BMP10_HUMAN
ID BMP10_HUMAN Reviewed; 424 AA.
AC O95393; Q53R17; Q6NTE0;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Bone morphogenetic protein 10;
DE Short=BMP-10;
DE Flags: Precursor;
GN Name=BMP10;
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 [MRNA].
RA Celeste A.J.;
RT "Homo sapiens bone morphogenetic protein 10 (BMP-10) mRNA.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
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., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., 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., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., 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., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
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 FUNCTION.
RX PubMed=16049014; DOI=10.1074/jbc.m504629200;
RA Mazerbourg S., Sangkuhl K., Luo C.-W., Sudo S., Klein C., Hsueh A.J.W.;
RT "Identification of receptors and signaling pathways for orphan bone
RT morphogenetic protein/growth differentiation factor ligands based on
RT genomic analyses.";
RL J. Biol. Chem. 280:32122-32132(2005).
RN [5]
RP FUNCTION.
RX PubMed=17068149; DOI=10.1182/blood-2006-07-034124;
RA David L., Mallet C., Mazerbourg S., Feige J.-J., Bailly S.;
RT "Identification of BMP9 and BMP10 as functional activators of the orphan
RT activin receptor-like kinase 1 (ALK1) in endothelial cells.";
RL Blood 109:1953-1961(2007).
RN [6]
RP INTERACTION WITH FBN1 AND FBN2.
RX PubMed=18339631; DOI=10.1074/jbc.m707820200;
RA Sengle G., Charbonneau N.L., Ono R.N., Sasaki T., Alvarez J., Keene D.R.,
RA Baechinger H.P., Sakai L.Y.;
RT "Targeting of bone morphogenetic protein growth factor complexes to
RT fibrillin.";
RL J. Biol. Chem. 283:13874-13888(2008).
RN [7]
RP INTERACTION WITH ENG.
RX PubMed=21737454; DOI=10.1074/jbc.m111.260133;
RA Castonguay R., Werner E.D., Matthews R.G., Presman E., Mulivor A.W.,
RA Solban N., Sako D., Pearsall R.S., Underwood K.W., Seehra J., Kumar R.,
RA Grinberg A.V.;
RT "Soluble endoglin specifically binds bone morphogenetic proteins 9 and 10
RT via its orphan domain, inhibits blood vessel formation, and suppresses
RT tumor growth.";
RL J. Biol. Chem. 286:30034-30046(2011).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=20608934; DOI=10.1111/j.1349-7006.2010.01648.x;
RA Ye L., Bokobza S., Li J., Moazzam M., Chen J., Mansel R.E., Jiang W.G.;
RT "Bone morphogenetic protein-10 (BMP-10) inhibits aggressiveness of breast
RT cancer cells and correlates with poor prognosis in breast cancer.";
RL Cancer Sci. 101:2137-2144(2010).
CC -!- FUNCTION: Required for maintaining the proliferative activity of
CC embryonic cardiomyocytes by preventing premature activation of the
CC negative cell cycle regulator CDKN1C/p57KIP and maintaining the
CC required expression levels of cardiogenic factors such as MEF2C and
CC NKX2-5. Acts as a ligand for ACVRL1/ALK1, BMPR1A/ALK3 and BMPR1B/ALK6,
CC leading to activation of SMAD1, SMAD5 and SMAD8 transcription factors.
CC Inhibits endothelial cell migration and growth. May reduce cell
CC migration and cell matrix adhesion in breast cancer cell lines.
CC {ECO:0000269|PubMed:16049014, ECO:0000269|PubMed:17068149,
CC ECO:0000269|PubMed:20608934}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Interacts with
CC FBN1 (via N-terminal domain) and FBN2 (PubMed:18339631). Interacts with
CC ENG (PubMed:21737454). {ECO:0000250|UniProtKB:P12643,
CC ECO:0000269|PubMed:18339631, ECO:0000269|PubMed:21737454}.
