GenomeNet

Database: UniProt
Entry: BMP15_HUMAN
LinkDB: BMP15_HUMAN
Original site: BMP15_HUMAN 
ID   BMP15_HUMAN             Reviewed;         392 AA.
AC   O95972; Q17RM6; Q5JST1; Q9UMS1;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   16-JAN-2019, entry version 156.
DE   RecName: Full=Bone morphogenetic protein 15;
DE            Short=BMP-15;
DE   AltName: Full=Growth/differentiation factor 9B;
DE            Short=GDF-9B;
DE   Flags: Precursor;
GN   Name=BMP15; Synonyms=GDF9B;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-103.
RX   PubMed=9849956; DOI=10.1210/mend.12.12.0206;
RA   Dube J.L., Wang P., Elvin J., Lyons K.M., Celeste A.J., Matzuk M.M.;
RT   "The bone morphogenetic protein 15 gene is X-linked and expressed in
RT   oocytes.";
RL   Mol. Endocrinol. 12:1809-1817(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10443672; DOI=10.1210/jcem.84.8.5921;
RA   Aaltonen J., Laitinen M.P., Vuojolainen K., Jaatinen R.,
RA   Horelli-Kuitunen N., Seppae L., Louhio H., Tuuri T., Sjoeberg J.,
RA   Buetzow R., Hovatta O., Dale L., Ritvos O.;
RT   "Human growth differentiation factor 9 (GDF-9) and its novel homolog
RT   GDF-9B are expressed in oocytes during early folliculogenesis.";
RL   J. Clin. Endocrinol. Metab. 84:2744-2750(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA   Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA   Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA   Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA   Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA   Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA   Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA   Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA   Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA   Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA   Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA   Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA   Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA   Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA   Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA   Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA   Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA   Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA   Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA   Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA   Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA   Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA   Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA   Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA   de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA   Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA   Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA   Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA   Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA   Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA   Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA   Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA   Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA   Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA   Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA   Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA   Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA   Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA   Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA   Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA   Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA   Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA   Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA   Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION, PYROGLUTAMATE FORMATION AT GLN-268, PHOSPHORYLATION AT
RP   SER-273, GLYCOSYLATION AT THR-277, AND HOMODIMERIZATION.
RX   PubMed=18227435; DOI=10.1110/ps.073232608;
RA   Saito S., Yano K., Sharma S., McMahon H.E., Shimasaki S.;
RT   "Characterization of the post-translational modification of
RT   recombinant human BMP-15 mature protein.";
RL   Protein Sci. 17:362-370(2008).
RN   [6]
RP   SPECIES-SPECIFIC OVULATION RATE DETERMINATION.
RX   PubMed=21970812; DOI=10.1016/j.mce.2011.09.033;
RA   Crawford J.L., McNatty K.P.;
RT   "The ratio of growth differentiation factor 9: bone morphogenetic
RT   protein 15 mRNA expression is tightly co-regulated and differs between
RT   species over a wide range of ovulation rates.";
RL   Mol. Cell. Endocrinol. 348:339-343(2012).
RN   [7]
RP   VARIANT ODG2 CYS-235, AND CHARACTERIZATION OF VARIANT ODG2 CYS-235.
RX   PubMed=15136966; DOI=10.1086/422103;
RA   Di Pasquale E., Beck-Peccoz P., Persani L.;
RT   "Hypergonadotropic ovarian failure associated with an inherited
RT   mutation of human bone morphogenetic protein-15 (BMP15) gene.";
RL   Am. J. Hum. Genet. 75:106-111(2004).
RN   [8]
RP   VARIANTS POF4 PRO-148 AND THR-180, AND VARIANT LEU-263 INS.
RX   PubMed=16645022; DOI=10.1530/eje.1.02135;
RA   Laissue P., Christin-Maitre S., Touraine P., Kuttenn F., Ritvos O.,
RA   Aittomaki K., Bourcigaux N., Jacquesson L., Bouchard P., Frydman R.,
RA   Dewailly D., Reyss A.-C., Jeffery L., Bachelot A., Massin N.,
RA   Fellous M., Veitia R.A.;
RT   "Mutations and sequence variants in GDF9 and BMP15 in patients with
RT   premature ovarian failure.";
RL   Eur. J. Endocrinol. 154:739-744(2006).
