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Growth/differentiation factor 2 (GDF-2) (Bone morphogenetic protein 9) (BMP-9)

 GDF2_HUMAN              Reviewed;         429 AA.
Q9UK05; Q5VSQ9; Q9Y571;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
12-SEP-2018, entry version 158.
RecName: Full=Growth/differentiation factor 2;
Short=GDF-2;
AltName: Full=Bone morphogenetic protein 9;
Short=BMP-9;
Flags: Precursor;
Name=GDF2; Synonyms=BMP9;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
Celeste A.J.;
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 316-429.
TISSUE=Liver;
Zimmers T.A., Koniaris L.G., Sitzmann J.V., Lee S.-J.;
"Growth/differentiation factor-2, a new TGF-beta family member with
bone promoting activities.";
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
[6]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18309101; DOI=10.1161/CIRCRESAHA.107.165530;
David L., Mallet C., Keramidas M., Lamande N., Gasc J.M.,
Dupuis-Girod S., Plauchu H., Feige J.J., Bailly S.;
"Bone morphogenetic protein-9 is a circulating vascular quiescence
factor.";
Circ. Res. 102:914-922(2008).
[7]
INTERACTION WITH ENG.
PubMed=21737454; DOI=10.1074/jbc.M111.260133;
Castonguay R., Werner E.D., Matthews R.G., Presman E., Mulivor A.W.,
Solban N., Sako D., Pearsall R.S., Underwood K.W., Seehra J.,
Kumar R., Grinberg A.V.;
"Soluble endoglin specifically binds bone morphogenetic proteins 9 and
10 via its orphan domain, inhibits blood vessel formation, and
suppresses tumor growth.";
J. Biol. Chem. 286:30034-30046(2011).
[8]
FUNCTION, AND INTERACTION WITH ACVRL1.
PubMed=22799562; DOI=10.1021/bi300942x;
Mahlawat P., Ilangovan U., Biswas T., Sun L.Z., Hinck A.P.;
"Structure of the Alk1 extracellular domain and characterization of
its bone morphogenetic protein (BMP) binding properties.";
Biochemistry 51:6328-6341(2012).
[9]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE SPECIFICITY.
PubMed=21710321; DOI=10.1007/s00018-011-0751-1;
Bidart M., Ricard N., Levet S., Samson M., Mallet C., David L.,
Subileau M., Tillet E., Feige J.J., Bailly S.;
"BMP9 is produced by hepatocytes and circulates mainly in an active
mature form complexed to its prodomain.";
Cell. Mol. Life Sci. 69:313-324(2012).
[10]
INTERACTION WITH ENG AND ACVRL1.
PubMed=22347366; DOI=10.1371/journal.pone.0029948;
Alt A., Miguel-Romero L., Donderis J., Aristorena M., Blanco F.J.,
Round A., Rubio V., Bernabeu C., Marina A.;
"Structural and functional insights into endoglin ligand recognition
and binding.";
PLoS ONE 7:E29948-E29948(2012).
[11]
FUNCTION.
PubMed=23300529; DOI=10.1371/journal.pone.0050920;
Nolan-Stevaux O., Zhong W., Culp S., Shaffer K., Hoover J.,
Wickramasinghe D., Ruefli-Brasse A.;
"Endoglin requirement for BMP9 signaling in endothelial cells reveals
new mechanism of action for selective anti-endoglin antibodies.";
PLoS ONE 7:E50920-E50920(2012).
[12]
X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) OF 320-429, AND DISULFIDE
BONDS.
PubMed=15851468; DOI=10.1074/jbc.M503328200;
Brown M.A., Zhao Q., Baker K.A., Naik C., Chen C., Pukac L., Singh M.,
Tsareva T., Parice Y., Mahoney A., Roschke V., Sanyal I., Choe S.;
"Crystal structure of BMP-9 and functional interactions with pro-
region and receptors.";
J. Biol. Chem. 280:25111-25118(2005).
[13]
X-RAY CRYSTALLOGRAPHY (3.36 ANGSTROMS) OF 320-429 IN COMPLEX WITH
ACVRL1 AND ACVR2B, AND DISULFIDE BONDS.
