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WLS_RAT
ID   WLS_RAT                 Reviewed;         541 AA.
AC   Q6P689;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Protein wntless homolog;
DE   AltName: Full=Integral membrane protein GPR177;
DE   AltName: Full=Protein evenness interrupted homolog;
DE            Short=EVI;
GN   Name=Wls; Synonyms=Gpr177;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=Wistar;
RX   PubMed=15326124; DOI=10.1167/iovs.04-0302;
RA   Ahmed F., Torrado M., Zinovieva R.D., Senatorov V.V., Wistow G.,
RA   Tomarev S.I.;
RT   "Gene expression profile of the rat eye iridocorneal angle: NEIBank
RT   expressed sequence tag analysis.";
RL   Invest. Ophthalmol. Vis. Sci. 45:3081-3090(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   TISSUE SPECIFICITY, AND GLYCOSYLATION.
RX   PubMed=20652957; DOI=10.1002/dvdy.22369;
RA   Jin J., Morse M., Frey C., Petko J., Levenson R.;
RT   "Expression of GPR177 (Wntless/Evi/Sprinter), a highly conserved Wnt-
RT   transport protein, in rat tissues, zebrafish embryos, and cultured human
RT   cells.";
RL   Dev. Dyn. 239:2426-2434(2010).
CC   -!- FUNCTION: Regulates Wnt proteins sorting and secretion in a feedback
CC       regulatory mechanism. This reciprocal interaction plays a key role in
CC       the regulation of expression, subcellular location, binding and
CC       organelle-specific association of Wnt proteins. Also plays an important
CC       role in establishment of the anterior-posterior body axis formation
CC       during development (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with WNT3A. Interacts with WNT1, WNT3 and WNT5A.
CC       {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q6P689; P33535: Oprm1; NbExp=2; IntAct=EBI-6113235, EBI-4392569;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:Q5T9L3}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q5T9L3}. Cytoplasmic vesicle membrane
CC       {ECO:0000250|UniProtKB:Q5T9L3}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q5T9L3}. Cell membrane
CC       {ECO:0000250|UniProtKB:Q5T9L3}; Multi-pass membrane protein
CC       {ECO:0000255}. Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q5T9L3}; Multi-pass membrane protein
CC       {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q5T9L3};
CC       Multi-pass membrane protein {ECO:0000255}. Early endosome membrane
CC       {ECO:0000250|UniProtKB:Q5T9L3}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in the brain, skeletal muscle, heart
CC       muscle, lung, gut, liver, and kidney (at protein level)
CC       (PubMed:20652957). In the brain, expressed in the cortex, striatum,
CC       ventral tegmentum, nucleus accumbens and to a lesser extent in the
CC       Purkinjie cells in the cerebellum (PubMed:20652957). Expressed in eye
CC       iridocorneal angle (PubMed:15326124). {ECO:0000269|PubMed:15326124,
CC       ECO:0000269|PubMed:20652957}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:20652957}.
CC   -!- SIMILARITY: Belongs to the wntless family. {ECO:0000305}.
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DR   EMBL; AY569010; AAS75313.1; -; mRNA.
DR   EMBL; BC062391; AAH62391.1; -; mRNA.
DR   RefSeq; NP_001078822.1; NM_001085353.1.
DR   RefSeq; NP_955440.1; NM_199408.2.
DR   AlphaFoldDB; Q6P689; -.
DR   SMR; Q6P689; -.
DR   IntAct; Q6P689; 1.
DR   STRING; 10116.ENSRNOP00000052120; -.
DR   PhosphoSitePlus; Q6P689; -.
DR   jPOST; Q6P689; -.
DR   PaxDb; Q6P689; -.
DR   Ensembl; ENSRNOT00000055245; ENSRNOP00000052120; ENSRNOG00000036816.
DR   GeneID; 362065; -.
DR   KEGG; rno:362065; -.
DR   CTD; 79971; -.
DR   RGD; 735139; Wls.
DR   eggNOG; ENOG502QSE2; Eukaryota.
DR   GeneTree; ENSGT00390000005897; -.
DR   HOGENOM; CLU_022911_0_0_1; -.
DR   InParanoid; Q6P689; -.
DR   OMA; YWRHLSA; -.
DR   OrthoDB; 418201at2759; -.
DR   PhylomeDB; Q6P689; -.
