S38A7_MOUSE
ID S38A7_MOUSE Reviewed; 463 AA.
AC Q8BWH0; Q3TBN9; Q8K2B1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Putative sodium-coupled neutral amino acid transporter 7;
DE AltName: Full=Solute carrier family 38 member 7;
GN Name=Slc38a7; Synonyms=Snat7;
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].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Lung;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21511949; DOI=10.1074/jbc.m110.162404;
RA Hagglund M.G., Sreedharan S., Nilsson V.C., Shaik J.H., Almkvist I.M.,
RA Backlin S., Wrange O., Fredriksson R.;
RT "Identification of SLC38A7 (SNAT7) protein as a glutamine transporter
RT expressed in neurons.";
RL J. Biol. Chem. 286:20500-20511(2011).
CC -!- FUNCTION: Mediates sodium-dependent transport of amino acids. Substrate
CC preference is ranked l-glutamine > l-histidine > l-serine > l-alanine >
CC l-asparagine > l-aspartic acid > l-glutamic acid > l-methionine > l-
CC leucine > l-glycine. {ECO:0000269|PubMed:21511949}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:21511949}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:21511949}. Note=In neurons,
CC located in soma and axons.
CC -!- TISSUE SPECIFICITY: Highly expressed in the brain, including the
CC hippocampus, especially in the granular layer of dentate gyrus cells
CC and the pyramidal cell layer of the hippocampus, amygdala, thalamus,
CC hypothalamus, in the layer of Purkinje cells in the cerebellum and the
CC layers of cortex. Particularly strong expression in neurons of the
CC ventromedial hypothalamus, basolateral amygdala, ventral tegmental
CC area, and locus coeruleus. Not detected in glial cells, including
CC astrocytes. In addition to brain, also expressed in the spinal cord (at
CC protein level). {ECO:0000269|PubMed:21511949}.
CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC {ECO:0000305}.
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DR EMBL; AK052548; BAC35035.1; -; mRNA.
DR EMBL; AK171137; BAE42270.1; -; mRNA.
DR EMBL; BC031853; AAH31853.1; -; mRNA.
DR CCDS; CCDS22567.1; -.
DR RefSeq; NP_766346.1; NM_172758.4.
DR RefSeq; XP_006530939.1; XM_006530876.3.
DR RefSeq; XP_006530940.1; XM_006530877.2.
DR AlphaFoldDB; Q8BWH0; -.
DR SMR; Q8BWH0; -.
DR STRING; 10090.ENSMUSP00000037023; -.
DR iPTMnet; Q8BWH0; -.
DR PhosphoSitePlus; Q8BWH0; -.
DR MaxQB; Q8BWH0; -.
DR PaxDb; Q8BWH0; -.
DR PeptideAtlas; Q8BWH0; -.
DR PRIDE; Q8BWH0; -.
DR ProteomicsDB; 256892; -.
DR Antibodypedia; 48949; 36 antibodies from 11 providers.
DR DNASU; 234595; -.
DR Ensembl; ENSMUST00000040481; ENSMUSP00000037023; ENSMUSG00000036534.
DR Ensembl; ENSMUST00000212270; ENSMUSP00000148659; ENSMUSG00000036534.
DR GeneID; 234595; -.
DR KEGG; mmu:234595; -.
DR UCSC; uc009mzg.1; mouse.
DR CTD; 55238; -.
DR MGI; MGI:2679005; Slc38a7.
DR VEuPathDB; HostDB:ENSMUSG00000036534; -.
DR eggNOG; KOG1305; Eukaryota.
DR GeneTree; ENSGT00940000158136; -.
DR HOGENOM; CLU_038973_0_0_1; -.
DR InParanoid; Q8BWH0; -.
DR OMA; FAFTGHQ; -.
DR OrthoDB; 697331at2759; -.
DR PhylomeDB; Q8BWH0; -.
DR TreeFam; TF328787; -.
DR BioGRID-ORCS; 234595; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Slc38a7; mouse.
DR PRO; PR:Q8BWH0; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8BWH0; protein.
DR Bgee; ENSMUSG00000036534; Expressed in chest bone and 246 other tissues.
DR ExpressionAtlas; Q8BWH0; baseline and differential.
DR Genevisible; Q8BWH0; MM.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0015180; F:L-alanine transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015182; F:L-asparagine transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015183; F:L-aspartate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005313; F:L-glutamate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015186; F:L-glutamine transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005290; F:L-histidine transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015190; F:L-leucine transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015191; F:L-methionine transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015194; F:L-serine transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:0006814; P:sodium ion transport; IDA:UniProtKB.
DR InterPro; IPR013057; AA_transpt_TM.
DR Pfam; PF01490; Aa_trans; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; Sodium; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..463
FT /note="Putative sodium-coupled neutral amino acid
FT transporter 7"
FT /id="PRO_0000319598"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NVC3"
FT CONFLICT 11
FT /note="S -> SG (in Ref. 2; AAH31853)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="C -> R (in Ref. 1; BAE42270)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="A -> V (in Ref. 2; AAH31853)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 463 AA; 49913 MW; 3DF98B8EAE2E12E3 CRC64;
MAQVSINSDY SEWASSTDAG ERARLLQSPC VDVVPKSEGE ASPGDPDSGT TSTLGAVFIV
VNACLGAGLL NFPAAFSTAG GVAAGIALQM GMLVFIISGL VILAYCSQAS NERTYQEVVW
AVCGKLTGVL CEVAIAVYTF GTCIAFLIII GDQQDKIIAV MSKEPDGASG SPWYTDRKFT
ISLTAFLFIL PLSIPKEIGF QKYASFLSVV GTWYVTAIII IKYIWPDKEM RPGDILTRPA
SWMAVFNAMP TICFGFQCHV SSVPVFNSMR QPEVKTWGGV VTAAMVIALA VYMGTGICGF
LTFGAAVDPD VLRSYPSEDV AVAVARAFII LSVLTSYPIL HFCGRAVVEG LWLRYKGMPV
EEDVGRERRR RVLQTLVWFL LTLLLALFIP DIGKVISVIG GLAACFIFIF PGLCLIQAKL
SEMEEVKPAS WWALVSYGVL LVTLGAFIFG QTTANAIFVD LLA
