S22A5_HUMAN
ID S22A5_HUMAN Reviewed; 557 AA.
AC O76082; A2Q0V1; B2R844; D3DQ87; Q6ZQZ8; Q96EH6;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Solute carrier family 22 member 5;
DE AltName: Full=High-affinity sodium-dependent carnitine cotransporter;
DE AltName: Full=Organic cation/carnitine transporter 2;
GN Name=SLC22A5; Synonyms=OCTN2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9618255; DOI=10.1006/bbrc.1998.8669;
RA Wu X., Prasad P.D., Leibach F.H., Ganapathy V.;
RT "cDNA sequence, transport function, and genomic organization of human
RT OCTN2, a new member of the organic cation transporter family.";
RL Biochem. Biophys. Res. Commun. 246:589-595(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=9685390; DOI=10.1074/jbc.273.32.20378;
RA Tamai I., Ohashi R., Nezu J., Yabuuchi H., Oku A., Shimane M., Sai Y.,
RA Tsuji A.;
RT "Molecular and functional identification of sodium ion-dependent, high
RT affinity human carnitine transporter OCTN2.";
RL J. Biol. Chem. 273:20378-20382(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=9916797; DOI=10.1038/5030;
RA Nezu J., Tamai I., Oku A., Ohashi R., Yabuuchi H., Hashimoto N.,
RA Nikaido H., Sai Y., Koizumi A., Shoji Y., Takada G., Matsuishi T.,
RA Yashino M., Kato H., Ohura T., Tsujimoto G., Hayakawa J., Shimane M.,
RA Tsuji A.;
RT "Primary systemic carnitine deficiency is caused by mutations in a gene
RT encoding sodium ion-dependent carnitine transporter.";
RL Nat. Genet. 21:91-94(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=17509700; DOI=10.1016/j.bbamcr.2007.04.005;
RA Maekawa S., Mori D., Nishiya T., Takikawa O., Horinouchi T., Nishimoto A.,
RA Kajita E., Miwa S.;
RT "OCTN2VT, a splice variant of OCTN2, does not transport carnitine because
RT of the retention in the endoplasmic reticulum caused by insertion of 24
RT amino acids in the first extracellular loop of OCTN2.";
RL Biochim. Biophys. Acta 1773:1000-1006(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=10454528;
RA Wu X., Huang W., Prasad P.D., Seth P., Rajan D.P., Leibach F.H., Chen J.,
RA Conway S.J., Ganapathy V.;
RT "Functional characteristics and tissue distribution pattern of organic
RT cation transporter 2 (OCTN2), an organic cation/carnitine transporter.";
RL J. Pharmacol. Exp. Ther. 290:1482-1492(1999).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-57 AND ASN-91.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-486, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-550, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP VARIANT CDSP GLN-169.
RX PubMed=10425211; DOI=10.1006/bbrc.1999.1060;
RA Burwinkel B., Kreuder J., Schweitzer S., Vorgerd M., Gempel K.,
RA Gerbitz K.-D., Kilimann M.W.;
RT "Carnitine transporter OCTN2 mutations in systemic primary carnitine
RT deficiency: a novel Arg169Gln mutation and a recurrent Arg282ter mutation
RT associated with an unconventional splicing abnormality.";
RL Biochem. Biophys. Res. Commun. 261:484-487(1999).
RN [14]
RP VARIANT CDSP CYS-211.
RX PubMed=10480371; DOI=10.1007/s004399900105;
RA Vaz F.M., Scholte H.R., Ruiter J., Hussaarts-Odijk L.M.,
RA Rodrigues Pereira R., Schweitzer S., de Klerk J.B.C., Waterham H.R.,
RA Wanders R.J.A.;
RT "Identification of two novel mutations in OCTN2 of three patients with
RT systemic carnitine deficiency.";
RL Hum. Genet. 105:157-161(1999).
RN [15]
RP VARIANT CDSP LEU-478.
RX PubMed=10072434; DOI=10.1093/hmg/8.4.655;
RA Tang N.L., Ganapathy V., Wu X., Hui J., Seth P., Yuen P.M., Wanders R.J.,
RA Fok T.F., Hjelm N.M.;
RT "Mutations of OCTN2, an organic cation/carnitine transporter, lead to
RT deficient cellular carnitine uptake in primary carnitine deficiency.";
RL Hum. Mol. Genet. 8:655-660(1999).
RN [16]
RP VARIANTS CDSP LEU-179; CYS-283 AND CYS-467, AND CHARACTERIZATION OF
RP VARIANTS CDSP LEU-179; CYS-283 AND CYS-467.
RX PubMed=10545605; DOI=10.1093/hmg/8.12.2247;
RA Koizumi A., Nozaki J., Ohura T., Kayo T., Wada Y., Nezu J., Ohashi R.,
RA Tamai I., Shoji Y., Takada G., Kibira S., Matsuishi T., Tsuji A.;
RT "Genetic epidemiology of the carnitine transporter OCTN2 gene in a Japanese
RT population and phenotypic characterization in Japanese pedigrees with
RT primary systemic carnitine deficiency.";
RL Hum. Mol. Genet. 8:2247-2254(1999).
RN [17]
RP CHARACTERIZATION OF VARIANT CDSP LEU-478, AND MUTAGENESIS.
RX PubMed=10559218; DOI=10.1074/jbc.274.47.33388;
RA Seth P., Wu X., Huang W., Leibach F.H., Ganapathy V.;
RT "Mutations in novel organic cation transporter (OCTN2), an organic
RT cation/carnitine transporter, with differential effects on the organic
RT cation transport function and the carnitine transport function.";
RL J. Biol. Chem. 274:33388-33392(1999).
RN [18]
RP VARIANTS CDSP ARG-283 AND PHE-446.
RX PubMed=10612840;
RX DOI=10.1002/(sici)1098-1004(200001)15:1<118::aid-humu28>3.0.co;2-8;
RA Mayatepek E., Nezu J., Tamai I., Oku A., Katsura M., Shimane M., Tsuji A.;
RT "Two novel missense mutations of the OCTN2 gene (W283R and V446F) in a
RT patient with primary systemic carnitine deficiency.";
RL Hum. Mutat. 15:118-118(2000).
RN [19]
RP SUBCELLULAR LOCATION, AND VARIANT CDSP LYS-452.
RX PubMed=10679939;
RX DOI=10.1002/(sici)1098-1004(200003)15:3<238::aid-humu4>3.0.co;2-3;
RA Wang Y., Kelly M.A., Cowan T.M., Longo N.;
RT "A missense mutation in the OCTN2 gene associated with residual carnitine
RT transport activity.";
RL Hum. Mutat. 15:238-245(2000).
RN [20]
RP VARIANTS CDSP TRP-169; VAL-242; ASP-301 AND ARG-351, AND CHARACTERIZATION
RP OF VARIANTS CDSP TRP-169; VAL-242; ASP-301 AND ARG-351.
RX PubMed=11058897;
RX DOI=10.1002/1098-1004(200011)16:5<401::aid-humu4>3.0.co;2-j;
RA Wang Y., Taroni F., Garavaglia B., Longo N.;
RT "Functional analysis of mutations in the OCTN2 transporter causing primary
RT carnitine deficiency: lack of genotype-phenotype correlation.";
RL Hum. Mutat. 16:401-407(2000).
