ANKH_XENLA
ID ANKH_XENLA Reviewed; 492 AA.
AC P58367;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2001, sequence version 1.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=Progressive ankylosis protein homolog;
DE Short=ANK;
GN Name=ankh;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11326272; DOI=10.1038/ng0501-37;
RA Nuernberg P., Thiele H., Chandler D., Hoehne W., Cunningham M.L.,
RA Ritter H., Leschik G., Uhlmann K., Mischung C., Harrop K., Goldblatt J.,
RA Borochowitz Z.U., Kotzot D., Westermann F., Mundlos S., Braun H.-S.,
RA Laing N., Tinschert S.;
RT "Heterozygous mutations in ANKH, the human ortholog of the mouse
RT progressive ankylosis gene, result in craniometaphyseal dysplasia.";
RL Nat. Genet. 28:37-41(2001).
CC -!- FUNCTION: Regulates intra- and extracellular levels of inorganic
CC pyrophosphate (PPi), probably functioning as PPi transporter.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ANKH family. {ECO:0000305}.
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DR EMBL; AJ302033; CAC40980.1; -; mRNA.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0030504; F:inorganic diphosphate transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015114; F:phosphate ion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0030500; P:regulation of bone mineralization; ISS:UniProtKB.
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 homolog"
FT /id="PRO_0000137470"
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..327
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 349..360
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 382..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"
SQ SEQUENCE 492 AA; 53953 MW; 753214B87D7E5F23 CRC64;
MVKLPSLTPY WPLIRFLVPL GITNIAIDFG EQALNRGIAA VKEDAIEMLA SYGLAYSLMK
FFTGPMSDFK NVGLVFVNSK RDRMKAVLCM VVAGIIAAVF HTLIAYSDLG YYIINKLHHV
DESVGGKTRK AFLYLAAVPF MDAMAWTHAG ILLKHKYSFL VGCASISDVI AQVVFVAILL
HSHLECREPL LIPILSLYIG ALVRCTTLCL GYYKNIHDKI PESSGPEIGG DATIKKMLSF
WWPLALILAT QRISRPIVNL FVSRDLGGST AATEAVAILT ATYPVGHMPY GWLTEIRAVY
PAFDKSNPGS KLANSSNPVS KTHIKNXTFA CMALSLTLCF VMFWTPNVSE KILVDIIGVD
FAFAELCVIP LRIFSFFPVP VTVRAHLTGW LMTLKKTFVL APSSILRIIV LISSLIVLPY
LGVHGATLGV GSLLAGFVGE STMVAIASLY VYRKQKKKSE TENAVEGEDS AMTDLPHNEE
LTDIVEIKED GE