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Sodium- and chloride-dependent creatine transporter 1 (CT1) (Creatine transporter 1) (Solute carrier family 6 member 8)

 SC6A8_HUMAN             Reviewed;         635 AA.
P48029; B2KY47; B4DIA3; E9PFC0; Q13032; Q66I36;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
27-SEP-2017, entry version 167.
RecName: Full=Sodium- and chloride-dependent creatine transporter 1;
Short=CT1;
Short=Creatine transporter 1;
AltName: Full=Solute carrier family 6 member 8;
Name=SLC6A8;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Kidney;
PubMed=7953292;
Nash S.R., Giros B., Kingsmore S.F., Rochelle J.M., Suter S.T.,
Gregor P., Seldin M.F., Caron M.G.;
"Cloning, pharmacological characterization, and genomic localization
of the human creatine transporter.";
Recept. Channels 2:165-174(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=7945388; DOI=10.1006/bbrc.1994.2475;
Sora I., Richman J., Santoro G., Wei H., Wang Y., Vanderah T.,
Horvath R., Nguyen M., Waite S., Roeske W.R.;
"The cloning and expression of a human creatine transporter.";
Biochem. Biophys. Res. Commun. 204:419-427(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8661155; DOI=10.1006/geno.1996.0373;
Sandoval N., Bauer D., Brenner V., Coy J.F., Drescher B., Kioschis P.,
Korn B., Nyakatura G., Poustka A., Reichwald K., Rosenthal A.,
Platzer M.;
"The genomic organization of a human creatine transporter (CRTR) gene
located in Xq28.";
Genomics 35:383-385(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Hippocampus;
PubMed=7622069; DOI=10.1016/0378-1119(95)00104-E;
Barnwell L.F., Chaudhuri G., Townsel J.G.;
"Cloning and sequencing of a cDNA encoding a novel member of the human
brain GABA/noradrenaline neurotransmitter transporter family.";
Gene 159:287-288(1995).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
PubMed=18515020; DOI=10.1016/j.gene.2008.04.003;
Martinez-Munoz C., Rosenberg E.H., Jakobs C., Salomons G.S.;
"Identification, characterization and cloning of SLC6A8C, a novel
splice variant of the creatine transporter gene.";
Gene 418:53-59(2008).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Eichler E.E., Lu F., Shen Y., Muzny D.M., Gibbs R.A., Nelson D.L.;
"Genomic organization of the human creatine transporter and CDM
genes.";
Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Hippocampus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Eye, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-42, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-42; THR-617 AND THR-620,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
VARIANT CCDS1 ARG-381.
PubMed=11898126; DOI=10.1086/340092;
Hahn K.A., Salomons G.S., Tackels-Horne D., Wood T.C., Taylor H.A.,
Schroer R.J., Lubs H.A., Jakobs C., Olson R.L., Holden K.R.,
Stevenson R.E., Schwartz C.E.;
"X-linked mental retardation with seizures and carrier manifestations
is caused by a mutation in the creatine-transporter gene (SLC6A8)
located in Xq28.";
Am. J. Hum. Genet. 70:1349-1356(2002).
[14]
VARIANT CCDS1 PHE-408 DEL.
PubMed=12210795; DOI=10.1002/ana.10246;
Bizzi A., Bugiani M., Salomons G.S., Hunneman D.H., Moroni I.,
Estienne M., Danesi U., Jakobs C., Uziel G.;
"X-linked creatine deficiency syndrome: a novel mutation in creatine
transporter gene SLC6A8.";
Ann. Neurol. 52:227-231(2002).
[15]
VARIANTS CCDS1 ARG-87; TRP-337; LEU-390 AND LEU-554, AND VARIANT
VAL-560.
PubMed=15154114; DOI=10.1086/422102;
Rosenberg E.H., Almeida L.S., Kleefstra T., deGrauw R.S., Yntema H.G.,
Bahi N., Moraine C., Ropers H.-H., Fryns J.-P., deGrauw T.J.,
Jakobs C., Salomons G.S.;
"High prevalence of SLC6A8 deficiency in X-linked mental
retardation.";
Am. J. Hum. Genet. 75:97-105(2004).
