S38A7_HUMAN
ID S38A7_HUMAN Reviewed; 462 AA.
AC Q9NVC3; Q53GJ9; Q9H9I5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 154.
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 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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Teratocarcinoma;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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-28, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Mediates sodium-dependent transport of amino acids,
CC preferentially L-glutamine. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9NVC3; Q5T8D3-2: ACBD5; NbExp=3; IntAct=EBI-10314552, EBI-10961679;
CC Q9NVC3; Q86WK6: AMIGO1; NbExp=3; IntAct=EBI-10314552, EBI-19125216;
CC Q9NVC3; Q96BI3: APH1A; NbExp=3; IntAct=EBI-10314552, EBI-2606935;
CC Q9NVC3; P41181: AQP2; NbExp=3; IntAct=EBI-10314552, EBI-12701138;
CC Q9NVC3; O43315: AQP9; NbExp=3; IntAct=EBI-10314552, EBI-17444777;
CC Q9NVC3; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-10314552, EBI-11343438;
CC Q9NVC3; Q6UXG8-3: BTNL9; NbExp=3; IntAct=EBI-10314552, EBI-17953245;
CC Q9NVC3; P51798: CLCN7; NbExp=3; IntAct=EBI-10314552, EBI-4402346;
CC Q9NVC3; O95471: CLDN7; NbExp=3; IntAct=EBI-10314552, EBI-740744;
CC Q9NVC3; Q8IUN9: CLEC10A; NbExp=3; IntAct=EBI-10314552, EBI-2873246;
CC Q9NVC3; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-10314552, EBI-18013275;
CC Q9NVC3; Q68CJ9: CREB3L3; NbExp=3; IntAct=EBI-10314552, EBI-852194;
CC Q9NVC3; P49447: CYB561; NbExp=3; IntAct=EBI-10314552, EBI-8646596;
CC Q9NVC3; P00387: CYB5R3; NbExp=3; IntAct=EBI-10314552, EBI-1046040;
CC Q9NVC3; Q15125: EBP; NbExp=3; IntAct=EBI-10314552, EBI-3915253;
CC Q9NVC3; Q92838: EDA; NbExp=3; IntAct=EBI-10314552, EBI-529425;
CC Q9NVC3; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-10314552, EBI-781551;
CC Q9NVC3; P30040: ERP29; NbExp=3; IntAct=EBI-10314552, EBI-946830;
CC Q9NVC3; P34910-2: EVI2B; NbExp=3; IntAct=EBI-10314552, EBI-17640610;
CC Q9NVC3; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-10314552, EBI-18304435;
CC Q9NVC3; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-10314552, EBI-3918971;
CC Q9NVC3; P48165: GJA8; NbExp=3; IntAct=EBI-10314552, EBI-17458373;
CC Q9NVC3; O95377: GJB5; NbExp=3; IntAct=EBI-10314552, EBI-3909454;
CC Q9NVC3; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-10314552, EBI-13345167;
CC Q9NVC3; O15529: GPR42; NbExp=3; IntAct=EBI-10314552, EBI-18076404;
CC Q9NVC3; Q9UM44: HHLA2; NbExp=3; IntAct=EBI-10314552, EBI-2867874;
CC Q9NVC3; Q13651: IL10RA; NbExp=3; IntAct=EBI-10314552, EBI-1031656;
CC Q9NVC3; P43628: KIR2DL3; NbExp=3; IntAct=EBI-10314552, EBI-8632435;
CC Q9NVC3; O95867: LY6G6C; NbExp=3; IntAct=EBI-10314552, EBI-9088345;
CC Q9NVC3; Q9Y5Y7: LYVE1; NbExp=3; IntAct=EBI-10314552, EBI-10329546;
CC Q9NVC3; Q8N4V1: MMGT1; NbExp=3; IntAct=EBI-10314552, EBI-6163737;
CC Q9NVC3; P15941-11: MUC1; NbExp=3; IntAct=EBI-10314552, EBI-17263240;