RN [21]
RP VARIANTS CDSP PRO-19 AND GLN-399, AND CHARACTERIZATION OF VARIANTS CDSP
RP PRO-19 AND GLN-399.
RX PubMed=11715001; DOI=10.1097/00125817-200111000-00002;
RA Wang Y., Korman S.H., Ye J., Gargus J.J., Gutman A., Taroni F.,
RA Garavaglia B., Longo N.;
RT "Phenotype and genotype variation in primary carnitine deficiency.";
RL Genet. Med. 3:387-392(2001).
RN [22]
RP VARIANT CDSP LEU-83.
RX PubMed=15617188; DOI=10.1023/b:boli.0000045837.23328.f4;
RA Makhseed N., Vallance H.D., Potter M., Waters P.J., Wong L.T.K.,
RA Lillquist Y., Pasquali M., Amat di San Filippo C., Longo N.;
RT "Carnitine transporter defect due to a novel mutation in the SLC22A5 gene
RT presenting with peripheral neuropathy.";
RL J. Inherit. Metab. Dis. 27:778-780(2004).
RN [23]
RP VARIANTS CDSP PRO-19; LEU-83; TRP-169; MET-232; VAL-242; ASP-301; ARG-351;
RP GLN-399; CYS-447; ASP-449; LYS-452 AND ARG-468, AND CHARACTERIZATION OF
RP VARIANTS MET-232 AND ARG-468.
RX PubMed=15714519; DOI=10.1002/humu.20137;
RA Dobrowolski S.F., McKinney J.T., Amat di San Filippo C., Giak Sim K.,
RA Wilcken B., Longo N.;
RT "Validation of dye-binding/high-resolution thermal denaturation for the
RT identification of mutations in the SLC22A5 gene.";
RL Hum. Mutat. 25:306-313(2005).
RN [24]
RP VARIANTS PHE-144; ILE-481; PHE-481; LEU-508; VAL-530 AND SER-549, AND
RP VARIANTS CDSP LEU-17 AND ASP-449.
RX PubMed=16931768; DOI=10.1124/mol.106.028126;
RA Urban T.J., Gallagher R.C., Brown C., Castro R.A., Lagpacan L.L.,
RA Brett C.M., Taylor T.R., Carlson E.J., Ferrin T.E., Burchard E.G.,
RA Packman S., Giacomini K.M.;
RT "Functional genetic diversity in the high-affinity carnitine transporter
RT OCTN2 (SLC22A5).";
RL Mol. Pharmacol. 70:1602-1611(2006).
RN [25]
RP VARIANTS CDSP SER-32; SER-46; CYS-467 AND CYS-488, AND CHARACTERIZATION OF
RP VARIANT CDSP SER-46.
RX PubMed=17126586; DOI=10.1016/j.ymgme.2006.10.003;
RA Schimmenti L.A., Crombez E.A., Schwahn B.C., Heese B.A., Wood T.C.,
RA Schroer R.J., Bentler K., Cederbaum S., Sarafoglou K., McCann M.,
RA Rinaldo P., Matern D., di San Filippo C.A., Pasquali M., Berry S.A.,
RA Longo N.;
RT "Expanded newborn screening identifies maternal primary carnitine
RT deficiency.";
RL Mol. Genet. Metab. 90:441-445(2007).
RN [26]
RP VARIANTS CDSP TRP-15; SER-46; LEU-83; SER-142; VAL-214; MET-232; TRP-399
RP AND ILE-442.
RX PubMed=20027113; DOI=10.1097/gim.0b013e3181c5e6f7;
RA El-Hattab A.W., Li F.-Y., Shen J., Powell B.R., Bawle E.V., Adams D.J.,
RA Wahl E., Kobori J.A., Graham B., Scaglia F., Wong L.-J.;
RT "Maternal systemic primary carnitine deficiency uncovered by newborn
RT screening: clinical, biochemical, and molecular aspects.";
RL Genet. Med. 12:19-24(2010).
RN [27]
RP VARIANTS CDSP SER-12; TRP-15; LEU-17; SER-32; SER-46; LEU-83; TYR-122;
RP SER-142; TRP-169; GLN-169; PRO-186; VAL-214; HIS-227; MET-232; TRP-257;
RP ARG-264; GLN-282; LEU-355; LEU-398; TRP-399; MET-440; ILE-442; VAL-443;
RP ASP-449; LYS-452; ARG-455; CYS-467; CYS-488 AND SER-507, AND VARIANTS
RP PRO-66; PRO-75; ALA-96; GLY-123; LEU-143; VAL-177; LEU-230; THR-240;
RP VAL-312; ASN-358 AND SER-549.
RX PubMed=20574985; DOI=10.1002/humu.21311;
RA Li F.-Y., El-Hattab A.W., Bawle E.V., Boles R.G., Schmitt E.S., Scaglia F.,
RA Wong L.-J.;
RT "Molecular spectrum of SLC22A5 (OCTN2) gene mutations detected in 143
RT subjects evaluated for systemic carnitine deficiency.";
RL Hum. Mutat. 31:E1632-E1651(2010).
RN [28]
RP VARIANTS CDSP LEU-17; ARG-234; GLN-282; LEU-362; CYS-467 AND CYS-471, AND
RP VARIANT LEU-143.
RX PubMed=20074989; DOI=10.1016/j.ymgme.2009.12.015;
RA Lee N.-C., Tang N.-L., Chien Y.-H., Chen C.-A., Lin S.-J., Chiu P.-C.,
RA Huang A.-C., Hwu W.-L.;
RT "Diagnoses of newborns and mothers with carnitine uptake defects through
RT newborn screening.";
RL Mol. Genet. Metab. 100:46-50(2010).
RN [29]
RP VARIANTS CDSP TRP-15; PRO-19; PHE-22 DEL; ASN-26; SER-32; SER-46; LEU-83;
RP SER-142; GLN-169; TRP-169; VAL-214; MET-232; PHE-280; GLN-282; ARG-283;
RP ARG-351; MET-440; ILE-442; PHE-446; CYS-447; CYS-467; PRO-471 AND HIS-488,
RP AND CHARACTERIZATION OF VARIANTS CDSP TRP-15; PRO-19; PHE-22 DEL; ASN-26;
RP SER-32; SER-46; LEU-83; GLN-169; TRP-169; VAL-214; MET-232; PHE-280;
RP GLN-282; ARG-283; ARG-351; MET-440; ILE-442; PHE-446; CYS-447; CYS-467 AND
RP PRO-471.
RX PubMed=21922592; DOI=10.1002/humu.21607;
RA Rose E.C., di San Filippo C.A., Ndukwe Erlingsson U.C., Ardon O.,
RA Pasquali M., Longo N.;
RT "Genotype-phenotype correlation in primary carnitine deficiency.";
RL Hum. Mutat. 33:118-123(2012).