CC -!- INTERACTION:
CC O95393; Q6Q788: APOA5; NbExp=3; IntAct=EBI-3922513, EBI-3936819;
CC O95393; Q13520: AQP6; NbExp=3; IntAct=EBI-3922513, EBI-13059134;
CC O95393; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-3922513, EBI-11343438;
CC O95393; Q13323: BIK; NbExp=3; IntAct=EBI-3922513, EBI-700794;
CC O95393; J3KQ12: BSCL2; NbExp=3; IntAct=EBI-3922513, EBI-11532900;
CC O95393; Q8WZ55: BSND; NbExp=3; IntAct=EBI-3922513, EBI-7996695;
CC O95393; Q6NSX1: CCDC70; NbExp=3; IntAct=EBI-3922513, EBI-6873045;
CC O95393; P20138: CD33; NbExp=3; IntAct=EBI-3922513, EBI-3906571;
CC O95393; Q8N5K1: CISD2; NbExp=3; IntAct=EBI-3922513, EBI-1045797;
CC O95393; O95471: CLDN7; NbExp=3; IntAct=EBI-3922513, EBI-740744;
CC O95393; O75208: COQ9; NbExp=3; IntAct=EBI-3922513, EBI-724524;
CC O95393; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-3922513, EBI-6942903;
CC O95393; O95424: DEXI; NbExp=3; IntAct=EBI-3922513, EBI-724515;
CC O95393; Q15125: EBP; NbExp=3; IntAct=EBI-3922513, EBI-3915253;
CC O95393; P30040: ERP29; NbExp=3; IntAct=EBI-3922513, EBI-946830;
CC O95393; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-3922513, EBI-18304435;
CC O95393; P12314: FCGR1A; NbExp=3; IntAct=EBI-3922513, EBI-2869867;
CC O95393; Q96PJ5: FCRL4; NbExp=3; IntAct=EBI-3922513, EBI-4314687;
CC O95393; O15552: FFAR2; NbExp=3; IntAct=EBI-3922513, EBI-2833872;
CC O95393; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-3922513, EBI-3918971;
CC O95393; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-3922513, EBI-12142257;
CC O95393; Q6P531: GGT6; NbExp=3; IntAct=EBI-3922513, EBI-2868927;
CC O95393; P08034: GJB1; NbExp=3; IntAct=EBI-3922513, EBI-17565645;
CC O95393; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-3922513, EBI-13345167;
CC O95393; Q8TED1: GPX8; NbExp=3; IntAct=EBI-3922513, EBI-11721746;
CC O95393; P26951: IL3RA; NbExp=3; IntAct=EBI-3922513, EBI-1757512;
CC O95393; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-3922513, EBI-10266796;
CC O95393; P43628: KIR2DL3; NbExp=3; IntAct=EBI-3922513, EBI-8632435;
CC O95393; P43629: KIR3DL1; NbExp=3; IntAct=EBI-3922513, EBI-3910993;
CC O95393; P26715: KLRC1; NbExp=3; IntAct=EBI-3922513, EBI-9018187;
CC O95393; Q8N386: LRRC25; NbExp=3; IntAct=EBI-3922513, EBI-11304917;
CC O95393; Q9HCJ2: LRRC4C; NbExp=3; IntAct=EBI-3922513, EBI-3925442;
CC O95393; O14880: MGST3; NbExp=3; IntAct=EBI-3922513, EBI-724754;
CC O95393; Q9Y676: MRPS18B; NbExp=3; IntAct=EBI-3922513, EBI-750085;
CC O95393; Q96HJ5: MS4A3; NbExp=3; IntAct=EBI-3922513, EBI-12806656;
CC O95393; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-3922513, EBI-3923617;
CC O95393; Q5VZY2: PLPP4; NbExp=3; IntAct=EBI-3922513, EBI-10485931;
CC O95393; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-3922513, EBI-7545592;
CC O95393; Q9Y3P8: SIT1; NbExp=3; IntAct=EBI-3922513, EBI-6977215;
CC O95393; Q14973: SLC10A1; NbExp=3; IntAct=EBI-3922513, EBI-3923031;
CC O95393; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-3922513, EBI-18159983;
CC O95393; Q9NQQ7-3: SLC35C2; NbExp=3; IntAct=EBI-3922513, EBI-17295964;
CC O95393; Q9H2H9: SLC38A1; NbExp=3; IntAct=EBI-3922513, EBI-9978441;
CC O95393; P02730: SLC4A1; NbExp=3; IntAct=EBI-3922513, EBI-7576138;
CC O95393; Q9NPE6: SPAG4; NbExp=3; IntAct=EBI-3922513, EBI-10819434;
CC O95393; P57738: TCTA; NbExp=3; IntAct=EBI-3922513, EBI-6447595;
CC O95393; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-3922513, EBI-8638294;
CC O95393; Q96B21: TMEM45B; NbExp=3; IntAct=EBI-3922513, EBI-3923061;
CC O95393; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-3922513, EBI-2548832;
CC O95393; O15393-2: TMPRSS2; NbExp=3; IntAct=EBI-3922513, EBI-12345267;
CC O95393; O43557: TNFSF14; NbExp=3; IntAct=EBI-3922513, EBI-524131;
CC O95393; P32971: TNFSF8; NbExp=3; IntAct=EBI-3922513, EBI-13076860;
CC O95393; Q12999: TSPAN31; NbExp=3; IntAct=EBI-3922513, EBI-17678331;
CC O95393; Q9H7M9: VSIR; NbExp=3; IntAct=EBI-3922513, EBI-744988;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in mammary epithelia (at protein level).