RN   [9]
RP   VARIANTS POF4 TRP-61; GLN-61; CYS-76; HIS-76; THR-180; LYS-196;
RP   HIS-206; ARG-221 AND VAL-243, AND VARIANTS SER-103; PHE-180 AND
RP   LEU-263 INS.
RX   PubMed=16508750; DOI=10.1007/s00439-006-0150-0;
RA   Dixit H., Rao L.K., Padmalatha V.V., Kanakavalli M., Deenadayal M.,
RA   Gupta N., Chakrabarty B., Singh L.;
RT   "Missense mutations in the BMP15 gene are associated with ovarian
RT   failure.";
RL   Hum. Genet. 119:408-415(2006).
RN   [10]
RP   VARIANTS POF4 TRP-68; THR-180 AND CYS-235, AND VARIANT LEU-263 INS.
RX   PubMed=16464940; DOI=10.1210/jc.2005-2650;
RA   Di Pasquale E., Rossetti R., Marozzi A., Bodega B., Borgato S.,
RA   Cavallo L., Einaudi S., Radetti G., Russo G., Sacco M., Wasniewska M.,
RA   Cole T., Beck-Peccoz P., Nelson L.M., Persani L.;
RT   "Identification of new variants of human BMP15 gene in a large cohort
RT   of women with premature ovarian failure.";
RL   J. Clin. Endocrinol. Metab. 91:1976-1979(2006).
RN   [11]
RP   VARIANTS POF4 TRP-68; HIS-138; PRO-148 AND THR-180, VARIANTS ARG-5 AND
RP   LEU-263 INS, CHARACTERIZATION OF VARIANTS POF4 TRP-68; HIS-138;
RP   PRO-148 AND THR-180, AND CHARACTERIZATION OF VARIANTS ARG-5 AND
RP   LEU-263 INS.
RX   PubMed=19263482; DOI=10.1002/humu.20961;
RA   Rossetti R., Di Pasquale E., Marozzi A., Bione S., Toniolo D.,
RA   Grammatico P., Nelson L.M., Beck-Peccoz P., Persani L.;
RT   "BMP15 mutations associated with primary ovarian insufficiency cause a
RT   defective production of bioactive protein.";
RL   Hum. Mutat. 30:804-810(2009).
RN   [12]
RP   VARIANT TYR-200, AND VARIANT POF4 CYS-329.
RX   PubMed=19438907; DOI=10.1111/j.1365-2265.2009.03613.x;
RA   Wang B., Wen Q., Ni F., Zhou S., Wang J., Cao Y., Ma X.;
RT   "Analyses of growth differentiation factor 9 (GDF9) and bone
RT   morphogenetic protein 15 (BMP15) mutation in Chinese women with
RT   premature ovarian failure.";
RL   Clin. Endocrinol. (Oxf.) 72:135-136(2010).
CC   -!- FUNCTION: May be involved in follicular development. Oocyte-
CC       specific growth/differentiation factor that stimulates
CC       folliculogenesis and granulosa cell (GC) growth.
CC       {ECO:0000269|PubMed:18227435}.
CC   -!- SUBUNIT: Homodimer. But, in contrast to other members of this
CC       family, cannot be disulfide-linked.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- DISEASE: Ovarian dysgenesis 2 (ODG2) [MIM:300510]: A disorder
CC       characterized by lack of spontaneous pubertal development, primary
CC       amenorrhea, uterine hypoplasia, and hypergonadotropic hypogonadism
CC       as a result of streak gonads. {ECO:0000269|PubMed:15136966}.
CC       Note=The disease is caused by mutations affecting the gene
CC       represented in this entry.
CC   -!- DISEASE: Premature ovarian failure 4 (POF4) [MIM:300510]: An
CC       ovarian disorder defined as the cessation of ovarian function
CC       under the age of 40 years. It is characterized by oligomenorrhea
CC       or amenorrhea, in the presence of elevated levels of serum
CC       gonadotropins and low estradiol. {ECO:0000269|PubMed:16464940,
CC       ECO:0000269|PubMed:16508750, ECO:0000269|PubMed:16645022,
CC       ECO:0000269|PubMed:19263482, ECO:0000269|PubMed:19438907}.
