O15245 (S22A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Solute carrier family 22 member 1

Alternative name(s):
Organic cation transporter 1
Short name=hOCT1

Gene names

Name:	SLC22A1
Synonyms:	OCT1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	554 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Translocates a broad array of organic cations with various structures and molecular weights including the model compounds 1-methyl-4-phenylpyridinium (MPP), tetraethylammonium (TEA), N-1-methylnicotinamide (NMN), 4-(4-(dimethylamino)styryl)-N-methylpyridinium (ASP), the endogenous compounds choline, guanidine, histamine, epinephrine, adrenaline, noradrenaline and dopamine, and the drugs quinine, and metformin. The transport of organic cations is inhibited by a broad array of compounds like tetramethylammonium (TMA), cocaine, lidocaine, NMDA receptor antagonists, atropine, prazosin, cimetidine, TEA and NMN, guanidine, cimetidine, choline, procainamide, quinine, tetrabutylammonium, and tetrapentylammonium. Translocates organic cations in an electrogenic and pH-independent manner. Translocates organic cations across the plasma membrane in both directions. Transports the polyamines spermine and spermidine. Transports pramipexole across the basolateral membrane of the proximal tubular epithelial cells. The choline transport is activated by MMTS. Regulated by various intracellular signaling pathways including inhibition by protein kinase A activation, and endogenously activation by the calmodulin complex, the calmodulin-dependent kinase II and LCK tyrosine kinase. Ref.1 Ref.2 Ref.3 Ref.8 Ref.9 Ref.10 Ref.12 Ref.14
Subcellular location	Basolateral cell membrane; Multi-pass membrane protein Ref.11.
Tissue specificity	Widely expressed with high level in liver. Isoform 1 and isoform 2 are expressed in liver. Isoform 1, isoform 2, isoform 3 and isoform 4 are expressed in glial cell lines. Ref.1 Ref.2 Ref.3
Induction	In the liver activated by HNF4A and suppressed by bile acids via NR0B2. Increased by cholesterol treatment in hepatocyte cells. Ref.13 Ref.15
Post-translational modification	Phosphorylated By similarity.
Sequence similarities	Belongs to the major facilitator (TC 2.A.1) superfamily. Organic cation transporter (TC 2.A.1.19) family. [View classification]
Biophysicochemical properties	Kinetic parameters: KM=1.47 mM for metformin Ref.2 Ref.8 Ref.12 KM=229 µM for TEA KM=14.6 µM for MPP Vmax=396 pmol/min/mg enzyme for metformin uptake Vmax=2.89 nmol/min/mg enzyme for TEA uptake

Ontologies

Keywords
Biological process	Ion transport Transport
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transmembrane Transmembrane helix
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	dopamine transport Inferred from electronic annotation. Source: Compara drug transmembrane transport Traceable author statement. Source: Reactome epinephrine transport Inferred from electronic annotation. Source: Compara establishment or maintenance of transmembrane electrochemical gradient Inferred from electronic annotation. Source: Compara norepinephrine transport Inferred from electronic annotation. Source: Compara small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	basolateral plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to plasma membrane Traceable author statement Ref.2. Source: UniProtKB
Molecular_function	acetylcholine transmembrane transporter activity Inferred from electronic annotation. Source: Compara dopamine transmembrane transporter activity Inferred from electronic annotation. Source: Compara norepinephrine transmembrane transporter activity Inferred from electronic annotation. Source: Compara organic cation transmembrane transporter activity Traceable author statement Ref.2. Source: UniProtKB secondary active organic cation transmembrane transporter activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CERS2	Q96G23	3	EBI-1172714,EBI-1057080

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O15245-1)

Also known as: hOCT1G/L554;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: O15245-2)

Also known as: hOCT1G/L506;

The sequence of this isoform differs from the canonical sequence as follows:
     462-506: RNLGVMVCSS...ILFAVLGLLA → SGVGPACRGS...SKAQRKHDLP
     507-554: Missing.

Isoform 3 (identifier: O15245-3)

Also known as: hOCT1G483;

The sequence of this isoform differs from the canonical sequence as follows:
     462-532: Missing.

