SOST_HUMAN
ID SOST_HUMAN Reviewed; 213 AA.
AC Q9BQB4; Q495N9;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Sclerostin {ECO:0000250|UniProtKB:Q99P68};
DE Flags: Precursor;
GN Name=SOST {ECO:0000312|HGNC:HGNC:13771}; ORFNames=UNQ2976/PRO7455/PRO7476;
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] (ISOFORM 1), AND INVOLVEMENT IN SOST1.
RX PubMed=11181578; DOI=10.1093/hmg/10.5.537;
RA Balemans W., Ebeling M., Patel N., van Hul E., Olson P., Dioszegi M.,
RA Lacza C., Wuyts W., van den Ende J., Willems P., Paes-Alves A.F., Hill S.,
RA Bueno M., Ramos F.J., Tacconi P., Dikkers F.G., Stratakis C.,
RA Lindpaintner K., Vickery B., Foernzler D., Van Hul W.;
RT "Increased bone density in sclerosteosis is due to the deficiency of a
RT novel secreted protein (SOST).";
RL Hum. Mol. Genet. 10:537-543(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND INVOLVEMENT IN
RP SOST1.
RX PubMed=11179006; DOI=10.1086/318811;
RA Brunkow M.E., Gardner J.C., Van Ness J., Paeper B.W., Kovacevich B.R.,
RA Proll S., Skonier J.E., Zhao L., Sabo P.J., Fu Y.H., Alisch R.S.,
RA Gillett L., Colbert T., Tacconi P., Galas D., Hamersma H., Beighton P.,
RA Mulligan J.T.;
RT "Bone dysplasia sclerosteosis results from loss of the SOST gene product, a
RT novel cystine knot-containing protein.";
RL Am. J. Hum. Genet. 68:577-589(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 PROTEIN SEQUENCE OF 24-38.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [7]
RP INVOLVEMENT IN VBCH.
RX PubMed=11836356; DOI=10.1136/jmg.39.2.91;
RA Balemans W., Patel N., Ebeling M., Van Hul E., Wuyts W., Lacza C.,
RA Dioszegi M., Dikkers F.G., Hildering P., Willems P.J., Verheij J.B.,
RA Lindpaintner K., Vickery B., Foernzler D., Van Hul W.;
RT "Identification of a 52 kb deletion downstream of the SOST gene in patients
RT with van Buchem disease.";
RL J. Med. Genet. 39:91-97(2002).
RN [8]
RP FUNCTION, AND INTERACTION WITH LRP5 AND LRP6.
RX PubMed=15908424; DOI=10.1074/jbc.m504308200;
RA Semenov M., Tamai K., He X.;
RT "SOST is a ligand for LRP5/LRP6 and a Wnt signaling inhibitor.";
RL J. Biol. Chem. 280:26770-26775(2005).
RN [9]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=20551380; DOI=10.1074/mcp.m110.001693;
RA Didangelos A., Yin X., Mandal K., Baumert M., Jahangiri M., Mayr M.;
RT "Proteomics characterization of extracellular space components in the human
RT aorta.";
RL Mol. Cell. Proteomics 9:2048-2062(2010).
RN [10]
RP INVOLVEMENT IN CDD, VARIANTS CDD MET-21 AND LEU-21, AND CHARACTERIZATION OF
RP VARIANTS CDD MET-21 AND LEU-21.
RX PubMed=21221996; DOI=10.1007/s00439-011-0947-3;
RA Kim S.J., Bieganski T., Sohn Y.B., Kozlowski K., Semenov M., Okamoto N.,
RA Kim C.H., Ko A.R., Ahn G.H., Choi Y.L., Park S.W., Ki C.S., Kim O.H.,
RA Nishimura G., Unger S., Superti-Furga A., Jin D.K.;
RT "Identification of signal peptide domain SOST mutations in autosomal
RT dominant craniodiaphyseal dysplasia.";
RL Hum. Genet. 129:497-502(2011).
RN [11]
RP INTERACTION WITH LRP4; LRP5 AND LRP6.
RX PubMed=21471202; DOI=10.1074/jbc.m110.190330;
RA Leupin O., Piters E., Halleux C., Hu S., Kramer I., Morvan F.,
RA Bouwmeester T., Schirle M., Bueno-Lozano M., Fuentes F.J., Itin P.H.,
RA Boudin E., de Freitas F., Jennes K., Brannetti B., Charara N.,
RA Ebersbach H., Geisse S., Lu C.X., Bauer A., Van Hul W., Kneissel M.;
RT "Bone overgrowth-associated mutations in the LRP4 gene impair sclerostin
RT facilitator function.";
RL J. Biol. Chem. 286:19489-19500(2011).
