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A disintegrin and metalloproteinase with thrombospondin motifs 4 (ADAM-TS 4) (ADAM-TS4) (ADAMTS-4) (EC 3.4.24.82) (ADMP-1) (Aggrecanase-1)

 ATS4_HUMAN              Reviewed;         837 AA.
O75173; Q2HYD0; Q5VTW2; Q6P4Q8; Q6UWA8; Q9UN83;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 3.
20-JUN-2018, entry version 187.
RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 4;
Short=ADAM-TS 4;
Short=ADAM-TS4;
Short=ADAMTS-4;
EC=3.4.24.82;
AltName: Full=ADMP-1;
AltName: Full=Aggrecanase-1;
Flags: Precursor;
Name=ADAMTS4; Synonyms=KIAA0688; ORFNames=UNQ769/PRO1563;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ARG-626.
PubMed=10356395; DOI=10.1126/science.284.5420.1664;
Tortorella M.D., Burn T.C., Pratta M.A., Abbaszade I., Hollis J.M.,
Liu R.-Q., Rosenfeld S.A., Copeland R.A., Decicco C.P., Wynn R.,
Rockwell A., Yang F., Duke J.L., Solomon K., George H., Bruckner R.,
Nagase H., Itoh Y., Ellis D.M., Ross H., Wiswall B.H., Murphy K.,
Hillman M.C. Jr., Hollis G.F., Newton R.C., Magolda R.L.,
Trzaskos J.M., Arner E.C.;
"Purification and cloning of aggrecanase-1: a member of the ADAMTS
family of proteins.";
Science 284:1664-1666(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 651-837 (ISOFORM 2), AND TISSUE
SPECIFICITY (ISOFORM 2).
TISSUE=Synovium;
PubMed=16723216; DOI=10.1016/j.matbio.2006.03.006;
Wainwright S.D., Bondeson J., Hughes C.E.;
"An alternative spliced transcript of ADAMTS4 is present in human
synovium from OA patients.";
Matrix Biol. 25:317-320(2006).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Sawaji Y., Nagase H., Saklatvala J., Clark A.R.;
"ADAMTS-4 genomic locus.";
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
THR-77 AND ARG-626.
TISSUE=Brain;
PubMed=9734811; DOI=10.1093/dnares/5.3.169;
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. X.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 5:169-176(1998).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ARG-626.
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
ILE-4; ASN-304; VAL-369; THR-552 AND ALA-564.
TISSUE=Brain;
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).
[8]
PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
PubMed=10827174; DOI=10.1074/jbc.M001065200;
Tortorella M.D., Pratta M.A., Liu R.-Q., Abbaszade I., Ross H.,
Burn T.C., Arner E.C.;
"The thrombospondin motif of aggrecanase-1 (ADAMTS-4) is critical for
aggrecan substrate recognition and cleavage.";
J. Biol. Chem. 275:25791-25797(2000).
[9]
INTERACTION WITH SRPX2.
PubMed=18718938; DOI=10.1093/hmg/ddn256;
Royer-Zemmour B., Ponsole-Lenfant M., Gara H., Roll P., Leveque C.,
Massacrier A., Ferracci G., Cillario J., Robaglia-Schlupp A.,
Vincentelli R., Cau P., Szepetowski P.;
"Epileptic and developmental disorders of the speech cortex:
ligand/receptor interaction of wild-type and mutant SRPX2 with the
plasminogen activator receptor uPAR.";
Hum. Mol. Genet. 17:3617-3630(2008).
[10]
ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY (ISOFORM 2).
PubMed=23897278; DOI=10.1002/art.38102;
Wainwright S.D., Bondeson J., Caterson B., Hughes C.E.;
"ADAMTS-4_v1 is a splice variant of ADAMTS-4 that is expressed as a
protein in human synovium and cleaves aggrecan at the interglobular
domain.";
Arthritis Rheum. 65:2866-2875(2013).
[11]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 213-520 ALONE AND IN COMPLEX
WITH INHIBITOR, ACTIVE SITE, COFACTOR, ZINC-BINDING SITES, AND
DISULFIDE BONDS.
