ID   CTR4_MOUSE              Reviewed;         635 AA.
AC   Q8BLQ7;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 140.
DE   RecName: Full=Cationic amino acid transporter 4;
DE            Short=CAT-4;
DE            Short=CAT4;
DE   AltName: Full=Solute carrier family 7 member 4;
GN   Name=Slc7a4;
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].
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex, and Diencephalon;
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   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-422 AND SER-427, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [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).
CC   -!- FUNCTION: Involved in the transport of the cationic amino acids
CC       (arginine, lysine and ornithine). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC       superfamily. Cationic amino acid transporter (CAT) (TC 2.A.3.3) family.
CC       {ECO:0000305}.
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DR   EMBL; AK043772; BAC31651.1; -; mRNA.
DR   EMBL; AK162398; BAE36893.1; -; mRNA.
DR   CCDS; CCDS28008.1; -.
DR   RefSeq; NP_659101.2; NM_144852.3.
DR   RefSeq; XP_017172438.1; XM_017316949.1.
DR   RefSeq; XP_017172439.1; XM_017316950.1.
DR   RefSeq; XP_017172440.1; XM_017316951.1.
DR   AlphaFoldDB; Q8BLQ7; -.
DR   SMR; Q8BLQ7; -.
DR   STRING; 10090.ENSMUSP00000127280; -.
DR   GlyCosmos; Q8BLQ7; 4 sites, No reported glycans.
DR   GlyGen; Q8BLQ7; 4 sites.
DR   iPTMnet; Q8BLQ7; -.
DR   PhosphoSitePlus; Q8BLQ7; -.
DR   SwissPalm; Q8BLQ7; -.
DR   PaxDb; 10090-ENSMUSP00000127280; -.
DR   ProteomicsDB; 285351; -.
DR   Antibodypedia; 23447; 109 antibodies from 25 providers.
DR   DNASU; 224022; -.
DR   Ensembl; ENSMUST00000063544.11; ENSMUSP00000067243.5; ENSMUSG00000022756.18.
DR   Ensembl; ENSMUST00000172164.10; ENSMUSP00000127280.2; ENSMUSG00000022756.18.
DR   GeneID; 224022; -.
DR   KEGG; mmu:224022; -.
DR   UCSC; uc007ylk.1; mouse.
DR   AGR; MGI:2146512; -.
DR   CTD; 6545; -.
DR   MGI; MGI:2146512; Slc7a4.
DR   VEuPathDB; HostDB:ENSMUSG00000022756; -.
DR   eggNOG; KOG1286; Eukaryota.
DR   GeneTree; ENSGT00940000154637; -.
DR   HOGENOM; CLU_007946_15_7_1; -.
DR   InParanoid; Q8BLQ7; -.
DR   OMA; WFAKTHP; -.
DR   OrthoDB; 1421713at2759; -.
DR   PhylomeDB; Q8BLQ7; -.
DR   TreeFam; TF315212; -.
DR   BioGRID-ORCS; 224022; 2 hits in 77 CRISPR screens.
DR   PRO; PR:Q8BLQ7; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; Q8BLQ7; Protein.
DR   Bgee; ENSMUSG00000022756; Expressed in prostate gland ventral lobe and 163 other cell types or tissues.
DR   ExpressionAtlas; Q8BLQ7; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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   Gene3D; 1.20.1740.10; Amino acid/polyamine transporter I; 2.
DR   InterPro; IPR002293; AA/rel_permease1.
DR   InterPro; IPR029485; CAT_C.
DR   PANTHER; PTHR43243:SF89; CATIONIC AMINO ACID TRANSPORTER 4; 1.
DR   PANTHER; PTHR43243; INNER MEMBRANE TRANSPORTER YGJI-RELATED; 1.
DR   Pfam; PF13520; AA_permease_2; 1.
DR   Pfam; PF13906; AA_permease_C; 1.
DR   PIRSF; PIRSF006060; AA_transporter; 1.
DR   Genevisible; Q8BLQ7; MM.
PE   1: Evidence at protein level;
KW   Amino-acid transport; Glycoprotein; Membrane; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..635
FT                   /note="Cationic amino acid transporter 4"
FT                   /id="PRO_0000304934"
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        66..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        113..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        197..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        229..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        270..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        318..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        365..385
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        391..411
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        478..498
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        508..528
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        539..559
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        567..587
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         422
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         427
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CARBOHYD        146
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        151
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        195
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        221
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   635 AA;  68350 MW;  B4A13B84EFED7587 CRC64;
     MARGLPSTAC LARFCQKLNR LKPLEESSME TSLRRCLSTL DLTLLGVGGM VGSGLYVLTG
     TVAKDMAGPA VLLSFLVAAV ASLLAALCYA EFGARVPRTG SAYLFTYVSM GEIWAFLIGW
     NVLLEYLIGG AAVARAWSGY LDAIFNHSIR NFTESHLGVW QVPFLAHYPD FLAAGILLVA
     SAFVSCGARV SSWLNHTFSA ISLIVILFII VLGFILARPH NWSAEEGGFA PFGFSGILAG
     TATCFYAFVG FDVIAASSEE AKNPRWAVPM AIAISLSLAA GAYILVSTVL TLMVPWHSLD
     PDSALADAFY RRGYSWAGFI VAVGSICAMN TVLLSNLFSL PRIVYAMAAD GLFFQVFARV
     HPRTQVPVVG ILVFGVLMAL LALLLDLEAL VQFLSIGTLL AYTFVATSII VLRFQKASPP
     SSPCLASPGP TAKKYDSFSD HIQLVGAEQT SMSEPGQLRP ALKPFLGFLD GCSPGTAVAW
     ALGILVASAI SLACVLVFGN SDLHLPQWGY VLLLVISGAV FLSSLLVLGA HQQQKKQDTF
     QIPLVPLTPA LSILLNTCLM LKLSYLTWLR FIFWLLVGLV VYFGYGIWHS KENQREPLEL
     TTAHYVVFPS GSLEETVQAV QPSSQSPVRE SGCTE
//