[16]
VARIANTS CCDS1 VAL-132 AND TRP-491.
PubMed=17101918; DOI=10.1212/01.wnl.0000239153.39710.81;
Lion-Francois L., Cheillan D., Pitelet G., Acquaviva-Bourdain C.,
Bussy G., Cotton F., Guibaud L., Gerard D., Rivier C.,
Vianey-Saban C., Jakobs C., Salomons G.S., des Portes V.;
"High frequency of creatine deficiency syndromes in patients with
unexplained mental retardation.";
Neurology 67:1713-1714(2006).
[17]
VARIANTS CCDS1 ARG-87; PHE-107 DEL; ASN-336 DEL; TRP-337; ILE-347 DEL;
LEU-390; TRP-391 AND LEU-554, VARIANTS ARG-4; ARG-26; VAL-560 AND
ILE-629, CHARACTERIZATION OF VARIANTS CCDS1 ARG-87; PHE-107 DEL;
ASN-336 DEL; TRP-337; ILE-347 DEL; LEU-390 AND TRP-391, AND
CHARACTERIZATION OF VARIANTS ARG-4; ARG-26; VAL-560 AND ILE-629.
PubMed=17465020; DOI=10.1002/humu.20532;
Rosenberg E.H., Martinez Munoz C., Betsalel O.T., van Dooren S.J.,
Fernandez M., Jakobs C., deGrauw T.J., Kleefstra T., Schwartz C.E.,
Salomons G.S.;
"Functional characterization of missense variants in the creatine
transporter gene (SLC6A8): improved diagnostic application.";
Hum. Mutat. 28:890-896(2007).
[18]
VARIANT CCDS1 ASN-336 DEL.
PubMed=23033978; DOI=10.1056/NEJMoa1206524;
de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P.,
Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B.,
Brunner H.G., Veltman J.A., Vissers L.E.;
"Diagnostic exome sequencing in persons with severe intellectual
disability.";
N. Engl. J. Med. 367:1921-1929(2012).
[19]
VARIANT SER-550.
PubMed=23092983; DOI=10.1038/tp.2012.102;
Nava C., Lamari F., Heron D., Mignot C., Rastetter A., Keren B.,
Cohen D., Faudet A., Bouteiller D., Gilleron M., Jacquette A.,
Whalen S., Afenjar A., Perisse D., Laurent C., Dupuits C., Gautier C.,
Gerard M., Huguet G., Caillet S., Leheup B., Leboyer M., Gillberg C.,
Delorme R., Bourgeron T., Brice A., Depienne C.;
"Analysis of the chromosome X exome in patients with autism spectrum
disorders identified novel candidate genes, including TMLHE.";
Transl. Psychiatry 2:E179-E179(2012).
[20]
VARIANT CCDS1 ASN-336 DEL.
PubMed=24123876; DOI=10.1136/jmedgenet-2013-101644;
Schuurs-Hoeijmakers J.H., Vulto-van Silfhout A.T., Vissers L.E.,
van de Vondervoort I.I., van Bon B.W., de Ligt J., Gilissen C.,
Hehir-Kwa J.Y., Neveling K., del Rosario M., Hira G., Reitano S.,
Vitello A., Failla P., Greco D., Fichera M., Galesi O., Kleefstra T.,
Greally M.T., Ockeloen C.W., Willemsen M.H., Bongers E.M.,
Janssen I.M., Pfundt R., Veltman J.A., Romano C., Willemsen M.A.,
van Bokhoven H., Brunner H.G., de Vries B.B., de Brouwer A.P.;
"Identification of pathogenic gene variants in small families with
intellectually disabled siblings by exome sequencing.";
J. Med. Genet. 50:802-811(2013).
[21]
VARIANTS CCDS1 HIS-80; CYS-383; ASP-448 AND ILE-539.
