MOT10_HUMAN
ID MOT10_HUMAN Reviewed; 515 AA.
AC Q8TF71; B3KWY0; Q6ZMG0; Q8WVI5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 157.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP FUNCTION.
RC TISSUE=Thymus;
RX PubMed=11827462; DOI=10.1006/geno.2001.6678;
RA Kim D.K., Kanai Y., Matsuo H., Kim J.Y., Chairoungdua A., Kobayashi Y.,
RA Enomoto A., Cha S.H., Goya T., Endou H.;
RT "The human T-type amino acid transporter-1: characterization, gene
RT organization, and chromosomal location.";
RL Genomics 79:95-103(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, Prostate, and Testis;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498 AND SER-501, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
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 (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:11827462}.
CC -!- INTERACTION:
CC Q8TF71; Q9BWH2: FUNDC2; NbExp=3; IntAct=EBI-17858931, EBI-714482;
CC Q8TF71; Q9Y5U4: INSIG2; NbExp=3; IntAct=EBI-17858931, EBI-8503746;
CC Q8TF71; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-17858931, EBI-8638294;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11827462};
CC Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in kidney and skeletal muscle
CC and at lower level in placenta and heart.
CC {ECO:0000269|PubMed:11827462}.
CC -!- PTM: Not N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC Monocarboxylate porter (TC 2.A.1.13) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH17968.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB057445; BAB84670.1; -; mRNA.
DR EMBL; AK126183; BAG54292.1; -; mRNA.
DR EMBL; AK172789; BAD18768.1; -; mRNA.
DR EMBL; AL360227; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48298.1; -; Genomic_DNA.
DR EMBL; BC017968; AAH17968.1; ALT_INIT; mRNA.
DR EMBL; BC066985; AAH66985.1; -; mRNA.
DR CCDS; CCDS5089.1; -.
DR RefSeq; NP_061063.2; NM_018593.4.
DR AlphaFoldDB; Q8TF71; -.
DR SMR; Q8TF71; -.
DR BioGRID; 125582; 33.
DR IntAct; Q8TF71; 15.
DR STRING; 9606.ENSP00000357844; -.
DR DrugBank; DB02952; 2-aminoisobutyric acid.
DR DrugBank; DB00160; Alanine.
DR DrugBank; DB00125; Arginine.
DR DrugBank; DB00174; Asparagine.
DR DrugBank; DB00128; Aspartic acid.
DR DrugBank; DB03107; beta-Alanine.
DR DrugBank; DB00151; Cysteine.
DR DrugBank; DB00138; Cystine.
DR DrugBank; DB01786; D-Alanine.
DR DrugBank; DB01746; D-Leucine.
DR DrugBank; DB02556; D-Phenylalanine.
DR DrugBank; DB03929; D-Serine.
DR DrugBank; DB03225; D-Tryptophan.
DR DrugBank; DB03839; D-Tyrosine.
DR DrugBank; DB06262; Droxidopa.
DR DrugBank; DB00142; Glutamic acid.
DR DrugBank; DB00145; Glycine.
DR DrugBank; DB00117; Histidine.
DR DrugBank; DB00167; Isoleucine.
DR DrugBank; DB00130; L-Glutamine.
DR DrugBank; DB04398; Lactic acid.
DR DrugBank; DB00149; Leucine.
DR DrugBank; DB01235; Levodopa.
DR DrugBank; DB00279; Liothyronine.
DR DrugBank; DB01583; Liotrix.
DR DrugBank; DB00123; Lysine.
DR DrugBank; DB00134; Methionine.
DR DrugBank; DB00120; Phenylalanine.
DR DrugBank; DB00172; Proline.
DR DrugBank; DB00119; Pyruvic acid.
DR DrugBank; DB00133; Serine.
DR DrugBank; DB00156; Threonine.
DR DrugBank; DB00150; Tryptophan.
DR DrugBank; DB00135; Tyrosine.
DR DrugBank; DB00161; Valine.
DR TCDB; 2.A.1.13.8; the major facilitator superfamily (mfs).
DR iPTMnet; Q8TF71; -.
DR PhosphoSitePlus; Q8TF71; -.
DR BioMuta; SLC16A10; -.
DR DMDM; 74751472; -.
DR EPD; Q8TF71; -.
DR jPOST; Q8TF71; -.
DR MassIVE; Q8TF71; -.
DR MaxQB; Q8TF71; -.
DR PaxDb; Q8TF71; -.
DR PeptideAtlas; Q8TF71; -.
DR PRIDE; Q8TF71; -.
DR ProteomicsDB; 74571; -.
DR Antibodypedia; 19300; 123 antibodies from 21 providers.
DR DNASU; 117247; -.
