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Database: UniProt
Entry: A0A2Y9TAB6_PHYMC
LinkDB: A0A2Y9TAB6_PHYMC
Original site: A0A2Y9TAB6_PHYMC 
ID   A0A2Y9TAB6_PHYMC        Unreviewed;       666 AA.
AC   A0A2Y9TAB6;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Frizzled-3 isoform X1 {ECO:0000313|RefSeq:XP_023986662.1};
GN   Name=FZD3 {ECO:0000313|RefSeq:XP_023986662.1};
OS   Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Physeteridae; Physeter.
OX   NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_023986662.1};
RN   [1] {ECO:0000313|RefSeq:XP_023986662.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_023986662.1};
RG   RefSeq;
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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00090}.
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DR   RefSeq; XP_023986662.1; XM_024130894.3.
DR   AlphaFoldDB; A0A2Y9TAB6; -.
DR   STRING; 9755.ENSPCTP00005003119; -.
DR   Ensembl; ENSPCTT00005003429; ENSPCTP00005003119; ENSPCTG00005002245.
DR   InParanoid; A0A2Y9TAB6; -.
DR   OrthoDB; 5483535at2759; -.
DR   Proteomes; UP000248484; Chromosome 9.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR   GO; GO:0030424; C:axon; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR   GO; GO:0032433; C:filopodium tip; IEA:Ensembl.
DR   GO; GO:0016328; C:lateral plasma membrane; IEA:Ensembl.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0048786; C:presynaptic active zone; IEA:Ensembl.
DR   GO; GO:0030165; F:PDZ domain binding; 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:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
DR   GO; GO:0033278; P:cell proliferation in midbrain; IEA:Ensembl.
DR   GO; GO:0071679; P:commissural neuron axon guidance; IEA:Ensembl.
DR   GO; GO:0036514; P:dopaminergic neuron axon guidance; IEA:Ensembl.
DR   GO; GO:0001736; P:establishment of planar polarity; IEA:Ensembl.
DR   GO; GO:0001942; P:hair follicle development; IEA:Ensembl.
DR   GO; GO:0042472; P:inner ear morphogenesis; IEA:Ensembl.
DR   GO; GO:0097475; P:motor neuron migration; IEA:Ensembl.
DR   GO; GO:1900118; P:negative regulation of execution phase of apoptosis; IEA:Ensembl.
DR   GO; GO:0045976; P:negative regulation of mitotic cell cycle, embryonic; IEA:Ensembl.
DR   GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR   GO; GO:0002052; P:positive regulation of neuroblast proliferation; IEA:Ensembl.
DR   GO; GO:0036342; P:post-anal tail morphogenesis; IEA:Ensembl.
DR   GO; GO:0036515; P:serotonergic neuron axon guidance; IEA:Ensembl.
DR   GO; GO:0061549; P:sympathetic ganglion development; IEA:Ensembl.
DR   GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; IEA:Ensembl.
DR   CDD; cd15033; 7tmF_FZD3; 1.
DR   CDD; cd07449; CRD_FZ3; 1.
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; IPR041769; FZ3_CRD.
DR   InterPro; IPR017981; GPCR_2-like_7TM.
DR   PANTHER; PTHR11309; FRIZZLED; 1.
DR   PANTHER; PTHR11309:SF22; FRIZZLED-3; 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:UP000248484};
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..666
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015910331"
FT   TRANSMEM        204..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        238..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        291..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        328..349
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        373..397
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        417..442
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        477..498
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          23..136
FT                   /note="FZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50038"
FT   DOMAIN          199..506
FT                   /note="G-protein coupled receptors family 2 profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50261"
FT   REGION          538..666
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        545..570
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        587..601
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        609..635
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        636..666
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        28..89
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT   DISULFID        36..82
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT   DISULFID        103..127
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ   SEQUENCE   666 AA;  76223 MW;  74FA6DFA370CAD2D CRC64;
     MAMSWIVFIL WPLTMFVGHI GGHSLFSCEP ITLRMCQDLP YNTTFMPNLL NHYDQQTAAL
     AMEPFHPMVN LDCSRDFRPF LCALYAPICM EYGRVTLPCR RLCQRAYSEC SKLMEMFGVP
     WPEDMECSRF PDCDEPYPRL VDLNLAGDPT EGAPVAVQRD YGFWCPRELK IDPDLGYSFL
     HVRDCSPPCP NMYFRREELS FARYFIGLIS IICLSATLFT FLTFLIDVTR FRYPERPIIF
     YAVCYMMVSL IFFIGFLLED RVACNASSPA QYKASTVTQG SHNKACTMLF MVLYFFTMAG
     SVWWVILTIT WFLAAVPKWG SEAIEKKALL FHASAWGIPG TLTIILLAMN KIEGDNISGV
     CFVGLYDVDS LRYFVLAPLC LYVVVGVSLL LAGIISLNRV RIEIPLEKEN QDKLVKFMIR
     IGVFSILYLV PLLVVIGCYF YEQAYRGIWE TTWIQERCRE YHIPCPYQVT QMSRPDLIVF
     LMKYLMALIV GIPSIFWVGS KKTCFEWASF FHGRRKKEIV NESRQVLQEP DFAQSLLRDP
     NTPIIRKSRG TSTQGTSTHA SSTQLAMVDD QRSKAGSVHS KVSSYHGSLH RSRDGRYTPC
     SYRGMEERLP HGSMSRLTDH SRHSSSHRLN EQSRHSSIRD LSNNPMTHIT HGTSMNRVIE
     EDGTSA
//
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