PubMed=23660394; DOI=10.1016/j.ymgme.2013.04.006;
Comeaux M.S., Wang J., Wang G., Kleppe S., Zhang V.W., Schmitt E.S.,
Craigen W.J., Renaud D., Sun Q., Wong L.J.;
"Biochemical, molecular, and clinical diagnoses of patients with
cerebral creatine deficiency syndromes.";
Mol. Genet. Metab. 109:260-268(2013).
[22]
VARIANT CCDS1 LEU-552, CHARACTERIZATION OF VARIANT CCDS1 LEU-552,
VARIANTS HIS-186; MET-270; GLN-294; LEU-314; THR-318; SER-550;
LEU-564; THR-611 AND LYS-624, AND CHARACTERIZATION OF VARIANTS
HIS-186; MET-270; GLN-294; LEU-314; THR-318; LEU-564; THR-611 AND
LYS-624.
PubMed=25861866; DOI=10.1016/j.gene.2015.04.011;
DesRoches C.L., Patel J., Wang P., Minassian B., Salomons G.S.,
Marshall C.R., Mercimek-Mahmutoglu S.;
"Estimated carrier frequency of creatine transporter deficiency in
females in the general population using functional characterization of
novel missense variants in the SLC6A8 gene.";
Gene 565:187-191(2015).
-!- FUNCTION: Required for the uptake of creatine in muscles and
brain.
-!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=CRT1;
IsoId=P48029-1; Sequence=Displayed;
Name=2; Synonyms=CRT2, SLC6A8B;
IsoId=P48029-2; Sequence=VSP_043917, VSP_043918, VSP_043919,
VSP_043920;
Name=3; Synonyms=SLC6A8C;
IsoId=P48029-3; Sequence=VSP_043916;
Name=4;
IsoId=P48029-4; Sequence=VSP_046316;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle and
kidney. Also found in brain, heart, colon, testis and prostate.
{ECO:0000269|PubMed:7945388, ECO:0000269|PubMed:7953292}.
-!- DISEASE: Cerebral creatine deficiency syndrome 1 (CCDS1)
[MIM:300352]: An X-linked disorder of creatine transport
characterized by mental retardation, severe speech delay,
behavioral abnormalities, and seizures. Carrier females may show
mild neuropsychologic impairment. {ECO:0000269|PubMed:11898126,
ECO:0000269|PubMed:12210795, ECO:0000269|PubMed:15154114,
ECO:0000269|PubMed:17101918, ECO:0000269|PubMed:17465020,
ECO:0000269|PubMed:23033978, ECO:0000269|PubMed:23660394,
ECO:0000269|PubMed:24123876, ECO:0000269|PubMed:25861866}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF)
(TC 2.A.22) family. SLC6A8 subfamily. {ECO:0000305}.
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EMBL; L31409; AAC41688.1; -; mRNA.
EMBL; S74039; AAB32284.1; -; mRNA.
EMBL; U17986; AAA86990.1; -; mRNA.
EMBL; EU280316; ABZ82022.1; -; mRNA.
EMBL; AK295495; BAG58415.1; -; mRNA.
EMBL; U52111; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z66539; CAA91442.1; -; Genomic_DNA.
EMBL; U36341; AAA79507.1; -; Genomic_DNA.
EMBL; BC012355; AAH12355.1; -; mRNA.
EMBL; BC081558; AAH81558.1; -; mRNA.
CCDS; CCDS14726.1; -. [P48029-1]
CCDS; CCDS48190.1; -. [P48029-4]
PIR; G02095; G02095.
PIR; JC2386; JC2386.
RefSeq; NP_001136277.1; NM_001142805.1.
RefSeq; NP_001136278.1; NM_001142806.1. [P48029-4]
RefSeq; NP_005620.1; NM_005629.3. [P48029-1]
UniGene; Hs.540696; -.
ProteinModelPortal; P48029; -.
BioGrid; 112426; 11.
IntAct; P48029; 4.
STRING; 9606.ENSP00000253122; -.
DrugBank; DB00148; Creatine.
TCDB; 2.A.22.3.11; the neurotransmitter:sodium symporter (nss) family.
iPTMnet; P48029; -.
PhosphoSitePlus; P48029; -.
SwissPalm; P48029; -.