RN [30]
RP VARIANTS CDSP 4-TYR--PHE-557 DEL; SER-12; TRP-15; LEU-16; LEU-17; PRO-19;
RP HIS-20; PHE-22 DEL; ASN-26; ILE-28; SER-32; VAL-44; LEU-46; SER-46; TYR-50;
RP PRO-66; PRO-75; LEU-83; TRP-93; VAL-95; ALA-96; GLY-115; 117-TRP--PHE-557
RP DEL; GLY-123; ASP-131; 132-TRP--PHE-557 DEL; 140-TRP--PHE-557 DEL; SER-142;
RP LEU-143; MET-151; GLN-169; PRO-169; TRP-169; MET-175; VAL-177; LEU-179;
RP PRO-186; ARG-205; SER-210; CYS-211; VAL-214; LYS-219; LEU-225; HIS-227;
RP LEU-230; PHE-231; MET-232; THR-240; VAL-242; ARG-247; 254-ARG--PHE-557 DEL;
RP GLN-254; 256-TRP--PHE-557 DEL; TRP-257; ARG-264; MET-264; PRO-269;
RP 275-TRP--PHE-557 DEL; PHE-280; 282-ARG--PHE-557 DEL; GLN-282; ARG-283;
RP CYS-283; 289-ARG--PHE-557 DEL; 295-VAL--PHE-557 DEL; ASP-301; VAL-312;
RP LYS-317; 319-GLN--PHE-557 DEL; THR-348; ARG-351; LEU-355; ASN-358; PRO-363;
RP 387-TYR--PHE-557 DEL; LEU-394 DEL; LEU-398; GLN-399; TRP-399; GLY-412;
RP GLY-439; MET-440; ILE-442; VAL-443; PHE-446; CYS-447; LEU-448; ASP-449;
RP LYS-452; ARG-455; VAL-462; CYS-467; ARG-468; PHE-470; HIS-471; PRO-471;
RP ARG-476; LEU-478; CYS-488; HIS-488 AND SER-507, VARIANTS PHE-481 AND
RP SER-549, CHARACTERIZATION OF VARIANTS CDSP SER-12; TRP-15; LEU-16; LEU-17;
RP PRO-19; HIS-20; PHE-23 DEL; ASN-26; ILE-28; SER-32; VAL-44; LEU-46; SER-46;
RP TYR-50; PRO-66; PRO-75; LEU-83; TRP-93; VAL-95; ALA-96; GLY-115; GLY-123;
RP ASP-131; SER-142; LEU-143; MET-151; GLN-169; PRO-169; TRP-169; MET-175;
RP VAL-177; LEU-179; PRO-186; ARG-205; SER-210; CYS-211; VAL-214; LYS-219;
RP LEU-225; HIS-227; LEU-230; PHE-231; MET-232; THR-240; VAL-242; ARG-247;
RP GLN-254; TRP-257; ARG-264; MET-264; PRO-269; PHE-280; GLN-282; ARG-283;
RP CYS-283; ASP-301; VAL-312; LYS-317; THR-348; ARG-351; LEU-355; ASN-358;
RP PRO-363; LEU-394 DEL; LEU-398; GLN-399; TRP-399; GLY-412; GLY-439; MET-440;
RP ILE-442; VAL-443; PHE-446; CYS-447; LEU-448; ASP-449; LYS-452; ARG-455;
RP VAL-462; CYS-467; ARG-468; PHE-470; HIS-471; PRO-471; ARG-476; LEU-478;
RP CYS-488; HIS-488 AND SER-507, AND CHARACTERIZATION OF VARIANTS PHE-481 AND
RP SER-549.
RX PubMed=28841266; DOI=10.1002/humu.23315;
RA Frigeni M., Balakrishnan B., Yin X., Calderon F.R.O., Mao R., Pasquali M.,
RA Longo N.;
RT "Functional and molecular studies in primary carnitine deficiency.";
RL Hum. Mutat. 38:1684-1699(2017).
CC -!- FUNCTION: Sodium-ion dependent, high affinity carnitine transporter.
CC Involved in the active cellular uptake of carnitine. Transports one
CC sodium ion with one molecule of carnitine. Also transports organic
CC cations such as tetraethylammonium (TEA) without the involvement of
CC sodium. Also relative uptake activity ratio of carnitine to TEA is
CC 11.3. {ECO:0000269|PubMed:10454528}.
CC -!- SUBUNIT: Interacts with PDZK1. {ECO:0000250}.
CC -!- INTERACTION:
CC O76082; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-9846338, EBI-3044087;
CC O76082; O76011: KRT34; NbExp=3; IntAct=EBI-9846338, EBI-1047093;
CC O76082; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-9846338, EBI-11522433;
CC O76082; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-9846338, EBI-22310682;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10679939}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:10679939}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O76082-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O76082-2; Sequence=VSP_011120, VSP_011121;
CC Name=3; Synonyms=OCTN2VT;
CC IsoId=O76082-3; Sequence=VSP_043904;
CC -!- TISSUE SPECIFICITY: Strongly expressed in kidney, skeletal muscle,
CC heart and placenta. Highly expressed in intestinal cell types affected
CC by Crohn disease, including epithelial cells. Expressed in CD68
CC macrophage and CD43 T-cells but not in CD20 B-cells.
CC {ECO:0000269|PubMed:10454528}.
CC -!- DISEASE: Systemic primary carnitine deficiency (CDSP) [MIM:212140]:
CC Autosomal recessive disorder of fatty acid oxidation caused by
CC defective carnitine transport. Present early in life with hypoketotic
CC hypoglycemia and acute metabolic decompensation, or later in life with
CC skeletal myopathy or cardiomyopathy. {ECO:0000269|PubMed:10072434,
CC ECO:0000269|PubMed:10425211, ECO:0000269|PubMed:10480371,
CC ECO:0000269|PubMed:10545605, ECO:0000269|PubMed:10559218,
CC ECO:0000269|PubMed:10612840, ECO:0000269|PubMed:10679939,
CC ECO:0000269|PubMed:11058897, ECO:0000269|PubMed:11715001,
CC ECO:0000269|PubMed:15617188, ECO:0000269|PubMed:15714519,
CC ECO:0000269|PubMed:16931768, ECO:0000269|PubMed:17126586,
CC ECO:0000269|PubMed:20027113, ECO:0000269|PubMed:20074989,
CC ECO:0000269|PubMed:20574985, ECO:0000269|PubMed:21922592,
CC ECO:0000269|PubMed:28841266}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: Inhibited by emetine, quinidine and verapamil. The
CC IC(50) of emetine is 4.2 uM. Not inhibited by valproic acid.
CC -!- MISCELLANEOUS: [Isoform 3]: Retained in the ER, unable to perform
CC carnitine uptake. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the major facilitator (TC 2.A.1) superfamily.
CC Organic cation transporter (TC 2.A.1.19) family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=The SLC22A5 database;
CC URL="http://www.arup.utah.edu/database/OCTN2/OCTN2_welcome.php";
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DR EMBL; AF057164; AAC24828.1; -; mRNA.
DR EMBL; AB015050; BAA29023.1; -; mRNA.
DR EMBL; AB016625; BAA36712.1; -; Genomic_DNA.
DR EMBL; AB291606; BAF45812.1; -; mRNA.
DR EMBL; AK128610; BAC87527.1; -; mRNA.
DR EMBL; AK313230; BAG36041.1; -; mRNA.
DR EMBL; AC118464; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW62337.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW62338.1; -; Genomic_DNA.