Isoform 4 (identifier: O15245-4)

Also known as: hOCT1G353;

The sequence of this isoform differs from the canonical sequence as follows:
     354-554: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 554	554	Solute carrier family 22 member 1		PRO_0000333875
Regions
	Topological domain	1 – 21	21	Cytoplasmic Potential
	Transmembrane	22 – 42	21	Helical; Potential
	Topological domain	43 – 149	107	Extracellular Potential
	Transmembrane	150 – 170	21	Helical; Potential
	Topological domain	171 – 176	6	Cytoplasmic Potential
	Transmembrane	177 – 197	21	Helical; Potential
	Topological domain	198 – 206	9	Extracellular Potential
	Transmembrane	207 – 229	23	Helical; Potential
	Topological domain	230 – 235	6	Cytoplasmic Potential
	Transmembrane	236 – 256	21	Helical; Potential
	Topological domain	257 – 262	6	Extracellular Potential
	Transmembrane	263 – 283	21	Helical; Potential
	Topological domain	284 – 347	64	Cytoplasmic Potential
	Transmembrane	348 – 368	21	Helical; Potential
	Topological domain	369 – 376	8	Extracellular Potential
	Transmembrane	377 – 397	21	Helical; Potential
	Topological domain	398 – 402	5	Cytoplasmic Potential
	Transmembrane	403 – 423	21	Helical; Potential
	Topological domain	424 – 431	8	Extracellular Potential
	Transmembrane	432 – 452	21	Helical; Potential
	Topological domain	453 – 464	12	Cytoplasmic Potential
	Transmembrane	465 – 485	21	Helical; Potential
	Topological domain	486 – 492	7	Extracellular Potential
	Transmembrane	493 – 513	21	Helical; Potential
	Topological domain	514 – 554	41	Cytoplasmic Potential
Sites
	Site	450	1	Involved in affinity and selectivity of cations as well as in translocation By similarity
Amino acid modifications
	Glycosylation	71	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	354 – 554	201	Missing in isoform 4.		VSP_033587
	Alternative sequence	462 – 532	71	Missing in isoform 3.		VSP_033588
	Alternative sequence	462 – 506	45	RNLGV…LGLLA → SGVGPACRGSDATSSRDQGG RFARDHEGRREPWEKSKAQR KHDLP in isoform 2.		VSP_033589
	Alternative sequence	507 – 554	48	Missing in isoform 2.		VSP_033590
	Natural variant	14	1	S → F Exclusively found in the African American population; increase of the MPP uptake; when associated with V-408. Ref.17 Corresponds to variant rs34447885 [ dbSNP | Ensembl ].		VAR_043319
	Natural variant	41	1	F → L. Ref.19 Corresponds to variant rs2297373 [ dbSNP | Ensembl ].		VAR_043320
	Natural variant	61	1	R → C Reduction of the MPP uptake. Reduction of the MPP uptake; when associated with V-408. Ref.16 Ref.17 Corresponds to variant rs12208357 [ dbSNP | Ensembl ].		VAR_043321
	Natural variant	85	1	L → F No changes in the MPP uptake; when associated with V-408. Ref.17 Corresponds to variant rs35546288 [ dbSNP | Ensembl ].		VAR_043322
	Natural variant	88	1	C → R. Ref.16 Corresponds to variant rs55918055 [ dbSNP | Ensembl ].		VAR_043323
