NTCP7_MOUSE
ID NTCP7_MOUSE Reviewed; 340 AA.
AC Q5PT53; Q5PT51; Q8BV58; Q8BYD0; Q9CWD6;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Sodium/bile acid cotransporter 7;
DE AltName: Full=Na(+)/bile acid cotransporter 7;
DE AltName: Full=Solute carrier family 10 member 7;
GN Name=Slc10a7; Synonyms=P7;
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] (ISOFORMS 1 AND 3), AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=17628207; DOI=10.1016/j.ejcb.2007.06.001;
RA Godoy J.R., Fernandes C., Doering B., Beuerlein K., Petzinger E., Geyer J.;
RT "Molecular and phylogenetic characterization of a novel putative membrane
RT transporter (SLC10A7), conserved in vertebrates and bacteria.";
RL Eur. J. Cell Biol. 86:445-460(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=30082715; DOI=10.1038/s41467-018-05191-8;
RA Dubail J., Huber C., Chantepie S., Sonntag S., Tueysuez B., Mihci E.,
RA Gordon C.T., Steichen-Gersdorf E., Amiel J., Nur B., Stolte-Dijkstra I.,
RA van Eerde A.M., van Gassen K.L., Breugem C.C., Stegmann A., Lekszas C.,
RA Maroofian R., Karimiani E.G., Bruneel A., Seta N., Munnich A.,
RA Papy-Garcia D., De La Dure-Molla M., Cormier-Daire V.;
RT "SLC10A7 mutations cause a skeletal dysplasia with amelogenesis imperfecta
RT mediated by GAG biosynthesis defects.";
RL Nat. Commun. 9:3087-3087(2018).
RN [5]
RP DEVELOPMENTAL STAGE.
RX PubMed=31191616; DOI=10.3389/fgene.2019.00504;
RA Laugel-Haushalter V., Baer S., Schaefer E., Stoetzel C., Geoffroy V.,
RA Alembik Y., Kharouf N., Huckert M., Hamm P., Hemmerle J., Maniere M.C.,
RA Friant S., Dollfus H., Bloch-Zupan A.;
RT "A new SLC10A7 homozygous missense mutation responsible for a milder
RT phenotype of skeletal dysplasia with amelogenesis imperfecta.";
RL Front. Genet. 10:504-504(2019).
CC -!- FUNCTION: Involved in teeth and skeletal development. Has an essential
CC role in the biosynthesis and trafficking of glycosaminoglycans and
CC glycoproteins to produce a proper functioning extracellular matrix.
CC Required for extracellular matrix mineralization (PubMed:30082715).
CC Also involved in the regulation of cellular calcium homeostasis (By
CC similarity). Does not show transport activity towards bile acids or
CC steroid sulfates (including taurocholate, cholate, chenodeoxycholate,
CC estrone-3-sulfate, dehydroepiandrosterone sulfate (DHEAS) and
CC pregnenolone sulfate). {ECO:0000250|UniProtKB:Q0GE19,
CC ECO:0000269|PubMed:30082715}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q0GE19};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q0GE19}. Endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:Q0GE19}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:Q0GE19}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q0GE19}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5PT53-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5PT53-2; Sequence=VSP_023226;
CC Name=3;
CC IsoId=Q5PT53-3; Sequence=VSP_023225;
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, colon, lung, liver,
CC adrenal gland, stomach and ovary. Also expressed weakly in small
CC intestine. Expressed in skeletal tissues (PubMed:30082715).
CC {ECO:0000269|PubMed:17628207, ECO:0000269|PubMed:30082715}.
