Slc22a1
entrez
24904
canonical
uniprot
Q63089
canonical
ensembl
ENSRNOG00000016337
resolver
ensembl
ENSRNOG00055027731
resolver
ensembl
ENSRNOG00060009846
resolver
ensembl
ENSRNOG00065029234
resolver
ensp
ENSRNOP00000022068
resolver
ensp
ENSRNOP00000022254
resolver
genesymbol
Slc22a1
resolver
genesymbol_syn
Oct1
resolver
uniprot
O35882
resolver
uniprot
Q6AYW1
resolver
uniprot_entry
S22A1_RAT
resolver
uniprot_sec
O35882
resolver
uniprot_sec
Q6AYW1
resolver
activity_regulation
ACTIVITY REGULATION: Phosphorylation of the transporter leads to changes in its substrate affinity, resulting in a regulation of the transport activity (PubMed:10864577). In contrast with human ortholog, ASP uptake is stimulated by protein kinase A (PKA) and C (PKC) and endogenous tyrosine kinase activation (PubMed:10864577). ASP affinity is induced by PKC-dependent phosphorylation (PubMed:10864577). Inhibited by cGMP, most likely through a cGMP-binding protein that interacts with OCT1 (PubMed:12395288). {ECO:0000269|PubMed:10864577, ECO:0000269|PubMed:12395288}.
uniprot
proteins
amino_acid_sequence
MPTVDDVLEQVGEFGWFQKQAFLLLCLISASLAPIYVGIVFLGFTPGHYCQNPGVAELSQRCGWSQAEELNYTVPGLGPSDEASFLSQCMRYEVDWNQSTLDCVDPLSSLVANRSQLPLGPCEHGWVYDTPGSSIVTEFNLVCGDAWKVDLFQSCVNLGFFLGSLVVGYIADRFGRKLCLLVTTLVTSVSGVLTAVAPDYTSMLLFRLLQGMVSKGSWVSGYTLITEFVGSGYRRTTAILYQMAFTVGLVGLAGVAYAIPDWRWLQLAVSLPTFLFLLYYWFVPESPRWLLSQKRTTRAVRIMEQIAQKNGKVPPADLKMLCLEEDASEKRSPSFADLFRTPNLRKHTVILMYLWFSCAVLYQGLIMHVGATGANLYLDFFYSSLVEFPAAFIILVTIDRIGRIYPIAASNLVTGAACLLMIFIPHELHWLNVTLACLGRMGATIVLQMVCLVNAELYPTFIRNLGMMVCSALCDLGGIFTPFMVFRLMEVWQALPLILFGVLGLTAGAMTLLLPETKGVALPETIEEAENLGRRKSKAKENTIYLQVQTGKSSST
uniprot
proteins
function
FUNCTION: Electrogenic voltage-dependent uniporter that mediates the transport of a variety of organic cations such as endogenous bioactive amines, cationic drugs and xenobiotics (PubMed:10570053, PubMed:10864577, PubMed:10997918, PubMed:11408531, PubMed:11502595, PubMed:12395288, PubMed:15640376, PubMed:15662044, PubMed:16142924, PubMed:16272756, PubMed:16581093, PubMed:17567940, PubMed:7990927, PubMed:8955087). Functions as a pH- and Na(+)-independent, bidirectional transporter (PubMed:16142924, PubMed:8955087). Cation cellular uptake or release is driven by the electrochemical potential (i.e. membrane potential and concentration gradient) and substrate selectivity (PubMed:16142924, PubMed:17567940, PubMed:8955087, PubMed:9405386). Hydrophobicity is a major requirement for recognition in polyvalent substrates and inhibitors (By similarity). Primarily expressed in the basolateral membrane of hepatocytes and proximal tubules and involved in the uptake and disposition of cationic compounds from the blood by hepatic and renal clearance (PubMed:10997918, PubMed:7990927, PubMed:9703985). Most likely functions