S7A14_MOUSE
ID S7A14_MOUSE Reviewed; 771 AA.
AC Q8BXR1; Q69ZE9;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Probable cationic amino acid transporter;
DE AltName: Full=Solute carrier family 7 member 14;
GN Name=Slc7a14; Synonyms=Kiaa1613;
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].
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Retina;
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 TISSUE=Eye;
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-465; SER-468; SER-475;
RP SER-488; SER-757 AND SER-769, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
RN [5]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=24670872; DOI=10.1038/ncomms4517;
RA Jin Z.B., Huang X.F., Lv J.N., Xiang L., Li D.Q., Chen J., Huang C., Wu J.,
RA Lu F., Qu J.;
RT "SLC7A14 linked to autosomal recessive retinitis pigmentosa.";
RL Nat. Commun. 5:3517-3517(2014).
CC -!- FUNCTION: May be involved in arginine transport. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Note=Exhibits a punctated pattern in
CC the cytoplasm, which partially ovelaps with lysosomes. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in retina, brain and spinal cord. In the
CC retina, expressed in the inner nuclear layer and photoreceptor layer
CC (at protein level). {ECO:0000269|PubMed:24670872}.
CC -!- DEVELOPMENTAL STAGE: Detected in the eyeball at 18.5 dpc. Expression
CC increases in the retina after birth from P4 to P90.
CC -!- DISRUPTION PHENOTYPE: Mutant mice exhibit slightly thinner retina,
CC including outer retinal layer, and abnormal electroretinography at 2
CC and 6 months of age compared to wild-type animals. They are viable and
CC fertile. They do not show any noticeable physical abnormalities.
CC {ECO:0000269|PubMed:24670872}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32495.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK173217; BAD32495.1; ALT_INIT; mRNA.
DR EMBL; AK044448; BAC31925.1; -; mRNA.
DR EMBL; BC061928; AAH61928.1; -; mRNA.
DR CCDS; CCDS17291.1; -.
DR RefSeq; NP_766449.1; NM_172861.3.
DR RefSeq; XP_006535535.1; XM_006535472.3.
DR AlphaFoldDB; Q8BXR1; -.
DR SMR; Q8BXR1; -.
DR STRING; 10090.ENSMUSP00000088803; -.
DR GlyGen; Q8BXR1; 2 sites.
DR iPTMnet; Q8BXR1; -.
DR PhosphoSitePlus; Q8BXR1; -.
DR SwissPalm; Q8BXR1; -.
DR MaxQB; Q8BXR1; -.
DR PaxDb; Q8BXR1; -.
DR PeptideAtlas; Q8BXR1; -.
DR PRIDE; Q8BXR1; -.
DR ProteomicsDB; 255449; -.
DR Antibodypedia; 18672; 58 antibodies from 18 providers.
DR DNASU; 241919; -.
DR Ensembl; ENSMUST00000091259; ENSMUSP00000088803; ENSMUSG00000069072.
DR GeneID; 241919; -.
DR KEGG; mmu:241919; -.
DR UCSC; uc008ovx.2; mouse.
DR CTD; 57709; -.
DR MGI; MGI:3040688; Slc7a14.
DR VEuPathDB; HostDB:ENSMUSG00000069072; -.
DR eggNOG; KOG1286; Eukaryota.
DR GeneTree; ENSGT00940000155893; -.
DR InParanoid; Q8BXR1; -.
DR OMA; KEACSPG; -.
DR OrthoDB; 439017at2759; -.
DR PhylomeDB; Q8BXR1; -.
DR TreeFam; TF315212; -.
DR BioGRID-ORCS; 241919; 4 hits in 73 CRISPR screens.
DR PRO; PR:Q8BXR1; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8BXR1; protein.
DR Bgee; ENSMUSG00000069072; Expressed in superior cervical ganglion and 88 other tissues.
DR ExpressionAtlas; Q8BXR1; baseline and differential.
DR Genevisible; Q8BXR1; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006865; P:amino acid transport; IBA:GO_Central.
DR InterPro; IPR002293; AA/rel_permease1.
DR InterPro; IPR029485; CAT_C.
DR Pfam; PF13520; AA_permease_2; 1.
DR Pfam; PF13906; AA_permease_C; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Glycoprotein; Lysosome; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..771
FT /note="Probable cationic amino acid transporter"
FT /id="PRO_0000307361"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 565..585
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 596..616
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 628..648
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 655..675
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 735..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 757
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 769
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 676
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 771 AA; 83984 MW; 52381841C32BC848 CRC64;
MSGFLASLDP RRVQWGAAWY AMHSRILRTK PVESMLEGTG TTSAHGTKLA QVLTTVDLIS
LGVGSCVGTG MYVVSGLVAK EMAGPGVIVS FIIAAVASIL SGVCYAEFGV RVPKTTGSAY
TYSYVTVGEF VAFFIGWNLI LEYLIGTAAG ASALSSMFDS LANHSISRWM VDTVGTLNGL
GKGEESYPDL LALVIAVIVT IIVALGVKNS VGFNNVLNVL NLAVWVFIMI AGLFFINGKY
WAEGQFLPHG WSGVLQGAAT CFYAFIGFDI IATTGEEAKN PNTSIPYAIT ASLVICLTAY
VSVSMILTLM VPYYAIDTES PLMEMFVAHG FYAAKFVVAI GSVAGLTVSL LGSLFPMPRV
IYAMAGDGLL FRFLAHVSSY TETPVVACIV SGFLAALLSL LVSLRDLIEM MSIGTLLAYT
LVSVCVLLLR YQPESDIDGF VKFLSEEHTK KKEGILADCE KETCSPVSEG EEFSSPATNT
CGAKNLPSLG DNEMLIGKSD KSAYNVNHPN YGTVDMTTGI EADESENIYL IKLKKLIGPR
YYTMRIRLGL PGKMDRPTAA TGHTVTICVL LLFILMFIFC SFIIFGSEYI SGQSWWAILL
VVLMMLLISV LVFVILQQPE NPKKLPYMAP CLPFVPAFAM LVNIYLMLKL STITWIRFAV
WCFVGMLIYF GYGIWNSTLE ISAREQALHQ STYQRYDVDD PFSVEEGFSY ATEGESQEDW
GGPAEDKGFY YQQMSDAKAN SRTSSKAKSK SKHKQNSEAL IANDELDCSP E
