ANKH_MOUSE
ID ANKH_MOUSE Reviewed; 492 AA.
AC Q9JHZ2; O35138; O35139;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Progressive ankylosis protein;
DE AltName: Full=Fn54 protein;
GN Name=Ankh; Synonyms=Ank;
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 [MRNA], AND VARIANT VAL-201.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=10894769; DOI=10.1126/science.289.5477.265;
RA Ho A.M., Johnson M.D., Kingsley D.M.;
RT "Role of the mouse ank gene in control of tissue calcification and
RT arthritis.";
RL Science 289:265-270(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RA Guo Y., Hsu D.K.W., Alberts G.F., Feng S.-L., Copeland N.G., Gilbert D.J.,
RA Jenkins N.A., Peifley K.A., Winkles J.A.;
RT "Molecular cloning and characterization of a mitogen-inducible gene
RT differentially expressed in androgen-dependent and independent prostate
RT carcinoma cell lines.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
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).
CC -!- FUNCTION: Regulates intra- and extracellular levels of inorganic
CC pyrophosphate (PPi), probably functioning as PPi transporter.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, liver, spleen, lung,
CC muscle, and kidney of adult animals. Strongly expressed in the
CC developing articular cartilage of joints in the shoulder, elbow, wrist,
CC and digits of the embryo.
CC -!- DISEASE: Note=Defects in Ankh are the cause of a generalized,
CC progressive form of arthritis. In ank mice hydroxyapatite crystals
CC develop in articular surfaces and synovial fluid leading to joint space
CC narrowing, cartilage erosion, and formation of bony outgrowths or
CC osteophytes that cause fusion and joint immobility and destruction.
CC -!- SIMILARITY: Belongs to the ANKH family. {ECO:0000305}.
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DR EMBL; AF274752; AAF88038.1; -; mRNA.
DR EMBL; AF001532; AAB65653.1; -; mRNA.
DR EMBL; AF001533; AAB65654.2; -; mRNA.
DR EMBL; BC054379; AAH54379.1; -; mRNA.
DR CCDS; CCDS27402.1; -.
DR RefSeq; NP_065065.3; NM_020332.4.
DR AlphaFoldDB; Q9JHZ2; -.
DR SMR; Q9JHZ2; -.
DR STRING; 10090.ENSMUSP00000022875; -.
DR iPTMnet; Q9JHZ2; -.
DR PhosphoSitePlus; Q9JHZ2; -.
DR MaxQB; Q9JHZ2; -.
DR PaxDb; Q9JHZ2; -.
DR PRIDE; Q9JHZ2; -.
DR ProteomicsDB; 296038; -.
DR Antibodypedia; 43269; 117 antibodies from 24 providers.
DR DNASU; 11732; -.
DR Ensembl; ENSMUST00000022875; ENSMUSP00000022875; ENSMUSG00000022265.
DR GeneID; 11732; -.
DR KEGG; mmu:11732; -.
DR UCSC; uc007vjo.2; mouse.
DR CTD; 11732; -.
DR MGI; MGI:3045421; Ank.
DR VEuPathDB; HostDB:ENSMUSG00000022265; -.
DR eggNOG; ENOG502QWCU; Eukaryota.
DR GeneTree; ENSGT00390000012189; -.
DR HOGENOM; CLU_044298_0_0_1; -.
DR InParanoid; Q9JHZ2; -.
DR OMA; RRFYQGI; -.
DR OrthoDB; 484099at2759; -.
DR PhylomeDB; Q9JHZ2; -.
DR TreeFam; TF333504; -.
DR Reactome; R-MMU-5223345; Miscellaneous transport and binding events.
DR BioGRID-ORCS; 11732; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Ank; mouse.
DR PRO; PR:Q9JHZ2; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9JHZ2; protein.
DR Bgee; ENSMUSG00000022265; Expressed in seminal vesicle and 272 other tissues.
DR ExpressionAtlas; Q9JHZ2; baseline and differential.
DR Genevisible; Q9JHZ2; MM.
DR GO; GO:0005576; C:extracellular region; IMP:MGI.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0030504; F:inorganic diphosphate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015114; F:phosphate ion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0110148; P:biomineralization; IDA:MGI.
DR GO; GO:0030282; P:bone mineralization; IDA:MGI.
DR GO; GO:0055074; P:calcium ion homeostasis; IMP:MGI.
DR GO; GO:0071529; P:cementum mineralization; IDA:MGI.
DR GO; GO:0071344; P:diphosphate metabolic process; IDA:MGI.
DR GO; GO:0010467; P:gene expression; IDA:MGI.
DR GO; GO:0030505; P:inorganic diphosphate transport; IMP:MGI.
DR GO; GO:0055062; P:phosphate ion homeostasis; IMP:MGI.
DR GO; GO:0030500; P:regulation of bone mineralization; IMP:UniProtKB.
DR GO; GO:1904383; P:response to sodium phosphate; IMP:MGI.
DR InterPro; IPR009887; ANKH.
DR PANTHER; PTHR28384; PTHR28384; 1.
DR Pfam; PF07260; ANKH; 1.
PE 2: Evidence at transcript level;
KW Membrane; Phosphate transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..492
FT /note="Progressive ankylosis protein"
FT /id="PRO_0000137468"
FT TOPO_DOM 1..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..131
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..189
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..326
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348..350
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 372..403
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..429
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 453..492
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 458..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 201
FT /note="A -> V (in strain: C3H)"
FT /evidence="ECO:0000269|PubMed:10894769"
SQ SEQUENCE 492 AA; 54298 MW; 8792B248C875688E CRC64;
MVKFPALTHY WPLIRFLVPL GITNIAIDFG EQALNRGIAA VKEDAVEMLA SYGLAYSLMK
FFTGPMSDFK NVGLVFVNSK RDRAKAVLCM VVAGAIAAVF HTLIAYSDLG YYIINKLHHV
DESVGSKTRR AFLYLAAFPF MDAMAWTHAG ILLKHKYSFL VGCASISDVI AQVVFVAILL
HSHLECREPL LIPILSLYMG ALVRCTTLCL GYYRNIHDII PDRSGPELGG DATIRKMLSF
WWPLALILAT QRISRPIVNL FVSRDLGGSS AATEAVAILT ATYPVGHMPY GWLTEIRAVY
PAFDKNNPSN KLANTSNTVT SAHIKKFTFV CMALSLTLCF VMFWTPNVSE KILIDIIGVD
FAFAELCVIP LRIFSFFPVP VTVRAHLTGW LMTLKKTFVL APSSVLRIIV LITSLVVLPY
LGVHGATLGV GSLLAGFVGE STMVALAACY VYRKQKKKME NESATEGEDS AMTDMPPTEE
VTDIVEMREE NE