BioMuta; SLC6A8; -.
DMDM; 1352529; -.
EPD; P48029; -.
PaxDb; P48029; -.
PeptideAtlas; P48029; -.
PRIDE; P48029; -.
DNASU; 6535; -.
Ensembl; ENST00000253122; ENSP00000253122; ENSG00000130821. [P48029-1]
Ensembl; ENST00000430077; ENSP00000403041; ENSG00000130821. [P48029-4]
GeneID; 6535; -.
KEGG; hsa:6535; -.
UCSC; uc011myx.2; human. [P48029-1]
CTD; 6535; -.
DisGeNET; 6535; -.
EuPathDB; HostDB:ENSG00000130821.15; -.
GeneCards; SLC6A8; -.
GeneReviews; SLC6A8; -.
H-InvDB; HIX0038627; -.
HGNC; HGNC:11055; SLC6A8.
MalaCards; SLC6A8; -.
MIM; 300036; gene.
MIM; 300352; phenotype.
neXtProt; NX_P48029; -.
OpenTargets; ENSG00000130821; -.
Orphanet; 52503; X-linked creatine transporter deficiency.
PharmGKB; PA35915; -.
eggNOG; KOG3659; Eukaryota.
eggNOG; COG0733; LUCA.
GeneTree; ENSGT00760000118857; -.
HOGENOM; HOG000203877; -.
HOVERGEN; HBG071421; -.
InParanoid; P48029; -.
KO; K05039; -.
OMA; VPPRETW; -.
OrthoDB; EOG091G08PX; -.
PhylomeDB; P48029; -.
TreeFam; TF343812; -.
Reactome; R-HSA-71288; Creatine metabolism.
GeneWiki; SLC6A8; -.
GenomeRNAi; 6535; -.
PRO; PR:P48029; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000130821; -.
CleanEx; HS_SLC6A8; -.
ExpressionAtlas; P48029; baseline and differential.
Genevisible; P48029; HS.
GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005308; F:creatine transmembrane transporter activity; NAS:UniProtKB.
GO; GO:0005309; F:creatine:sodium symporter activity; IBA:GO_Central.
GO; GO:0005328; F:neurotransmitter:sodium symporter activity; IEA:InterPro.
GO; GO:0006600; P:creatine metabolic process; TAS:Reactome.
GO; GO:0015881; P:creatine transport; IMP:UniProtKB.
GO; GO:0006936; P:muscle contraction; TAS:ProtInc.
GO; GO:0006810; P:transport; TAS:ProtInc.
InterPro; IPR000175; Na/ntran_symport.
InterPro; IPR002984; Na/ntran_symport_creatine.
PANTHER; PTHR11616; PTHR11616; 1.
Pfam; PF00209; SNF; 1.
PRINTS; PR01199; CRTTRANSPORT.
PRINTS; PR00176; NANEUSMPORT.
PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1.
PROSITE; PS00754; NA_NEUROTRAN_SYMP_2; 1.
PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Disease mutation;
Glycoprotein; Ion transport; Membrane; Mental retardation;
Phosphoprotein; Polymorphism; Reference proteome; Sodium;
Sodium transport; Symport; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 635 Sodium- and chloride-dependent creatine
transporter 1.
/FTId=PRO_0000214774.
TOPO_DOM 1 60 Cytoplasmic. {ECO:0000255}.
TRANSMEM 61 81 Helical. {ECO:0000255}.
TOPO_DOM 82 87 Extracellular. {ECO:0000255}.
TRANSMEM 88 108 Helical. {ECO:0000255}.
TOPO_DOM 109 138 Cytoplasmic. {ECO:0000255}.
TRANSMEM 139 159 Helical. {ECO:0000255}.
TOPO_DOM 160 230 Extracellular. {ECO:0000255}.
TRANSMEM 231 251 Helical. {ECO:0000255}.
TOPO_DOM 252 269 Cytoplasmic. {ECO:0000255}.
TRANSMEM 270 290 Helical. {ECO:0000255}.
TOPO_DOM 291 304 Extracellular. {ECO:0000255}.