DR EMBL; BC012325; AAH12325.1; -; mRNA.
DR CCDS; CCDS4154.1; -. [O76082-1]
DR CCDS; CCDS78058.1; -. [O76082-3]
DR PIR; JW0089; JW0089.
DR RefSeq; NP_001295051.1; NM_001308122.1. [O76082-3]
DR RefSeq; NP_003051.1; NM_003060.3. [O76082-1]
DR AlphaFoldDB; O76082; -.
DR SMR; O76082; -.
DR BioGRID; 112471; 27.
DR IntAct; O76082; 11.
DR MINT; O76082; -.
DR STRING; 9606.ENSP00000245407; -.
DR BindingDB; O76082; -.
DR ChEMBL; CHEMBL2073693; -.
DR DrugBank; DB08842; Acetylcarnitine.
DR DrugBank; DB03128; Acetylcholine.
DR DrugBank; DB04630; Aldosterone.
DR DrugBank; DB00345; Aminohippuric acid.
DR DrugBank; DB00182; Amphetamine.
DR DrugBank; DB00415; Ampicillin.
DR DrugBank; DB00125; Arginine.
DR DrugBank; DB08795; Azidocillin.
DR DrugBank; DB01053; Benzylpenicillin.
DR DrugBank; DB01140; Cefadroxil.
DR DrugBank; DB00456; Cefalotin.
DR DrugBank; DB00535; Cefdinir.
DR DrugBank; DB01413; Cefepime.
DR DrugBank; DB00671; Cefixime.
DR DrugBank; DB01333; Cefradine.
DR DrugBank; DB00567; Cephalexin.
DR DrugBank; DB00689; Cephaloglycin.
DR DrugBank; DB00122; Choline.
DR DrugBank; DB14006; Choline salicylate.
DR DrugBank; DB00501; Cimetidine.
DR DrugBank; DB00575; Clonidine.
DR DrugBank; DB00148; Creatine.
DR DrugBank; DB01000; Cyclacillin.
DR DrugBank; DB00970; Dactinomycin.
DR DrugBank; DB04133; Degraded Cephaloridine.
DR DrugBank; DB01151; Desipramine.
DR DrugBank; DB01075; Diphenhydramine.
DR DrugBank; DB00988; Dopamine.
DR DrugBank; DB00983; Formoterol.
DR DrugBank; DB00695; Furosemide.
DR DrugBank; DB00365; Grepafloxacin.
DR DrugBank; DB00536; Guanidine.
DR DrugBank; DB05381; Histamine.
DR DrugBank; DB00332; Ipratropium.
DR DrugBank; DB09237; Levamlodipine.
DR DrugBank; DB00583; Levocarnitine.
DR DrugBank; DB00281; Lidocaine.
DR DrugBank; DB00978; Lomefloxacin.
DR DrugBank; DB06691; Mepyramine.
DR DrugBank; DB01577; Metamfetamine.
DR DrugBank; DB06709; Methacholine.
DR DrugBank; DB00627; Niacin.
DR DrugBank; DB00184; Nicotine.
DR DrugBank; DB00368; Norepinephrine.
DR DrugBank; DB01059; Norfloxacin.
DR DrugBank; DB01165; Ofloxacin.
DR DrugBank; DB01032; Probenecid.
DR DrugBank; DB01035; Procainamide.
DR DrugBank; DB00908; Quinidine.
DR DrugBank; DB00468; Quinine.
DR DrugBank; DB14754; Solriamfetol.
DR DrugBank; DB01208; Sparfloxacin.
DR DrugBank; DB00871; Terbutaline.
DR DrugBank; DB08837; Tetraethylammonium.
DR DrugBank; DB00152; Thiamine.
DR DrugBank; DB01409; Tiotropium.
DR DrugBank; DB00313; Valproic acid.
DR DrugBank; DB00661; Verapamil.
DR TCDB; 2.A.1.19.3; the major facilitator superfamily (mfs).
DR GlyGen; O76082; 3 sites.
DR iPTMnet; O76082; -.
DR PhosphoSitePlus; O76082; -.
DR BioMuta; SLC22A5; -.
DR EPD; O76082; -.
DR MassIVE; O76082; -.
DR MaxQB; O76082; -.
DR PaxDb; O76082; -.
DR PeptideAtlas; O76082; -.
DR PRIDE; O76082; -.
DR ProteomicsDB; 50388; -. [O76082-1]
DR ProteomicsDB; 50389; -. [O76082-2]
DR ProteomicsDB; 50390; -. [O76082-3]
DR Antibodypedia; 45160; 181 antibodies from 30 providers.
DR DNASU; 6584; -.
DR Ensembl; ENST00000245407.8; ENSP00000245407.3; ENSG00000197375.14. [O76082-1]
DR Ensembl; ENST00000435065.7; ENSP00000402760.2; ENSG00000197375.14. [O76082-3]
DR GeneID; 6584; -.
DR KEGG; hsa:6584; -.
DR MANE-Select; ENST00000245407.8; ENSP00000245407.3; NM_003060.4; NP_003051.1.
DR UCSC; uc003kww.5; human. [O76082-1]
DR CTD; 6584; -.
DR DisGeNET; 6584; -.
DR GeneCards; SLC22A5; -.
DR GeneReviews; SLC22A5; -.
DR HGNC; HGNC:10969; SLC22A5.
DR HPA; ENSG00000197375; Tissue enhanced (skeletal).
DR MalaCards; SLC22A5; -.
DR MIM; 212140; phenotype.
DR MIM; 603377; gene.
DR neXtProt; NX_O76082; -.
DR OpenTargets; ENSG00000197375; -.
DR Orphanet; 158; Systemic primary carnitine deficiency.
DR PharmGKB; PA333; -.
DR VEuPathDB; HostDB:ENSG00000197375; -.
DR eggNOG; KOG0255; Eukaryota.
DR GeneTree; ENSGT00940000154155; -.
DR HOGENOM; CLU_001265_33_4_1; -.
DR InParanoid; O76082; -.
DR OMA; MSWWLVP; -.
DR OrthoDB; 396963at2759; -.
DR PhylomeDB; O76082; -.
DR TreeFam; TF315847; -.
DR PathwayCommons; O76082; -.
DR Reactome; R-HSA-200425; Carnitine metabolism.
DR Reactome; R-HSA-549127; Organic cation transport.
DR Reactome; R-HSA-5619053; Defective SLC22A5 causes systemic primary carnitine deficiency (CDSP).
DR SignaLink; O76082; -.
DR BioGRID-ORCS; 6584; 13 hits in 1076 CRISPR screens.
DR ChiTaRS; SLC22A5; human.
DR GeneWiki; SLC22A5; -.
DR GenomeRNAi; 6584; -.
DR Pharos; O76082; Tbio.
DR PRO; PR:O76082; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; O76082; protein.
DR Bgee; ENSG00000197375; Expressed in gastrocnemius and 145 other tissues.
DR ExpressionAtlas; O76082; baseline and differential.
DR Genevisible; O76082; HS.
DR GO; GO:0016324; C:apical plasma membrane; IDA:BHF-UCL.
DR GO; GO:0031526; C:brush border membrane; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISS:ARUK-UCL.