	Natural variant	160	1	L → F No changes in both TEA and MPP uptake. No MPP uptake; when associated with S-401. Largely localized in the plasma membrane. Ref.1 Ref.5 Ref.7 Ref.16 Ref.17 Ref.18 Ref.19 Corresponds to variant rs683369 [ dbSNP | Ensembl ].		VAR_043324
	Natural variant	189	1	S → L No changes in the MPP uptake. No changes in the MPP uptake; when associated with V-408. Ref.17		VAR_043325
	Natural variant	220	1	G → V No MPP uptake. Reduction of the MPP uptake; when associated with V-408. Ref.17		VAR_043326
	Natural variant	283	1	P → L. Ref.18 Corresponds to variant rs4646277 [ dbSNP | Ensembl ].		VAR_043327
	Natural variant	287	1	R → G. Ref.18 Corresponds to variant rs4646278 [ dbSNP | Ensembl ].		VAR_043328
	Natural variant	341	1	P → L Reduction of the MPP uptake. Reduction of the MPP uptake; when associated with V-408. Partly reduction of TEA uptake. Largely localized in the plasma membrane. Ref.17 Ref.18 Ref.19 Corresponds to variant rs2282143 [ dbSNP | Ensembl ].		VAR_043329
	Natural variant	342	1	R → H No changes in the MPP uptake; when associated with V-408. Ref.17 Corresponds to variant rs34205214 [ dbSNP | Ensembl ].		VAR_043330
	Natural variant	401	1	G → S No MPP uptake. Reduction of the serotonin uptake. No MPP uptake; when associated with L-160. Ref.16 Ref.17 Corresponds to variant rs34130495 [ dbSNP | Ensembl ].		VAR_043331
	Natural variant	408	1	M → V No changes in the MPP uptake. No changes in the MPP uptake; when associated with F-14. No changes in the MPP uptake; when associated with F-85. No changes in the MPP uptake; when associated with L-189. No changes in the MPP uptake; when associated with His-342. No changes in the MPP uptake; when associated with M-420 del. No changes in the MPP uptake; when associated with I-440. No changes in the MPP uptake; when associated with I-461. No changes in the MPP uptake; when associated with M-488. Reduction of the MPP uptake; when associated with C-61. No MPP uptake; when associated with V-220. Reduction of the MPP uptake; when associated with L-341. No MPP uptake; when associated with S-401. No MPP uptake; when associated with R-465. Ref.5 Ref.17 Ref.19 Corresponds to variant rs628031 [ dbSNP | Ensembl ].		VAR_043332
	Natural variant	420	1	Missing No changes in the MPP uptake. No changes in the MPP uptake; when associated with V-408. Ref.5 Ref.16 Ref.17		VAR_043333
	Natural variant	440	1	M → I. Ref.17 Corresponds to variant rs35956182 [ dbSNP | Ensembl ].		VAR_043334
	Natural variant	461	1	V → I No changes in the MPP uptake; when associated with V-408. Ref.17 Corresponds to variant rs34295611 [ dbSNP | Ensembl ].		VAR_043335
	Natural variant	465	1	G → R Reduction of the localization to the basolateral membrane. No MPP uptake; when associated with V-408. Ref.5 Ref.17 Corresponds to variant rs34059508 [ dbSNP | Ensembl ].		VAR_043336
	Natural variant	488	1	R → M No changes in the MPP uptake; when associated with V-408. Ref.17 Corresponds to variant rs35270274 [ dbSNP | Ensembl ].		VAR_043337
Experimental info
	Mutagenesis	465	1	G → A: No changes in the MPP uptake. Ref.17