RN [12]
RP STRUCTURE BY NMR OF 25-213, HEPARIN-BINDING, AND DISULFIDE BONDS.
RX PubMed=19208630; DOI=10.1074/jbc.m807994200;
RA Veverka V., Henry A.J., Slocombe P.M., Ventom A., Mulloy B., Muskett F.W.,
RA Muzylak M., Greenslade K., Moore A., Zhang L., Gong J., Qian X., Paszty C.,
RA Taylor R.J., Robinson M.K., Carr M.D.;
RT "Characterization of the structural features and interactions of
RT sclerostin: molecular insight into a key regulator of Wnt-mediated bone
RT formation.";
RL J. Biol. Chem. 284:10890-10900(2009).
RN [13]
RP VARIANT SOST1 ARG-167, AND CHARACTERIZATION OF VARIANT SOST1 ARG-167.
RX PubMed=20583295; DOI=10.1002/humu.21274;
RA Piters E., Culha C., Moester M., Van Bezooijen R., Adriaensen D.,
RA Mueller T., Weidauer S., Jennes K., de Freitas F., Loewik C.,
RA Timmermans J.-P., Van Hul W., Papapoulos S.;
RT "First missense mutation in the SOST gene causing sclerosteosis by loss of
RT sclerostin function.";
RL Hum. Mutat. 31:E1526-E1543(2010).
CC -!- FUNCTION: Negative regulator of bone growth that acts through
CC inhibition of Wnt signaling and bone formation.
CC {ECO:0000269|PubMed:15908424}.
CC -!- SUBUNIT: Interacts with LRP4 (via the extracellular domain); the
CC interaction facilitates the inhibition of Wnt signaling. Interacts with
CC LRP5 (via the first two YWTD-EGF repeat domains); the interaction
CC inhibits Wnt-mediated signaling. Interacts with LRP6.
CC {ECO:0000269|PubMed:15908424, ECO:0000269|PubMed:21471202}.
CC -!- INTERACTION:
CC Q9BQB4; O75096: LRP4; NbExp=5; IntAct=EBI-5746563, EBI-310873;
CC Q9BQB4; O75197: LRP5; NbExp=3; IntAct=EBI-5746563, EBI-2466421;
CC Q9BQB4; O75581: LRP6; NbExp=7; IntAct=EBI-5746563, EBI-910915;
CC Q9BQB4; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-5746563, EBI-742388;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:20551380}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BQB4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BQB4-2; Sequence=VSP_010189;
CC -!- TISSUE SPECIFICITY: Widely expressed at low levels with highest levels
CC in bone, cartilage, kidney, liver, bone marrow and primary osteoblasts
CC differentiated for 21 days. Detected in the subendothelial layer of the
CC aortic intima (at protein level). {ECO:0000269|PubMed:20551380}.
CC -!- DISEASE: Sclerosteosis 1 (SOST1) [MIM:269500]: An autosomal recessive
CC sclerosing bone dysplasia characterized by a generalized hyperostosis
CC and sclerosis leading to a markedly thickened skull, with mandible,
CC ribs, clavicles and all long bones also being affected. Due to
CC narrowing of the foramina of the cranial nerves, facial nerve palsy,
CC hearing loss and atrophy of the optic nerves can occur. Sclerosteosis
CC is clinically and radiologically very similar to van Buchem disease,
CC mainly differentiated by hand malformations and a large stature in
CC sclerosteosis patients. {ECO:0000269|PubMed:11179006,
CC ECO:0000269|PubMed:11181578, ECO:0000269|PubMed:20583295}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Van Buchem disease (VBCH) [MIM:239100]: VBCH is an autosomal
CC recessive sclerosing bone dysplasia characterized by endosteal
CC hyperostosis of the mandible, skull, ribs, clavicles, and diaphyses of
CC the long bones. Affected patients present a symmetrically increased
CC thickness of bones, most frequently found as an enlarged jawbone, but
CC also an enlargement of the skull, ribs, diaphysis of long bones, as
CC well as tubular bones of hands and feet. The clinical consequence of
CC increased thickness of the skull include facial nerve palsy causing
CC hearing loss, visual problems, neurological pain, and, very rarely,
CC blindness as a consequence of optic atrophy. Serum alkaline phosphatase
CC levels are elevated. {ECO:0000269|PubMed:11836356}. Note=The disease is
CC caused by variants affecting the gene represented in this entry. A 52
CC kb deletion downstream of SOST results in SOST transcription
CC suppression causing van Buchem disease.