TRANSMEM 305 325 Helical. {ECO:0000255}.
TOPO_DOM 326 341 Cytoplasmic. {ECO:0000255}.
TRANSMEM 342 362 Helical. {ECO:0000255}.
TOPO_DOM 363 394 Extracellular. {ECO:0000255}.
TRANSMEM 395 415 Helical. {ECO:0000255}.
TOPO_DOM 416 444 Cytoplasmic. {ECO:0000255}.
TRANSMEM 445 465 Helical. {ECO:0000255}.
TOPO_DOM 466 479 Extracellular. {ECO:0000255}.
TRANSMEM 480 500 Helical. {ECO:0000255}.
TOPO_DOM 501 520 Cytoplasmic. {ECO:0000255}.
TRANSMEM 521 541 Helical. {ECO:0000255}.
TOPO_DOM 542 560 Extracellular. {ECO:0000255}.
TRANSMEM 561 581 Helical. {ECO:0000255}.
TOPO_DOM 582 635 Cytoplasmic. {ECO:0000255}.
MOD_RES 42 42 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 617 617 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 620 620 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 623 623 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VBW1}.
CARBOHYD 192 192 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 197 197 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 548 548 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 365 Missing (in isoform 3).
{ECO:0000303|PubMed:18515020}.
/FTId=VSP_043916.
VAR_SEQ 1 259 MAKKSAENGIYSVSGDEKKGPLIAPGPDGAPAKGDGPVGLG
TPGGRLAVPPRETWTRQMDFIMSCVGFAVGLGNVWRFPYLC
YKNGGGVFLIPYVLIALVGGIPIFFLEISLGQFMKAGSINV
WNICPLFKGLGYASMVIVFYCNTYYIMVLAWGFYYLVKSFT
TTLPWATCGHTWNTPDCVEIFRHEDCANASLANLTCDQLAD
RRSPVIEFWENKVLRLSGGLEVPGALNWEVTLCLLACWVLV
YFCVWKGVKSTGK -> MLPTLQIQGPAAFAPGDRGPGRHC
PFPVPITPTGALLPVSDSCDSLVDLVWPSVTYLALGTQSRV
WPHPLGAPGQAGESPEQRRQCLELWDMASSLGDKVPRAACG
KRGQTVWQLHLACLCLAQFHSPPAQPPPLSRRGGGPDPDPI
SRSLPGPPTPALPTHSYSSHSPRAPRLLSPLRRAPRGSPAP
HRHASLQTNEAPRELPHCTWPGLPGRSLAPSFLWREPWLGG
QWGPLNIPARKGDRRRWEWGCEGGGATASAEQPGPQ (in
isoform 2). {ECO:0000303|PubMed:7622069}.
/FTId=VSP_043917.
VAR_SEQ 1 115 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046316.
VAR_SEQ 417 417 S -> SQVCMGLWDREPGGGRREGCRQGKGWRRCGDRPELP
WP (in isoform 2).
{ECO:0000303|PubMed:7622069}.
/FTId=VSP_043918.
VAR_SEQ 464 464 D -> DVSGVGGLPVTSGGRLPSSLTGLCPQ (in
isoform 2). {ECO:0000303|PubMed:7622069}.
/FTId=VSP_043919.
VAR_SEQ 498 498 Y -> YGRSWLRAGLGDGGGEGRSPAWPSRLTSPQ (in
isoform 2). {ECO:0000303|PubMed:7622069}.
/FTId=VSP_043920.
VARIANT 4 4 K -> R (polymorphism; no effect on
creatine transporter activity).
{ECO:0000269|PubMed:17465020}.
/FTId=VAR_075562.
VARIANT 26 26 G -> R (polymorphism; no effect on
creatine transporter activity).
{ECO:0000269|PubMed:17465020}.
/FTId=VAR_075563.
VARIANT 80 80 Y -> H (in CCDS1).
{ECO:0000269|PubMed:23660394}.
/FTId=VAR_071791.
VARIANT 87 87 G -> R (in CCDS1; decreased creatine
transporter activity; dbSNP:rs122453115).