PubMed=22718755; DOI=10.1074/jbc.M112.377960;
Townson S.A., Martinez-Hackert E., Greppi C., Lowden P., Sako D.,
Liu J., Ucran J.A., Liharska K., Underwood K.W., Seehra J., Kumar R.,
Grinberg A.V.;
"Specificity and structure of a high affinity activin receptor-like
kinase 1 (ALK1) signaling complex.";
J. Biol. Chem. 287:27313-27325(2012).
[14] {ECO:0000244|PDB:4MPL}
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 321-429, SUBUNIT,
INTERACTION WITH ACVRL1, SUBCELLULAR LOCATION, AND DISULFIDE BONDS.
PubMed=25237187; DOI=10.1074/jbc.M114.579771;
Wei Z., Salmon R.M., Upton P.D., Morrell N.W., Li W.;
"Regulation of bone morphogenetic protein 9 (BMP9) by redox-dependent
proteolysis.";
J. Biol. Chem. 289:31150-31159(2014).
[15] {ECO:0000244|PDB:4YCG, ECO:0000244|PDB:4YCI}
X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 320-429, FUNCTION,
INTERACTION WITH ACVRL1; BMPR2; ACVR2B AND ACVR2A, SUBUNIT, AND
DISULFIDE BONDS.
PubMed=25751889; DOI=10.1073/pnas.1501303112;
Mi L.Z., Brown C.T., Gao Y., Tian Y., Le V.Q., Walz T., Springer T.A.;
"Structure of bone morphogenetic protein 9 procomplex.";
Proc. Natl. Acad. Sci. U.S.A. 112:3710-3715(2015).
[16] {ECO:0000244|PDB:5HZW, ECO:0000244|PDB:5I05}
X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 320-429, X-RAY
CRYSTALLOGRAPHY (4.45 ANGSTROMS) OF 320-429 IN COMPLEX WITH ENG,
SUBUNIT, AND DISULFIDE BONDS.
PubMed=28564608; DOI=10.1016/j.celrep.2017.05.011;
Saito T., Bokhove M., Croci R., Zamora-Caballero S., Han L.,
Letarte M., de Sanctis D., Jovine L.;
"Structural Basis of the Human Endoglin-BMP9 Interaction: Insights
into BMP Signaling and HHT1.";
Cell Rep. 19:1917-1928(2017).
[17]
VARIANTS HHT5 LEU-68; LEU-85 AND TRP-333, AND PROTEOLYTIC PROCESSING.
PubMed=23972370; DOI=10.1016/j.ajhg.2013.07.004;
Wooderchak-Donahue W.L., McDonald J., O'Fallon B., Upton P.D., Li W.,
Roman B.L., Young S., Plant P., Fulop G.T., Langa C., Morrell N.W.,
Botella L.M., Bernabeu C., Stevenson D.A., Runo J.R.,
Bayrak-Toydemir P.;
"BMP9 mutations cause a vascular-anomaly syndrome with phenotypic
overlap with hereditary hemorrhagic telangiectasia.";
Am. J. Hum. Genet. 93:530-537(2013).
-!- FUNCTION: Potent circulating inhibitor of angiogenesis. Signals
through the type I activin receptor ACVRL1 but not other Alks.
Signaling through SMAD1 in endothelial cells requires TGF-beta
coreceptor endoglin/ENG. {ECO:0000269|PubMed:18309101,
ECO:0000269|PubMed:21710321, ECO:0000269|PubMed:22799562,
ECO:0000269|PubMed:23300529, ECO:0000269|PubMed:25237187}.
-!- SUBUNIT: Homodimer; disulfide-linked (PubMed:25237187,
PubMed:28564608). Detected in extracellular fluid as mature
homodimer, and in complex with its propeptide (PubMed:21710321,
PubMed:25237187). Interacts with ACVRL1, BMPR2 and ACVR2B with
high affinity (in vitro) (PubMed:22799562, PubMed:22347366,
PubMed:25237187, PubMed:25751889). Identified in a complex with
ACVRL1 and ACVR2B (PubMed:22718755). Has ten times lower affinity
for ACVR2A (in vitro) (PubMed:25751889). Interacts with ENG,
forming a heterotetramer with a 2:2 stoichiometry
(PubMed:21737454, PubMed:28564608). Can form a heteromeric complex
with ENG and ACVRL1 (PubMed:28564608).