CC -!- DISEASE: Craniodiaphyseal dysplasia autosomal dominant (CDD)
CC [MIM:122860]: A severe bone dysplasia characterized by massive
CC generalized hyperostosis and sclerosis, especially involving the skull
CC and facial bones. The sclerosis is so severe that the resulting facial
CC distortion is referred to as 'leontiasis ossea' (leonine faces) and the
CC bone deposition results in progressive stenosis of craniofacial
CC foramina. Respiratory obstruction due to choanal stenosis compromises
CC the clinical outcomes of affected patients.
CC {ECO:0000269|PubMed:21221996}. Note=The disease is caused by variants
CC affecting the gene represented in this entry. Heterozygous mutations
CC located in the secretion signal of the SOST gene prevent sclerostin
CC secretion and can be responsible for craniodiaphyseal dysplasia.
CC -!- SIMILARITY: Belongs to the sclerostin family. {ECO:0000305}.
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DR EMBL; AF331844; AAK16158.1; -; mRNA.
DR EMBL; AF326736; AAK13451.1; -; Genomic_DNA.
DR EMBL; AF326739; AAK13454.1; -; mRNA.
DR EMBL; AY358203; AAQ88570.1; -; mRNA.
DR EMBL; AY358627; AAQ88990.1; -; mRNA.
DR EMBL; AC055813; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC101086; AAI01087.1; -; mRNA.
DR EMBL; BC101087; AAI01088.1; -; mRNA.
DR EMBL; BC101088; AAI01089.1; -; mRNA.
DR EMBL; BC101089; AAI01090.1; -; mRNA.
DR CCDS; CCDS11468.1; -. [Q9BQB4-1]
DR RefSeq; NP_079513.1; NM_025237.2. [Q9BQB4-1]
DR PDB; 2K8P; NMR; -; A=25-213.
DR PDB; 3SOV; X-ray; 1.27 A; Z=115-121.
DR PDB; 6L6R; X-ray; 3.80 A; C/D=24-177.
DR PDBsum; 2K8P; -.
DR PDBsum; 3SOV; -.
DR PDBsum; 6L6R; -.
DR AlphaFoldDB; Q9BQB4; -.
DR SMR; Q9BQB4; -.
DR BioGRID; 119186; 144.
DR DIP; DIP-59407N; -.
DR ELM; Q9BQB4; -.
DR IntAct; Q9BQB4; 120.
DR STRING; 9606.ENSP00000301691; -.
DR ChEMBL; CHEMBL3580487; -.
DR DrugBank; DB11866; Romosozumab.
DR DrugCentral; Q9BQB4; -.
DR GlyGen; Q9BQB4; 2 sites.
DR BioMuta; SOST; -.
DR DMDM; 20140220; -.
DR MassIVE; Q9BQB4; -.
DR PaxDb; Q9BQB4; -.
DR PeptideAtlas; Q9BQB4; -.
DR PRIDE; Q9BQB4; -.
DR ProteomicsDB; 78650; -. [Q9BQB4-1]
DR ProteomicsDB; 78651; -. [Q9BQB4-2]
DR ABCD; Q9BQB4; 12 sequenced antibodies.
DR Antibodypedia; 29585; 532 antibodies from 33 providers.
DR DNASU; 50964; -.
DR Ensembl; ENST00000301691.3; ENSP00000301691.1; ENSG00000167941.3. [Q9BQB4-1]
DR GeneID; 50964; -.
DR KEGG; hsa:50964; -.
DR MANE-Select; ENST00000301691.3; ENSP00000301691.1; NM_025237.3; NP_079513.1.
DR UCSC; uc002iec.1; human. [Q9BQB4-1]
DR CTD; 50964; -.
DR DisGeNET; 50964; -.
DR GeneCards; SOST; -.
DR GeneReviews; SOST; -.
DR HGNC; HGNC:13771; SOST.
DR HPA; ENSG00000167941; Tissue enriched (kidney).
DR MalaCards; SOST; -.
DR MIM; 122860; phenotype.
DR MIM; 239100; phenotype.
DR MIM; 269500; phenotype.
DR MIM; 605740; gene.
DR neXtProt; NX_Q9BQB4; -.
DR OpenTargets; ENSG00000167941; -.
DR Orphanet; 1513; Craniodiaphyseal dysplasia.
DR Orphanet; 3416; Hyperostosis corticalis generalisata.
DR Orphanet; 3152; Sclerosteosis.
DR PharmGKB; PA37809; -.
DR VEuPathDB; HostDB:ENSG00000167941; -.
DR eggNOG; ENOG502QTBG; Eukaryota.
