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   27-MAR-2024, entry version 126.
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)
CC       (TC 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; 10090-ENSMUSP00000034111; -.
DR   ProteomicsDB; 291914; -. [Q5PT53-1]
DR   ProteomicsDB; 291915; -. [Q5PT53-2]
DR   ProteomicsDB; 291916; -. [Q5PT53-3]
DR   Antibodypedia; 27520; 112 antibodies from 21 providers.
DR   DNASU; 76775; -.
DR   Ensembl; ENSMUST00000034111.10; ENSMUSP00000034111.9; ENSMUSG00000031684.12. [Q5PT53-1]
DR   Ensembl; ENSMUST00000209490.2; ENSMUSP00000148199.2; ENSMUSG00000031684.12. [Q5PT53-2]
DR   Ensembl; ENSMUST00000209992.2; ENSMUSP00000147659.2; ENSMUSG00000031684.12. [Q5PT53-3]
DR   Ensembl; ENSMUST00000211286.2; ENSMUSP00000147724.2; ENSMUSG00000031684.12. [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   AGR; MGI:1924025; -.
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; 3290500at2759; -.
DR   PhylomeDB; Q5PT53; -.
DR   TreeFam; TF329411; -.
DR   BioGRID-ORCS; 76775; 4 hits in 79 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 223 other cell types or tissues.
DR   ExpressionAtlas; Q5PT53; baseline and differential.
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:0005886; C:plasma membrane; ISS:UniProtKB.
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: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:0006874; P:intracellular calcium ion homeostasis; ISO:MGI.
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:SF5; SODIUM_BILE ACID COTRANSPORTER 7; 1.
DR   PANTHER; PTHR18640; SOLUTE CARRIER FAMILY 10 MEMBER 7; 1.
DR   Pfam; PF13593; SBF_like; 1.
DR   PIRSF; PIRSF026166; UCP026166; 1.
DR   Genevisible; Q5PT53; MM.
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
//