AAA1_MOUSE
ID AAA1_MOUSE Reviewed; 530 AA.
AC P63115; Q9CW25; Q9JMH8;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Asc-type amino acid transporter 1;
DE Short=Asc-1;
DE AltName: Full=D-serine transporter;
DE AltName: Full=Solute carrier family 7 member 10;
GN Name=Slc7a10; Synonyms=Asc1;
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, SUBUNIT, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10734121; DOI=10.1074/jbc.275.13.9690;
RA Fukasawa Y., Segawa H., Kim J.Y., Chairoungdua A., Kim D.K., Matsuo H.,
RA Cha S.H., Endou H., Kanai Y.;
RT "Identification and characterization of a Na+-independent neutral amino
RT acid transporter that associates with the 4F2 heavy chain and exhibits
RT substrate selectivity for small neutral D- and L- amino acids.";
RL J. Biol. Chem. 275:9690-9698(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 170-530.
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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).
CC -!- FUNCTION: Sodium-independent, high affinity transport of small neutral
CC D- and L-amino acids and amino acid-related compounds. May play a role
CC in the modulation of glutamatergic transmission through mobilization of
CC D-serine at the glutamatergic synapse. {ECO:0000269|PubMed:10734121}.
CC -!- SUBUNIT: Disulfide-linked heterodimer with the amino acid transport
CC protein SLC3A2/4F2hc. {ECO:0000269|PubMed:10734121}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain and lung, and to a lesser
CC extent in placenta and small intestine. {ECO:0000269|PubMed:10734121}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. {ECO:0000305}.
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DR EMBL; AB026688; BAA93617.1; -; mRNA.
DR EMBL; BC054765; AAH54765.1; -; mRNA.
DR EMBL; AK005282; BAB23930.1; -; mRNA.
DR CCDS; CCDS21146.1; -.
DR RefSeq; NP_059090.3; NM_017394.4.
DR AlphaFoldDB; P63115; -.
DR SMR; P63115; -.
DR STRING; 10090.ENSMUSP00000001854; -.
DR TCDB; 2.A.3.8.13; the amino acid-polyamine-organocation (apc) family.
DR iPTMnet; P63115; -.
DR PhosphoSitePlus; P63115; -.
DR SwissPalm; P63115; -.
DR jPOST; P63115; -.
DR MaxQB; P63115; -.
DR PaxDb; P63115; -.
DR PRIDE; P63115; -.
DR ProteomicsDB; 296429; -.
DR Antibodypedia; 47948; 96 antibodies from 19 providers.
DR DNASU; 53896; -.
DR Ensembl; ENSMUST00000001854; ENSMUSP00000001854; ENSMUSG00000030495.
DR GeneID; 53896; -.
DR KEGG; mmu:53896; -.
DR UCSC; uc009gjn.2; mouse.
DR CTD; 56301; -.
DR MGI; MGI:1858261; Slc7a10.
DR VEuPathDB; HostDB:ENSMUSG00000030495; -.
DR eggNOG; KOG1287; Eukaryota.
DR GeneTree; ENSGT00940000156469; -.
DR HOGENOM; CLU_007946_3_0_1; -.
DR InParanoid; P63115; -.
DR OMA; YDGWILI; -.
DR OrthoDB; 867824at2759; -.
DR PhylomeDB; P63115; -.
DR TreeFam; TF313355; -.
DR Reactome; R-MMU-210991; Basigin interactions.
DR Reactome; R-MMU-352230; Amino acid transport across the plasma membrane.
DR BioGRID-ORCS; 53896; 3 hits in 72 CRISPR screens.
DR PRO; PR:P63115; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P63115; protein.
DR Bgee; ENSMUSG00000030495; Expressed in lumbar subsegment of spinal cord and 138 other tissues.
DR ExpressionAtlas; P63115; baseline and differential.
DR Genevisible; P63115; MM.
DR GO; GO:0097440; C:apical dendrite; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0042941; P:D-alanine transport; IMP:MGI.
DR GO; GO:0042942; P:D-serine transport; IMP:MGI.
DR GO; GO:0015804; P:neutral amino acid transport; IDA:UniProtKB.
DR InterPro; IPR002293; AA/rel_permease1.
DR Pfam; PF13520; AA_permease_2; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Disulfide bond; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..530
FT /note="Asc-type amino acid transporter 1"
FT /id="PRO_0000054277"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..414
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..450
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 454..474
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..33
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 530 AA; 57549 MW; 0C5A80BF922DB54D CRC64;
MRRDSDMASH IQQPGGHGNP GPAPSPSPGP GPGPGASERV ALKKEIGLVS ACTIIIGNII
GSGIFISPKG VLEHSGSVGL ALFVWVLGGG VTALGSLCYA ELGVAIPKSG GDYAYVTEIF
GGLAGFLLLW SAVLIMYPTS LAVISMTFSN YVLQPVFPNC IPPATASRVL SMACLMLLTW
VNSSSVRWAT RIQVIFTGGK LLALSLIITV GFVQIFQGHF EELRPTNAFA FWMTPSVGHL
ALAFLQGSFA FSGWNFLNYV TEELVDPRKN LPRAIFISIP LVTFVYTFTN VAYFTAMSPQ
ELLSSNAVAV TFGEKLLGYF SWVMPVSVAL STFGGINGYL FTSSRLCFSG AREGHLPSFL
AMIHVRRCTP IPALLVCCGA TAVIMLVGDT YTLINYVSFI NYLCYGVTIL GLLVLRWRRP
ALHRPIKVNL LVPVVYLVFW AFLLVFSFIS EPMVCGVGII IILTGVPIFF LGVFWRSKPK
CVHRFTESMT RWGQELCFVV YPQGSLEEEE NGPMGQPSPL PITDKPLKTQ
