ANKHB_DANRE
ID ANKHB_DANRE Reviewed; 501 AA.
AC P58368; B0UY66; Q66I27;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Progressive ankylosis protein homolog B;
DE Short=ANK-B;
GN Name=ankhb; Synonyms=ankh; ORFNames=si:dkeyp-106c5.1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
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; AJ302035; CAC40781.1; -; mRNA.
DR EMBL; CR391940; CAQ14932.1; -; Genomic_DNA.
DR EMBL; BC081575; AAH81575.1; -; mRNA.
DR RefSeq; NP_919351.1; NM_194370.1.
DR AlphaFoldDB; P58368; -.
DR SMR; P58368; -.
DR STRING; 7955.ENSDARP00000002526; -.
DR PaxDb; P58368; -.
DR Ensembl; ENSDART00000012413; ENSDARP00000002526; ENSDARG00000014969.
DR Ensembl; ENSDART00000192611; ENSDARP00000145514; ENSDARG00000014969.
DR GeneID; 323738; -.
DR KEGG; dre:323738; -.
DR CTD; 323738; -.
DR ZFIN; ZDB-GENE-030131-2458; ankhb.
DR eggNOG; ENOG502QWCU; Eukaryota.
DR GeneTree; ENSGT00390000012189; -.
DR HOGENOM; CLU_044298_0_0_1; -.
DR InParanoid; P58368; -.
DR OMA; RRFYQGI; -.
DR OrthoDB; 484099at2759; -.
DR PhylomeDB; P58368; -.
DR TreeFam; TF333504; -.
DR Reactome; R-DRE-5223345; Miscellaneous transport and binding events.
DR PRO; PR:P58368; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 2.
DR Bgee; ENSDARG00000014969; Expressed in swim bladder and 23 other tissues.
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; IBA:GO_Central.
DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IBA:GO_Central.
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..501
FT /note="Progressive ankylosis protein homolog B"
FT /id="PRO_0000137471"
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..362
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 384..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..501
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 457..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..488
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 2..3
FT /note="MK -> KE (in Ref. 1; CAC40781)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 501 AA; 55417 MW; 62A4F52BF5B2F28C CRC64;
MMKFPALTHY WPLIRFLVPL AITNIAIDLG EQALNRGIAA VKEDAVEMLA SYGLAYSLMK
FFTGPMSDFK NVGLVFVNSK RDRTKAVLCM VVAGTVAIVF HTLIAYTNLG YYIINKLHHV
DESVGSKTRK AFLYLAAFPL LDAMAWTHAG ILLKHKHSLL VGCASISDVV AQIVFVGILL
HSHLECVEPM LIPILSLYMG ALVRFTIVGL GYYKVIHDNI PESSGPEVGG DATIKKMLSF
WWPLALILAT QRISRPIVNL FVSRDLKGST AATEAVAVLT ATYPVGHMPY GWLTELRAVY
PAFDKNNPSN KLINSGTVVT KSHIKRFTFF CLALSITLCF MVFWAPHISE SILVDIIGVD
HAFAELCITP LRIFSFFPIP VTIRAHLTGW LMTLKKTFVL APSSVLRIIV LISSLIVLPY
MGVHGATLGV GSLLAGFLGE STMVAIAACY VYRKQKKKKD SDEDMTIDGE DSAPMNEVRS
RGRMDDIVEL REEDEEELDE D