DR GO; GO:0005829; C:cytosol; ISS:ARUK-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:ARUK-UCL.
DR GO; GO:1901235; F:(R)-carnitine transmembrane transporter activity; IMP:ARUK-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0015226; F:carnitine transmembrane transporter activity; IDA:BHF-UCL.
DR GO; GO:0030165; F:PDZ domain binding; IPI:BHF-UCL.
DR GO; GO:0015651; F:quaternary ammonium group transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IC:BHF-UCL.
DR GO; GO:1902270; P:(R)-carnitine transmembrane transport; IMP:ARUK-UCL.
DR GO; GO:1902603; P:carnitine transmembrane transport; TAS:Reactome.
DR GO; GO:0015879; P:carnitine transport; IDA:BHF-UCL.
DR GO; GO:0060731; P:positive regulation of intestinal epithelial structure maintenance; IMP:BHF-UCL.
DR GO; GO:0015697; P:quaternary ammonium group transport; IDA:ARUK-UCL.
DR GO; GO:0009609; P:response to symbiotic bacterium; IMP:BHF-UCL.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR GO; GO:0070715; P:sodium-dependent organic cation transport; IDA:BHF-UCL.
DR GO; GO:0150104; P:transport across blood-brain barrier; ISS:ARUK-UCL.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IC:BHF-UCL.
DR CDD; cd17376; MFS_SLC22A4_5_OCTN1_2; 1.
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; IPR045915; S22A4/5.
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 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Disease variant; Glycoprotein;
KW Ion transport; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Sodium; Sodium transport; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..557
FT /note="Solute carrier family 22 member 5"
FT /id="PRO_0000220500"
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..341
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 363..373
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 395..406
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..430
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 431..451
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 452..462
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 463..483
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 484..488
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 489..509
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT REGION 535..557
FT /note="Disordered"
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 MOD_RES 486
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 550
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
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:0000269|PubMed:19349973"
FT VAR_SEQ 1..336
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_011120"
FT VAR_SEQ 131
FT /note="E -> EQDSGAYNAMKNRMGKKPALCLPAQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17509700"
FT /id="VSP_043904"
FT VAR_SEQ 337..351
FT /note="TWNIRMVTIMSIMLW -> MWILLFQLSSALCFR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_011121"
FT VARIANT 4..557
FT /note="Missing (in CDSP)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079640"
FT VARIANT 12
FT /note="G -> S (in CDSP; unknown pathological significance;
FT reduces carnitine transport but the mutant retains 50% of
FT wild-type activity; dbSNP:rs139203363)"
FT /evidence="ECO:0000269|PubMed:20574985,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_064109"
FT VARIANT 15
FT /note="G -> W (in CDSP; carnitine transport reduced to less
FT than 20% of wild-type; dbSNP:rs267607052)"
FT /evidence="ECO:0000269|PubMed:20027113,
FT ECO:0000269|PubMed:20574985, ECO:0000269|PubMed:21922592,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_064110"
FT VARIANT 16
FT /note="P -> L (in CDSP; loss of carnitine transport)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079641"
FT VARIANT 17
FT /note="F -> L (in CDSP; carnitine transport reduced to less
FT than 20% of wild-type; dbSNP:rs11568520)"
FT /evidence="ECO:0000269|PubMed:16931768,
FT ECO:0000269|PubMed:20074989, ECO:0000269|PubMed:20574985,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_020347"
FT VARIANT 19
FT /note="R -> P (in CDSP; carnitine transport is reduced to
FT less than 5% of normal; dbSNP:rs72552723)"
FT /evidence="ECO:0000269|PubMed:11715001,
FT ECO:0000269|PubMed:15714519, ECO:0000269|PubMed:21922592,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_064111"
FT VARIANT 20
FT /note="L -> H (in CDSP; unknown pathological significance;
FT reduces carnitine transport but the mutant retains 50% of
FT wild-type activity; dbSNP:rs144020613)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079642"
FT VARIANT 22
FT /note="Missing (in CDSP; reduces carnitine transport to
FT less than 1% of normal)"
FT /evidence="ECO:0000269|PubMed:21922592,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_066842"
FT VARIANT 26
FT /note="S -> N (in CDSP; carnitine transport reduced to less
FT than 6% of wild-type; dbSNP:rs772578415)"
FT /evidence="ECO:0000269|PubMed:21922592,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_066843"
FT VARIANT 28
FT /note="S -> I (in CDSP; carnitine transport reduced to 1%
FT of wild-type; dbSNP:rs72552724)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079643"
FT VARIANT 32
FT /note="N -> S (in CDSP; carnitine transport reduced to less
FT than 1% of wild-type; dbSNP:rs72552725)"
FT /evidence="ECO:0000269|PubMed:17126586,
FT ECO:0000269|PubMed:20574985, ECO:0000269|PubMed:21922592,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_064112"
FT VARIANT 44
FT /note="A -> V (in CDSP; carnitine transport reduced to less
FT than 10% of wild-type; dbSNP:rs199689597)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079644"
FT VARIANT 46
FT /note="P -> L (in CDSP; carnitine transport reduced to less
FT than 5% of wild-type; dbSNP:rs377767445)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079645"
FT VARIANT 46
FT /note="P -> S (in CDSP; carnitine transport is reduced to
FT less than 5% of normal; dbSNP:rs202088921)"
FT /evidence="ECO:0000269|PubMed:17126586,
FT ECO:0000269|PubMed:20027113, ECO:0000269|PubMed:20574985,
FT ECO:0000269|PubMed:21922592, ECO:0000269|PubMed:28841266"
FT /id="VAR_064113"
FT VARIANT 50
FT /note="C -> Y (in CDSP; loss of carnitine transport)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079646"
FT VARIANT 66
FT /note="T -> P (in CDSP; carnitine transport reduced to 2%
FT of wild-type)"
FT /evidence="ECO:0000269|PubMed:20574985,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_064114"
FT VARIANT 75
FT /note="R -> P (in CDSP; carnitine transport reduced to 2%
FT of wild-type; dbSNP:rs757711838)"
FT /evidence="ECO:0000269|PubMed:20574985,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_064115"
FT VARIANT 83
FT /note="R -> L (in CDSP; loss of carnitine transport;
FT dbSNP:rs72552726)"