DR GeneTree; ENSGT00390000014900; -.
DR HOGENOM; CLU_087969_1_0_1; -.
DR InParanoid; Q9BQB4; -.
DR OMA; MQISWAV; -.
DR OrthoDB; 1008844at2759; -.
DR PhylomeDB; Q9BQB4; -.
DR TreeFam; TF353019; -.
DR PathwayCommons; Q9BQB4; -.
DR Reactome; R-HSA-201681; TCF dependent signaling in response to WNT.
DR Reactome; R-HSA-3772470; Negative regulation of TCF-dependent signaling by WNT ligand antagonists.
DR SignaLink; Q9BQB4; -.
DR SIGNOR; Q9BQB4; -.
DR BioGRID-ORCS; 50964; 10 hits in 1061 CRISPR screens.
DR EvolutionaryTrace; Q9BQB4; -.
DR GeneWiki; Sclerostin; -.
DR GeneWiki; SOST; -.
DR GenomeRNAi; 50964; -.
DR Pharos; Q9BQB4; Tclin.
DR PRO; PR:Q9BQB4; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9BQB4; protein.
DR Bgee; ENSG00000167941; Expressed in trabecular bone tissue and 61 other tissues.
DR Genevisible; Q9BQB4; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0036122; F:BMP binding; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IDA:UniProtKB.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0030509; P:BMP signaling pathway; IEA:Ensembl.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0071374; P:cellular response to parathyroid hormone stimulus; IDA:UniProtKB.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IDA:MGI.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:BHF-UCL.
DR GO; GO:0030279; P:negative regulation of ossification; NAS:UniProtKB.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IDA:BHF-UCL.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0001503; P:ossification; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:UniProtKB.
DR DisProt; DP00926; -.
DR Gene3D; 2.10.90.10; -; 1.
DR IDEAL; IID00584; -.
DR InterPro; IPR006207; Cys_knot_C.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR008835; Sclerostin/SOSTDC1.
DR InterPro; IPR015665; SOST.
DR PANTHER; PTHR14903; PTHR14903; 1.
DR PANTHER; PTHR14903:SF4; PTHR14903:SF4; 1.
DR Pfam; PF05463; Sclerostin; 1.
DR SMART; SM00041; CT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing;
KW Disease variant; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Heparin-binding; Reference proteome; Secreted; Signal;
KW Wnt signaling pathway.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 24..213
FT /note="Sclerostin"
FT /id="PRO_0000033177"
FT DOMAIN 82..172
FT /note="CTCK"
FT REGION 41..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 80..134
FT /evidence="ECO:0000269|PubMed:19208630"
FT DISULFID 94..148
FT /evidence="ECO:0000269|PubMed:19208630"
FT DISULFID 105..165
FT /evidence="ECO:0000269|PubMed:19208630"
FT DISULFID 109..167
FT /evidence="ECO:0000269|PubMed:19208630"
FT VAR_SEQ 64..73
FT /note="RPPHHPFETK -> WPGGRPPSRAPLST (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_010189"
FT VARIANT 21
FT /note="V -> L (in CDD; affects protein secretion;
FT dbSNP:rs387907169)"
FT /evidence="ECO:0000269|PubMed:21221996"
FT /id="VAR_065766"
FT VARIANT 21
FT /note="V -> M (in CDD; de novo mutation; affects protein
FT secretion; dbSNP:rs387907169)"
FT /evidence="ECO:0000269|PubMed:21221996"
FT /id="VAR_065767"
FT VARIANT 167
FT /note="C -> R (in SOST1; leads to retention of the mutant
FT protein in the endoplasmic reticulum; leads to a complete
FT loss of function of the protein)"
FT /evidence="ECO:0000269|PubMed:20583295"
FT /id="VAR_063982"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:2K8P"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:2K8P"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:2K8P"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:2K8P"
FT STRAND 139..147
FT /evidence="ECO:0007829|PDB:2K8P"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:2K8P"
SQ SEQUENCE 213 AA; 24031 MW; 30DBD55CE73D5BB2 CRC64;
MQLPLALCLV CLLVHTAFRV VEGQGWQAFK NDATEIIPEL GEYPEPPPEL ENNKTMNRAE
NGGRPPHHPF ETKDVSEYSC RELHFTRYVT DGPCRSAKPV TELVCSGQCG PARLLPNAIG
RGKWWRPSGP DFRCIPDRYR AQRVQLLCPG GEAPRARKVR LVASCKCKRL TRFHNQSELK
DFGTEAARPQ KGRKPRPRAR SAKANQAELE NAY