CC       Note=The disease is caused by mutations affecting the gene
CC       represented in this entry.
CC   -!- MISCELLANEOUS: The mature protein migrates in two distinct mature
CC       proteins, P16 (16KDa) and P17 (17KDa).
CC   -!- MISCELLANEOUS: Ovarian physiology and fertility are controlled by
CC       endocrine and paracrine signals. These act in a species-dependent
CC       manner and determine the ovulation quota in different mammalian
CC       species. While humans, and mammals such as the cow or red deer,
CC       normally ovulate only one egg per cycle, other mammals such as
CC       mouse and pig can ovulate in excess of ten per cycle. The
CC       mechanisms that regulate the species-specific differences in the
CC       number of follicles that go onto ovulate during each reproductive
CC       cycle are poorly understood. According to PubMed:21970812, mRNA
CC       expression levels of GDF9 and BMP15 are tightly coregulated within
CC       each species and influence species-specific ovulation-rates.
CC   -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
DR   EMBL; AF082350; AAC99768.1; -; Genomic_DNA.
DR   EMBL; AF082349; AAC99768.1; JOINED; Genomic_DNA.
DR   EMBL; AJ132405; CAB43531.1; -; Genomic_DNA.
DR   EMBL; AL359914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC069155; AAH69155.1; -; mRNA.
DR   EMBL; BC117264; AAI17265.1; -; mRNA.
DR   EMBL; BC117266; AAI17267.1; -; mRNA.
DR   CCDS; CCDS14334.1; -.
DR   RefSeq; NP_005439.2; NM_005448.2.
DR   UniGene; Hs.532692; -.
DR   ProteinModelPortal; O95972; -.
DR   BioGrid; 114644; 4.
DR   IntAct; O95972; 1.
DR   STRING; 9606.ENSP00000252677; -.
DR   iPTMnet; O95972; -.
DR   PhosphoSitePlus; O95972; -.
DR   BioMuta; BMP15; -.
DR   PaxDb; O95972; -.
DR   PeptideAtlas; O95972; -.
DR   PRIDE; O95972; -.
DR   ProteomicsDB; 51155; -.
DR   DNASU; 9210; -.
DR   Ensembl; ENST00000252677; ENSP00000252677; ENSG00000130385.
DR   GeneID; 9210; -.
DR   KEGG; hsa:9210; -.
DR   UCSC; uc011mnw.3; human.
DR   CTD; 9210; -.
DR   DisGeNET; 9210; -.
DR   EuPathDB; HostDB:ENSG00000130385.5; -.
DR   GeneCards; BMP15; -.
DR   HGNC; HGNC:1068; BMP15.
DR   MalaCards; BMP15; -.
DR   MIM; 300247; gene.
DR   MIM; 300510; phenotype.
DR   neXtProt; NX_O95972; -.
DR   OpenTargets; ENSG00000130385; -.
DR   Orphanet; 243; 46,XX gonadal dysgenesis.
DR   Orphanet; 619; NON RARE IN EUROPE: Primary ovarian failure.
DR   PharmGKB; PA25378; -.
DR   eggNOG; KOG3900; Eukaryota.
DR   eggNOG; ENOG410XT8Z; LUCA.
DR   GeneTree; ENSGT00940000160940; -.
DR   HOGENOM; HOG000095242; -.
DR   HOVERGEN; HBG004660; -.
DR   InParanoid; O95972; -.
DR   KO; K05498; -.
DR   OMA; LYTPNYC; -.
DR   OrthoDB; 724783at2759; -.
DR   PhylomeDB; O95972; -.
DR   TreeFam; TF316134; -.
DR   Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR   SignaLink; O95972; -.
DR   SIGNOR; O95972; -.
DR   GeneWiki; Bone_morphogenetic_protein_15; -.
DR   GenomeRNAi; 9210; -.
DR   PRO; PR:O95972; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   Bgee; ENSG00000130385; Expressed in 9 organ(s), highest expression level in secondary oocyte.
DR   CleanEx; HS_BMP15; -.
DR   Genevisible; O95972; HS.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005160; F:transforming growth factor beta receptor binding; IBA:GO_Central.
DR   GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central.