FT /evidence="ECO:0000269|PubMed:15617188,
FT ECO:0000269|PubMed:15714519, ECO:0000269|PubMed:20027113,
FT ECO:0000269|PubMed:20574985, ECO:0000269|PubMed:21922592,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_064116"
FT VARIANT 93
FT /note="S -> W (in CDSP; loss of carnitine transport;
FT dbSNP:rs386134190)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079647"
FT VARIANT 95
FT /note="L -> V (in CDSP; unknown pathological significance;
FT reduces carnitine transport but the mutant retains 30% of
FT wild-type activity; dbSNP:rs386134191)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079648"
FT VARIANT 96
FT /note="G -> A (in CDSP; carnitine transport reduced to 20%
FT of wild-type; dbSNP:rs377767450)"
FT /evidence="ECO:0000269|PubMed:20574985,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_064117"
FT VARIANT 115
FT /note="D -> G (in CDSP; carnitine transport reduced to less
FT than 5% of wild-type; dbSNP:rs386134192)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079649"
FT VARIANT 117..557
FT /note="Missing (in CDSP)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079650"
FT VARIANT 122
FT /note="D -> Y (in CDSP; dbSNP:rs201082652)"
FT /evidence="ECO:0000269|PubMed:20574985"
FT /id="VAR_064118"
FT VARIANT 123
FT /note="V -> G (in CDSP; carnitine transport reduced to less
FT than 20% of wild-type; dbSNP:rs748605096)"
FT /evidence="ECO:0000269|PubMed:20574985,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_064119"
FT VARIANT 131
FT /note="E -> D (in CDSP; may affect splicing; unknown
FT pathological significance; reduces carnitine transport but
FT the mutant retains 30% of wild-type activity)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079651"
FT VARIANT 132..557
FT /note="Missing (in CDSP)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079652"
FT VARIANT 140..557
FT /note="Missing (in CDSP)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079653"
FT VARIANT 142
FT /note="A -> S (in CDSP; unknown pathological significance;
FT reduces carnitine transport but the mutant retains more
FT than 25% of wild-type activity; dbSNP:rs151231558)"
FT /evidence="ECO:0000269|PubMed:20027113,
FT ECO:0000269|PubMed:20574985, ECO:0000269|PubMed:21922592,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_064120"
FT VARIANT 143
FT /note="P -> L (in CDSP; carnitine transport reduced to less
FT than 2% of wild-type; dbSNP:rs1178584184)"
FT /evidence="ECO:0000269|PubMed:20074989,
FT ECO:0000269|PubMed:20574985, ECO:0000269|PubMed:28841266"
FT /id="VAR_064121"
FT VARIANT 144
FT /note="L -> F (in dbSNP:rs10040427)"
FT /evidence="ECO:0000269|PubMed:16931768"
FT /id="VAR_020348"
FT VARIANT 151
FT /note="V -> M (in CDSP; unknown pathological significance;
FT reduces carnitine transport but the mutant retains more
FT than 60% of wild-type activity; dbSNP:rs386134193)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079654"
FT VARIANT 169
FT /note="R -> P (in CDSP; loss of carnitine transport)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079655"
FT VARIANT 169
FT /note="R -> Q (in CDSP; loss of carnitine transport;
FT dbSNP:rs121908889)"
FT /evidence="ECO:0000269|PubMed:10425211,
FT ECO:0000269|PubMed:20574985, ECO:0000269|PubMed:21922592,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_009252"
FT VARIANT 169
FT /note="R -> W (in CDSP; loss of carnitine transport;
FT dbSNP:rs121908890)"
FT /evidence="ECO:0000269|PubMed:11058897,
FT ECO:0000269|PubMed:15714519, ECO:0000269|PubMed:20574985,
FT ECO:0000269|PubMed:21922592, ECO:0000269|PubMed:28841266"
FT /id="VAR_064122"
FT VARIANT 175
FT /note="V -> M (in CDSP; carnitine transport reduced to less
FT than 10% of wild-type; dbSNP:rs781721860)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079656"
FT VARIANT 177
FT /note="M -> V (in CDSP; carnitine transport reduced to less
FT than 20% of wild-type; dbSNP:rs145068530)"
FT /evidence="ECO:0000269|PubMed:20574985,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_064123"
FT VARIANT 179
FT /note="M -> L (in CDSP; unknown pathological significance;
FT reduces carnitine transport but the mutant retains more
FT than 40% of wild-type activity; dbSNP:rs386134196)"
FT /evidence="ECO:0000269|PubMed:10545605,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_022564"
FT VARIANT 186
FT /note="L -> P (in CDSP; loss of carnitine transport;
FT dbSNP:rs386134197)"
FT /evidence="ECO:0000269|PubMed:20574985,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_064124"
FT VARIANT 205
FT /note="M -> R (in CDSP; loss of carnitine transport;
FT dbSNP:rs796052033)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079657"
FT VARIANT 210
FT /note="N -> S (in CDSP; loss of carnitine transport;
FT dbSNP:rs386134198)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079658"
FT VARIANT 211
FT /note="Y -> C (in CDSP; loss of carnitine transport;
FT dbSNP:rs121908888)"
FT /evidence="ECO:0000269|PubMed:10480371,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_009253"
FT VARIANT 214
FT /note="A -> V (in CDSP; unknown pathological significance;
FT reduces carnitine transport but the mutant retains 30% of
FT wild-type activity; dbSNP:rs386134199)"
FT /evidence="ECO:0000269|PubMed:20027113,
FT ECO:0000269|PubMed:20574985, ECO:0000269|PubMed:21922592,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_064125"
FT VARIANT 219
FT /note="T -> K (in CDSP; unknown pathological significance;
FT reduces carnitine transport but the mutant retains 30% of
FT wild-type activity)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079659"
FT VARIANT 225
FT /note="S -> L (in CDSP; reduces carnitine transport to less
FT than 20% of wild-type activity; dbSNP:rs386134205)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079660"
FT VARIANT 227
FT /note="R -> H (in CDSP; reduces carnitine transport to less
FT than 10% of wild-type activity; dbSNP:rs185551386)"
FT /evidence="ECO:0000269|PubMed:20574985,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_064126"
FT VARIANT 230
FT /note="F -> L (in CDSP; reduces carnitine transport to less
FT than 1% of wild-type activity; dbSNP:rs756650860)"
FT /evidence="ECO:0000269|PubMed:20574985,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_064127"
FT VARIANT 231
FT /note="S -> F (in CDSP; loss of carnitine transport;
FT dbSNP:rs386134206)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079661"
FT VARIANT 232
FT /note="T -> M (in CDSP; reduces carnitine transport to less
FT than 20% of wild-type activity; dbSNP:rs114269482)"
FT /evidence="ECO:0000269|PubMed:15714519,
FT ECO:0000269|PubMed:20027113, ECO:0000269|PubMed:20574985,
FT ECO:0000269|PubMed:21922592, ECO:0000269|PubMed:28841266"
FT /id="VAR_064128"
FT VARIANT 234
FT /note="G -> R (in CDSP; dbSNP:rs1457258524)"
