YLAT1_MOUSE
ID YLAT1_MOUSE Reviewed; 510 AA.
AC Q9Z1K8; Q9QWS1;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Y+L amino acid transporter 1;
DE AltName: Full=Solute carrier family 7 member 7;
DE AltName: Full=y(+)L-type amino acid transporter 1;
DE Short=Y+LAT1;
DE Short=y+LAT-1;
GN Name=Slc7a7;
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], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, TISSUE SPECIFICITY, AND VARIANT THR-4.
RC STRAIN=BALB/cJ, and NIH Swiss; TISSUE=Heart, and Kidney;
RX PubMed=9878049; DOI=10.1093/emboj/18.1.49;
RA Pfeiffer R., Rossier G., Spindler B., Meier C., Kuehn L.C., Verrey F.;
RT "Amino acid transport of y+L-type by heterodimers of 4F2hc/CD98 and members
RT of the glycoprotein-associated amino acid transporter family.";
RL EMBO J. 18:49-57(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow;
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].
RC STRAIN=FVB/N; 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY
RP 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-26, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, 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: Involved in the sodium-independent uptake of dibasic amino
CC acids and sodium-dependent uptake of some neutral amino acids. Requires
CC coexpression with SLC3A2/4F2hc to mediate the uptake of arginine,
CC leucine and glutamine. Plays a role in nitric oxide synthesis via
CC transport of L-arginine, and is involved in the transport of L-arginine
CC in monocytes. {ECO:0000269|PubMed:9878049}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=91.5 uM for L-arginine (in the absence of NaCl)
CC {ECO:0000269|PubMed:9878049};
CC KM=340.8 uM for L-arginine (in the presence of 0.1 M NaCl)
CC {ECO:0000269|PubMed:9878049};
CC KM=21.7 uM for L-leucine (in the presence of 0.1 M NaCl)
CC {ECO:0000269|PubMed:9878049};
CC KM=1.36 mM for L-alanine (in the presence of 0.1 M NaCl)
CC {ECO:0000269|PubMed:9878049};
CC KM=47.9 uM for L-leucine (in the presence of 0.1 M LiCl)
CC {ECO:0000269|PubMed:9878049};
CC -!- SUBUNIT: Disulfide-linked heterodimer with the amino acid transport
CC protein SLC3A2/4F2hc. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in kidney and intestine. Weaker
CC expression observed in epididymis, testis, ovary, thyroid pancreas,
CC sub-gland and liver. {ECO:0000269|PubMed:9878049}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. L-type amino acid transporter (LAT) (TC 2.A.3.8) family.
CC {ECO:0000305}.
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DR EMBL; AJ012754; CAA10170.1; -; mRNA.
DR EMBL; AJ130943; CAA10255.1; -; mRNA.
DR EMBL; AK150950; BAE29983.1; -; mRNA.
DR EMBL; AK151718; BAE30637.1; -; mRNA.
DR EMBL; AK152637; BAE31379.1; -; mRNA.
DR EMBL; AK170851; BAE42073.1; -; mRNA.
DR EMBL; BC014709; AAH14709.1; -; mRNA.
DR CCDS; CCDS27087.1; -.
DR RefSeq; NP_001240608.1; NM_001253679.1.
DR RefSeq; NP_001240609.1; NM_001253680.1.
DR RefSeq; NP_035535.2; NM_011405.4.
DR RefSeq; XP_006518811.1; XM_006518748.2.
DR RefSeq; XP_006518814.1; XM_006518751.2.
DR RefSeq; XP_006518815.1; XM_006518752.1.
DR RefSeq; XP_006518816.1; XM_006518753.1.
DR RefSeq; XP_006518817.1; XM_006518754.3.
DR RefSeq; XP_006518818.1; XM_006518755.3.
DR AlphaFoldDB; Q9Z1K8; -.
DR SMR; Q9Z1K8; -.
DR BioGRID; 203319; 1.
DR STRING; 10090.ENSMUSP00000000984; -.
DR GlyGen; Q9Z1K8; 2 sites.