PubMed=18042673; DOI=10.1110/ps.073287008;
Mosyak L., Georgiadis K., Shane T., Svenson K., Hebert T.,
McDonagh T., Mackie S., Olland S., Lin L., Zhong X., Kriz R.,
Reifenberg E.L., Collins-Racie L.A., Corcoran C., Freeman B.,
Zollner R., Marvell T., Vera M., Sum P.E., Lavallie E.R., Stahl M.,
Somers W.;
"Crystal structures of the two major aggrecan degrading enzymes,
ADAMTS4 and ADAMTS5.";
Protein Sci. 17:16-21(2008).
-!- FUNCTION: Cleaves aggrecan, a cartilage proteoglycan, and may be
involved in its turnover. May play an important role in the
destruction of aggrecan in arthritic diseases. Could also be a
critical factor in the exacerbation of neurodegeneration in
Alzheimer disease. Cleaves aggrecan at the '392-Glu-|-Ala-393'
site.
-!- CATALYTIC ACTIVITY: Glutamyl endopeptidase; bonds cleaved include
370-Thr-Glu-Gly-Glu-|-Ala-Arg-Gly-Ser-377 in the interglobular
domain of mammalian aggrecan.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:18042673};
Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:18042673};
-!- SUBUNIT: Interacts with SRPX2. {ECO:0000269|PubMed:18042673,
ECO:0000269|PubMed:18718938}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O75173-1; Sequence=Displayed;
Name=2; Synonyms=ADAMTS4_v1;
IsoId=O75173-2; Sequence=VSP_057293;
Note=Functional aggrecanase. {ECO:0000269|PubMed:23897278};
-!- TISSUE SPECIFICITY: Expressed in brain, lung and heart
(PubMed:23897278). Expressed at very low level in placenta and
skeletal muscles (PubMed:23897278). Isoform 2: Detected in
osteoarthritic synovium (PubMed:16723216, PubMed:23897278).
{ECO:0000269|PubMed:16723216, ECO:0000269|PubMed:23897278}.
-!- INDUCTION: By IL1/interleukin-1.
-!- DOMAIN: The spacer domain and the TSP type-1 domains are important
for a tight interaction with the extracellular matrix.
-!- DOMAIN: The conserved cysteine present in the cysteine-switch
motif binds the catalytic zinc ion, thus inhibiting the enzyme.
The dissociation of the cysteine from the zinc ion upon the
activation-peptide release activates the enzyme.
-!- PTM: The precursor is cleaved by a furin endopeptidase.
-!- PTM: Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a
threonine residue found within the consensus sequence C1-X(2)-
(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are
the first and second cysteine residue of the repeat, respectively.
Fucosylated repeats can then be further glycosylated by the
addition of a beta-1,3-glucose residue by the glucosyltransferase,
B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS
family members. Also can be C-glycosylated with one or two mannose
molecules on tryptophan residues within the consensus sequence W-
X-X-W of the TPRs, and N-glycosylated. These other glycosylations
can also facilitate secretion (By similarity). {ECO:0000250}.
-!- CAUTION: Has sometimes been referred to as ADAMTS2. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=ABC88384.1; Type=Frameshift; Positions=697; Evidence={ECO:0000305};
Sequence=BAA31663.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AF148213; AAD41494.1; -; mRNA.
EMBL; DQ364570; ABC88384.1; ALT_FRAME; mRNA.
EMBL; AY044847; AAL02262.1; -; Genomic_DNA.
EMBL; AB014588; BAA31663.2; ALT_INIT; mRNA.
EMBL; AY358886; AAQ89245.1; -; mRNA.
EMBL; AL590714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC063293; AAH63293.1; -; mRNA.
CCDS; CCDS1223.1; -. [O75173-1]
PIR; T00355; T00355.
RefSeq; NP_001307265.1; NM_001320336.1. [O75173-2]
RefSeq; NP_005090.3; NM_005099.5. [O75173-1]
UniGene; Hs.211604; -.
PDB; 2RJP; X-ray; 2.80 A; A/B/C/D=213-520.
PDB; 3B2Z; X-ray; 2.80 A; A/B/C/D/E/F/G/H=213-520.
PDB; 4WK7; X-ray; 1.24 A; A=213-439.
PDB; 4WKE; X-ray; 1.62 A; A=213-439.
PDB; 4WKI; X-ray; 1.60 A; A=213-439.