FT /evidence="ECO:0000269|PubMed:20074989"
FT /id="VAR_064129"
FT VARIANT 240
FT /note="A -> T (in CDSP; reduces carnitine transport to less
FT than 2% of wild-type activity)"
FT /evidence="ECO:0000269|PubMed:20574985,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_064130"
FT VARIANT 242
FT /note="G -> V (in CDSP; loss of carnitine transport;
FT dbSNP:rs72552728)"
FT /evidence="ECO:0000269|PubMed:11058897,
FT ECO:0000269|PubMed:15714519, ECO:0000269|PubMed:28841266"
FT /id="VAR_064131"
FT VARIANT 247
FT /note="P -> R (in CDSP; loss of carnitine transport)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079662"
FT VARIANT 254..557
FT /note="Missing (in CDSP)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079663"
FT VARIANT 254
FT /note="R -> Q (in CDSP; unknown pathological significance;
FT reduces carnitine transport but the mutant retains more
FT than 30% of wild-type activity; dbSNP:rs200699819)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079664"
FT VARIANT 256..557
FT /note="Missing (in CDSP)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079665"
FT VARIANT 257
FT /note="R -> W (in CDSP; reduces carnitine transport to less
FT than 10% of wild-type activity; dbSNP:rs386134203)"
FT /evidence="ECO:0000269|PubMed:20574985,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_064132"
FT VARIANT 264
FT /note="T -> M (in CDSP; unknown pathological significance;
FT reduces carnitine transport but the mutant retains more
FT than 40% of wild-type activity; dbSNP:rs201262157)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079666"
FT VARIANT 264
FT /note="T -> R (in CDSP; reduces carnitine transport to less
FT than 5% of wild-type activity; dbSNP:rs201262157)"
FT /evidence="ECO:0000269|PubMed:20574985,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_064133"
FT VARIANT 269
FT /note="L -> P (in CDSP; unknown pathological significance;
FT reduces carnitine transport but the mutant retains more
FT than 40% of wild-type activity)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079667"
FT VARIANT 275..557
FT /note="Missing (in CDSP)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079668"
FT VARIANT 280
FT /note="S -> F (in CDSP; reduces carnitine transport to less
FT than 1% of wild-type activity; dbSNP:rs386134208)"
FT /evidence="ECO:0000269|PubMed:21922592,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_066844"
FT VARIANT 282..557
FT /note="Missing (in CDSP)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079669"
FT VARIANT 282
FT /note="R -> Q (in CDSP; reduces carnitine transport to 5%
FT of wild-type activity; dbSNP:rs386134210)"
FT /evidence="ECO:0000269|PubMed:20074989,
FT ECO:0000269|PubMed:20574985, ECO:0000269|PubMed:21922592,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_064134"
FT VARIANT 283
FT /note="W -> C (in CDSP; loss of carnitine transport;
FT dbSNP:rs386134211)"
FT /evidence="ECO:0000269|PubMed:10545605,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_022565"
FT VARIANT 283
FT /note="W -> R (in CDSP; reduces carnitine transport to less
FT than 1% of wild-type activity; dbSNP:rs72552729)"
FT /evidence="ECO:0000269|PubMed:10612840,
FT ECO:0000269|PubMed:21922592, ECO:0000269|PubMed:28841266"
FT /id="VAR_009254"
FT VARIANT 289..557
FT /note="Missing (in CDSP; dbSNP:rs1554087707)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079670"
FT VARIANT 295..557
FT /note="Missing (in CDSP)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079671"
FT VARIANT 301
FT /note="A -> D (in CDSP; reduces carnitine transport to
FT less-than-1% to 3% of wild-type activity;
FT dbSNP:rs72552730)"
FT /evidence="ECO:0000269|PubMed:11058897,
FT ECO:0000269|PubMed:15714519, ECO:0000269|PubMed:28841266"
FT /id="VAR_064135"
FT VARIANT 312
FT /note="I -> V (in CDSP; unknown pathological significance;
FT reduces carnitine transport but the mutant retains 70% of
FT wild-type activity; dbSNP:rs77300588)"
FT /evidence="ECO:0000269|PubMed:20574985,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_064136"
FT VARIANT 317
FT /note="E -> K (in CDSP; unknown pathological significance;
FT no effect on carnitine transport; dbSNP:rs774792831)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079672"
FT VARIANT 319..557
FT /note="Missing (in CDSP)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079673"
FT VARIANT 348
FT /note="I -> T (in CDSP; unknown pathological significance;
FT reduces carnitine transport but the mutant retains 60% of
FT wild-type activity; dbSNP:rs150544263)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079674"
FT VARIANT 351
FT /note="W -> R (in CDSP; loss of carnitine transport;
FT dbSNP:rs68018207)"
FT /evidence="ECO:0000269|PubMed:11058897,
FT ECO:0000269|PubMed:15714519, ECO:0000269|PubMed:21922592,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_064137"
FT VARIANT 355
FT /note="S -> L (in CDSP; reduces carnitine transport to less
FT than 2% of wild-type activity; dbSNP:rs1385634398)"
FT /evidence="ECO:0000269|PubMed:20574985,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_064138"
FT VARIANT 358
FT /note="Y -> N (in CDSP; loss of carnitine transport;
FT dbSNP:rs61731073)"
FT /evidence="ECO:0000269|PubMed:20574985,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_064139"
FT VARIANT 362
FT /note="S -> L (in CDSP; dbSNP:rs886042092)"
FT /evidence="ECO:0000269|PubMed:20074989"
FT /id="VAR_064140"
FT VARIANT 363
FT /note="L -> P (in CDSP; loss of carnitine transport;
FT dbSNP:rs386134214)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079675"
FT VARIANT 387..557
FT /note="Missing (in CDSP)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079676"
FT VARIANT 394
FT /note="Missing (in CDSP; reduces carnitine transport to 5%
FT of wild-type activity)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079677"
FT VARIANT 398
FT /note="P -> L (in CDSP; reduces carnitine transport to less
FT than 1% of wild-type activity; dbSNP:rs144547521)"
FT /evidence="ECO:0000269|PubMed:20574985,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_064141"
FT VARIANT 399
FT /note="R -> Q (in CDSP; carnitine transport is reduced to
FT less than 1% of normal; dbSNP:rs121908891)"
FT /evidence="ECO:0000269|PubMed:11715001,
FT ECO:0000269|PubMed:15714519, ECO:0000269|PubMed:28841266"
FT /id="VAR_064142"
FT VARIANT 399
FT /note="R -> W (in CDSP; reduces carnitine transport to less
FT than 5% of wild-type activity; dbSNP:rs267607054)"
FT /evidence="ECO:0000269|PubMed:20027113,
FT ECO:0000269|PubMed:20574985, ECO:0000269|PubMed:28841266"
FT /id="VAR_064143"
FT VARIANT 412
FT /note="S -> G (in CDSP; unknown pathological significance;
FT no effect on carnitine transport)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079678"