DR iPTMnet; Q9Z1K8; -.
DR PhosphoSitePlus; Q9Z1K8; -.
DR jPOST; Q9Z1K8; -.
DR MaxQB; Q9Z1K8; -.
DR PaxDb; Q9Z1K8; -.
DR PeptideAtlas; Q9Z1K8; -.
DR PRIDE; Q9Z1K8; -.
DR ProteomicsDB; 275226; -.
DR Antibodypedia; 22283; 79 antibodies from 19 providers.
DR DNASU; 20540; -.
DR Ensembl; ENSMUST00000000984; ENSMUSP00000000984; ENSMUSG00000000958.
DR Ensembl; ENSMUST00000195970; ENSMUSP00000143091; ENSMUSG00000000958.
DR Ensembl; ENSMUST00000197440; ENSMUSP00000143743; ENSMUSG00000000958.
DR Ensembl; ENSMUST00000226753; ENSMUSP00000154533; ENSMUSG00000000958.
DR GeneID; 20540; -.
DR KEGG; mmu:20540; -.
DR UCSC; uc007tvv.2; mouse.
DR CTD; 9056; -.
DR MGI; MGI:1337120; Slc7a7.
DR VEuPathDB; HostDB:ENSMUSG00000000958; -.
DR eggNOG; KOG1287; Eukaryota.
DR GeneTree; ENSGT00940000160134; -.
DR HOGENOM; CLU_007946_3_0_1; -.
DR InParanoid; Q9Z1K8; -.
DR OMA; VLAYYSF; -.
DR OrthoDB; 867824at2759; -.
DR PhylomeDB; Q9Z1K8; -.
DR TreeFam; TF313355; -.
DR Reactome; R-MMU-210991; Basigin interactions.
DR Reactome; R-MMU-352230; Amino acid transport across the plasma membrane.
DR SABIO-RK; Q9Z1K8; -.
DR BioGRID-ORCS; 20540; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q9Z1K8; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9Z1K8; protein.
DR Bgee; ENSMUSG00000000958; Expressed in small intestine Peyer's patch and 131 other tissues.
DR ExpressionAtlas; Q9Z1K8; baseline and differential.
DR Genevisible; Q9Z1K8; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015174; F:basic amino acid transmembrane transporter activity; IMP:MGI.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0000821; P:regulation of arginine metabolic process; IMP:MGI.
DR InterPro; IPR002293; AA/rel_permease1.
DR Pfam; PF13520; AA_permease_2; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Disulfide bond; Glycoprotein;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..510
FT /note="Y+L amino acid transporter 1"
FT /id="PRO_0000304935"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 4
FT /note="S -> T"
FT /evidence="ECO:0000269|PubMed:9878049"
SQ SEQUENCE 510 AA; 55677 MW; 9F30FB1B88126F6C CRC64;
MVNSTKYEVA AQHEADDGSA LGDGASPVAE QVKLKKEISL LNGVCLIVGN MIGSGIFVSP
KGVLMYSASF GLSLVIWAVG GIFSVFGALC YAELGTTIKK SGASYAYILE AFGGFLAFIR
LWTSLLIIEP TSQAVIAITF ANYMVQPLFP SCGAPYAAGR LLAAACICLL TFINCAYVKW
GTLVQDIFTY AKVLALIAVI IAGIVRLGQG ATANFENSFE GSSFAMGDIA LALYSALFSY
SGWDTLNYVT EEIRNPERNL PLSIGISMPI VTIIYLLTNV AYYSVLDIKE ILASDAVAVT
FADQIFGVFN WIIPVAVAFS CFGGLNASIV AASRLLFVGS REGHLPDAIC MVHVERFTPV
PSLLFNGVLS LVYLCVEDIF QLINYYSFSY WFFVGLSIVG QLYLRWKDPD RPRPLKLSLF
FPIIFCLCTI FLVAVPLYSD TINSLIGIGI ALSGLPFYFF IIRVPEHKRP LFLRRIVASI
TRYLQILCMS VAAEMDLEDG ELSKQDPKSK
