TIKI2_MOUSE
ID TIKI2_MOUSE Reviewed; 517 AA.
AC B1ATG9;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Metalloprotease TIKI2;
DE EC=3.4.-.-;
DE AltName: Full=Heart, kidney and adipose-enriched transmembrane protein;
DE AltName: Full=TRAB domain-containing protein 2B;
DE Flags: Precursor;
GN Name=Trabd2b; Synonyms=Gm12824, Hkat, Tiki2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=23152936; DOI=10.1038/srep00825;
RA Zhang R.;
RT "Hkat, a novel nutritionally regulated transmembrane protein in adipose
RT tissues.";
RL Sci. Rep. 2:825-825(2012).
CC -!- FUNCTION: Metalloprotease that acts as a negative regulator of the Wnt
CC signaling pathway by mediating the cleavage of the 8 N-terminal
CC residues of a subset of Wnt proteins. Following cleavage, Wnt proteins
CC become oxidized and form large disulfide-bond oligomers, leading to
CC their inactivation. Able to cleave WNT3A, WNT5, but not WNT11. Required
CC for head formation (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC Note=Divalent metal cations. Mn(2+) or Co(2+). {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23152936};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:23152936}.
CC -!- TISSUE SPECIFICITY: Highly expressed in heart and kidney. Also found in
CC white and brown adipose tissue. {ECO:0000269|PubMed:23152936}.
CC -!- INDUCTION: Transiently induced during 3T3-L1 cell differentiation into
CC adipocytes. In vivo, down-regulated by fasting in both white and brown
CC adipose tissues. High-fat diet down-regulates expression in white
CC adipose tissue and up-regulates it in brown adipose tissue.
CC {ECO:0000269|PubMed:23152936}.
CC -!- SIMILARITY: Belongs to the TIKI family. {ECO:0000305}.
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DR EMBL; AL646006; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL670175; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS38843.1; -.
DR RefSeq; NP_001079018.1; NM_001085549.1.
DR AlphaFoldDB; B1ATG9; -.
DR STRING; 10090.ENSMUSP00000092494; -.
DR MEROPS; G04.002; -.
DR GlyGen; B1ATG9; 2 sites.
DR iPTMnet; B1ATG9; -.
DR PhosphoSitePlus; B1ATG9; -.
DR PaxDb; B1ATG9; -.
DR PRIDE; B1ATG9; -.
DR ProteomicsDB; 259450; -.
DR Antibodypedia; 75203; 12 antibodies from 7 providers.
DR Ensembl; ENSMUST00000094894; ENSMUSP00000092494; ENSMUSG00000070867.
DR GeneID; 666048; -.
DR KEGG; mmu:666048; -.
DR UCSC; uc008ueb.1; mouse.
DR CTD; 388630; -.
DR MGI; MGI:3650152; Trabd2b.
DR VEuPathDB; HostDB:ENSMUSG00000070867; -.
DR eggNOG; ENOG502QPR1; Eukaryota.
DR GeneTree; ENSGT00940000161273; -.
DR HOGENOM; CLU_035548_1_0_1; -.
DR InParanoid; B1ATG9; -.
DR OMA; FVKSSHQ; -.
DR OrthoDB; 1407303at2759; -.
DR PhylomeDB; B1ATG9; -.
DR TreeFam; TF313392; -.
DR BioGRID-ORCS; 666048; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Trabd2b; mouse.
DR PRO; PR:B1ATG9; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; B1ATG9; protein.
DR Bgee; ENSMUSG00000070867; Expressed in adult mammalian kidney and 154 other tissues.
DR Genevisible; B1ATG9; MM.
DR GO; GO:0031301; C:integral component of organelle membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; ISS:UniProtKB.
DR GO; GO:0017147; F:Wnt-protein binding; ISS:UniProtKB.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:1904808; P:positive regulation of protein oxidation; ISO:MGI.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR040230; TIKI1/2-like.
DR InterPro; IPR002816; TraB/PrgY/GumN_fam.
DR PANTHER; PTHR31120; PTHR31120; 1.
DR Pfam; PF01963; TraB_PrgY_gumN; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Wnt signaling pathway.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..517
FT /note="Metalloprotease TIKI2"
FT /id="PRO_0000346437"
FT TOPO_DOM 20..494
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 495..515
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 516..517
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 355..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..377
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 517 AA; 57368 MW; 5F1284F6B398D9DD CRC64;
MHAALAGPLL AALLATARAR PQPPDGGQCR PPGSQRDLNS FLWTIRRHPP AYLFGTIHVP
YTRVWDFIPD NSKAAFQAST HVYFELDLTD PYTISALASC QLLPHGENLQ DVLPRELYWR
LKRHLDYVKL MIPSWMTPAQ RGKGLYADYL FNAIAGNWER KRPVWVMLMV NSLTETDVRS
RGVPVLDLYL AQQAEKMKKS TGAVERVEEQ CHPLNGLNFS QVLFALNQTL LQHESVRAGS
LQAPYTTEDL IKHYNCGDLN AVIFNHDTSQ LPNFINTTLP PHEQVTAQEI DSYFRQELIY
KRNERMGKRV MALLQENQDK ICFFAFGAGH FLGNNTVIDV LRQAGLEVDH TPAGQAIHGP
AAVGSPAPPP EITSPASPAP ATPAAAVPEA TSATPTTPPE EEDPVLSPHL LLPDSLSQLE
EFGRQKWRKR LNKHQRPRQF NDLWVRIEDS TTISPPPLPL QPTPSSETTK PFVKSSHQLQ
QQDAVGPTSS SAPTLGLLHA ITASIVAPFL LHSLGPS
