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Phosphate-regulating neutral endopeptidase (EC 3.4.24.-) (Metalloendopeptidase homolog PEX) (Vitamin D-resistant hypophosphatemic rickets protein) (X-linked hypophosphatemia protein) (HYP)

 PHEX_HUMAN              Reviewed;         749 AA.
P78562; O00678; Q13646; Q2M325; Q93032; Q99827;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
20-JUN-2018, entry version 173.
RecName: Full=Phosphate-regulating neutral endopeptidase;
EC=3.4.24.-;
AltName: Full=Metalloendopeptidase homolog PEX;
AltName: Full=Vitamin D-resistant hypophosphatemic rickets protein;
AltName: Full=X-linked hypophosphatemia protein;
Short=HYP;
Name=PHEX; Synonyms=PEX;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS XLHR ARG-85; LEU-534;
ARG-579 AND PRO-651.
PubMed=9199930;
Francis F., Strom T.M., Hennig S., Boeddrich A., Lorenz B.,
Brandau O., Mohnike K.L., Cagnoli M., Steffens C., Klages S.,
Borzym K., Pohl T., Oudet C.L., Econs M.J., Rowe P.S.N., Reinhardt R.,
Meitinger T., Lehrach H.;
"Genomic organization of the human PEX gene mutated in X-linked
dominant hypophosphatemic rickets.";
Genome Res. 7:573-585(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9077527; DOI=10.1172/JCI119276;
Beck L., Soumounou Y., Martel J., Krishnamurthy G., Gauthier C.,
Goodyer C.G., Tenenhouse H.S.;
"Pex/PEX tissue distribution and evidence for a deletion in the 3'
region of the Pex gene in X-linked hypophosphatemic mice.";
J. Clin. Invest. 99:1200-1209(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Bone;
PubMed=9199999; DOI=10.1359/jbmr.1997.12.7.1009;
Guo R., Quarles L.D.;
"Cloning and sequencing of human PEX from a bone cDNA library:
evidence for its developmental stage-specific regulation in
osteoblasts.";
J. Bone Miner. Res. 12:1009-1017(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9070861; DOI=10.1006/bbrc.1997.6153;
Grieff M., Mumm S., Waeltz P., Mazzarella R., Whyte M.P.,
Thakker R.V., Schlessinger D.;
"Expression and cloning of the human X-linked hypophosphatemia gene
cDNA.";
Biochem. Biophys. Res. Commun. 231:635-639(1997).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS XLHR TYR-85; CYS-166;
SER-252; ILE-253 AND VAL-579.
PubMed=9106524;
Holm I.A., Huang X., Kunkel L.M.;
"Mutational analysis of the PEX gene in patients with X-linked
hypophosphatemic rickets.";
Am. J. Hum. Genet. 60:790-797(1997).
[6]
NUCLEOTIDE SEQUENCE [MRNA].
Lipman M.L., Panda D., Henderson J.E., Shen Y., Goltzman D.,
Karaplis A.C.;
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 4-641.
PubMed=7550339;
The HYP consortium;
Francis F., Hennig S., Korn B., Reinhardt R., de Jong P., Poustka A.,
Lehrach H., Rowe P.S.N., Goulding J.N., Summerfield T., Mountford R.,
Read A.P., Popowska E., Pronicka E., Davies K.E., Oriordan J.L.H.,
Econs M.J., Nesbitt T., Drezner M.K., Oudet C.L., Pannetier S.,
Hanauer A., Strom T.M., Meindl A., Lorenz B., Cagnoli M.,
Mohnike K.L., Murken J., Meitinger T.;
"A gene (PEX) with homologies to endopeptidases is mutated in patients
with X-linked hypophosphatemic rickets.";
Nat. Genet. 11:130-136(1995).
[10]
VARIANTS XLHR SER-77; PRO-138; LEU-534 AND ARG-579.
PubMed=9097956; DOI=10.1093/hmg/6.4.539;
Rowe P.S.N., Oudet C.L., Francis F., Sinding C., Pannetier S.,
Econs M.J., Strom T.M., Meitinger T., Garabedian M., David A.,
Macher M.-A., Questiaux E., Popowska E., Pronicka E., Read A.P.,
Mokrzycki A., Glorieux F.H., Drezner M.K., Hanauer A., Lehrach H.,
Goulding J.N., O'Riordan J.L.H.;
"Distribution of mutations in the PEX gene in families with X-linked
hypophosphataemic rickets (HYP).";
Hum. Mol. Genet. 6:539-549(1997).
[11]
VARIANT XLHR PRO-555.