DR   GO; GO:0048468; P:cell development; IBA:GO_Central.
DR   GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
DR   GO; GO:0007292; P:female gamete generation; TAS:ProtInc.
DR   GO; GO:0060016; P:granulosa cell development; IEA:InterPro.
DR   GO; GO:0001541; P:ovarian follicle development; IEA:InterPro.
DR   GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
DR   GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR   GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR   GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR   GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
DR   Gene3D; 2.10.90.10; -; 1.
DR   InterPro; IPR015923; BMP-15.
DR   InterPro; IPR029034; Cystine-knot_cytokine.
DR   InterPro; IPR001839; TGF-b_C.
DR   InterPro; IPR015615; TGF-beta-rel.
DR   InterPro; IPR017948; TGFb_CS.
DR   PANTHER; PTHR11848; PTHR11848; 1.
DR   PANTHER; PTHR11848:SF22; PTHR11848:SF22; 1.
DR   Pfam; PF00019; TGF_beta; 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   Complete proteome; Cytokine; Disease mutation; Disulfide bond;
KW   Glycoprotein; Growth factor; Phosphoprotein;
KW   Premature ovarian failure; Pyrrolidone carboxylic acid;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL        1     18       {ECO:0000255}.
FT   PROPEP       19    267
FT                                /FTId=PRO_0000033892.
FT   CHAIN       268    392       Bone morphogenetic protein 15.
FT                                /FTId=PRO_0000033893.
FT   MOD_RES     268    268       Pyrrolidone carboxylic acid; in P16 and
FT                                P17. {ECO:0000269|PubMed:18227435}.
FT   MOD_RES     273    273       Phosphoserine; in P16.
FT                                {ECO:0000269|PubMed:18227435}.
FT   CARBOHYD     87     87       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    147    147       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    237    237       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    277    277       O-linked (HexNAc...) threonine; in P17.
FT                                {ECO:0000269|PubMed:18227435}.
FT   CARBOHYD    373    373       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    291    357       {ECO:0000250}.
FT   DISULFID    320    389       {ECO:0000250}.
FT   DISULFID    324    391       {ECO:0000250}.
FT   VARIANT       5      5       S -> R (polymorphism; no or minor
FT                                deleterious effect observed;
FT                                dbSNP:rs113099187).
FT                                {ECO:0000269|PubMed:19263482}.
FT                                /FTId=VAR_058974.
FT   VARIANT      61     61       R -> Q (in POF4).
FT                                {ECO:0000269|PubMed:16508750}.
FT                                /FTId=VAR_058975.
FT   VARIANT      61     61       R -> W (in POF4; dbSNP:rs144392417).
FT                                {ECO:0000269|PubMed:16508750}.
FT                                /FTId=VAR_058976.
FT   VARIANT      68     68       R -> W (in POF4; leads to marked
FT                                reduction of mature protein production;
FT                                does not generate a complete recovery of
FT                                wild-type activity in granulosa cell line
FT                                transfected with defective mutant and
FT                                with equal amount of wild-type protein;
FT                                dbSNP:rs104894763).
FT                                {ECO:0000269|PubMed:16464940,
FT                                ECO:0000269|PubMed:19263482}.
FT                                /FTId=VAR_058977.
FT   VARIANT      76     76       R -> C (in POF4; dbSNP:rs104894766).
FT                                {ECO:0000269|PubMed:16508750}.
FT                                /FTId=VAR_058978.
FT   VARIANT      76     76       R -> H (in POF4).
FT                                {ECO:0000269|PubMed:16508750}.
FT                                /FTId=VAR_058979.
FT   VARIANT     103    103       N -> S (in dbSNP:rs41308602).
FT                                {ECO:0000269|PubMed:16508750,
FT                                ECO:0000269|PubMed:9849956}.
FT                                /FTId=VAR_058980.
FT   VARIANT     138    138       R -> H (in POF4; leads to marked
FT                                reduction of mature protein production;
FT                                does not generate a complete recovery of
FT                                wild-type activity in granulosa cell line
FT                                transfected with defective mutant and
FT                                with equal amount of wild-type protein;
FT                                dbSNP:rs371418883).
FT                                {ECO:0000269|PubMed:19263482}.