{ECO:0000269|PubMed:15154114,
ECO:0000269|PubMed:17465020}.
/FTId=VAR_020525.
VARIANT 107 107 Missing (in CCDS1; decreased creatine
transporter activity).
{ECO:0000269|PubMed:17465020}.
/FTId=VAR_075564.
VARIANT 132 132 G -> V (in CCDS1; dbSNP:rs122453117).
{ECO:0000269|PubMed:17101918}.
/FTId=VAR_063707.
VARIANT 164 164 T -> S (in dbSNP:rs642454).
/FTId=VAR_034483.
VARIANT 186 186 R -> H (polymorphism; 82.0% of wild type
creatine transporter activity;
dbSNP:rs372601430).
{ECO:0000269|PubMed:25861866}.
/FTId=VAR_074262.
VARIANT 270 270 V -> M (polymorphism; no effect on
creatine transporter activity;
dbSNP:rs146985734).
{ECO:0000269|PubMed:25861866}.
/FTId=VAR_074263.
VARIANT 294 294 K -> Q (polymorphism; no effect on
creatine transporter activity;
dbSNP:rs376937460).
{ECO:0000269|PubMed:25861866}.
/FTId=VAR_074264.
VARIANT 314 314 F -> L (polymorphism; 65.0% of wild type
creatine transporter activity;
dbSNP:rs144678921).
{ECO:0000269|PubMed:25861866}.
/FTId=VAR_074265.
VARIANT 318 318 A -> T (polymorphism; 78.0% of wild type
creatine transporter activity;
dbSNP:rs373953317).
{ECO:0000269|PubMed:25861866}.
/FTId=VAR_074266.
VARIANT 336 336 Missing (in CCDS1; decreased creatine
transporter activity).
{ECO:0000269|PubMed:17465020,
ECO:0000269|PubMed:23033978,
ECO:0000269|PubMed:24123876}.
/FTId=VAR_070563.
VARIANT 337 337 C -> W (in CCDS1; decreased creatine
transporter activity; dbSNP:rs122453116).
{ECO:0000269|PubMed:15154114,
ECO:0000269|PubMed:17465020}.
/FTId=VAR_063708.
VARIANT 347 347 Missing (in CCDS1; decreased creatine
transporter activity).
{ECO:0000269|PubMed:17465020}.
/FTId=VAR_075565.
VARIANT 381 381 G -> R (in CCDS1; dbSNP:rs122453114).
{ECO:0000269|PubMed:11898126}.
/FTId=VAR_020526.
VARIANT 383 383 G -> C (in CCDS1).
{ECO:0000269|PubMed:23660394}.
/FTId=VAR_071792.
VARIANT 390 390 P -> L (in CCDS1; decreased creatine
transporter activity).
{ECO:0000269|PubMed:15154114,
ECO:0000269|PubMed:17465020}.
/FTId=VAR_020527.
VARIANT 391 391 R -> W (in CCDS1; decreased creatine
transporter activity).
{ECO:0000269|PubMed:17465020}.
/FTId=VAR_075566.
VARIANT 408 408 Missing (in CCDS1).
{ECO:0000269|PubMed:12210795}.
/FTId=VAR_020528.
VARIANT 448 448 A -> D (in CCDS1).
{ECO:0000269|PubMed:23660394}.
/FTId=VAR_071793.
VARIANT 491 491 C -> W (in CCDS1; dbSNP:rs122453118).
{ECO:0000269|PubMed:17101918}.
/FTId=VAR_063709.
VARIANT 539 539 V -> I (in CCDS1; dbSNP:rs782354054).
{ECO:0000269|PubMed:23660394}.
/FTId=VAR_071794.
VARIANT 550 550 T -> S (in dbSNP:rs199635059).
{ECO:0000269|PubMed:23092983,
ECO:0000269|PubMed:25861866}.
/FTId=VAR_074267.
VARIANT 552 552 V -> L (in CCDS1; unknown pathological
significance; 35.0% of wild type creatine
transporter activity; dbSNP:rs372567920).
{ECO:0000269|PubMed:25861866}.