DR Ensembl; ENST00000368851.10; ENSP00000357844.4; ENSG00000112394.18.
DR GeneID; 117247; -.
DR KEGG; hsa:117247; -.
DR MANE-Select; ENST00000368851.10; ENSP00000357844.4; NM_018593.5; NP_061063.2.
DR UCSC; uc003pus.4; human.
DR CTD; 117247; -.
DR DisGeNET; 117247; -.
DR GeneCards; SLC16A10; -.
DR HGNC; HGNC:17027; SLC16A10.
DR HPA; ENSG00000112394; Tissue enhanced (choroid plexus, pancreas, skeletal muscle).
DR MIM; 607550; gene.
DR neXtProt; NX_Q8TF71; -.
DR OpenTargets; ENSG00000112394; -.
DR PharmGKB; PA38197; -.
DR VEuPathDB; HostDB:ENSG00000112394; -.
DR eggNOG; KOG2504; Eukaryota.
DR GeneTree; ENSGT00940000157966; -.
DR HOGENOM; CLU_001265_59_1_1; -.
DR InParanoid; Q8TF71; -.
DR OMA; LSYRIWA; -.
DR OrthoDB; 916876at2759; -.
DR PhylomeDB; Q8TF71; -.
DR TreeFam; TF313792; -.
DR PathwayCommons; Q8TF71; -.
DR Reactome; R-HSA-352230; Amino acid transport across the plasma membrane.
DR SignaLink; Q8TF71; -.
DR BioGRID-ORCS; 117247; 10 hits in 1073 CRISPR screens.
DR ChiTaRS; SLC16A10; human.
DR GeneWiki; SLC16A10; -.
DR GenomeRNAi; 117247; -.
DR Pharos; Q8TF71; Tbio.
DR PRO; PR:Q8TF71; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q8TF71; protein.
DR Bgee; ENSG00000112394; Expressed in gastrocnemius and 134 other tissues.
DR ExpressionAtlas; Q8TF71; baseline and differential.
DR Genevisible; Q8TF71; HS.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
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; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; TAS:Reactome.
DR GO; GO:0015173; F:aromatic amino acid transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015349; F:thyroid hormone transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0006865; P:amino acid transport; TAS:Reactome.
DR GO; GO:0015801; P:aromatic amino acid transport; TAS:HGNC-UCL.
DR GO; GO:0006590; P:thyroid hormone generation; IEA:Ensembl.
DR GO; GO:0070327; P:thyroid hormone transport; IDA:ARUK-UCL.
DR GO; GO:0070460; P:thyroid-stimulating hormone secretion; IEA:Ensembl.
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 Cell membrane; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..515
FT /note="Monocarboxylate transporter 10"
FT /id="PRO_0000314253"
FT TOPO_DOM 1..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 473..515
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..37
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91Y77"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U9N9"
FT MOD_RES 504
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U9N9"
FT VARIANT 508
FT /note="K -> Q (in dbSNP:rs17072442)"
FT /id="VAR_037874"
FT CONFLICT 422
FT /note="F -> L (in Ref. 5; AAH17968)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="M -> T (in Ref. 2; BAD18768)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="D -> G (in Ref. 2; BAD18768)"
FT /evidence="ECO:0000305"
FT CONFLICT 508
FT /note="K -> E (in Ref. 5; AAH17968)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 515 AA; 55493 MW; A870E4DDC26B918E CRC64;
MVLSQEEPDS ARGTSEAQPL GPAPTGAAPP PGPGPSDSPE AAVEKVEVEL AGPATAEPHE
PPEPPEGGWG WLVMLAAMWC NGSVFGIQNA CGVLFVSMLE TFGSKDDDKM VFKTAWVGSL
SMGMIFFCCP IVSVFTDLFG CRKTAVVGAA VGFVGLMSSS FVSSIEPLYL TYGIIFACGC
SFAYQPSLVI LGHYFKKRLG LVNGIVTAGS SVFTILLPLL LRVLIDSVGL FYTLRVLCIF
MFVLFLAGFT YRPLATSTKD KESGGSGSSL FSRKKFSPPK KIFNFAIFKV TAYAVWAVGI
PLALFGYFVP YVHLMKHVNE RFQDEKNKEV VLMCIGVTSG VGRLLFGRIA DYVPGVKKVY
LQVLSFFFIG LMSMMIPLCS IFGALIAVCL IMGLFDGCFI SIMAPIAFEL VGAQDVSQAI
GFLLGFMSIP MTVGPPIAGL LRDKLGSYDV AFYLAGVPPL IGGAVLCFIP WIHSKKQREI
SKTTGKEKME KMLENQNSLL SSSSGMFKKE SDSII