FT                                /FTId=VAR_058981.
FT   VARIANT     148    148       L -> P (in POF4; leads to marked
FT                                reduction of mature protein production;
FT                                does not generate a complete recovery of
FT                                wild-type activity in granulosa cell line
FT                                transfected with defective mutant and
FT                                with equal amount of wild-type protein;
FT                                dbSNP:rs114823607).
FT                                {ECO:0000269|PubMed:16645022,
FT                                ECO:0000269|PubMed:19263482}.
FT                                /FTId=VAR_058982.
FT   VARIANT     180    180       A -> F (requires 2 nucleotide
FT                                substitutions).
FT                                {ECO:0000269|PubMed:16508750}.
FT                                /FTId=VAR_058983.
FT   VARIANT     180    180       A -> T (in POF4; unknown pathological
FT                                significance; no or minor deleterious
FT                                effect detected; dbSNP:rs104894767).
FT                                {ECO:0000269|PubMed:16464940,
FT                                ECO:0000269|PubMed:16508750,
FT                                ECO:0000269|PubMed:16645022,
FT                                ECO:0000269|PubMed:19263482}.
FT                                /FTId=VAR_058984.
FT   VARIANT     196    196       N -> K (in POF4).
FT                                {ECO:0000269|PubMed:16508750}.
FT                                /FTId=VAR_058985.
FT   VARIANT     200    200       H -> Y (in dbSNP:rs202165852).
FT                                {ECO:0000269|PubMed:19438907}.
FT                                /FTId=VAR_066932.
FT   VARIANT     206    206       R -> H (in POF4; dbSNP:rs782516193).
FT                                {ECO:0000269|PubMed:16508750}.
FT                                /FTId=VAR_058986.
FT   VARIANT     221    221       W -> R (in POF4; dbSNP:rs375284458).
FT                                {ECO:0000269|PubMed:16508750}.
FT                                /FTId=VAR_058987.
FT   VARIANT     235    235       Y -> C (in ODG2; dominant-negative
FT                                effect; may cause relevant modifications
FT                                in the conformation of the precursor
FT                                protein possibly leading to altered
FT                                processing and impaired activation of
FT                                latent forms or to abnormal dimerization;
FT                                dbSNP:rs104894765).
FT                                {ECO:0000269|PubMed:15136966,
FT                                ECO:0000269|PubMed:16464940}.
FT                                /FTId=VAR_021195.
FT   VARIANT     243    243       I -> V (in POF4; dbSNP:rs782379521).
FT                                {ECO:0000269|PubMed:16508750}.
FT                                /FTId=VAR_058988.
FT   VARIANT     263    263       L -> LL (no or minor deleterious effect
FT                                detected). {ECO:0000269|PubMed:16464940,
FT                                ECO:0000269|PubMed:16508750,
FT                                ECO:0000269|PubMed:16645022,
FT                                ECO:0000269|PubMed:19263482}.
FT                                /FTId=VAR_058989.
FT   VARIANT     329    329       R -> C (in POF4; dbSNP:rs782375794).
FT                                {ECO:0000269|PubMed:19438907}.
FT                                /FTId=VAR_066933.
SQ   SEQUENCE   392 AA;  45055 MW;  A957275EF275A2E8 CRC64;
     MVLLSILRIL FLCELVLFME HRAQMAEGGQ SSIALLAEAP TLPLIEELLE ESPGEQPRKP
     RLLGHSLRYM LELYRRSADS HGHPRENRTI GATMVRLVKP LTNVARPHRG TWHIQILGFP
     LRPNRGLYQL VRATVVYRHH LQLTRFNLSC HVEPWVQKNP TNHFPSSEGD SSKPSLMSNA
     WKEMDITQLV QQRFWNNKGH RILRLRFMCQ QQKDSGGLEL WHGTSSLDIA FLLLYFNDTH
     KSIRKAKFLP RGMEEFMERE SLLRRTRQAD GISAEVTASS SKHSGPENNQ CSLHPFQISF
     RQLGWDHWII APPFYTPNYC KGTCLRVLRD GLNSPNHAII QNLINQLVDQ SVPRPSCVPY
     KYVPISVLMI EANGSILYKE YEGMIAESCT CR
//
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