PubMed=9768646; DOI=10.1210/jcem.83.10.5167;
Econs M.J., Friedman N.E., Rowe P.S.N., Speer M.C., Francis F.,
Strom T.M., Oudet C.L., Smith J.A., Ninomiya J.T., Lee B.E.,
Bergen H.;
"A PHEX gene mutation is responsible for adult-onset vitamin D-
resistant hypophosphatemic osteomalacia: evidence that the disorder is
not a distinct entity from X-linked hypophosphatemic rickets.";
J. Clin. Endocrinol. Metab. 83:3459-3462(1998).
[12]
VARIANTS XLHR PHE-317; LEU-534; ARG-579; ARG-621; ASN-680 DEL;
THR-720; TYR-731 AND ARG-749.
PubMed=9768674; DOI=10.1210/jcem.83.10.5180;
Dixon P.H., Christie P.T., Wooding C., Trump D., Grieff M., Holm I.A.,
Gertner J.M., Schmidtke J., Shah B., Shaw N., Smith C., Tau C.,
Schlessinger D., Whyte M.P., Thakker R.V.;
"Mutational analysis of PHEX gene in X-linked hypophosphatemia.";
J. Clin. Endocrinol. Metab. 83:3615-3623(1998).
[13]
VARIANTS XLHR SER-80; PHE-142; GLY-237; CYS-530; ASP-573; SER-733 AND
TRP-746.
PubMed=10439971; DOI=10.1038/sj.ejhg.5200341;
Filisetti D., Ostermann G., von Bredow M., Strom T.M., Filler G.,
Ehrich J., Pannetier S., Garnier J.-M., Rowe P.S.N., Francis F.,
Julienne A., Hanauer A., Econs M.J., Oudet C.L.;
"Non-random distribution of mutations in the PHEX gene, and under-
detected missense mutations at non-conserved residues.";
Eur. J. Hum. Genet. 7:615-619(1999).
[14]
VARIANTS XLHR PHE-85; PRO-141; VAL-341 DEL; PRO-567; LYS-680 AND
TYR-693.
PubMed=10737991;
DOI=10.1002/(SICI)1098-1004(200004)15:4<383::AID-HUMU18>3.0.CO;2-#;
Tyynismaa H., Kaitila I., Naentoe-Salonen K., Ala-Houhala M.,
Alitalo T.;
"Identification of fifteen novel PHEX gene mutations in Finnish
patients with hypophosphatemic rickets.";
Hum. Mutat. 15:383-384(2000).
[15]
VARIANTS XLHR ARG-160 AND ASN-444 INS.
PubMed=11004247; DOI=10.1203/00006450-200010000-00019;
Sato K., Tajima T., Nakae J., Adachi M., Asakura Y., Tachibana K.,
Suwa S., Katsumata N., Tanaka T., Hayashi Y., Abe S., Murashita M.,
Okuhara K., Shinohara N., Fujieda K.;
"Three novel PHEX gene mutations in Japanese patients with X-linked
hypophosphatemic rickets.";
Pediatr. Res. 48:536-540(2000).
-!- FUNCTION: Probably involved in bone and dentin mineralization and
renal phosphate reabsorption.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
membrane protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Lymphocytes and fetal brain; not in adult
brain, placenta, skeletal muscle and pancreas; not in adult and
fetal heart, lung, liver and kidney.
-!- DISEASE: Hypophosphatemic rickets, X-linked dominant (XLHR)
[MIM:307800]: A disorder characterized by impaired phosphate
uptake in the kidney, which is likely to be caused by abnormal
regulation of sodium phosphate cotransport in the proximal
tubules. Clinical manifestations include skeletal deformities,
growth failure, craniosynostosis, paravertebral calcifications,
pseudofractures in lower extremities, and muscular hypotonia with
onset in early childhood. X-linked hypophosphatemic rickets is the
most common form of hypophosphatemia with an incidence of 1 in
20000. {ECO:0000269|PubMed:10439971, ECO:0000269|PubMed:10737991,
ECO:0000269|PubMed:11004247, ECO:0000269|PubMed:9097956,
ECO:0000269|PubMed:9106524, ECO:0000269|PubMed:9199930,
ECO:0000269|PubMed:9768646, ECO:0000269|PubMed:9768674}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the peptidase M13 family. {ECO:0000305}.
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EMBL; Y08111; CAA69326.1; -; Genomic_DNA.
EMBL; Y08112; CAA69326.1; JOINED; Genomic_DNA.
EMBL; Y08113; CAA69326.1; JOINED; Genomic_DNA.
EMBL; Y08114; CAA69326.1; JOINED; Genomic_DNA.
EMBL; Y08115; CAA69326.1; JOINED; Genomic_DNA.