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (hOCT1G/L554) [UniParc]. Last modified November 30, 2010. Version 2. Checksum: 55206B897DE32202	FASTA	554	61,154
	10 20 30 40 50 60 MPTVDDILEQ VGESGWFQKQ AFLILCLLSA AFAPICVGIV FLGFTPDHHC QSPGVAELSQ 70 80 90 100 110 120 RCGWSPAEEL NYTVPGLGPA GEAFLGQCRR YEVDWNQSAL SCVDPLASLA TNRSHLPLGP 130 140 150 160 170 180 CQDGWVYDTP GSSIVTEFNL VCADSWKLDL FQSCLNAGFL FGSLGVGYFA DRFGRKLCLL 190 200 210 220 230 240 GTVLVNAVSG VLMAFSPNYM SMLLFRLLQG LVSKGNWMAG YTLITEFVGS GSRRTVAIMY 250 260 270 280 290 300 QMAFTVGLVA LTGLAYALPH WRWLQLAVSL PTFLFLLYYW CVPESPRWLL SQKRNTEAIK 310 320 330 340 350 360 IMDHIAQKNG KLPPADLKML SLEEDVTEKL SPSFADLFRT PRLRKRTFIL MYLWFTDSVL 370 380 390 400 410 420 YQGLILHMGA TSGNLYLDFL YSALVEIPGA FIALITIDRV GRIYPMAMSN LLAGAACLVM 430 440 450 460 470 480 IFISPDLHWL NIIIMCVGRM GITIAIQMIC LVNAELYPTF VRNLGVMVCS SLCDIGGIIT 490 500 510 520 530 540 PFIVFRLREV WQALPLILFA VLGLLAAGVT LLLPETKGVA LPETMKDAEN LGRKAKPKEN 550 TIYLKVQTSE PSGT
	Isoform 2 (hOCT1G/L506) [UniParc]. Checksum: FDD376F7F8547B5D	FASTA	506	56,094
	10 20 30 40 50 60 MPTVDDILEQ VGESGWFQKQ AFLILCLLSA AFAPICVGIV FLGFTPDHHC QSPGVAELSQ 70 80 90 100 110 120 RCGWSPAEEL NYTVPGLGPA GEAFLGQCRR YEVDWNQSAL SCVDPLASLA TNRSHLPLGP 130 140 150 160 170 180 CQDGWVYDTP GSSIVTEFNL VCADSWKLDL FQSCLNAGFL FGSLGVGYFA DRFGRKLCLL 190 200 210 220 230 240 GTVLVNAVSG VLMAFSPNYM SMLLFRLLQG LVSKGNWMAG YTLITEFVGS GSRRTVAIMY 250 260 270 280 290 300 QMAFTVGLVA LTGLAYALPH WRWLQLAVSL PTFLFLLYYW CVPESPRWLL SQKRNTEAIK 310 320 330 340 350 360 IMDHIAQKNG KLPPADLKML SLEEDVTEKL SPSFADLFRT PRLRKRTFIL MYLWFTDSVL 370 380 390 400 410 420 YQGLILHMGA TSGNLYLDFL YSALVEIPGA FIALITIDRV GRIYPMAMSN LLAGAACLVM 430 440 450 460 470 480 IFISPDLHWL NIIIMCVGRM GITIAIQMIC LVNAELYPTF VSGVGPACRG SDATSSRDQG 490 500 GRFARDHEGR REPWEKSKAQ RKHDLP
	Isoform 3 (hOCT1G483) [UniParc]. Checksum: 843CF89CFB1D9827	FASTA	483	53,593
	10 20 30 40 50 60 MPTVDDILEQ VGESGWFQKQ AFLILCLLSA AFAPICVGIV FLGFTPDHHC QSPGVAELSQ 70 80 90 100 110 120 RCGWSPAEEL NYTVPGLGPA GEAFLGQCRR YEVDWNQSAL SCVDPLASLA TNRSHLPLGP 130 140 150 160 170 180 CQDGWVYDTP GSSIVTEFNL VCADSWKLDL FQSCLNAGFL FGSLGVGYFA DRFGRKLCLL 190 200 210 220 230 240 GTVLVNAVSG VLMAFSPNYM SMLLFRLLQG LVSKGNWMAG YTLITEFVGS GSRRTVAIMY 250 260 270 280 290 300 QMAFTVGLVA LTGLAYALPH WRWLQLAVSL PTFLFLLYYW CVPESPRWLL SQKRNTEAIK 310 320 330 340 350 360 IMDHIAQKNG KLPPADLKML SLEEDVTEKL SPSFADLFRT PRLRKRTFIL MYLWFTDSVL 370 380 390 400 410 420 YQGLILHMGA TSGNLYLDFL YSALVEIPGA FIALITIDRV GRIYPMAMSN LLAGAACLVM 430 440 450 460 470 480 IFISPDLHWL NIIIMCVGRM GITIAIQMIC LVNAELYPTF VRKAKPKENT IYLKVQTSEP SGT
	Isoform 4 (hOCT1G353) [UniParc]. Checksum: 88073B911A5E5633	FASTA	353	39,224
	10 20 30 40 50 60 MPTVDDILEQ VGESGWFQKQ AFLILCLLSA AFAPICVGIV FLGFTPDHHC QSPGVAELSQ 70 80 90 100 110 120 RCGWSPAEEL NYTVPGLGPA GEAFLGQCRR YEVDWNQSAL SCVDPLASLA TNRSHLPLGP 130 140 150 160 170 180 CQDGWVYDTP GSSIVTEFNL VCADSWKLDL FQSCLNAGFL FGSLGVGYFA DRFGRKLCLL 190 200 210 220 230 240 GTVLVNAVSG VLMAFSPNYM SMLLFRLLQG LVSKGNWMAG YTLITEFVGS GSRRTVAIMY 250 260 270 280 290 300 QMAFTVGLVA LTGLAYALPH WRWLQLAVSL PTFLFLLYYW CVPESPRWLL SQKRNTEAIK 310 320 330 340 350 IMDHIAQKNG KLPPADLKML SLEEDVTEKL SPSFADLFRT PRLRKRTFIL MYL