PDBsum; 2RJP; -.
PDBsum; 3B2Z; -.
PDBsum; 4WK7; -.
PDBsum; 4WKE; -.
PDBsum; 4WKI; -.
ProteinModelPortal; O75173; -.
SMR; O75173; -.
BioGrid; 114885; 29.
IntAct; O75173; 2.
STRING; 9606.ENSP00000356975; -.
BindingDB; O75173; -.
ChEMBL; CHEMBL2318; -.
DrugBank; DB06822; Tinzaparin.
GuidetoPHARMACOLOGY; 1677; -.
MEROPS; M12.221; -.
TCDB; 8.A.77.1.7; the sheddase (sheddase) family.
iPTMnet; O75173; -.
PhosphoSitePlus; O75173; -.
BioMuta; ADAMTS4; -.
EPD; O75173; -.
PaxDb; O75173; -.
PeptideAtlas; O75173; -.
PRIDE; O75173; -.
ProteomicsDB; 49841; -.
Ensembl; ENST00000367996; ENSP00000356975; ENSG00000158859. [O75173-1]
GeneID; 9507; -.
KEGG; hsa:9507; -.
UCSC; uc001fyt.5; human. [O75173-1]
CTD; 9507; -.
DisGeNET; 9507; -.
EuPathDB; HostDB:ENSG00000158859.9; -.
GeneCards; ADAMTS4; -.
H-InvDB; HIX0001237; -.
HGNC; HGNC:220; ADAMTS4.
HPA; CAB025876; -.
HPA; HPA051296; -.
HPA; HPA068374; -.
MIM; 603876; gene.
neXtProt; NX_O75173; -.
OpenTargets; ENSG00000158859; -.
PharmGKB; PA24548; -.
eggNOG; KOG3538; Eukaryota.
eggNOG; ENOG410XPKZ; LUCA.
GeneTree; ENSGT00900000140774; -.
HOGENOM; HOG000004799; -.
HOVERGEN; HBG004313; -.
InParanoid; O75173; -.
KO; K07764; -.
OMA; KFRYGYN; -.
OrthoDB; EOG091G00AX; -.
PhylomeDB; O75173; -.
TreeFam; TF331949; -.
BioCyc; MetaCyc:ENSG00000158859-MONOMER; -.
Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
Reactome; R-HSA-5083635; Defective B3GALTL causes Peters-plus syndrome (PpS).
Reactome; R-HSA-5173214; O-glycosylation of TSR domain-containing proteins.
ChiTaRS; ADAMTS4; human.
EvolutionaryTrace; O75173; -.
GeneWiki; ADAMTS4; -.
GenomeRNAi; 9507; -.
PMAP-CutDB; O75173; -.
PRO; PR:O75173; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000158859; -.
CleanEx; HS_ADAMTS4; -.
ExpressionAtlas; O75173; baseline and differential.
Genevisible; O75173; HS.
GO; GO:0031012; C:extracellular matrix; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; TAS:Reactome.
GO; GO:0008237; F:metallopeptidase activity; TAS:ProtInc.
GO; GO:0008233; F:peptidase activity; TAS:ProtInc.
GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
GO; GO:0006508; P:proteolysis; TAS:ProtInc.
GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
Gene3D; 2.20.100.10; -; 1.
Gene3D; 3.40.390.10; -; 1.
InterPro; IPR006586; ADAM_Cys-rich.
InterPro; IPR010294; ADAM_spacer1.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR001590; Peptidase_M12B.
InterPro; IPR002870; Peptidase_M12B_N.
InterPro; IPR000884; TSP1_rpt.
InterPro; IPR036383; TSP1_rpt_sf.
Pfam; PF05986; ADAM_spacer1; 1.
Pfam; PF01562; Pep_M12B_propep; 1.
Pfam; PF01421; Reprolysin; 1.
Pfam; PF00090; TSP_1; 1.
SMART; SM00608; ACR; 1.
SMART; SM00209; TSP1; 1.
SUPFAM; SSF82895; SSF82895; 1.
PROSITE; PS50215; ADAM_MEPRO; 1.
PROSITE; PS50092; TSP1; 1.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing;
Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Disulfide bond; Extracellular matrix;
Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Polymorphism;
Protease; Reference proteome; Secreted; Signal; Zinc; Zymogen.