{ECO:0000269|PubMed:15851468, ECO:0000269|PubMed:21710321,
ECO:0000269|PubMed:21737454, ECO:0000269|PubMed:22347366,
ECO:0000269|PubMed:22718755, ECO:0000269|PubMed:22799562,
ECO:0000269|PubMed:25751889, ECO:0000269|PubMed:28564608}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18309101,
ECO:0000269|PubMed:21710321, ECO:0000269|PubMed:25237187}.
-!- TISSUE SPECIFICITY: Detected in blood plasma (at protein level).
{ECO:0000269|PubMed:21710321}.
-!- PTM: A reversible disulfide bond can be formed between the two
subunits in the homodimer; this has no effect on GDF2 activity.
{ECO:0000269|PubMed:25237187}.
-!- DISEASE: Telangiectasia, hereditary hemorrhagic, 5 (HHT5)
[MIM:615506]: A multisystemic vascular dysplasia leading to
dilation of permanent blood vessels and arteriovenous
malformations of skin, mucosa, and viscera. The disease is
characterized by recurrent epistaxis and gastro-intestinal
hemorrhage. Visceral involvement includes arteriovenous
malformations of the lung, liver, and brain.
{ECO:0000269|PubMed:23972370}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
-!- CAUTION: Can promote osteogenic differentiation in vitro
(PubMed:25237187, PubMed:25751889). This is probably not
physiologically relevant. {ECO:0000269|PubMed:25237187,
ECO:0000269|PubMed:25751889, ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=GDF2 entry;
URL="https://en.wikipedia.org/wiki/GDF2";
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EMBL; AF188285; AAD56960.1; -; mRNA.
EMBL; AL731561; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471251; EAW50660.1; -; Genomic_DNA.
EMBL; BC069643; AAH69643.1; -; mRNA.
EMBL; BC074921; AAH74921.1; -; mRNA.
EMBL; AF156891; AAD40309.1; -; mRNA.
CCDS; CCDS73118.1; -.
RefSeq; NP_057288.1; NM_016204.3.
UniGene; Hs.279463; -.
PDB; 1ZKZ; X-ray; 2.33 A; A=320-429.
PDB; 4FAO; X-ray; 3.36 A; A/B/G/H/M/N/S/T/a/b/g/h=320-429.
PDB; 4MPL; X-ray; 1.90 A; A=321-429.
PDB; 4YCG; X-ray; 3.30 A; C/D=320-429.
PDB; 4YCI; X-ray; 3.25 A; C/D=320-429.
PDB; 5HZW; X-ray; 4.45 A; B=320-429.
PDB; 5I05; X-ray; 1.87 A; A=320-429.
PDBsum; 1ZKZ; -.
PDBsum; 4FAO; -.
PDBsum; 4MPL; -.
PDBsum; 4YCG; -.
PDBsum; 4YCI; -.
PDBsum; 5HZW; -.
PDBsum; 5I05; -.
ProteinModelPortal; Q9UK05; -.
SMR; Q9UK05; -.
BioGrid; 108928; 3.
IntAct; Q9UK05; 2.
STRING; 9606.ENSP00000249598; -.
ChEMBL; CHEMBL3831181; -.
iPTMnet; Q9UK05; -.
PhosphoSitePlus; Q9UK05; -.
BioMuta; GDF2; -.
DMDM; 13124266; -.
PaxDb; Q9UK05; -.
PeptideAtlas; Q9UK05; -.
PRIDE; Q9UK05; -.
ProteomicsDB; 84699; -.
DNASU; 2658; -.
Ensembl; ENST00000581492; ENSP00000463051; ENSG00000263761.
GeneID; 2658; -.
KEGG; hsa:2658; -.
UCSC; uc001jfa.2; human.
CTD; 2658; -.
DisGeNET; 2658; -.
EuPathDB; HostDB:ENSG00000263761.2; -.
GeneCards; GDF2; -.
HGNC; HGNC:4217; GDF2.
HPA; CAB023357; -.
MalaCards; GDF2; -.