References

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[1]	"Cloning and characterization of two human polyspecific organic cation transporters." Gorboulev V., Ulzheimer J.C., Akhoundova A., Ulzheimer-Teuber I., Karbach U., Quester S., Baumann C., Lang F., Busch A.E., Koepsell H. DNA Cell Biol. 16:871-881(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, VARIANT PHE-160. Tissue: Liver.
[2]	"Cloning and functional expression of a human liver organic cation transporter." Zhang L., Dresser M.J., Gray A.T., Yost S.C., Terashita S., Giacomini K.M. Mol. Pharmacol. 51:913-921(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
[3]	"Molecular cloning, functional characterization and genomic organization of four alternatively spliced isoforms of the human organic cation transporter 1 (hOCT1/SLC22A1)." Hayer M., Boenisch H., Bruess M. Ann. Hum. Genet. 63:473-482(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3 AND 4).
[4]	Erratum Hayer M., Bonisch H., Bruss M. Ann. Hum. Genet. 64:267-267(2000) Cited for: SEQUENCE REVISION.
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS PHE-160; VAL-408; MET-420 DEL AND ARG-465. Tissue: Caudate nucleus.
[6]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT PHE-160.
[8]	"Functional characterization of an organic cation transporter (hOCT1) in a transiently transfected human cell line (HeLa)." Zhang L., Schaner M.E., Giacomini K.M. J. Pharmacol. Exp. Ther. 286:354-361(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[9]	"Comparison of 'type I' and 'type II' organic cation transport by organic cation transporters and organic anion-transporting polypeptides." van Montfoort J.E., Mueller M., Groothuis G.M.M., Meijer D.K.F., Koepsell H., Meier P.J. J. Pharmacol. Exp. Ther. 298:110-115(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"Regulation of the human organic cation transporter hOCT1." Ciarimboli G., Struwe K., Arndt P., Gorboulev V., Koepsell H., Schlatter E., Hirsch J.R. J. Cell. Physiol. 201:420-428(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"Drug specificity and intestinal membrane localization of human organic cation transporters (OCT)." Mueller J., Lips K.S., Metzner L., Neubert R.H.H., Koepsell H., Brandsch M. Biochem. Pharmacol. 70:1851-1860(2005) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[12]	"Metformin is a superior substrate for renal organic cation transporter OCT2 rather than hepatic OCT1." Kimura N., Masuda S., Tanihara Y., Ueo H., Okuda M., Katsura T., Inui K. Drug Metab. Pharmacokinet. 20:379-386(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[13]	"The human organic cation transporter-1 gene is transactivated by hepatocyte nuclear factor-4alpha." Saborowski M., Kullak-Ublick G.A., Eloranta J.J. J. Pharmacol. Exp. Ther. 317:778-785(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[14]	"Differential pharmacological in vitro properties of organic cation transporters and regional distribution in rat brain." Amphoux A., Vialou V., Drescher E., Bruess M., Mannoury La Cour C., Rochat C., Millan M.J., Giros B., Boenisch H., Gautron S. Neuropharmacology 50:941-952(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[15]	"The expression of the solute carriers NTCP and OCT-1 is regulated by cholesterol in HepG2 cells." Dias V., Ribeiro V. Fundam. Clin. Pharmacol. 21:445-450(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[16]	"Identification of genetic variations of the human organic cation transporter hOCT1 and their functional consequences." Kerb R., Brinkmann U., Chatskaia N., Gorbunov D., Gorboulev V., Mornhinweg E., Keil A., Eichelbaum M., Koepsell H. Pharmacogenetics 12:591-595(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CYS-61; ARG-88; PHE-160; SER-401 AND MET-420 DEL, CHARACTERIZATION OF VARIANTS CYS-61; ARG-88; PHE-160; SER-401 AND MET-420 DEL.