SIGNAL 1 51 {ECO:0000255}.
PROPEP 52 212
/FTId=PRO_0000029164.
CHAIN 213 837 A disintegrin and metalloproteinase with
thrombospondin motifs 4.
/FTId=PRO_0000029165.
DOMAIN 218 428 Peptidase M12B. {ECO:0000255|PROSITE-
ProRule:PRU00276}.
DOMAIN 437 519 Disintegrin.
DOMAIN 520 575 TSP type-1. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
REGION 686 837 Spacer.
MOTIF 192 199 Cysteine switch. {ECO:0000250}.
COMPBIAS 247 252 Poly-Ala.
COMPBIAS 577 685 Cys-rich.
ACT_SITE 362 362 {ECO:0000255|PROSITE-ProRule:PRU00276,
ECO:0000255|PROSITE-ProRule:PRU10095,
ECO:0000269|PubMed:18042673}.
METAL 194 194 Zinc; in inhibited form. {ECO:0000250}.
METAL 361 361 Zinc; catalytic.
{ECO:0000269|PubMed:18042673}.
METAL 365 365 Zinc; catalytic.
{ECO:0000269|PubMed:18042673}.
METAL 371 371 Zinc; catalytic.
{ECO:0000269|PubMed:18042673}.
CARBOHYD 68 68 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 293 345 {ECO:0000269|PubMed:18042673}.
DISULFID 322 327 {ECO:0000269|PubMed:18042673}.
DISULFID 339 423 {ECO:0000269|PubMed:18042673}.
DISULFID 377 407 {ECO:0000269|PubMed:18042673}.
DISULFID 449 472 {ECO:0000269|PubMed:18042673}.
DISULFID 460 482 {ECO:0000269|PubMed:18042673}.
DISULFID 467 501 {ECO:0000269|PubMed:18042673}.
DISULFID 495 506 {ECO:0000269|PubMed:18042673}.
DISULFID 532 569 {ECO:0000250}.
DISULFID 536 574 {ECO:0000250}.
DISULFID 547 559 {ECO:0000250}.
VAR_SEQ 697 837 YGYNNVVTIPAGATHILVRQQGNPGHRSIYLALKLPDGSYA
LNGEYTLMPSPTDVVLPGAVSLRYSGATAASETLSGHGPLA
QPLTLQVLVAGNPQDTRLRYSFFVPRPTPSTPRPTPQDWLH
RRAQILEILRRRPWAGRK -> CGTAWGSQLALQRGHCSLR
DTVRPWATGPAFDTASPSGWQPPGHTPPIQLLRAPADPFNA
TPHSPGLAAPKSTDSGDPSAAPLGGQEITSLSRLPFLGTGA
SDLAGRKRELLLLPHAKTQWGGAVGVRPAPPLCPNAQAGPA
LVSCPGRQ (in isoform 2).
{ECO:0000303|PubMed:16723216}.
/FTId=VSP_057293.
VARIANT 4 4 T -> I (in dbSNP:rs17855814).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_030636.
VARIANT 77 77 A -> T (in dbSNP:rs34448954).
{ECO:0000269|PubMed:9734811}.
/FTId=VAR_057073.
VARIANT 304 304 D -> N (in dbSNP:rs17855813).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_030637.
VARIANT 369 369 M -> V (in dbSNP:rs17855812).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_030638.
VARIANT 552 552 P -> T (in dbSNP:rs17855815).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_030639.
VARIANT 564 564 T -> A (in dbSNP:rs17855816).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_030640.
VARIANT 626 626 Q -> R (in dbSNP:rs4233367).
{ECO:0000269|PubMed:10356395,
ECO:0000269|PubMed:12975309,
ECO:0000269|PubMed:9734811}.
/FTId=VAR_022450.
VARIANT 836 836 R -> K (in dbSNP:rs11807350).
/FTId=VAR_030641.
CONFLICT 306 306 D -> G (in Ref. 5; AAQ89245).
{ECO:0000305}.
CONFLICT 682 682 G -> R (in Ref. 3; AAL02262).
{ECO:0000305}.
STRAND 219 226 {ECO:0000244|PDB:4WK7}.