FT VARIANT 439
FT /note="V -> G (in CDSP; reduces carnitine transport to less
FT than 1% of wild-type activity)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079679"
FT VARIANT 440
FT /note="T -> M (in CDSP; loss of carnitine transport;
FT dbSNP:rs72552732)"
FT /evidence="ECO:0000269|PubMed:20574985,
FT ECO:0000269|PubMed:21922592, ECO:0000269|PubMed:28841266"
FT /id="VAR_064144"
FT VARIANT 442
FT /note="A -> I (in CDSP; requires 2 nucleotide
FT substitutions; reduces carnitine transport to less than 20%
FT of wild-type activity; dbSNP:rs267607053)"
FT /evidence="ECO:0000269|PubMed:20027113,
FT ECO:0000269|PubMed:20574985, ECO:0000269|PubMed:21922592,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_064145"
FT VARIANT 443
FT /note="F -> V (in CDSP; reduces carnitine transport to less
FT than 1% of wild-type)"
FT /evidence="ECO:0000269|PubMed:20574985,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_064146"
FT VARIANT 446
FT /note="V -> F (in CDSP; reduces carnitine transport to less
FT than 1% of wild-type; dbSNP:rs72552733)"
FT /evidence="ECO:0000269|PubMed:10612840,
FT ECO:0000269|PubMed:21922592, ECO:0000269|PubMed:28841266"
FT /id="VAR_009255"
FT VARIANT 447
FT /note="Y -> C (in CDSP; loss of carnitine transport;
FT dbSNP:rs386134218)"
FT /evidence="ECO:0000269|PubMed:15714519,
FT ECO:0000269|PubMed:21922592, ECO:0000269|PubMed:28841266"
FT /id="VAR_064147"
FT VARIANT 448
FT /note="V -> L (in CDSP; reduces carnitine transport to less
FT than 20% of wild-type; dbSNP:rs386134219)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079680"
FT VARIANT 449
FT /note="Y -> D (in CDSP; unknown pathological significance;
FT reduces carnitine transport to less than 20% of wild-type;
FT dbSNP:rs11568514)"
FT /evidence="ECO:0000269|PubMed:15714519,
FT ECO:0000269|PubMed:16931768, ECO:0000269|PubMed:20574985,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_029315"
FT VARIANT 452
FT /note="E -> K (in CDSP; reduces carnitine transport to less
FT than 5% of wild-type; dbSNP:rs72552734)"
FT /evidence="ECO:0000269|PubMed:10679939,
FT ECO:0000269|PubMed:15714519, ECO:0000269|PubMed:20574985,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_009256"
FT VARIANT 455
FT /note="P -> R (in CDSP; loss of carnitine transport;
FT dbSNP:rs1408166345)"
FT /evidence="ECO:0000269|PubMed:20574985,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_064148"
FT VARIANT 462
FT /note="G -> V (in CDSP; reduces carnitine transport to less
FT than 5% of wild-type)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079681"
FT VARIANT 467
FT /note="S -> C (in CDSP; reduces carnitine transport to less
FT than 20% of wild-type activity; dbSNP:rs60376624)"
FT /evidence="ECO:0000269|PubMed:10545605,
FT ECO:0000269|PubMed:17126586, ECO:0000269|PubMed:20074989,
FT ECO:0000269|PubMed:20574985, ECO:0000269|PubMed:21922592,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_022566"
FT VARIANT 468
FT /note="T -> R (in CDSP; markedly reduced carnitine
FT transport compared to the wild-type protein; less than 1%
FT of wild-type activity; dbSNP:rs386134221)"
FT /evidence="ECO:0000269|PubMed:15714519,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_064149"
FT VARIANT 470
FT /note="S -> F (in CDSP; loss of carnitine transport;
FT dbSNP:rs386134222)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079682"
FT VARIANT 471
FT /note="R -> C (in CDSP; dbSNP:rs749282641)"
FT /evidence="ECO:0000269|PubMed:20074989"
FT /id="VAR_064150"
FT VARIANT 471
FT /note="R -> H (in CDSP; reduces carnitine transport to less
FT than 2% of wild-type; dbSNP:rs386134223)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079683"
FT VARIANT 471
FT /note="R -> P (in CDSP; loss of carnitine transport)"
FT /evidence="ECO:0000269|PubMed:21922592,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_066845"
FT VARIANT 476
FT /note="L -> R (in CDSP; loss of carnitine transport)"
FT /evidence="ECO:0000269|PubMed:28841266"
FT /id="VAR_079684"
FT VARIANT 478
FT /note="P -> L (in CDSP; loss of carnitine transport but
FT stimulated organic cation transport; dbSNP:rs72552735)"
FT /evidence="ECO:0000269|PubMed:10072434,
FT ECO:0000269|PubMed:10559218, ECO:0000269|PubMed:28841266"
FT /id="VAR_009257"
FT VARIANT 481
FT /note="V -> F (reduces carnitine transport but the mutant
FT retains more than 60% of wild-type activity;
FT dbSNP:rs11568513)"
FT /evidence="ECO:0000269|PubMed:16931768,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_020349"
FT VARIANT 481
FT /note="V -> I (in dbSNP:rs11568513)"
FT /evidence="ECO:0000269|PubMed:16931768"
FT /id="VAR_036816"
FT VARIANT 488
FT /note="R -> C (in CDSP; reduces carnitine transport to less
FT than 10% of wild-type; dbSNP:rs377216516)"
FT /evidence="ECO:0000269|PubMed:17126586,
FT ECO:0000269|PubMed:20574985, ECO:0000269|PubMed:28841266"
FT /id="VAR_064151"
FT VARIANT 488
FT /note="R -> H (in CDSP; unknown pathological significance;
FT reduces carnitine transport to 40% of wild-type;
FT dbSNP:rs28383481)"
FT /evidence="ECO:0000269|PubMed:21922592,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_066846"
FT VARIANT 507
FT /note="L -> S (in CDSP; reduces carnitine transport to 5%
FT of wild-type; dbSNP:rs1157198543)"
FT /evidence="ECO:0000269|PubMed:20574985,
FT ECO:0000269|PubMed:28841266"
FT /id="VAR_064152"
FT VARIANT 508
FT /note="F -> L (in dbSNP:rs11568521)"
FT /evidence="ECO:0000269|PubMed:16931768"
FT /id="VAR_029316"
FT VARIANT 530
FT /note="M -> V (in dbSNP:rs11568524)"
FT /evidence="ECO:0000269|PubMed:16931768"
FT /id="VAR_029317"
FT VARIANT 549
FT /note="P -> S (reduces carnitine transport but the mutant
FT retains more than 20% of wild-type activity;
FT dbSNP:rs11568525)"
FT /evidence="ECO:0000269|PubMed:16931768,
FT ECO:0000269|PubMed:20574985, ECO:0000269|PubMed:28841266"
FT /id="VAR_020350"
FT MUTAGEN 352
FT /note="M->R: Loss of both carnitine and organic cation
FT transport functionalities."
FT /evidence="ECO:0000269|PubMed:10559218"
FT CONFLICT 114
FT /note="L -> P (in Ref. 8; AAH12325)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 557 AA; 62752 MW; 928B1F6EFF63C48D CRC64;
MRDYDEVTAF LGEWGPFQRL IFFLLSASII PNGFTGLSSV FLIATPEHRC RVPDAANLSS
AWRNHTVPLR LRDGREVPHS CRRYRLATIA NFSALGLEPG RDVDLGQLEQ ESCLDGWEFS
QDVYLSTIVT EWNLVCEDDW KAPLTISLFF VGVLLGSFIS GQLSDRFGRK NVLFVTMGMQ
TGFSFLQIFS KNFEMFVVLF VLVGMGQISN YVAAFVLGTE ILGKSVRIIF STLGVCIFYA
FGYMVLPLFA YFIRDWRMLL VALTMPGVLC VALWWFIPES PRWLISQGRF EEAEVIIRKA
AKANGIVVPS TIFDPSELQD LSSKKQQSHN ILDLLRTWNI RMVTIMSIML WMTISVGYFG
LSLDTPNLHG DIFVNCFLSA MVEVPAYVLA WLLLQYLPRR YSMATALFLG GSVLLFMQLV
PPDLYYLATV LVMVGKFGVT AAFSMVYVYT AELYPTVVRN MGVGVSSTAS RLGSILSPYF
VYLGAYDRFL PYILMGSLTI LTAILTLFLP ESFGTPLPDT IDQMLRVKGM KHRKTPSHTR
MLKDGQERPT ILKSTAF