[17]	"Evolutionary conservation predicts function of variants of the human organic cation transporter, OCT1." Shu Y., Leabman M.K., Feng B., Mangravite L.M., Huang C.C., Stryke D., Kawamoto M., Johns S.J., DeYoung J., Carlson E., Ferrin T.E., Herskowitz I., Giacomini K.M. Proc. Natl. Acad. Sci. U.S.A. 100:5902-5907(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PHE-14; CYS-61; PHE-85; PHE-160; LEU-189; VAL-220; LEU-341; HIS-342; SER-401; VAL-408; MET-420 DEL; ILE-440; ILE-461; ARG-465 AND MET-488, CHARACTERIZATION OF VARIANTS PHE-14; CYS-61; PHE-85; PHE-160; LEU-189; VAL-220; LEU-341; HIS-342; SER-401; VAL-408; MET-420 DEL; ILE-440; ILE-461; ARG-465 AND MET-488, MUTAGENESIS OF GLY-465.
[18]	"Novel single nucleotide polymorphisms of organic cation transporter 1 (SLC22A1) affecting transport functions." Sakata T., Anzai N., Shin H.J., Noshiro R., Hirata T., Yokoyama H., Kanai Y., Endou H. Biochem. Biophys. Res. Commun. 313:789-793(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PHE-160; LEU-283; GLY-287 AND LEU-341.
[19]	"Seven novel single nucleotide polymorphisms in the human SLC22A1 gene encoding organic cation transporter 1 (OCT1)." Itoda M., Saito Y., Maekawa K., Hichiya H., Komamura K., Kamakura S., Kitakaze M., Tomoike H., Ueno K., Ozawa S., Sawada J. Drug Metab. Pharmacokinet. 19:308-312(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS LEU-41; PHE-160; LEU-341 AND VAL-408.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X98332 mRNA. Translation: CAA66977.1. U77086 mRNA. Translation: AAB67703.1. AJ243995 , AJ243996, AJ243998, AJ243999, AJ244000, AJ245460, AJ276051, AJ276052, AJ276053 Genomic DNA. Translation: CAB95971.1. AK289887 mRNA. Translation: BAF82576.1. AL353625 Genomic DNA. Translation: CAH72016.1. BC126364 mRNA. Translation: AAI26365.1.
IPI	IPI00289507. IPI00893835. IPI00893977. IPI00953438.
RefSeq	NP_003048.1. NM_003057.2. NP_694857.1. NM_153187.1.
UniGene	Hs.117367.
3D structure databases
ProteinModelPortal	O15245.
SMR	O15245. Positions 153-305.
ModBase	Search...
Protein-protein interaction databases
IntAct	O15245. 1 interaction.
STRING	9606.ENSP00000355930.
PTM databases
PhosphoSite	O15245.
Proteomic databases
PaxDb	O15245.
PRIDE	O15245.
Protocols and materials databases
DNASU	6580.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000324965; ENSP00000318103; ENSG00000175003. ENST00000366963; ENSP00000355930; ENSG00000175003. ENST00000457470; ENSP00000409557; ENSG00000175003. ENST00000460902; ENSP00000439274; ENSG00000175003.
GeneID	6580.
KEGG	hsa:6580.
UCSC	uc003qtc.3. human. uc003qtd.3. human.
Organism-specific databases
CTD	6580.
GeneCards	GC06P160542.
HGNC	HGNC:10963. SLC22A1.
HPA	HPA029846.
MIM	602607. gene.
neXtProt	NX_O15245.
PharmGKB	PA329.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0477.
HOGENOM	HOG000234568.
HOVERGEN	HBG061545.
InParanoid	O15245.
KO	K08198.
OMA	TIYLQVQ.
OrthoDB	EOG4S4PG6.
PhylomeDB	O15245.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism. REACT_15518. Transmembrane transport of small molecules.
Gene expression databases
ArrayExpress	O15245.
Bgee	O15245.
CleanEx	HS_SLC22A1.
Genevestigator	O15245.
Family and domain databases
InterPro	IPR020846. MFS_dom. IPR016196. MFS_dom_general_subst_transpt. IPR004749. Orgcat_transp. IPR005828. Sub_transporter. IPR005829. Sugar_transporter_CS. [Graphical view]
Pfam	PF00083. Sugar_tr. 1 hit. [Graphical view]
SUPFAM	SSF103473. MFS_gen_substrate_transporter. 1 hit.
TIGRFAMs	TIGR00898. 2A0119. 1 hit.
PROSITE	PS50850. MFS. 1 hit. PS00216. SUGAR_TRANSPORT_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	O15245.
ChEMBL	CHEMBL5685.
GenomeRNAi	6580.
NextBio	25603.
SOURCE	Search...

Entry information

Entry name

S22A1_HUMAN

Accession

Primary (citable) accession number: O15245
Secondary accession number(s): A6NFF3 , A8K1H2, C9JSU6, O15395, Q9NQD4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	November 30, 2010
Last modified:	May 1, 2013
This is version 109 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.