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Database: UniProt
Entry: H2PLY5_PONAB
LinkDB: H2PLY5_PONAB
Original site: H2PLY5_PONAB 
ID   H2PLY5_PONAB            Unreviewed;       591 AA.
AC   H2PLY5; A0A2J8XV26; A0A6D2X859;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=FZD9 isoform 1 {ECO:0000313|EMBL:PNJ85873.1};
DE   SubName: Full=Frizzled class receptor 9 {ECO:0000313|Ensembl:ENSPPYP00000019620.1};
GN   Name=FZD9 {ECO:0000313|Ensembl:ENSPPYP00000019620.1};
GN   ORFNames=CR201_G0040374 {ECO:0000313|EMBL:PNJ85873.1};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000019620.1, ECO:0000313|Proteomes:UP000001595};
RN   [1] {ECO:0000313|Ensembl:ENSPPYP00000019620.1, ECO:0000313|Proteomes:UP000001595}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wilson R.K., Mardis E.;
RT   "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PNJ85873.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Susie {ECO:0000313|EMBL:PNJ85873.1};
RA   Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA   Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA   Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA   Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA   Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT   "High-resolution comparative analysis of great ape genomes.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSPPYP00000019620.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family.
CC       {ECO:0000256|ARBA:ARBA00008077}.
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DR   EMBL; NDHI03003309; PNJ85873.1; -; Genomic_DNA.
DR   RefSeq; XP_002817910.1; XM_002817864.3.
DR   STRING; 9601.ENSPPYP00000019620; -.
DR   Ensembl; ENSPPYT00000020392.2; ENSPPYP00000019620.1; ENSPPYG00000017504.2.
DR   GeneID; 100438736; -.
DR   KEGG; pon:100438736; -.
DR   CTD; 8326; -.
DR   eggNOG; KOG3577; Eukaryota.
DR   GeneTree; ENSGT00940000161226; -.
DR   HOGENOM; CLU_007873_2_1_1; -.
DR   OMA; CEGIGYN; -.
DR   OrthoDB; 5483535at2759; -.
DR   TreeFam; TF317907; -.
DR   Proteomes; UP000001595; Chromosome 7.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0031527; C:filopodium membrane; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0042813; F:Wnt receptor activity; IEA:Ensembl.
DR   GO; GO:0017147; F:Wnt-protein binding; IEA:Ensembl.
DR   GO; GO:0030183; P:B cell differentiation; IEA:Ensembl.
DR   GO; GO:1990523; P:bone regeneration; IEA:Ensembl.
DR   GO; GO:0007611; P:learning or memory; IEA:Ensembl.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:1904394; P:negative regulation of skeletal muscle acetylcholine-gated channel clustering; IEA:Ensembl.
DR   GO; GO:0007405; P:neuroblast proliferation; IEA:Ensembl.
DR   GO; GO:0001503; P:ossification; IEA:Ensembl.
DR   GO; GO:0030501; P:positive regulation of bone mineralization; IEA:Ensembl.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR   GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; IEA:Ensembl.
DR   GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR   Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR015526; Frizzled/SFRP.
DR   InterPro; IPR000539; Frizzled/Smoothened_7TM.
DR   InterPro; IPR020067; Frizzled_dom.
DR   InterPro; IPR036790; Frizzled_dom_sf.
DR   InterPro; IPR017981; GPCR_2-like_7TM.
DR   PANTHER; PTHR11309; FRIZZLED; 1.
DR   PANTHER; PTHR11309:SF79; FRIZZLED-9; 1.
DR   Pfam; PF01534; Frizzled; 1.
DR   Pfam; PF01392; Fz; 1.
DR   PRINTS; PR00489; FRIZZLED.
DR   SMART; SM00063; FRI; 1.
DR   SMART; SM01330; Frizzled; 1.
DR   SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR   PROSITE; PS50038; FZ; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00090};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001595};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..591
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014575178"
FT   TRANSMEM        231..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        267..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        319..343
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        355..376
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        396..427
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        448..469
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        508..529
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          34..155
FT                   /note="FZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50038"
FT   DOMAIN          231..536
FT                   /note="G-protein coupled receptors family 2 profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50261"
FT   DISULFID        39..100
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT   DISULFID        47..93
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT   DISULFID        84..122
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT   DISULFID        111..152
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT   DISULFID        115..139
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ   SEQUENCE   591 AA;  64501 MW;  4C7ED8043BBEDC84 CRC64;
     MAVAPLRGAL LLWQLLAAGG AALEIGRFDP ERGRGAAPCQ AVEIPMCRGI GYNLTRMPNL
     LGHTSQGEAA AELAEFAPLV QYGCHSHLRF FLCSLYAPMC TDQVSTPIPA CRPMCEQARL
     RCAPIMEQFN FGWPDSLDCA RLPTRNDPHA LCMEAPENAT AGPAEPHKGL GMLPVAPRPA
     RPPGDLGQGA GGSGTCENPE KFQYVEKSRS CAPRCGPGVE VFWSRRDKDF ALVWMAVWSA
     LCFFSTAFTV LTFLLEPHRF QYPERPIIFL SMCYNVYSLA FLIRAVAGAQ SVACDQEAGA
     LYVIQEGLEN TGCTLVFLLL YYFGMASSLW WVVLTLTWFL AAGKKWGHEA IEAHGSYFHM
     AAWGLPALKT IVILTLRKVA GDELTGLCYV ASTDAAALTG FVLVPLSGYL VLGSSFLLTG
     FVALFHIRKI MKTGGTNTEK LEKLMVKIGV FSILYTVPAT CVIVCYVYER LNMDFWRLRA
     TEQPCAAAAG PGGRRDCSLP GGSVPTVAVF MLKIFMSLVV GITSGVWVWS SKTFQTWQSL
     CHRKIAAGRA RAKACRAPGS YGRGMHCHYK APTVVLHMTK TDPSLENPTH L
//
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