S22AL_MOUSE
ID S22AL_MOUSE Reviewed; 564 AA.
AC Q9WTN6; Q5SWV0;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Solute carrier family 22 member 21;
DE AltName: Full=Organic cation/carnitine transporter 3;
DE AltName: Full=Solute carrier family 22 member 9;
GN Name=Slc22a21; Synonyms=Octn3, Slc22a9;
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, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=11010964; DOI=10.1074/jbc.m005340200;
RA Tamai I., Ohashi R., Nezu J., Sai Y., Kobayashi D., Oku A., Shimane M.,
RA Tsuji A.;
RT "Molecular and functional characterization of organic cation/carnitine
RT transporter family in mice.";
RL J. Biol. Chem. 275:40064-40072(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=12535646; DOI=10.1016/s0006-291x(02)02946-7;
RA Lamhonwah A.-M., Skaug J., Scherer S.W., Tein I.;
RT "A third human carnitine/organic cation transporter (OCTN3) as a candidate
RT for the 5q31 Crohn's disease locus (IBD5).";
RL Biochem. Biophys. Res. Commun. 301:98-101(2003).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=16288981; DOI=10.1016/j.bbrc.2005.10.170;
RA Lamhonwah A.-M., Ackerley C.A., Tilups A., Edwards V.D., Wanders R.J.,
RA Tein I.;
RT "OCTN3 is a mammalian peroxisomal membrane carnitine transporter.";
RL Biochem. Biophys. Res. Commun. 338:1966-1972(2005).
CC -!- FUNCTION: Sodium-ion independent, medium affinity carnitine
CC transporter. Also transports organic cations such as tetraethylammonium
CC (TEA) without the involvement of sodium. Relative uptake activity ratio
CC of carnitine to TEA is 746. {ECO:0000269|PubMed:11010964}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:11010964,
CC ECO:0000269|PubMed:12535646, ECO:0000269|PubMed:16288981}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:11010964,
CC ECO:0000269|PubMed:12535646, ECO:0000269|PubMed:16288981}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in testis.
CC {ECO:0000269|PubMed:11010964}.
CC -!- SIMILARITY: Belongs to the major facilitator (TC 2.A.1) superfamily.
CC Organic cation transporter (TC 2.A.1.19) family. {ECO:0000305}.
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DR EMBL; AB018436; BAA78343.1; -; mRNA.
DR EMBL; AK133431; BAE21654.1; -; mRNA.
DR EMBL; AK161508; BAE36432.1; -; mRNA.
DR EMBL; AL596444; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS24688.1; -.
DR RefSeq; NP_062697.1; NM_019723.2.
DR AlphaFoldDB; Q9WTN6; -.
DR SMR; Q9WTN6; -.
DR BioGRID; 208030; 23.
DR IntAct; Q9WTN6; 1.
DR STRING; 10090.ENSMUSP00000075814; -.
DR ChEMBL; CHEMBL2073715; -.
DR DrugBank; DB08842; Acetylcarnitine.
DR TCDB; 2.A.1.19.41; the major facilitator superfamily (mfs).
DR GlyGen; Q9WTN6; 3 sites.
DR iPTMnet; Q9WTN6; -.
DR PhosphoSitePlus; Q9WTN6; -.
DR jPOST; Q9WTN6; -.
DR MaxQB; Q9WTN6; -.
DR PaxDb; Q9WTN6; -.
DR PRIDE; Q9WTN6; -.
DR ProteomicsDB; 260762; -.
DR DNASU; 56517; -.
DR Ensembl; ENSMUST00000076493; ENSMUSP00000075814; ENSMUSG00000063652.
DR GeneID; 56517; -.
DR KEGG; mmu:56517; -.
DR UCSC; uc007ixd.1; mouse.
DR CTD; 56517; -.
DR MGI; MGI:1929481; Slc22a21.
DR VEuPathDB; HostDB:ENSMUSG00000063652; -.
DR eggNOG; KOG0255; Eukaryota.
DR GeneTree; ENSGT00940000154155; -.
DR HOGENOM; CLU_001265_33_4_1; -.
DR InParanoid; Q9WTN6; -.
DR OMA; VILHINH; -.
DR OrthoDB; 704438at2759; -.
DR PhylomeDB; Q9WTN6; -.
DR TreeFam; TF315847; -.
DR BioGRID-ORCS; 56517; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q9WTN6; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9WTN6; protein.
DR Bgee; ENSMUSG00000063652; Expressed in spermatocyte and 126 other tissues.
DR ExpressionAtlas; Q9WTN6; baseline and differential.
DR Genevisible; Q9WTN6; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0031526; C:brush border membrane; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031231; C:intrinsic component of peroxisomal membrane; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:1901235; F:(R)-carnitine transmembrane transporter activity; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0015226; F:carnitine transmembrane transporter activity; IDA:MGI.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0015651; F:quaternary ammonium group transmembrane transporter activity; ISO:MGI.
DR GO; GO:1902270; P:(R)-carnitine transmembrane transport; ISO:MGI.
DR GO; GO:0015879; P:carnitine transport; IDA:MGI.
DR GO; GO:0060731; P:positive regulation of intestinal epithelial structure maintenance; ISO:MGI.
DR GO; GO:0015697; P:quaternary ammonium group transport; ISO:MGI.
DR GO; GO:0009609; P:response to symbiotic bacterium; ISO:MGI.
DR GO; GO:0070715; P:sodium-dependent organic cation transport; ISO:MGI.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR004749; Orgcat_transp/SVOP.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF00083; Sugar_tr; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00898; 2A0119; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Glycoprotein; Ion transport; Membrane; Nucleotide-binding;
KW Peroxisome; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..564
FT /note="Solute carrier family 22 member 21"
FT /id="PRO_0000220506"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..41
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..142
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 164..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..197
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 219..232
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..257
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..344
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..365
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 366..376
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..409
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..433
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 434..454
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 455..465
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 466..486
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 487..491
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 492..512
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 513..564
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 532..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 218..225
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 564 AA; 63321 MW; C37FDCA6395DAD01 CRC64;
MLDYDEVTAF LGEWGTFQRL IFFLLSASII PNGFTGLSAV FLTAIPEHRC RIPDTVNLSS
AWRNHSIPME TKDGPEVPQK CRRYRLATIA NFSELGLEPG RDVDLEQLEQ ENCLDGWEYD
KDIFLSTIVT EWDLVCKDDW KAPLTTSFFY VGVLLGSFIS GQLSDRFGRK NILFLTMAMH
TGFSFIQVFS VNFEMFTLLY TLVGMGHISN YVAAFVLGTE MLSKSVRIIF ATLGVCIFFA
FGFMVLPLFA YFIREWRRLL LAITLPGVLC GALWWFIPES PRWLISQGRI KEAEVIIRKA
AKINGIVAPS TIFDPSETNK LQDDSSKKPQ SHHIYDLVRT PNIRILTIMS IILWLTISVG
YFGLSLDTPN LNGNIYVNCF LLAAVEVPAY VLAWLLLQHV SRRYSMAGSL FLGGSVLLLV
QLVPSDLHYL STTLVMVGKF GITSAYSMVY VYTAELYPTV VRNMGVGVSS TASRLGSILS
PYFVYLGAYD RRLPYILMGS LTILTAIITL FFPESSGVSL PETIDEMQKV KKLKQRQSLS
KKGSPKESKG NVSRTSRTSE PKGF