as an uptake carrier in enterocytes contributing to the intestinal excretion and elimination of organic cations from the systemic circulation (By similarity). Transports endogenous monoamines such as N-1-methylnicotinamide (NMN), guanidine, neurotransmitters dopamine, serotonin, noradrenaline, adrenaline and histamine, and quaternary ammonium compound such as choline (PubMed:10570053, PubMed:11408531, PubMed:11502595, PubMed:11758759, PubMed:15662044, PubMed:16581093, PubMed:17567940, PubMed:8955087, PubMed:9776363). Also transports natural polyamines such as spermidine, agmatine and putrescine at low affinity, but relatively high turnover (By similarity). Involved in the hepatic uptake of vitamin B1/thiamine, hence regulating hepatic lipid and energy metabolism (By similarity). Contributes to the influx and efflux of fatty acid carriers carnitines and acylcarnitines across the basolateral membrane of hepatocytes, from the liver to the systemic circulation and inversely and may be involved in regulating the systemic availability of hepatic acylcarnitines (By similarity). Mediates the bidirectional transport of acetylcholine (ACh) at the apical membrane of ciliated cell in airway epithelium, thereby playing a role in luminal release of ACh from bronchial epithelium (PubMed:15817714). Transports dopaminergic neuromodulators cyclo(his-pro) and salsolinol with lower efficiency (By similarity). Also capable of transporting non-amine endogenous compounds such as prostaglandin E2 (PGE2) and prostaglandin F2-alpha (PGF2-alpha) (By similarity). May contribute to the transport of cationic compounds in testis across the blood-testis-barrier (Probable). Also mediates the uptake of xenobiotics tributylmethylammonium (TBuMA), quinidine, N-methyl-quinine (NMQ), N-methyl-quinidine (NMQD) N-(4,4-azo-n-pentyl)-quinuclidine (APQ), azidoprocainamide methoiodide (AMP), N-(4,4-azo-n-pentyl)-21-deoxyajmalinium (APDA) and 4-(4-(dimethylamino)styryl)-N-methylpyridinium (ASP) (PubMed:10864577, PubMed:11408531, PubMed:12395288, PubMed:8955087). {ECO:0000250|UniProtKB:O08966, ECO:0000250|UniProtKB:O15245, ECO:0000269|PubMed:10570053, ECO:0000269|PubMed:10864577, ECO:0000269|PubMed:10997918, ECO:0000269|PubMed:11408531, ECO:0000269|PubMed:11502595, ECO:0000269|PubMed:11758759, ECO:0000269|PubMed:12395288, ECO:0000269|PubMed:15640376, ECO:0000269|PubMed:15662044, ECO:0000269|PubMed:15817714, ECO:0000269|PubMed:16142924, ECO:0000269|PubMed:16272756, ECO:0000269|PubMed:16581093, ECO:0000269|PubMed:17567940, ECO:0000269|PubMed:7990927, ECO:0000269|PubMed:8955087, ECO:0000269|PubMed:9405386, ECO:0000269|PubMed:9703985, ECO:0000269|PubMed:9776363, ECO:0000305|PubMed:17616214}.; FUNCTION: [Isoform 2]: Functional isoform capable of transporting TEA. {ECO:0000269|PubMed:9195965}.