CC Q9NVC3; Q2M2E3: ODF4; NbExp=3; IntAct=EBI-10314552, EBI-12382569;
CC Q9NVC3; P35372-10: OPRM1; NbExp=3; IntAct=EBI-10314552, EBI-12807478;
CC Q9NVC3; Q96RD7: PANX1; NbExp=3; IntAct=EBI-10314552, EBI-7037612;
CC Q9NVC3; Q9BQ51: PDCD1LG2; NbExp=3; IntAct=EBI-10314552, EBI-16427978;
CC Q9NVC3; Q99942: RNF5; NbExp=8; IntAct=EBI-10314552, EBI-348482;
CC Q9NVC3; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-10314552, EBI-3920694;
CC Q9NVC3; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-10314552, EBI-17247926;
CC Q9NVC3; Q8N6R1: SERP2; NbExp=3; IntAct=EBI-10314552, EBI-749270;
CC Q9NVC3; Q3SXP7: SHISAL1; NbExp=3; IntAct=EBI-10314552, EBI-18037857;
CC Q9NVC3; Q14973: SLC10A1; NbExp=3; IntAct=EBI-10314552, EBI-3923031;
CC Q9NVC3; P54219-3: SLC18A1; NbExp=3; IntAct=EBI-10314552, EBI-17595455;
CC Q9NVC3; Q9BRI3: SLC30A2; NbExp=3; IntAct=EBI-10314552, EBI-8644112;
CC Q9NVC3; Q9H2J7: SLC6A15; NbExp=3; IntAct=EBI-10314552, EBI-11343466;
CC Q9NVC3; O43278-2: SPINT1; NbExp=3; IntAct=EBI-10314552, EBI-12078338;
CC Q9NVC3; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-10314552, EBI-17280858;
CC Q9NVC3; Q5VXT5-2: SYPL2; NbExp=3; IntAct=EBI-10314552, EBI-18196631;
CC Q9NVC3; Q96Q45-2: TMEM237; NbExp=5; IntAct=EBI-10314552, EBI-10982110;
CC Q9NVC3; Q4KMG9: TMEM52B; NbExp=3; IntAct=EBI-10314552, EBI-18178701;
CC Q9NVC3; O15393-2: TMPRSS2; NbExp=3; IntAct=EBI-10314552, EBI-12345267;
CC Q9NVC3; P19075: TSPAN8; NbExp=3; IntAct=EBI-10314552, EBI-4289938;
CC Q9NVC3; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-10314552, EBI-751210;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Note=In neurons, located in soma and axons.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NVC3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NVC3-2; Sequence=VSP_031511;
CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC {ECO:0000305}.
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DR EMBL; AK001677; BAA91830.1; -; mRNA.
DR EMBL; AK022786; BAB14244.1; -; mRNA.
DR EMBL; CR457236; CAG33517.1; -; mRNA.
DR EMBL; AK222932; BAD96652.1; -; mRNA.
DR EMBL; CH471092; EAW82985.1; -; Genomic_DNA.
DR EMBL; BC001961; AAH01961.1; -; mRNA.
DR CCDS; CCDS10800.1; -. [Q9NVC3-1]
DR RefSeq; NP_060701.1; NM_018231.2. [Q9NVC3-1]
DR RefSeq; XP_016878882.1; XM_017023393.1.
DR RefSeq; XP_016878886.1; XM_017023397.1.
DR AlphaFoldDB; Q9NVC3; -.
DR SMR; Q9NVC3; -.
DR BioGRID; 120531; 65.
DR IntAct; Q9NVC3; 63.
DR STRING; 9606.ENSP00000454646; -.
DR TCDB; 2.A.18.6.13; the amino acid/auxin permease (aaap) family.
DR iPTMnet; Q9NVC3; -.
DR PhosphoSitePlus; Q9NVC3; -.
DR BioMuta; SLC38A7; -.
DR DMDM; 74734488; -.
DR EPD; Q9NVC3; -.
DR jPOST; Q9NVC3; -.
DR MassIVE; Q9NVC3; -.
DR MaxQB; Q9NVC3; -.
DR PaxDb; Q9NVC3; -.
DR PeptideAtlas; Q9NVC3; -.
DR PRIDE; Q9NVC3; -.
DR ProteomicsDB; 82775; -. [Q9NVC3-1]
DR ProteomicsDB; 82776; -. [Q9NVC3-2]
DR Antibodypedia; 48949; 36 antibodies from 11 providers.
DR DNASU; 55238; -.
