LAAT1_RAT
ID LAAT1_RAT Reviewed; 293 AA.
AC B0BMY1; F7FC79;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Lysosomal amino acid transporter 1 homolog {ECO:0000305};
DE AltName: Full=PQ-loop repeat-containing protein 2;
DE AltName: Full=Solute carrier family 66 member 1 {ECO:0000305};
GN Name=Slc66a1; Synonyms=Pqlc2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 290-LEU-LEU-291, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=23169667; DOI=10.1073/pnas.1211198109;
RA Jezegou A., Llinares E., Anne C., Kieffer-Jaquinod S., O'Regan S.,
RA Aupetit J., Chabli A., Sagne C., Debacker C., Chadefaux-Vekemans B.,
RA Journet A., Andre B., Gasnier B.;
RT "Heptahelical protein PQLC2 is a lysosomal cationic amino acid exporter
RT underlying the action of cysteamine in cystinosis therapy.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:E3434-E3443(2012).
CC -!- FUNCTION: Amino acid transporter that specifically mediates the pH-
CC dependent export of the cationic amino acids arginine, histidine and
CC lysine from lysosomes. {ECO:0000269|PubMed:23169667}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.36 mM for arginine {ECO:0000269|PubMed:23169667};
CC pH dependence:
CC Optimum pH is acidic with no activity detected at a pH higher that
CC 7.0. {ECO:0000269|PubMed:23169667};
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:23169667};
CC Multi-pass membrane protein {ECO:0000269|PubMed:23169667}.
CC -!- DOMAIN: The di-leucine motif mediates lysosomal localization.
CC {ECO:0000269|PubMed:23169667}.
CC -!- SIMILARITY: Belongs to the laat-1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDL80912.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EDL80913.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AABR06040567; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06040568; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473968; EDL80912.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH473968; EDL80913.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC158607; AAI58608.1; -; mRNA.
DR RefSeq; NP_001102159.1; NM_001108689.2.
DR RefSeq; XP_006239301.1; XM_006239239.3.
DR RefSeq; XP_006239302.1; XM_006239240.3.
DR AlphaFoldDB; B0BMY1; -.
DR STRING; 10116.ENSRNOP00000023896; -.
DR GlyGen; B0BMY1; 1 site.
DR PaxDb; B0BMY1; -.
DR PeptideAtlas; B0BMY1; -.
DR GeneID; 362642; -.
DR KEGG; rno:362642; -.
DR CTD; 54896; -.
DR RGD; 1311627; Pqlc2.
DR VEuPathDB; HostDB:ENSRNOG00000017706; -.
DR eggNOG; KOG2913; Eukaryota.
DR HOGENOM; CLU_019699_3_0_1; -.
DR OMA; LAQCFYY; -.
DR OrthoDB; 977963at2759; -.
DR TreeFam; TF313694; -.
DR Reactome; R-RNO-5223345; Miscellaneous transport and binding events.
DR PRO; PR:B0BMY1; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Proteomes; UP000234681; Chromosome 5.
DR Bgee; ENSRNOG00000017706; Expressed in spleen and 18 other tissues.
DR Genevisible; B0BMY1; RN.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0031301; C:integral component of organelle membrane; ISO:RGD.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0015174; F:basic amino acid transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0061459; F:L-arginine transmembrane transporter activity; ISO:RGD.
DR GO; GO:0015189; F:L-lysine transmembrane transporter activity; ISO:RGD.
DR GO; GO:0080144; P:amino acid homeostasis; IMP:UniProtKB.
DR GO; GO:1903826; P:L-arginine transmembrane transport; ISO:RGD.
DR GO; GO:0015819; P:lysine transport; ISO:RGD.
DR InterPro; IPR006603; PQ-loop_rpt.
DR Pfam; PF04193; PQ-loop; 2.
DR SMART; SM00679; CTNS; 2.
PE 1: Evidence at protein level;
KW Amino-acid transport; Glycoprotein; Lysosome; Membrane; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..293
FT /note="Lysosomal amino acid transporter 1 homolog"
FT /id="PRO_0000423746"
FT TOPO_DOM 1..37
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..96
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..126
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..182
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..214
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..254
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..293
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 34..100
FT /note="PQ-loop 1"
FT DOMAIN 191..243
FT /note="PQ-loop 2"
FT MOTIF 290..291
FT /note="Di-leucine motif"
FT CARBOHYD 10
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 290..291
FT /note="LL->AA: Abolishes lysosomal localization."
FT /evidence="ECO:0000269|PubMed:23169667"
SQ SEQUENCE 293 AA; 32232 MW; 357C081C690128E7 CRC64;
MVWRTLVASN FSTCPNGSIQ WIWDVFGECA QDGWDEASVA LGLVSIFCFA ASTFPQYIKA
CKTGNMDQAL SLWFLLGWIG GDSCNLIGSF LADQLPLQTY TAVYYVLADL LMLTLYFHYK
FKKQPSLLSA PINSVLLFIL GTVCITPLLS STDPVAVPRE GFRGRTLLSV EPGNKPFTKK
EVVGFVIGSA SSVLYLLSRL PQIRTNFVRQ STQGISYSLF ALVMLGNTLY GLSVLLKNPE
VGQSEGSYLL HHLPWLVGSL GVLLLDTIIS IQFLVYRSHD ADAASEREPL LPS