EMBL; Y08116; CAA69326.1; JOINED; Genomic_DNA.
EMBL; Y08117; CAA69326.1; JOINED; Genomic_DNA.
EMBL; Y08118; CAA69326.1; JOINED; Genomic_DNA.
EMBL; Y08119; CAA69326.1; JOINED; Genomic_DNA.
EMBL; Y08120; CAA69326.1; JOINED; Genomic_DNA.
EMBL; Y08121; CAA69326.1; JOINED; Genomic_DNA.
EMBL; Y08122; CAA69326.1; JOINED; Genomic_DNA.
EMBL; Y08123; CAA69326.1; JOINED; Genomic_DNA.
EMBL; Y08124; CAA69326.1; JOINED; Genomic_DNA.
EMBL; Y08125; CAA69326.1; JOINED; Genomic_DNA.
EMBL; Y08126; CAA69326.1; JOINED; Genomic_DNA.
EMBL; Y08127; CAA69326.1; JOINED; Genomic_DNA.
EMBL; Y08128; CAA69326.1; JOINED; Genomic_DNA.
EMBL; Y08129; CAA69326.1; JOINED; Genomic_DNA.
EMBL; Y08130; CAA69326.1; JOINED; Genomic_DNA.
EMBL; Y08131; CAA69326.1; JOINED; Genomic_DNA.
EMBL; Y08132; CAA69326.1; JOINED; Genomic_DNA.
EMBL; U75645; AAB47749.1; -; mRNA.
EMBL; U87284; AAB47562.1; -; mRNA.
EMBL; AD000712; AAB51604.1; -; mRNA.
EMBL; AH004966; AAB42219.1; -; Genomic_DNA.
EMBL; U82970; AAC24487.1; -; mRNA.
EMBL; U73024; AAD08630.1; -; Genomic_DNA.
EMBL; Y10196; CAA71258.1; -; Genomic_DNA.
EMBL; BC105057; AAI05058.1; -; mRNA.
EMBL; BC105059; AAI05060.1; -; mRNA.
EMBL; U60475; AAC50552.1; -; mRNA.
CCDS; CCDS14204.1; -.
RefSeq; NP_000435.3; NM_000444.5.
RefSeq; NP_001269683.1; NM_001282754.1.
UniGene; Hs.495834; -.
ProteinModelPortal; P78562; -.
SMR; P78562; -.
BioGrid; 111270; 2.
IntAct; P78562; 1.
STRING; 9606.ENSP00000368682; -.
MEROPS; M13.091; -.
iPTMnet; P78562; -.
PhosphoSitePlus; P78562; -.
DMDM; 2499917; -.
EPD; P78562; -.
PaxDb; P78562; -.
PeptideAtlas; P78562; -.
PRIDE; P78562; -.
ProteomicsDB; 57655; -.
Ensembl; ENST00000379374; ENSP00000368682; ENSG00000102174.
GeneID; 5251; -.
KEGG; hsa:5251; -.
UCSC; uc004dah.5; human.
CTD; 5251; -.
DisGeNET; 5251; -.
EuPathDB; HostDB:ENSG00000102174.8; -.
GeneCards; PHEX; -.
GeneReviews; PHEX; -.
HGNC; HGNC:8918; PHEX.
MalaCards; PHEX; -.
MIM; 300550; gene.
MIM; 307800; phenotype.
neXtProt; NX_P78562; -.
OpenTargets; ENSG00000102174; -.
Orphanet; 89936; X-linked hypophosphatemia.
PharmGKB; PA33258; -.
eggNOG; KOG3624; Eukaryota.
eggNOG; COG3590; LUCA.
GeneTree; ENSGT00760000119162; -.
HOGENOM; HOG000245574; -.
HOVERGEN; HBG005554; -.
InParanoid; P78562; -.
KO; K08636; -.
OMA; VPKTEWF; -.
OrthoDB; EOG091G025Y; -.
PhylomeDB; P78562; -.
TreeFam; TF315192; -.
BRENDA; 3.4.24.B15; 2681.
ChiTaRS; PHEX; human.
GeneWiki; PHEX; -.
GenomeRNAi; 5251; -.
PRO; PR:P78562; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000102174; -.
CleanEx; HS_PHEX; -.
Genevisible; P78562; HS.
GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; TAS:ProtInc.
GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
GO; GO:0060348; P:bone development; IEA:Ensembl.
GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:0006464; P:cellular protein modification process; TAS:ProtInc.
GO; GO:0071374; P:cellular response to parathyroid hormone stimulus; IEA:Ensembl.
GO; GO:0071305; P:cellular response to vitamin D; IEA:Ensembl.