uniprot
proteins
mass_dalton
61541
uniprot
proteins
mutagenesis
MUTAGEN 26; /note="C->A: Choline affinity is increased fourfold by MMTS; when associated with A-155; A-179; S-322; A-358; A-418; S-437; A-470 and A-474."; /evidence="ECO:0000269|PubMed:17567940"; MUTAGEN 155; /note="C->A: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-179; S-322; A-358; A-418; S-437; A-470 and A-474."; /evidence="ECO:0000269|PubMed:17567940"; MUTAGEN 179; /note="C->A: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; S-322; A-358; A-418; S-437; A-470 and A-474."; /evidence="ECO:0000269|PubMed:17567940"; MUTAGEN 212; /note="M->L: No change in TEA and MPP(+) uptake."; /evidence="ECO:0000269|PubMed:15662044"; MUTAGEN 213; /note="V->G: Decreased TEA uptake. No change in MPP(+) uptake."; /evidence="ECO:0000269|PubMed:15662044"; MUTAGEN 214; /note="S->G: Decreased TEA and MPP(+) uptake."; /evidence="ECO:0000269|PubMed:15662044"; MUTAGEN 215; /note="K->Q: Loss of TEA and MPP(+) uptake activity."; /evidence="ECO:0000269|PubMed:15662044"; MUTAGEN 215; /note="K->R: Loss of TEA and MPP(+) uptake activity."; /evidence="ECO:0000269|PubMed:15662044"; MUTAGEN 216; /note="G->A: Decreased TEA and MPP(+) uptake."; /evidence="ECO:0000269|PubMed:15662044"; MUTAGEN 217; /note="S->G: No change in TEA and MPP(+) uptake."; /evidence="ECO:0000269|PubMed:15662044"; MUTAGEN 218; /note="W->F: Decreased guanidine, histamine, serotonin and TEA uptake. No change in MPP(+) uptake. No change in TEA and MPP(+) affinity. Decreased TEAVmax. No change in MPP(+) Vmax."; /evidence="ECO:0000269|PubMed:15662044"; MUTAGEN 218; /note="W->L: Decreased guanidine, histamine, serotonin, TEA and MPP(+) uptake. Decreased TEA affinity. No change in MPP(+) affinity. Decreased TEA and MPP(+) Vmax."; /evidence="ECO:0000269|PubMed:15662044"; MUTAGEN 218; /note="W->Y: Decreased guanidine, histamine, serotonin and TEA uptake. No change in MPP(+) uptake. Increased TEA and MPP(+) affinity. Decreased TEA and MPP(+) Vmax."; /evidence="ECO:0000269|PubMed:15662044"; MUTAGEN 219; /note="V->L: No change in TEA and MPP(+) uptake."; /evidence="ECO:0000269|PubMed:15662044"; MUTAGEN 220; /note="S->I: Decreased TEA and MPP(+) uptake."; /evidence="ECO:0000269|PubMed:15662044"; MUTAGEN 221; /note="G->A: Decreased TEA and MPP(+) uptake."; /evidence="ECO:0000269|PubMed:15662044"; MUTAGEN 222; /note="Y->F: No change in guanidine, histamine, serotonin, TEA and MPP(+) uptake. Increased TEA affinity. No change in MPP(+) affinity. Decreased TEAVmax. No change in MPP(+) Vmax."; /evidence="ECO:0000269|PubMed:15662044"; MUTAGEN 222; /note="Y->L: Decreased guanidine, serotonin, TEA and MPP(+) uptake. No change in histamine uptake. Increased TEA and MPP(+) affinity. Decreased TEA and MPP(+) Vmax."; /evidence="ECO:0000269|PubMed:15662044"; MUTAGEN 223; /note="T->I: Decreased TEA uptake. No change in MPP(+) uptake."; /evidence="ECO:0000269|PubMed:15662044"; MUTAGEN 224; /note="L->V: Decreased TEA and MPP(+) uptake."; /evidence="ECO:0000269|PubMed:15662044"; MUTAGEN 225; /note="I->G: No change in TEA and MPP(+) uptake."; /evidence="ECO:0000269|PubMed:15662044"; MUTAGEN 226; /note="T->A: Decreased TEA uptake. No change in MPP(+) uptake."; /evidence="ECO:0000269|PubMed:15662044"; MUTAGEN 227; /note="E->D: Loss of TEA and MPP(+) uptake activity."; /evidence="ECO:0000269|PubMed:15662044"; MUTAGEN 227; /note="E->Q: Loss of TEA and MPP(+) uptake activity."; /evidence="ECO:0000269|PubMed:15662044"; MUTAGEN 228; /note="F->I: No change in TEA and MPP(+) uptake."; /evidence="ECO:0000269|PubMed:15662044"; MUTAGEN 229; /note="V->A: Decreased TEA and MPP(+) uptake."; /evidence="ECO:0000269|PubMed:15662044"; MUTAGEN 229; /note="V->L: Loss of TEA and MPP(+) uptake activity."; /evidence="ECO:0000269|PubMed:15662044"; MUTAGEN 286; /note="S->A: No effect of PKC-induced stimulation on ASP uptake. No effect of PKC-induced stimulation on ASP uptake; when associated with A-292; A-296; A-328 and A-550. No effect of PKA activation on ASP uptake. No effect of PKA activation on ASP uptake; when associated with A-292; A-296; A-328 and A-550. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition; when associated with A-292; A-296; A-328 and A-550. No significant effect on trafficking from intracellular pools to the cell membrane; when associated with A-292; A-296; A-328 and A-550. suppresses phosphorylation by PKC; when associated with A-292; A-296; A-328 and A-550."; /evidence="ECO:0000269|PubMed:15829703"; MUTAGEN 292; /note="S->A: No effect of PKC-induced stimulation on ASP uptake. No effect of PKC-induced stimulation on ASP uptake; when associated with A-286; A-296; A-328 and A-550. No effect of PKA activation on ASP uptake. No effect of PKA activation on ASP uptake; when associated with A-286; A-296; A-328 and A-550. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition; when associated with A-286; A-296; A-328 and A-550. No significant effect on trafficking from intracellular pools to the cell membrane; when associated with A-286; A-296; A-328 and A-550. suppresses phosphorylation by PKC; when associated with A-286; A-296; A-328 and A-550."; /evidence="ECO:0000269|PubMed:15829703"; MUTAGEN 296; /note="T->A: No effect of PKC-induced stimulation on ASP uptake. No effect of PKC-induced stimulation on ASP uptake; when associated with A-286; A-292; A-328; A-550. Significant increase of the ASP uptake by PKA activation. No effect of PKA activation on ASP uptake; when associated with A-286; A-292; A-328; A-550. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition; when associated with A-286; A-292; A-328; A-550. No significant effect on trafficking from intracellular pools to the cell membrane; when associated with A-286; A-292; A-328 and A-550. suppresses phosphorylation by PKC; when associated with A-286; A-292; A-328 and A-550."; /evidence="ECO:0000269|PubMed:15829703"; MUTAGEN 322; /note="C->S: Reduces the activation by MMTS. Abolishes the activation by MMTs; when associated with M-451. Choline affinity is increased fivefold by MMTS. Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; A-179; A-358; A-418; S-437; A-470 and A-474. Choline affinity is increased four- to fivefold; when associated with M-451."; /evidence="ECO:0000269|PubMed:17567940"; MUTAGEN 328; /note="S->A: No effect of PKC-induced stimulation on ASP uptake. No effect of PKC-induced stimulation on ASP uptake; when associated with A-286; A-292; A-296 and A-550. No effect of PKA activation on ASP uptake. No effect of PKA activation on ASP uptake; when associated with A-286; A-292; A-296 and A-550. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition; when associated with A-286; A-292; A-296; A-550. No significant effect on trafficking from intracellular pools to the cell membrane; when associated with A-286; A-292; A-296 and A-550. suppresses phosphorylation by PKC; when associated with A-286; A-292; A-296 and A-550."; /evidence="ECO:0000269|PubMed:15829703"; MUTAGEN 358; /note="C->A: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; A-179; S-322; A-418; S-437; A-470 and A-474."; /evidence="ECO:0000269|PubMed:17567940"; MUTAGEN 