MIM; 605120; gene.
MIM; 615506; phenotype.
neXtProt; NX_Q9UK05; -.
OpenTargets; ENSG00000263761; -.
Orphanet; 774; Hereditary hemorrhagic telangiectasia.
PharmGKB; PA28632; -.
eggNOG; KOG3900; Eukaryota.
eggNOG; ENOG410XT8Z; LUCA.
GeneTree; ENSGT00760000118883; -.
HOGENOM; HOG000249477; -.
HOVERGEN; HBG106648; -.
InParanoid; Q9UK05; -.
KO; K05503; -.
OMA; ILYKDDM; -.
OrthoDB; EOG091G075U; -.
PhylomeDB; Q9UK05; -.
TreeFam; TF316134; -.
Reactome; R-HSA-201451; Signaling by BMP.
SIGNOR; Q9UK05; -.
EvolutionaryTrace; Q9UK05; -.
GeneWiki; GDF2; -.
GenomeRNAi; 2658; -.
PRO; PR:Q9UK05; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000263761; Expressed in 59 organ(s), highest expression level in liver.
CleanEx; HS_GDF2; -.
Genevisible; Q9UK05; HS.
GO; GO:0005623; C:cell; IEA:GOC.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0005160; F:transforming growth factor beta receptor binding; IBA:GO_Central.
GO; GO:0032924; P:activin receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0001525; P:angiogenesis; IMP:UniProtKB.
GO; GO:0048514; P:blood vessel morphogenesis; IDA:DFLAT.
GO; GO:0030509; P:BMP signaling pathway; IDA:BHF-UCL.
GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IDA:DFLAT.
GO; GO:0051216; P:cartilage development; TAS:DFLAT.
GO; GO:0048468; P:cell development; IBA:GO_Central.
GO; GO:0006879; P:cellular iron ion homeostasis; TAS:DFLAT.
GO; GO:0071773; P:cellular response to BMP stimulus; IDA:BHF-UCL.
GO; GO:0016525; P:negative regulation of angiogenesis; TAS:DFLAT.
GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; TAS:DFLAT.
GO; GO:0030308; P:negative regulation of cell growth; IDA:BHF-UCL.
GO; GO:2000279; P:negative regulation of DNA biosynthetic process; IDA:BHF-UCL.
GO; GO:0008156; P:negative regulation of DNA replication; TAS:DFLAT.
GO; GO:0010596; P:negative regulation of endothelial cell migration; IDA:BHF-UCL.
GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IDA:DFLAT.
GO; GO:0001503; P:ossification; TAS:DFLAT.
GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
GO; GO:0045766; P:positive regulation of angiogenesis; IDA:DFLAT.
GO; GO:0030513; P:positive regulation of BMP signaling pathway; IEA:Ensembl.
GO; GO:0061036; P:positive regulation of cartilage development; IEA:Ensembl.
GO; GO:0045603; P:positive regulation of endothelial cell differentiation; IEA:Ensembl.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IDA:DFLAT.
GO; GO:0032757; P:positive regulation of interleukin-8 production; IDA:BHF-UCL.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
Gene3D; 2.10.90.10; -; 1.
InterPro; IPR029034; Cystine-knot_cytokine.
InterPro; IPR001839; TGF-b_C.
InterPro; IPR001111; TGF-b_propeptide.
InterPro; IPR015615; TGF-beta-rel.
InterPro; IPR017948; TGFb_CS.
PANTHER; PTHR11848; PTHR11848; 1.
Pfam; PF00019; TGF_beta; 1.
Pfam; PF00688; TGFb_propeptide; 1.
SMART; SM00204; TGFB; 1.
SUPFAM; SSF57501; SSF57501; 1.
PROSITE; PS00250; TGF_BETA_1; 1.
PROSITE; PS51362; TGF_BETA_2; 1.
1: Evidence at protein level;
3D-structure; Angiogenesis; Cleavage on pair of basic residues;
Complete proteome; Cytokine; Disease mutation; Disulfide bond;
Glycoprotein; Growth factor; Reference proteome; Secreted; Signal.
SIGNAL 1 22 {ECO:0000255}.
PROPEP 23 319 {ECO:0000250}.