GO; GO:0030324; P:lung development; IEA:Ensembl.
GO; GO:0019637; P:organophosphate metabolic process; IEA:Ensembl.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
GO; GO:0060416; P:response to growth hormone; IEA:Ensembl.
GO; GO:1990418; P:response to insulin-like growth factor stimulus; IEA:Ensembl.
GO; GO:1904383; P:response to sodium phosphate; IEA:Ensembl.
GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
CDD; cd08662; M13; 1.
Gene3D; 3.40.390.10; -; 3.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR000718; Peptidase_M13.
InterPro; IPR018497; Peptidase_M13_C.
InterPro; IPR008753; Peptidase_M13_N.
PANTHER; PTHR11733; PTHR11733; 1.
Pfam; PF01431; Peptidase_M13; 1.
Pfam; PF05649; Peptidase_M13_N; 1.
PRINTS; PR00786; NEPRILYSIN.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
Aminopeptidase; Biomineralization; Complete proteome;
Disease mutation; Glycoprotein; Hydrolase; Membrane; Metal-binding;
Metalloprotease; Protease; Reference proteome; Signal-anchor;
Transmembrane; Transmembrane helix; Zinc.
CHAIN 1 749 Phosphate-regulating neutral
endopeptidase.
/FTId=PRO_0000078228.
TOPO_DOM 1 20 Cytoplasmic. {ECO:0000255}.
TRANSMEM 21 41 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 42 641 Extracellular. {ECO:0000255}.
ACT_SITE 581 581 {ECO:0000255|PROSITE-ProRule:PRU10095}.
ACT_SITE 646 646 Proton donor. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 580 580 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 584 584 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 642 642 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
CARBOHYD 71 71 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 238 238 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 263 263 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 290 290 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 301 301 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 377 377 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 484 484 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 736 736 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 77 77 C -> S (in XLHR).
{ECO:0000269|PubMed:9097956}.
/FTId=VAR_006738.
VARIANT 80 80 F -> S (in XLHR; sporadic).
{ECO:0000269|PubMed:10439971}.
/FTId=VAR_010616.
VARIANT 85 85 C -> F (in XLHR; sporadic).
{ECO:0000269|PubMed:10737991}.
/FTId=VAR_010617.
VARIANT 85 85 C -> R (in XLHR).
{ECO:0000269|PubMed:9199930}.
/FTId=VAR_010618.
VARIANT 85 85 C -> Y (in XLHR; dbSNP:rs137853269).
{ECO:0000269|PubMed:9106524}.
/FTId=VAR_006739.
VARIANT 138 138 L -> P (in XLHR).
{ECO:0000269|PubMed:9097956}.
/FTId=VAR_006740.
VARIANT 141 141 S -> P (in XLHR; sporadic).
{ECO:0000269|PubMed:10737991}.
/FTId=VAR_010619.
VARIANT 142 142 C -> F (in XLHR).
{ECO:0000269|PubMed:10439971}.
/FTId=VAR_010620.
VARIANT 160 160 L -> R (in XLHR).
{ECO:0000269|PubMed:11004247}.
/FTId=VAR_010621.
VARIANT 166 166 R -> C (in XLHR; dbSNP:rs751230094).
{ECO:0000269|PubMed:9106524}.
/FTId=VAR_006741.
VARIANT 237 237 D -> G (in XLHR; sporadic).
{ECO:0000269|PubMed:10439971}.
/FTId=VAR_010622.
VARIANT 252 252 F -> S (in XLHR; dbSNP:rs267606945).
{ECO:0000269|PubMed:9106524}.
/FTId=VAR_006742.
VARIANT 253 253 M -> I (in XLHR; dbSNP:rs267606946).
{ECO:0000269|PubMed:9106524}.
/FTId=VAR_006743.
VARIANT 317 317 Y -> F (in XLHR).
{ECO:0000269|PubMed:9768674}.
/FTId=VAR_010623.
VARIANT 341 341 Missing (in XLHR; sporadic).
{ECO:0000269|PubMed:10737991}.
/FTId=VAR_010624.
VARIANT 444 444 W -> WN (in XLHR).
{ECO:0000269|PubMed:11004247}.
/FTId=VAR_010625.
VARIANT 530 530 W -> C (in XLHR).
{ECO:0000269|PubMed:10439971}.
/FTId=VAR_010626.
VARIANT 534 534 P -> L (in XLHR; dbSNP:rs886041363).
{ECO:0000269|PubMed:9097956,
ECO:0000269|PubMed:9199930,
ECO:0000269|PubMed:9768674}.
/FTId=VAR_006744.