CC {ECO:0000269|PubMed:20608934}.
CC -!- INDUCTION: Down-regulated in some breast cancer subtypes and breast
CC cancer cell lines. {ECO:0000269|PubMed:20608934}.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Bone morphogenetic protein 10 entry;
CC URL="https://en.wikipedia.org/wiki/Bone_morphogenetic_protein_10";
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DR EMBL; AF101441; AAC77462.1; -; mRNA.
DR EMBL; AC097495; AAY15075.1; -; Genomic_DNA.
DR EMBL; BC069080; AAH69080.1; -; mRNA.
DR EMBL; BC101734; AAI01735.1; -; mRNA.
DR EMBL; BC105063; AAI05064.1; -; mRNA.
DR CCDS; CCDS1890.1; -.
DR RefSeq; NP_055297.1; NM_014482.2.
DR PDB; 6SF1; X-ray; 2.80 A; B=317-424.
DR PDB; 6SF3; X-ray; 2.30 A; B=317-424.
DR PDBsum; 6SF1; -.
DR PDBsum; 6SF3; -.
DR AlphaFoldDB; O95393; -.
DR SMR; O95393; -.
DR BioGRID; 118125; 59.
DR IntAct; O95393; 55.
DR STRING; 9606.ENSP00000295379; -.
DR BindingDB; O95393; -.
DR ChEMBL; CHEMBL3713453; -.
DR GlyGen; O95393; 2 sites.
DR iPTMnet; O95393; -.
DR PhosphoSitePlus; O95393; -.
DR BioMuta; BMP10; -.
DR MassIVE; O95393; -.
DR MaxQB; O95393; -.
DR PaxDb; O95393; -.
DR PeptideAtlas; O95393; -.
DR PRIDE; O95393; -.
DR ProteomicsDB; 50844; -.
DR Antibodypedia; 16182; 402 antibodies from 37 providers.
DR DNASU; 27302; -.
DR Ensembl; ENST00000295379.2; ENSP00000295379.1; ENSG00000163217.2.
DR GeneID; 27302; -.
DR KEGG; hsa:27302; -.
DR MANE-Select; ENST00000295379.2; ENSP00000295379.1; NM_014482.3; NP_055297.1.
DR UCSC; uc002sez.1; human.
DR CTD; 27302; -.
DR DisGeNET; 27302; -.
DR GeneCards; BMP10; -.
DR HGNC; HGNC:20869; BMP10.
DR HPA; ENSG00000163217; Tissue enriched (heart).
DR MIM; 608748; gene.
DR neXtProt; NX_O95393; -.
DR OpenTargets; ENSG00000163217; -.
DR PharmGKB; PA134953092; -.
DR VEuPathDB; HostDB:ENSG00000163217; -.
DR eggNOG; KOG3900; Eukaryota.
DR GeneTree; ENSGT00940000156279; -.
DR HOGENOM; CLU_020515_2_0_1; -.
DR InParanoid; O95393; -.
DR OMA; MIAHEQL; -.
DR OrthoDB; 749511at2759; -.
DR PhylomeDB; O95393; -.
DR TreeFam; TF316134; -.
DR PathwayCommons; O95393; -.
DR Reactome; R-HSA-201451; Signaling by BMP.
DR Reactome; R-HSA-2129379; Molecules associated with elastic fibres.
DR SignaLink; O95393; -.
DR SIGNOR; O95393; -.
DR BioGRID-ORCS; 27302; 9 hits in 1058 CRISPR screens.
DR GeneWiki; Bone_morphogenetic_protein_10; -.
DR GenomeRNAi; 27302; -.
DR Pharos; O95393; Tbio.
DR PRO; PR:O95393; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O95393; protein.
DR Bgee; ENSG00000163217; Expressed in cardiac muscle of right atrium and 67 other tissues.
DR Genevisible; O95393; HS.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0030018; C:Z disc; IDA:BHF-UCL.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0005179; F:hormone activity; IDA:BHF-UCL.
DR GO; GO:0033612; F:receptor serine/threonine kinase binding; IDA:UniProtKB.
DR GO; GO:0031433; F:telethonin binding; IPI:BHF-UCL.
DR GO; GO:0032924; P:activin receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0007512; P:adult heart development; ISS:BHF-UCL.
DR GO; GO:0055009; P:atrial cardiac muscle tissue morphogenesis; ISS:BHF-UCL.
