEx; HS_BMPR1B; -.
DR Genevestigator; O00238; -.
DR GermOnline; ENSG00000138696; Homo sapiens.
DR GO; GO:0005887; C:integral to plasma membrane; IC:UniProtKB.
DR GO; GO:0043235; C:receptor complex; TAS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:HGNC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004702; F:receptor signaling protein serine/threonine kinase activity; IEA:InterPro.
DR GO; GO:0046332; F:SMAD binding; IDA:HGNC.
DR GO; GO:0005025; F:transforming growth factor beta receptor activity, type I; IEA:Compara.
DR GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IMP:UniProtKB.
DR GO; GO:0030509; P:BMP signaling pathway; NAS:UniProtKB.
DR GO; GO:0001502; P:cartilage condensation; NAS:UniProtKB.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IEA:Compara.
DR GO; GO:0001654; P:eye development; ISS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IEA:Compara.
DR GO; GO:0035108; P:limb morphogenesis; IMP:UniProtKB.
DR GO; GO:0001550; P:ovarian cumulus expansion; ISS:UniProtKB.
DR GO; GO:0030501; P:positive regulation of bone mineralization; IMP:BHF-UCL.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:BHF-UCL.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Compara.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; IEA:Compara.
DR GO; GO:0023014; P:signal transduction by phosphorylation; IEA:GOC.
DR InterPro; IPR000333; Activin_II/TGFBeta-II_recpt.
DR InterPro; IPR000472; Activin_rcpt.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR000719; Prot_kinase_cat_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR003605; TGF_beta_rcpt_GS.
DR Pfam; PF01064; Activin_recp; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08515; TGF_beta_GS; 1.
DR PRINTS; PR00653; ACTIVIN2R.
DR SMART; SM00467; GS; 1.
DR SUPFAM; SSF56112; Kinase_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.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Chondrogenesis;
KW Complete proteome; Disease mutation; Disulfide bond; Dwarfism; Kinase;
KW Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding;
KW Polymorphism; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1 13 Potential.
FT CHAIN 14 502 Bone morphogenetic protein receptor type-
FT 1B.
FT /FTId=PRO_0000024412.
FT TOPO_DOM 14 126 Extracellular (Potential).
FT TRANSMEM 127 148 Helical; (Potential).
FT TOPO_DOM 149 502 Cytoplasmic (Potential).
FT DOMAIN 174 203 GS.
FT DOMAIN 204 494 Protein kinase.
FT NP_BIND 210 218 ATP (By similarity).
FT ACT_SITE 332 332 Proton acceptor (By similarity).
FT BINDING 231 231 ATP (By similarity).
FT DISULFID 32 53 By similarity.
FT DISULFID 34 38 By similarity.
FT DISULFID 47 71 By similarity.
FT DISULFID 81 95 By similarity.
FT DISULFID 96 102 By similarity.
FT VAR_SEQ 1 1 M -> MGWLEELNWQLHIFLLILLSMHTRANFLDNM (in
FT isoform 2).
FT /FTId=VSP_045100.
FT VARIANT 31 31 R -> H (in a gastric adenocarcinoma
FT sample; somatic mutation).
FT /FTId=VAR_041401.
FT VARIANT 149 149 R -> W (in dbSNP:rs34231464).
FT /FTId=VAR_041402.
FT VARIANT 200 200 I -> K (in BDA2; dbSNP:rs28939703).
FT /FTId=VAR_023819.
FT VARIANT 224 224 R -> H (in dbSNP:rs35973133).
FT /FTId=VAR_041403.
FT VARIANT 297 297 D -> N (in a metastatic melanoma sample;
FT somatic mutation).
FT /FTId=VAR_041404.
FT VARIANT 371 371 R -> Q (in dbSNP:rs34970181).
FT /FTId=VAR_041405.
FT VARIANT 486 486 R -> Q (in brachydactyly type C and BDA2;
FT with also additional features of
FT symphalangism-1).
FT /FTId=VAR_037967.
FT VARIANT 486 486 R -> W (in BDA2; dbSNP:rs28939704).
FT /FTId=VAR_023820.
FT HELIX 176 186
FT STRAND 190 192
FT HELIX 194 197
FT HELIX 200 203
FT STRAND 205 213
FT STRAND 216 223
FT STRAND 226 234
FT HELIX 235 237
FT HELIX 238 248
FT STRAND 261 268
FT HELIX 270 272
FT STRAND 274 279
FT HELIX 287 293
FT HELIX 298 316
FT STRAND 337 340
FT STRAND 346 348
FT HELIX 375 377
FT HELIX 380 383
FT HELIX 393 411
FT TURN 426 430
FT HELIX 437 444
FT HELIX 455 459
FT HELIX 461 473
FT HELIX 478 480
FT HELIX 484 496
FT TURN 497 499
SQ SEQUENCE 502 AA; 56930 MW; B283D9BF45535C79 CRC64;
MLLRSAGKLN VGTKKEDGES TAPTPRPKVL RCKCHHHCPE DSVNNICSTD GYCFTMIEED
DSGLPVVTSG CLGLEGSDFQ CRDTPIPHQR RSIECCTERN ECNKDLHPTL PPLKNRDFVD
GPIHHRALLI SVTVCSLLLV LIILFCYFRY KRQETRPRYS IGLEQDETYI PPGESLRDLI
EQSQSSGSGS GLPLLVQRTI AKQIQMVKQI GKGRYGEVWM GKWRGEKVAV KVFFTTEEAS
WFRETEIYQT VLMRHENILG FIAADIKGTG SWTQLYLITD YHENGSLYDY LKSTTLDAKS
MLKLAYSSVS GLCHLHTEIF STQGKPAIAH RDLKSKNILV KKNGTCCIAD LGLAVKFISD
TNEVDIPPNT RVGTKRYMPP EVLDESLNRN HFQSYIMADM YSFGLILWEV ARRCVSGGIV
EEYQLPYHDL VPSDPSYEDM REIVCIKKLR PSFPNRWSSD ECLRQMGKLM TECWAHNPAS
RLTALRVKKT LAKMSESQDI KL
//
