MOT10_MOUSE
ID MOT10_MOUSE Reviewed; 512 AA.
AC Q3U9N9; Q3TNJ1; Q3UAN9; Q8BWR7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Monocarboxylate transporter 10;
DE Short=MCT 10;
DE AltName: Full=Aromatic amino acid transporter 1;
DE AltName: Full=Solute carrier family 16 member 10;
DE AltName: Full=T-type amino acid transporter 1;
GN Name=Slc16a10; Synonyms=Mct10, Tat1;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Spleen;
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 [2]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION, AND LACK OF
RP GLYCOSYLATION.
RX PubMed=16245314; DOI=10.1002/jcp.20531;
RA Ramadan T., Camargo S.M., Summa V., Hunziker P., Chesnov S., Pos K.M.,
RA Verrey F.;
RT "Basolateral aromatic amino acid transporter TAT1 (Slc16a10) functions as
RT an efflux pathway.";
RL J. Cell. Physiol. 206:771-779(2006).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495; SER-498 AND SER-501, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498; SER-500 AND SER-501, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Sodium-independent transporter that mediates the uptake of
CC aromatic acids. Can function as a net efflux pathway for aromatic amino
CC acids in the basosolateral epithelial cells.
CC {ECO:0000269|PubMed:16245314}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16245314};
CC Multi-pass membrane protein {ECO:0000269|PubMed:16245314}. Basolateral
CC cell membrane {ECO:0000269|PubMed:16245314}. Note=Detected in
CC basolateral membrane of kidney proximal tubule starting at he beginning
CC of the proximal tubule epithelium within the glomerular capsule and
CC extending to the S1 and S2 segments. Localizes also to the basolateral
CC membrane of small intestine enterocytes and to sinusoidal side of
CC perivenous hepatocytes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3U9N9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3U9N9-2; Sequence=VSP_030252, VSP_030253;
CC -!- TISSUE SPECIFICITY: Highly expressed in small intestine, particularly
CC in jejunum and ileum, scarcely in colon and substantially in kidney,
CC liver and skeletal muscle. {ECO:0000269|PubMed:16245314}.
CC -!- PTM: Not N-glycosylated.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC Monocarboxylate porter (TC 2.A.1.13) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE38097.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK050229; BAC34135.1; -; mRNA.
DR EMBL; AK151290; BAE30275.1; -; mRNA.
DR EMBL; AK151704; BAE30627.1; -; mRNA.
DR EMBL; AK157355; BAE34061.1; -; mRNA.
DR EMBL; AK165240; BAE38097.1; ALT_INIT; mRNA.
DR EMBL; AK165579; BAE38270.1; -; mRNA.
DR CCDS; CCDS48543.1; -. [Q3U9N9-1]
DR CCDS; CCDS87990.1; -. [Q3U9N9-2]
DR RefSeq; NP_001107804.1; NM_001114332.1. [Q3U9N9-1]
DR RefSeq; NP_082523.1; NM_028247.4. [Q3U9N9-2]
DR AlphaFoldDB; Q3U9N9; -.
DR SMR; Q3U9N9; -.
DR STRING; 10090.ENSMUSP00000090227; -.
DR iPTMnet; Q3U9N9; -.
DR PhosphoSitePlus; Q3U9N9; -.
DR EPD; Q3U9N9; -.
DR jPOST; Q3U9N9; -.
DR MaxQB; Q3U9N9; -.
DR PaxDb; Q3U9N9; -.
DR PeptideAtlas; Q3U9N9; -.
DR PRIDE; Q3U9N9; -.
DR ProteomicsDB; 291482; -. [Q3U9N9-1]
DR ProteomicsDB; 291483; -. [Q3U9N9-2]
DR Antibodypedia; 19300; 123 antibodies from 21 providers.
DR DNASU; 72472; -.
DR Ensembl; ENSMUST00000092566; ENSMUSP00000090227; ENSMUSG00000019838. [Q3U9N9-1]
DR Ensembl; ENSMUST00000213488; ENSMUSP00000150416; ENSMUSG00000019838. [Q3U9N9-2]
DR GeneID; 72472; -.
DR KEGG; mmu:72472; -.
DR UCSC; uc007ewm.2; mouse. [Q3U9N9-1]
DR UCSC; uc007ewn.2; mouse. [Q3U9N9-2]
DR CTD; 117247; -.
DR MGI; MGI:1919722; Slc16a10.
DR VEuPathDB; HostDB:ENSMUSG00000019838; -.
DR eggNOG; KOG2504; Eukaryota.
DR GeneTree; ENSGT00940000157966; -.
DR HOGENOM; CLU_001265_59_1_1; -.
DR InParanoid; Q3U9N9; -.
DR OMA; LSYRIWA; -.
DR OrthoDB; 916876at2759; -.
DR PhylomeDB; Q3U9N9; -.
DR TreeFam; TF313792; -.
DR Reactome; R-MMU-352230; Amino acid transport across the plasma membrane.
DR BioGRID-ORCS; 72472; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Slc16a10; mouse.
DR PRO; PR:Q3U9N9; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q3U9N9; protein.
DR Bgee; ENSMUSG00000019838; Expressed in small intestine Peyer's patch and 159 other tissues.
DR ExpressionAtlas; Q3U9N9; baseline and differential.
DR Genevisible; Q3U9N9; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0015173; F:aromatic amino acid transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015349; F:thyroid hormone transmembrane transporter activity; ISO:MGI.
DR GO; GO:0006590; P:thyroid hormone generation; IGI:MGI.
DR GO; GO:0070327; P:thyroid hormone transport; IGI:MGI.
DR GO; GO:0070460; P:thyroid-stimulating hormone secretion; IGI:MGI.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR030762; MCT10.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR11360:SF119; PTHR11360:SF119; 1.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..512
FT /note="Monocarboxylate transporter 10"
FT /id="PRO_0000314254"
FT TOPO_DOM 1..63
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..469
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 470..512
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91Y77"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 312..320
FT /note="MNHVKERFQ -> VSMHLWLCL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030252"
FT VAR_SEQ 321..512
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030253"
FT CONFLICT 211
FT /note="T -> I (in Ref. 1; BAE30275)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 512 AA; 55320 MW; 4EF7A1400C8E0B04 CRC64;
MVPSQEEPAA ERETNEAQPP GPAPSDDAPL PGPGPSDVSD VAAEKVEVEL TRSAGSEPPV
PPEGGWGWLV MLAAMWCNGS VFGIQNAYGV LFVSMLDTFK AKDDDNMAFK TAWVGSLSMG
MIFFCCPIVS VFTDMFGCRR TAVVGAAVGF IGLMSSSFVS SIEPLYLTYG IIFACGCSFA
YQPSLVILGH YFKKRLGLVN GIVTAGSSVF TILLPLLLGN LISSVKLFNT LRILCIFMFV
LFLAGFTYRP LVPSTKEKES GGSRSSFFSR RKLSPPKKVF NFALFKETTY AVWAAGIPLA
LFGYFVPYVH LMNHVKERFQ DVNNKEVLFM CIGITSGVGR LLFGRIADYL PGVKKVYLQV
LSFFFIGLMS MMIPLCSAFG ALIAVCLAMG LFDGCFISIM APIAFELVGP QDASQAIGFL
LGFMSIPMTV GPPIAGLLHD KLGTYDVAFY LAGIPPFVGG VVLCLIPWIH SKKQRKISKN
AGGEKMEKML ENQSSLLSGS SGIFKKDSAS II