DR GO; GO:0030509; P:BMP signaling pathway; IDA:BHF-UCL.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0060347; P:heart trabecula formation; ISS:BHF-UCL.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0010614; P:negative regulation of cardiac muscle hypertrophy; ISS:BHF-UCL.
DR GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; IDA:UniProtKB.
DR GO; GO:0010596; P:negative regulation of endothelial cell migration; IDA:BHF-UCL.
DR GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
DR GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; ISS:BHF-UCL.
DR GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; IMP:BHF-UCL.
DR GO; GO:0061036; P:positive regulation of cartilage development; IEA:Ensembl.
DR GO; GO:2000138; P:positive regulation of cell proliferation involved in heart morphogenesis; ISS:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
DR GO; GO:0060298; P:positive regulation of sarcomere organization; IDA:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR GO; GO:0055117; P:regulation of cardiac muscle contraction; IMP:BHF-UCL.
DR GO; GO:1903242; P:regulation of cardiac muscle hypertrophy in response to stress; IDA:BHF-UCL.
DR GO; GO:0045214; P:sarcomere organization; ISS:BHF-UCL.
DR GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
DR GO; GO:0055015; P:ventricular cardiac muscle cell development; ISS:BHF-UCL.
DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; ISS:BHF-UCL.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR001839; TGF-b_C.
DR InterPro; IPR001111; TGF-b_propeptide.
DR InterPro; IPR015615; TGF-beta-rel.
DR InterPro; IPR017948; TGFb_CS.
DR PANTHER; PTHR11848; PTHR11848; 1.
DR Pfam; PF00019; TGF_beta; 1.
DR Pfam; PF00688; TGFb_propeptide; 1.
DR SMART; SM00204; TGFB; 1.
DR SUPFAM; SSF57501; SSF57501; 1.
DR PROSITE; PS00250; TGF_BETA_1; 1.
DR PROSITE; PS51362; TGF_BETA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cleavage on pair of basic residues; Cytokine;
KW Developmental protein; Disulfide bond; Glycoprotein; Growth factor;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..316
FT /evidence="ECO:0000255"
FT /id="PRO_0000033888"
FT CHAIN 317..424
FT /note="Bone morphogenetic protein 10"
FT /id="PRO_0000033889"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 323..389
FT /evidence="ECO:0000250"
FT DISULFID 352..421
FT /evidence="ECO:0000250"
FT DISULFID 356..423
FT /evidence="ECO:0000250"
FT DISULFID 388
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT VARIANT 200
FT /note="T -> S (in dbSNP:rs2231342)"
FT /id="VAR_052572"
FT VARIANT 250
FT /note="N -> K (in dbSNP:rs2231345)"
FT /id="VAR_052573"
FT CONFLICT 143
FT /note="A -> T (in Ref. 3; AAH69080)"
FT /evidence="ECO:0000305"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:6SF3"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:6SF3"
FT TURN 332..336
FT /evidence="ECO:0007829|PDB:6SF3"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:6SF3"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:6SF3"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:6SF3"
FT STRAND 351..356
FT /evidence="ECO:0007829|PDB:6SF3"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:6SF3"
FT HELIX 368..379
FT /evidence="ECO:0007829|PDB:6SF3"
FT TURN 381..383
FT /evidence="ECO:0007829|PDB:6SF3"
FT STRAND 389..403
FT /evidence="ECO:0007829|PDB:6SF3"
FT STRAND 406..423
FT /evidence="ECO:0007829|PDB:6SF3"
SQ SEQUENCE 424 AA; 48047 MW; 3FDB3B7221BB2254 CRC64;
MGSLVLTLCA LFCLAAYLVS GSPIMNLEQS PLEEDMSLFG DVFSEQDGVD FNTLLQSMKD
EFLKTLNLSD IPTQDSAKVD PPEYMLELYN KFATDRTSMP SANIIRSFKN EDLFSQPVSF
NGLRKYPLLF NVSIPHHEEV IMAELRLYTL VQRDRMIYDG VDRKITIFEV LESKGDNEGE
RNMLVLVSGE IYGTNSEWET FDVTDAIRRW QKSGSSTHQL EVHIESKHDE AEDASSGRLE
IDTSAQNKHN PLLIVFSDDQ SSDKERKEEL NEMISHEQLP ELDNLGLDSF SSGPGEEALL
QMRSNIIYDS TARIRRNAKG NYCKRTPLYI DFKEIGWDSW IIAPPGYEAY ECRGVCNYPL
AEHLTPTKHA IIQALVHLKN SQKASKACCV PTKLEPISIL YLDKGVVTYK FKYEGMAVSE
CGCR