HELIX 228 234 {ECO:0000244|PDB:4WK7}.
HELIX 235 237 {ECO:0000244|PDB:4WK7}.
HELIX 238 254 {ECO:0000244|PDB:4WK7}.
HELIX 256 258 {ECO:0000244|PDB:4WK7}.
STRAND 263 271 {ECO:0000244|PDB:4WK7}.
STRAND 274 276 {ECO:0000244|PDB:3B2Z}.
HELIX 285 297 {ECO:0000244|PDB:4WK7}.
STRAND 304 306 {ECO:0000244|PDB:2RJP}.
STRAND 311 317 {ECO:0000244|PDB:4WK7}.
TURN 322 324 {ECO:0000244|PDB:3B2Z}.
STRAND 331 333 {ECO:0000244|PDB:4WK7}.
TURN 341 343 {ECO:0000244|PDB:4WK7}.
STRAND 345 349 {ECO:0000244|PDB:4WK7}.
STRAND 352 354 {ECO:0000244|PDB:4WK7}.
HELIX 355 366 {ECO:0000244|PDB:4WK7}.
HELIX 375 381 {ECO:0000244|PDB:4WK7}.
STRAND 392 394 {ECO:0000244|PDB:4WK7}.
HELIX 406 417 {ECO:0000244|PDB:4WK7}.
TURN 418 423 {ECO:0000244|PDB:4WK7}.
HELIX 439 442 {ECO:0000244|PDB:2RJP}.
HELIX 445 453 {ECO:0000244|PDB:2RJP}.
STRAND 463 465 {ECO:0000244|PDB:3B2Z}.
TURN 466 468 {ECO:0000244|PDB:3B2Z}.
STRAND 472 476 {ECO:0000244|PDB:2RJP}.
STRAND 479 483 {ECO:0000244|PDB:2RJP}.
STRAND 494 496 {ECO:0000244|PDB:2RJP}.
STRAND 499 502 {ECO:0000244|PDB:2RJP}.
STRAND 505 507 {ECO:0000244|PDB:2RJP}.
SEQUENCE 837 AA; 90197 MW; 0C05299D7FB23A8D CRC64;
MSQTGSHPGR GLAGRWLWGA QPCLLLPIVP LSWLVWLLLL LLASLLPSAR LASPLPREEE
IVFPEKLNGS VLPGSGAPAR LLCRLQAFGE TLLLELEQDS GVQVEGLTVQ YLGQAPELLG
GAEPGTYLTG TINGDPESVA SLHWDGGALL GVLQYRGAEL HLQPLEGGTP NSAGGPGAHI
LRRKSPASGQ GPMCNVKAPL GSPSPRPRRA KRFASLSRFV ETLVVADDKM AAFHGAGLKR
YLLTVMAAAA KAFKHPSIRN PVSLVVTRLV ILGSGEEGPQ VGPSAAQTLR SFCAWQRGLN
TPEDSDPDHF DTAILFTRQD LCGVSTCDTL GMADVGTVCD PARSCAIVED DGLQSAFTAA
HELGHVFNML HDNSKPCISL NGPLSTSRHV MAPVMAHVDP EEPWSPCSAR FITDFLDNGY
GHCLLDKPEA PLHLPVTFPG KDYDADRQCQ LTFGPDSRHC PQLPPPCAAL WCSGHLNGHA
MCQTKHSPWA DGTPCGPAQA CMGGRCLHMD QLQDFNIPQA GGWGPWGPWG DCSRTCGGGV
QFSSRDCTRP VPRNGGKYCE GRRTRFRSCN TEDCPTGSAL TFREEQCAAY NHRTDLFKSF
PGPMDWVPRY TGVAPQDQCK LTCQAQALGY YYVLEPRVVD GTPCSPDSSS VCVQGRCIHA
GCDRIIGSKK KFDKCMVCGG DGSGCSKQSG SFRKFRYGYN NVVTIPAGAT HILVRQQGNP
GHRSIYLALK LPDGSYALNG EYTLMPSPTD VVLPGAVSLR YSGATAASET LSGHGPLAQP
LTLQVLVAGN PQDTRLRYSF FVPRPTPSTP RPTPQDWLHR RAQILEILRR RPWAGRK


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