/FTId=VAR_074268.
VARIANT 554 554 P -> L (in CCDS1; decreased creatine
transporter activity; dbSNP:rs397515559).
{ECO:0000269|PubMed:15154114,
ECO:0000269|PubMed:17465020}.
/FTId=VAR_020529.
VARIANT 560 560 M -> V (polymorphism; no effect on
creatine transporter activity;
dbSNP:rs145438966).
{ECO:0000269|PubMed:15154114,
ECO:0000269|PubMed:17465020}.
/FTId=VAR_063710.
VARIANT 564 564 F -> L (polymorphism; no effect on
creatine transporter activity;
dbSNP:rs201044530).
{ECO:0000269|PubMed:25861866}.
/FTId=VAR_074269.
VARIANT 611 611 A -> T (polymorphism; no effect on
creatine transporter activity;
dbSNP:rs146949376).
{ECO:0000269|PubMed:25861866}.
/FTId=VAR_074270.
VARIANT 624 624 E -> K (polymorphism; no effect on
creatine transporter activity;
dbSNP:rs368555229).
{ECO:0000269|PubMed:25861866}.
/FTId=VAR_074271.
VARIANT 629 629 V -> I (polymorphism; no effect on
creatine transporter activity;
dbSNP:rs781899045).
{ECO:0000269|PubMed:17465020}.
/FTId=VAR_075567.
CONFLICT 24 25 AP -> VS (in Ref. 2; AAB32284).
{ECO:0000305}.
CONFLICT 32 32 A -> S (in Ref. 2; AAB32284).
{ECO:0000305}.
CONFLICT 38 38 V -> A (in Ref. 2; AAB32284).
{ECO:0000305}.
CONFLICT 42 45 TPGG -> APSS (in Ref. 2; AAB32284).
{ECO:0000305}.
CONFLICT 136 136 A -> G (in Ref. 7; BAG58415).
{ECO:0000305}.
CONFLICT 193 193 A -> D (in Ref. 2; AAB32284).
{ECO:0000305}.
CONFLICT 223 223 G -> T (in Ref. 2; AAB32284).
{ECO:0000305}.
CONFLICT 285 285 A -> P (in Ref. 1; AAC41688).
{ECO:0000305}.
CONFLICT 368 368 A -> T (in Ref. 2; AAB32284).
{ECO:0000305}.
CONFLICT 434 434 P -> R (in Ref. 9; AAH81558).
{ECO:0000305}.
SEQUENCE 635 AA; 70523 MW; 9FAFE100B2A5B845 CRC64;
MAKKSAENGI YSVSGDEKKG PLIAPGPDGA PAKGDGPVGL GTPGGRLAVP PRETWTRQMD
FIMSCVGFAV GLGNVWRFPY LCYKNGGGVF LIPYVLIALV GGIPIFFLEI SLGQFMKAGS
INVWNICPLF KGLGYASMVI VFYCNTYYIM VLAWGFYYLV KSFTTTLPWA TCGHTWNTPD
CVEIFRHEDC ANASLANLTC DQLADRRSPV IEFWENKVLR LSGGLEVPGA LNWEVTLCLL
ACWVLVYFCV WKGVKSTGKI VYFTATFPYV VLVVLLVRGV LLPGALDGII YYLKPDWSKL
GSPQVWIDAG TQIFFSYAIG LGALTALGSY NRFNNNCYKD AIILALINSG TSFFAGFVVF
SILGFMAAEQ GVHISKVAES GPGLAFIAYP RAVTLMPVAP LWAALFFFML LLLGLDSQFV
GVEGFITGLL DLLPASYYFR FQREISVALC CALCFVIDLS MVTDGGMYVF QLFDYYSASG
TTLLWQAFWE CVVVAWVYGA DRFMDDIACM IGYRPCPWMK WCWSFFTPLV CMGIFIFNVV
YYEPLVYNNT YVYPWWGEAM GWAFALSSML CVPLHLLGCL LRAKGTMAER WQHLTQPIWG
LHHLEYRAQD ADVRGLTTLT PVSESSKVVV VESVM


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