DR   Reactome; R-RNO-3238698; WNT ligand biogenesis and trafficking.
DR   PRO; PR:Q6P689; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Bgee; ENSRNOG00000036816; Expressed in adult mammalian kidney and 19 other tissues.
DR   ExpressionAtlas; Q6P689; baseline and differential.
DR   Genevisible; Q6P689; RN.
DR   GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR   GO; GO:0032839; C:dendrite cytoplasm; IDA:RGD.
DR   GO; GO:0032590; C:dendrite membrane; IDA:RGD.
DR   GO; GO:0005769; C:early endosome; ISO:RGD.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031301; C:integral component of organelle membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0005802; C:trans-Golgi network; ISO:RGD.
DR   GO; GO:0031852; F:mu-type opioid receptor binding; IPI:RGD.
DR   GO; GO:0017147; F:Wnt-protein binding; ISO:RGD.
DR   GO; GO:0009948; P:anterior/posterior axis specification; ISS:UniProtKB.
DR   GO; GO:0071529; P:cementum mineralization; ISO:RGD.
DR   GO; GO:0031017; P:exocrine pancreas development; ISO:RGD.
DR   GO; GO:0030902; P:hindbrain development; ISO:RGD.
DR   GO; GO:0006886; P:intracellular protein transport; ISO:RGD.
DR   GO; GO:0001707; P:mesoderm formation; ISO:RGD.
DR   GO; GO:0030901; P:midbrain development; ISO:RGD.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:RGD.
DR   GO; GO:0061357; P:positive regulation of Wnt protein secretion; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0061355; P:Wnt protein secretion; ISO:RGD.
DR   GO; GO:0016055; P:Wnt signaling pathway; ISS:UniProtKB.
DR   InterPro; IPR009551; Wntless.
DR   PANTHER; PTHR13449; PTHR13449; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Cytoplasmic vesicle; Developmental protein;
KW   Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix;
KW   Wnt signaling pathway.
FT   CHAIN           1..541
FT                   /note="Protein wntless homolog"
FT                   /id="PRO_0000271780"
FT   TOPO_DOM        1..15
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q5T9L3"
FT   TRANSMEM        16..36
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        37..232
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q5T9L3"
FT   TRANSMEM        233..253
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        254..268
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q5T9L3"
FT   TRANSMEM        269..289
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        290..303
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q5T9L3"
FT   TRANSMEM        304..324
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        325..331
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q5T9L3"
FT   TRANSMEM        332..352
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        353..380
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q5T9L3"
FT   TRANSMEM        381..401
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        402..431
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q5T9L3"
FT   TRANSMEM        432..452
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        453..471
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q5T9L3"
FT   TRANSMEM        472..492
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        493..541
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q5T9L3"
FT   REGION          101..202
FT                   /note="Interaction with Wnt proteins"
SQ   SEQUENCE   541 AA;  62202 MW;  58DCC18634B86668 CRC64;
     MAGAIIENMS TKKLCIVGGI LLVFQIVAFL VGGLIAPAPT TAVSYVAAKC VDVRKNHHKT
     RWLMPWGPNK CNKINDFEEA IPREIEANDI VFSVHIPLPS MEMSPWFQFM LFILQIDIAF
     KLNNQIRENA EVSMDVSLGY RDDMFSEWTE MAHERVPRKL RCTFTSPKTP EHEGRHYECD
     VLPFMEIGSV AHKYYLLNIR LPVNEKKKIN VGIGEIKDIR LVGIHQNGGF TKVWFAMKTF
     LTPSIFIIMV WYWRRITMMS RPPVLLEKVI FALGISMTFI NIPVEWFSIG FDWTWMLLFG
     DIRQGIFYAM LLSFWIIFCG EHMMDQHERN HIAGYWKQVG PIAVGSFCLF IFDMCERGVQ
     LTNPFYSIWT TDVGTELAMA FIIVAGICLC LYFLFLCFMV FQVFRNISGK QSSLPAMSKV
     RRLHYEGLIF RFKFLMLITL ACAAMTVIFF IVSQVTEGHW KWGGVTVQVS SAFFTGIYGM
     WNLYVFALMF LYAPSHKNYG EDQSNGDLGV HSGEELQLTT TITHVDGPTE IYKLTRKEAQ
     E
 
 
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