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SMO_CHICK
ID   SMO_CHICK               Reviewed;         794 AA.
AC   O42224;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Smoothened homolog;
DE            Short=SMO;
DE   Flags: Precursor; Fragment;
GN   Name=SMO; Synonyms=SMOH;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9598354;
RA   Quirk J., van den Heuvel M., Henrique D., Marigo V., Sheer D., Tabin C.,
RA   Ingham P.W.;
RT   "The smoothened gene and hedgehog signal transduction in Drosophila and
RT   vertebrate development.";
RL   Cold Spring Harb. Symp. Quant. Biol. 62:217-226(1997).
CC   -!- FUNCTION: G protein-coupled receptor that probably associates with the
CC       patched protein (PTCH) to transduce the hedgehog's proteins signal.
CC       Binding of sonic hedgehog (SHH) to its receptor patched is thought to
CC       prevent normal inhibition by patched of smoothened (SMO).
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family.
CC       {ECO:0000305}.
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DR   EMBL; AF019977; AAB84389.1; -; mRNA.
DR   AlphaFoldDB; O42224; -.
DR   SMR; O42224; -.
DR   STRING; 9031.ENSGALP00000039562; -.
DR   VEuPathDB; HostDB:geneid_395949; -.
DR   eggNOG; KOG3577; Eukaryota.
DR   InParanoid; O42224; -.
DR   PhylomeDB; O42224; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005929; C:cilium; IBA:GO_Central.
DR   GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005113; F:patched binding; IBA:GO_Central.
DR   GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR   GO; GO:0071679; P:commissural neuron axon guidance; IBA:GO_Central.
DR   GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IBA:GO_Central.
DR   GO; GO:0007224; P:smoothened signaling pathway; IBA:GO_Central.
DR   CDD; cd15030; 7tmF_SMO_homolog; 1.
DR   CDD; cd07451; CRD_SMO; 1.
DR   Gene3D; 1.10.2000.10; -; 1.
DR   InterPro; IPR015526; Frizzled/SFRP.
DR   InterPro; IPR000539; Frizzled/Smoothened_TM.
DR   InterPro; IPR020067; Frizzled_dom.
DR   InterPro; IPR036790; Frizzled_dom_sf.
DR   InterPro; IPR017981; GPCR_2-like.
DR   InterPro; IPR026544; SMO.
DR   InterPro; IPR035683; SMO_7TM.
DR   InterPro; IPR041771; SMO_CRD.
DR   PANTHER; PTHR11309; PTHR11309; 1.
DR   PANTHER; PTHR11309:SF35; PTHR11309:SF35; 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; SSF63501; 1.
DR   PROSITE; PS50038; FZ; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE   2: Evidence at transcript level;
KW   Developmental protein; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Membrane; Receptor; Reference proteome; Signal; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          <1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..794
FT                   /note="Smoothened homolog"
FT                   /id="PRO_0000013018"
FT   TOPO_DOM        16..201
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..222
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        223..231
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        232..252
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        253..283
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        284..304
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        305..327
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        328..348
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        349..371
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        372..392
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        393..420
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        421..440
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        441..493
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        494..514
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        515..794
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          35..151
FT                   /note="FZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   REGION          634..655
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          723..773
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        25
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        158
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        278
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        462
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        40..104
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   DISULFID        48..97
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   DISULFID        88..124
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   DISULFID        117..139
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   DISULFID        163..183
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   DISULFID        187..264
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   DISULFID        283..359
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   DISULFID        459..476
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   NON_TER         1
SQ   SEQUENCE   794 AA;  88255 MW;  CE71AE9864A6C0CB CRC64;
     GPCWLWALAL GLALGPRRCP AAPLNASAAP PERCRRPAAC ERLRFGSCLG SALPYAHTST
     LLAADSGSQE EAHGKLLLWS GLRNAPRCWD VIQPLLCAVY MPKCEDGQVE LPSQTLCQAT
     RAPCTIVERE RGWPDFLKCT PDRFPEGCPN EVQNIKFNSS GQCEAPLVRT YNPKSWYEDV
     EGCGIQCQNP LFTETEHREM HVYIAFSSVT ISCTFFTLAT FVADWRNSNR YPAVILFYVN
     ACFFVGSIGC VAQFMDGARD EIVCRADGTM RLGEPTSNET LSCVIIFVIV YYSLMSGVIW
     FVMLTYAWHT SFKALGTTYQ PLLGKTSYFH LITWSIPFVL TVAILAVAQV DGDSVSGICF
     VGYKNYRYRA GFVLAPIGLV LIVGGYFLIR GVMTLFSIKS NHPGLLSEKA ASKINETMLR
     LGIFGFLAFG FVFITFGCHF YDFFNQAEWE RSFREYVLCE ANVTIATQTN KPIPECEIKN
     RPSLLVEKIN LFAMFGTGIS MSTWVWTKAT LLIWKRTWCR LTGQSDDQPK RIKKSKMIAK
     AFSKRKELLR DPGRELSFSM HTVSHDGPVA GLAFDINEPS ADVSSAWAQH VTKMVARRGA
     ILPQDVSVTP VATPVPPEER SNLWVVEADV SPELQKRSRK KKRRKKKKEE VCPERRAGLS
     VAPLTPSSVP RLPRLPQQPC LVAIPRHRGD TFIPTVLPGL SNGAGGLWDG RRRAHVPHFI
     TNPFCPESGS PEDEENPGPS VGHRQHNGGR RWPPEPLPGG SGVTRTRGRR AGLAPIHSRT
     NLVNAELLDA DLDF
 
 
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