VARIANT 555 555 L -> P (in XLHR; dbSNP:rs137853270).
{ECO:0000269|PubMed:9768646}.
/FTId=VAR_010627.
VARIANT 567 567 R -> P (in XLHR; sporadic;
dbSNP:rs760870713).
{ECO:0000269|PubMed:10737991}.
/FTId=VAR_010628.
VARIANT 573 573 A -> D (in XLHR; sporadic).
{ECO:0000269|PubMed:10439971}.
/FTId=VAR_010629.
VARIANT 579 579 G -> R (in XLHR; dbSNP:rs875989883).
{ECO:0000269|PubMed:9097956,
ECO:0000269|PubMed:9199930,
ECO:0000269|PubMed:9768674}.
/FTId=VAR_006745.
VARIANT 579 579 G -> V (in XLHR; dbSNP:rs1057517980).
{ECO:0000269|PubMed:9106524}.
/FTId=VAR_006746.
VARIANT 621 621 Q -> R (in XLHR).
{ECO:0000269|PubMed:9768674}.
/FTId=VAR_010630.
VARIANT 651 651 R -> P (in XLHR).
{ECO:0000269|PubMed:9199930}.
/FTId=VAR_010631.
VARIANT 680 680 N -> K (in XLHR; sporadic).
{ECO:0000269|PubMed:10737991}.
/FTId=VAR_010633.
VARIANT 680 680 Missing (in XLHR).
{ECO:0000269|PubMed:9768674}.
/FTId=VAR_010632.
VARIANT 693 693 C -> Y (in XLHR; sporadic).
{ECO:0000269|PubMed:10737991}.
/FTId=VAR_010634.
VARIANT 720 720 A -> T (in XLHR).
{ECO:0000269|PubMed:9768674}.
/FTId=VAR_010635.
VARIANT 731 731 F -> Y (in XLHR).
{ECO:0000269|PubMed:9768674}.
/FTId=VAR_010636.
VARIANT 733 733 C -> S (in XLHR; sporadic).
{ECO:0000269|PubMed:10439971}.
/FTId=VAR_010637.
VARIANT 746 746 C -> W (in XLHR; sporadic).
{ECO:0000269|PubMed:10439971}.
/FTId=VAR_010638.
VARIANT 749 749 W -> R (in XLHR).
{ECO:0000269|PubMed:9768674}.
/FTId=VAR_010639.
CONFLICT 363 363 A -> D (in Ref. 9; AAC50552).
{ECO:0000305}.
CONFLICT 403 403 W -> R (in Ref. 9; AAC50552).
{ECO:0000305}.
CONFLICT 641 641 G -> A (in Ref. 9; AAC50552).
{ECO:0000305}.
SEQUENCE 749 AA; 86474 MW; 7C4F9F3E2471C6A8 CRC64;
MEAETGSSVE TGKKANRGTR IALVVFVGGT LVLGTILFLV SQGLLSLQAK QEYCLKPECI
EAAAAILSKV NLSVDPCDNF FRFACDGWIS NNPIPEDMPS YGVYPWLRHN VDLKLKELLE
KSISRRRDTE AIQKAKILYS SCMNEKAIEK ADAKPLLHIL RHSPFRWPVL ESNIGPEGVW
SERKFSLLQT LATFRGQYSN SVFIRLYVSP DDKASNEHIL KLDQATLSLA VREDYLDNST
EAKSYRDALY KFMVDTAVLL GANSSRAEHD MKSVLRLEIK IAEIMIPHEN RTSEAMYNKM
NISELSAMIP QFDWLGYIKK VIDTRLYPHL KDISPSENVV VRVPQYFKDL FRILGSERKK
TIANYLVWRM VYSRIPNLSR RFQYRWLEFS RVIQGTTTLL PQWDKCVNFI ESALPYVVGK
MFVDVYFQED KKEMMEELVE GVRWAFIDML EKENEWMDAG TKRKAKEKAR AVLAKVGYPE
FIMNDTHVNE DLKAIKFSEA DYFGNVLQTR KYLAQSDFFW LRKAVPKTEW FTNPTTVNAF
YSASTNQIRF PAGELQKPFF WGTEYPRSLS YGAIGVIVGH EFTHGFDNNG RKYDKNGNLD
PWWSTESEEK FKEKTKCMIN QYSNYYWKKA GLNVKGKRTL GENIADNGGL REAFRAYRKW
INDRRQGLEE PLLPGITFTN NQLFFLSYAH VRCNSYRPEA AREQVQIGAH SPPQFRVNGA
ISNFEEFQKA FNCPPNSTMN RGMDSCRLW


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