DR Ensembl; ENST00000219320.9; ENSP00000219320.3; ENSG00000103042.9. [Q9NVC3-1]
DR Ensembl; ENST00000570101.5; ENSP00000454646.1; ENSG00000103042.9. [Q9NVC3-1]
DR GeneID; 55238; -.
DR KEGG; hsa:55238; -.
DR MANE-Select; ENST00000219320.9; ENSP00000219320.3; NM_018231.3; NP_060701.1.
DR UCSC; uc002eod.2; human. [Q9NVC3-1]
DR CTD; 55238; -.
DR DisGeNET; 55238; -.
DR GeneCards; SLC38A7; -.
DR HGNC; HGNC:25582; SLC38A7.
DR HPA; ENSG00000103042; Tissue enhanced (testis).
DR MIM; 614236; gene.
DR neXtProt; NX_Q9NVC3; -.
DR OpenTargets; ENSG00000103042; -.
DR PharmGKB; PA162403772; -.
DR VEuPathDB; HostDB:ENSG00000103042; -.
DR eggNOG; KOG1305; Eukaryota.
DR GeneTree; ENSGT00940000158136; -.
DR InParanoid; Q9NVC3; -.
DR OMA; FAFTGHQ; -.
DR OrthoDB; 697331at2759; -.
DR PhylomeDB; Q9NVC3; -.
DR TreeFam; TF328787; -.
DR PathwayCommons; Q9NVC3; -.
DR SignaLink; Q9NVC3; -.
DR BioGRID-ORCS; 55238; 63 hits in 1080 CRISPR screens.
DR ChiTaRS; SLC38A7; human.
DR GenomeRNAi; 55238; -.
DR Pharos; Q9NVC3; Tdark.
DR PRO; PR:Q9NVC3; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9NVC3; protein.
DR Bgee; ENSG00000103042; Expressed in sperm and 177 other tissues.
DR ExpressionAtlas; Q9NVC3; baseline and differential.
DR Genevisible; Q9NVC3; HS.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0015180; F:L-alanine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015182; F:L-asparagine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015183; F:L-aspartate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005313; F:L-glutamate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015186; F:L-glutamine transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0005290; F:L-histidine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015190; F:L-leucine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015191; F:L-methionine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015194; F:L-serine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:0006814; P:sodium ion transport; ISS:UniProtKB.
DR InterPro; IPR013057; AA_transpt_TM.
DR Pfam; PF01490; Aa_trans; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Amino-acid transport; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Sodium; Sodium transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..462
FT /note="Putative sodium-coupled neutral amino acid
FT transporter 7"
FT /id="PRO_0000319597"
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 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..448
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 345..462
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_031511"
FT VARIANT 46
FT /note="L -> P (in dbSNP:rs7193572)"
FT /id="VAR_039015"
FT VARIANT 78
FT /note="T -> I (in dbSNP:rs7191331)"
FT /id="VAR_039016"
FT CONFLICT 145
FT /note="A -> T (in Ref. 1; BAB14244)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="V -> A (in Ref. 3; BAD96652)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 462 AA; 49966 MW; B4F46C19D7E6EADB CRC64;
MAQVSINNDY SEWDLSTDAG ERARLLQSPC VDTAPKSEWE ASPGGLDRGT TSTLGAIFIV
VNACLGAGLL NFPAAFSTAG GVAAGIALQM GMLVFIISGL VILAYCSQAS NERTYQEVVW
AVCGKLTGVL CEVAIAVYTF GTCIAFLIII GDQQDKIIAV MAKEPEGASG PWYTDRKFTI
SLTAFLFILP LSIPREIGFQ KYASFLSVVG TWYVTAIVII KYIWPDKEMT PGNILTRPAS
WMAVFNAMPT ICFGFQCHVS SVPVFNSMQQ PEVKTWGGVV TAAMVIALAV YMGTGICGFL
TFGAAVDPDV LLSYPSEDMA VAVARAFIIL SVLTSYPILH FCGRAVVEGL WLRYQGVPVE
EDVGRERRRR VLQTLVWFLL TLLLALFIPD IGKVISVIGG LAACFIFVFP GLCLIQAKLS
EMEEVKPASW WVLVSYGVLL VTLGAFIFGQ TTANAIFVDL LA