/FTId=PRO_0000033902.
CHAIN 320 429 Growth/differentiation factor 2.
/FTId=PRO_0000033903.
REGION 402 416 Interaction with ENG.
{ECO:0000269|PubMed:28564608}.
CARBOHYD 71 71 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 136 136 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 327 393 {ECO:0000244|PDB:1ZKZ,
ECO:0000244|PDB:4FAO,
ECO:0000244|PDB:4MPL,
ECO:0000244|PDB:4YCG,
ECO:0000244|PDB:4YCI,
ECO:0000244|PDB:5HZW,
ECO:0000244|PDB:5I05,
ECO:0000269|PubMed:25237187}.
DISULFID 356 426 {ECO:0000244|PDB:1ZKZ,
ECO:0000244|PDB:4FAO,
ECO:0000244|PDB:4MPL,
ECO:0000244|PDB:4YCG,
ECO:0000244|PDB:4YCI,
ECO:0000244|PDB:5HZW,
ECO:0000244|PDB:5I05}.
DISULFID 360 428 {ECO:0000244|PDB:1ZKZ,
ECO:0000244|PDB:4FAO,
ECO:0000244|PDB:4MPL,
ECO:0000244|PDB:4YCG,
ECO:0000244|PDB:4YCI,
ECO:0000244|PDB:5HZW,
ECO:0000244|PDB:5I05}.
DISULFID 392 392 Interchain. {ECO:0000244|PDB:4FAO,
ECO:0000269|PubMed:25237187}.
VARIANT 68 68 R -> L (in HHT5; impaired protein
processing and function;
dbSNP:rs200330818).
{ECO:0000269|PubMed:23972370}.
/FTId=VAR_070689.
VARIANT 85 85 P -> L (in HHT5; impaired protein
processing and function;
dbSNP:rs199804679).
{ECO:0000269|PubMed:23972370}.
/FTId=VAR_070690.
VARIANT 333 333 R -> W (in HHT5; impaired protein
processing and function;
dbSNP:rs35129734).
{ECO:0000269|PubMed:23972370}.
/FTId=VAR_070691.
STRAND 326 330 {ECO:0000244|PDB:5I05}.
STRAND 333 335 {ECO:0000244|PDB:5I05}.
TURN 336 340 {ECO:0000244|PDB:5I05}.
TURN 342 344 {ECO:0000244|PDB:5I05}.
STRAND 345 347 {ECO:0000244|PDB:5I05}.
STRAND 349 352 {ECO:0000244|PDB:5I05}.
STRAND 355 359 {ECO:0000244|PDB:5I05}.
HELIX 366 368 {ECO:0000244|PDB:5I05}.
HELIX 372 383 {ECO:0000244|PDB:5I05}.
TURN 385 387 {ECO:0000244|PDB:5I05}.
STRAND 393 406 {ECO:0000244|PDB:5I05}.
STRAND 408 410 {ECO:0000244|PDB:4MPL}.
STRAND 412 428 {ECO:0000244|PDB:5I05}.
SEQUENCE 429 AA; 47320 MW; 5AC15DCA205FF086 CRC64;
MCPGALWVAL PLLSLLAGSL QGKPLQSWGR GSAGGNAHSP LGVPGGGLPE HTFNLKMFLE
NVKVDFLRSL NLSGVPSQDK TRVEPPQYMI DLYNRYTSDK STTPASNIVR SFSMEDAISI
TATEDFPFQK HILLFNISIP RHEQITRAEL RLYVSCQNHV DPSHDLKGSV VIYDVLDGTD
AWDSATETKT FLVSQDIQDE GWETLEVSSA VKRWVRSDST KSKNKLEVTV ESHRKGCDTL
DISVPPGSRN LPFFVVFSND HSSGTKETRL ELREMISHEQ ESVLKKLSKD GSTEAGESSH
EEDTDGHVAA GSTLARRKRS AGAGSHCQKT SLRVNFEDIG WDSWIIAPKE YEAYECKGGC
FFPLADDVTP TKHAIVQTLV HLKFPTKVGK ACCVPTKLSP ISVLYKDDMG VPTLKYHYEG
MSVAECGCR


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