CC -!- DEVELOPMENTAL STAGE: Embryos at gestational age 12.5 dpc show the
CC weakest SLC10A7 expression, mainly in the heart trabeculae of the
CC developing heart and the cartilage of the vertebrae. From 14.5 dpc
CC onwards, expression becomes more ubiquitous, with the strongest level
CC observed at 16.5 dpc and postnatal day P0. At 14.5 dpc, it is strongly
CC expressed in cartilaginous structures in the mandible, in the
CC epithelial compartment of cap stage teeth, in the digits, in the spine
CC and in the lung. At 16.5 dpc, transcripts are mostly localized in the
CC inner dental epithelium and in the epithelial loop of bell stage teeth.
CC At 18.5 dpc expression is observed in the inner dental epithelium of
CC incisors, and in ameloblasts and odontoblasts of molars. At postnatal
CC day P0 there is strong expression in the papillary layer of the oral
CC mucous membrane underneath the palate, as well as in the ameloblast
CC layer of emerging teeth. At postnatal day P10, it is localized to the
CC growth plate of several long bones, such as the forefoot digits, the
CC hindfoot tarsals and the humerus, and expression is more intense in the
CC chondrocytes of the hypertrophic zone. {ECO:0000269|PubMed:30082715,
CC ECO:0000269|PubMed:31191616}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice present with skeletal dysplasia
CC including growth retardation at birth and at 8 weeks, alteration of
CC long-bone morphology, craniofacial anomalies and advanced tarsal
CC maturation at birth, associated with enamel defects. The proportion of
CC heparan sulfate (HS) in cartilage of knockout mice is significantly
CC reduced compared with wild-type animals. SLC10A7 deficiency has no
CC impact on skeletal muscle heparan sulfate levels.
CC {ECO:0000269|PubMed:30082715}.
CC -!- SIMILARITY: Belongs to the bile acid:sodium symporter (BASS) (TC
CC 2.A.28) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC30613.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY825926; AAV80709.1; -; mRNA.
DR EMBL; AY825928; AAV80711.1; -; mRNA.
DR EMBL; AK010834; BAB27214.1; -; mRNA.
DR EMBL; AK040517; BAC30613.1; ALT_SEQ; mRNA.
DR EMBL; AK079901; BAC37779.1; -; mRNA.
DR EMBL; AK152752; BAE31467.1; -; mRNA.
DR EMBL; AK152849; BAE31542.1; -; mRNA.
DR EMBL; BC116666; AAI16667.1; -; mRNA.
DR EMBL; BC116717; AAI16718.1; -; mRNA.
DR CCDS; CCDS40395.1; -. [Q5PT53-1]
DR CCDS; CCDS85567.1; -. [Q5PT53-2]
DR CCDS; CCDS85568.1; -. [Q5PT53-3]
DR RefSeq; NP_001009981.1; NM_001009981.2. [Q5PT53-3]
DR RefSeq; NP_001269037.1; NM_001282108.1. [Q5PT53-2]
DR RefSeq; NP_084012.1; NM_029736.2. [Q5PT53-1]
DR AlphaFoldDB; Q5PT53; -.
DR SMR; Q5PT53; -.
DR STRING; 10090.ENSMUSP00000034111; -.
DR MaxQB; Q5PT53; -.
DR PaxDb; Q5PT53; -.
DR PRIDE; Q5PT53; -.
DR ProteomicsDB; 291914; -. [Q5PT53-1]
DR ProteomicsDB; 291915; -. [Q5PT53-2]
DR ProteomicsDB; 291916; -. [Q5PT53-3]
DR Antibodypedia; 27520; 96 antibodies from 21 providers.
DR DNASU; 76775; -.
DR Ensembl; ENSMUST00000034111; ENSMUSP00000034111; ENSMUSG00000031684. [Q5PT53-1]
DR Ensembl; ENSMUST00000209490; ENSMUSP00000148199; ENSMUSG00000031684. [Q5PT53-2]
DR Ensembl; ENSMUST00000209992; ENSMUSP00000147659; ENSMUSG00000031684. [Q5PT53-3]
DR Ensembl; ENSMUST00000211286; ENSMUSP00000147724; ENSMUSG00000031684. [Q5PT53-1]
DR GeneID; 76775; -.
DR KEGG; mmu:76775; -.
DR UCSC; uc009mid.2; mouse. [Q5PT53-1]
DR UCSC; uc012ggi.2; mouse. [Q5PT53-3]
DR UCSC; uc012ggk.2; mouse. [Q5PT53-2]
DR CTD; 84068; -.
DR MGI; MGI:1924025; Slc10a7.
DR VEuPathDB; HostDB:ENSMUSG00000031684; -.
DR eggNOG; KOG4821; Eukaryota.
DR GeneTree; ENSGT00390000011932; -.
DR HOGENOM; CLU_039013_0_0_1; -.
DR InParanoid; Q5PT53; -.
DR OMA; FFFYGLK; -.
DR OrthoDB; 949808at2759; -.
DR PhylomeDB; Q5PT53; -.
DR TreeFam; TF329411; -.
DR BioGRID-ORCS; 76775; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Slc10a7; mouse.
DR PRO; PR:Q5PT53; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q5PT53; protein.
DR Bgee; ENSMUSG00000031684; Expressed in humerus cartilage element and 220 other tissues.
DR ExpressionAtlas; Q5PT53; baseline and differential.
DR Genevisible; Q5PT53; MM.
DR GO; GO:0005801; C:cis-Golgi network; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005797; C:Golgi medial cisterna; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0015125; F:bile acid transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0060348; P:bone development; IMP:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISO:MGI.
DR GO; GO:0034436; P:glycoprotein transport; ISS:UniProtKB.
DR GO; GO:0048193; P:Golgi vesicle transport; ISS:UniProtKB.
DR GO; GO:0030210; P:heparin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1530.20; -; 1.
DR InterPro; IPR038770; Na+/solute_symporter_sf.
DR InterPro; IPR016833; Put_Na-Bile_cotransptr.
DR PANTHER; PTHR18640; PTHR18640; 1.
DR Pfam; PF13593; SBF_like; 1.
DR PIRSF; PIRSF026166; UCP026166; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Endoplasmic reticulum;
KW Golgi apparatus; Ion transport; Membrane; Reference proteome; Sodium;
KW Sodium transport; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..340
FT /note="Sodium/bile acid cotransporter 7"
FT /id="PRO_0000278251"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q0GE19"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..37
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q0GE19"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q0GE19"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..116
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q0GE19"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q0GE19"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..163
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q0GE19"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..201
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q0GE19"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..234
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q0GE19, ECO:0000305"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..270
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q0GE19"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..298
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q0GE19"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 320..340
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q0GE19"
FT VAR_SEQ 158..185
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17628207"
FT /id="VSP_023225"
FT VAR_SEQ 241..283
FT /note="IVSVQLSFMLLTFIFSTRNNSGFTPADTVAIIFCSTHKSLTLG -> R (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023226"
FT CONFLICT 144
FT /note="F -> V (in Ref. 2; BAB27214)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 340 AA; 37256 MW; E373F9E2F4848A5C CRC64;
MRLLERARKE WFMVGIVVAI GAAKLEPSVG VNGGPLKPEI TVSYIAVATI FFNSGLSLKT
EELTSALVHL RLHLFIQIFT LAFFPAAIWL FLQLLSVTSI NEWLLKGLQT VGCMPPPVSS
AVILTKAVGG NEAAAIFNSA FGSFLGIVVT PVLLLLFLGS SSSVPFTSIF SQLFMTVVVP
LVIGQIVRRY IKDWLERKKP PFGVVSSSVL LMIIYTTFCD TFSNPNIDLD KFSLILILFI
IVSVQLSFML LTFIFSTRNN SGFTPADTVA IIFCSTHKSL TLGIPMLKIV FAGHEHLSLI
SVPLLIYHPA QILLGSVLVP TIKSWMVSRQ KGVKLTRPTV