418; /note="C->A: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; A-179; S-322; A-358; S-437; A-470 and A-474."; /evidence="ECO:0000269|PubMed:17567940"; MUTAGEN 437; /note="C->S: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; A-179; S-322; A-358; A-418; A-470 and A-474."; /evidence="ECO:0000269|PubMed:17567940"; MUTAGEN 451; /note="C->M: Reduces the activation by MMTS. Abolishes the activation by MMTs; when associated with S-322. Abolishes the effect of MMTs on choline-induced currents. Choline affinity is not influenced by MMTS. Choline affinity is increased four- to fivefold; when associated with S-322."; /evidence="ECO:0000269|PubMed:17567940"; MUTAGEN 470; /note="C->A: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; A-179; S-322; A-358; A-418; A-437 and A-474."; /evidence="ECO:0000269|PubMed:17567940"; MUTAGEN 474; /note="C->A: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; A-179; S-322; A-358; A-418; A-437 and A-470."; /evidence="ECO:0000269|PubMed:17567940"; MUTAGEN 475; /note="D->E: Decreased MPP(+) uptake, no change in MPP(+) affinity. Decreased NMN uptake, increased NMN affinity. Decreased choline uptake, increased choline affinity."; /evidence="ECO:0000269|PubMed:10570053"; MUTAGEN 475; /note="D->N: Decreased MPP(+) uptake."; /evidence="ECO:0000269|PubMed:10570053"; MUTAGEN 475; /note="D->R: Decreased MPP(+) uptake."; /evidence="ECO:0000269|PubMed:10570053"; MUTAGEN 550; /note="T->A: No effect of PKC-induced stimulation on ASP uptake. No effect of PKC-induced stimulation on ASP uptake; when associated with A-286; A-292; A-296; A-328. Significant increase of the ASP uptake by PKA activation. No effect of PKA activation on ASP uptake; when associated with A-286; A-292; A-296 and A-328. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition; when associated with A-286; A-292; A-296; A-328. No significant effect on trafficking from intracellular pools to the cell membrane; when associated with A-286; A-292; A-296 and A-328. suppresses phosphorylation by PKC; when associated with A-286; A-292; A-296 and A-328."; /evidence="ECO:0000269|PubMed:15829703
uniprot
proteins
post_translational_modification
PTM: Phosphorylated. {ECO:0000269|PubMed:10864577, ECO:0000269|PubMed:15829703}.
uniprot
proteins
protein_family
Major facilitator (TC 2.A.1) superfamily
uniprot
proteins
protein_family
Organic cation transporter (TC 2.A.1.19) family
uniprot
proteins
pubmed
10570053
uniprot
proteins
pubmed
10864577
uniprot
proteins
pubmed
10997918
uniprot
proteins
pubmed
11083459
uniprot
proteins
pubmed
11408531
uniprot
proteins
pubmed
11502595
uniprot
proteins
pubmed
11758759
uniprot
proteins
pubmed
11792693
uniprot
proteins
pubmed
12395288
uniprot
proteins
pubmed
15122767
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15640376
uniprot
proteins
pubmed
15662044
uniprot
proteins
pubmed
15817714
uniprot
proteins
pubmed
15829703
uniprot
proteins
pubmed
16142924
uniprot
proteins
pubmed
16272756
uniprot
proteins
pubmed
16581093
uniprot
proteins
pubmed
17553914
uniprot
proteins
pubmed
17567940
uniprot
proteins
pubmed
17616214
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
7990927
uniprot
proteins
pubmed
8955087
uniprot
proteins
pubmed
9195965
uniprot
proteins
pubmed
9405386
uniprot
proteins
pubmed
9703985
uniprot
proteins
pubmed
9776363
uniprot
proteins
pubmed
9808712
uniprot
proteins
pubmed
9830022
uniprot
proteins
sequence_length
556
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:10997918, ECO:0000269|PubMed:11083459, ECO:0000269|PubMed:7990927, ECO:0000269|PubMed:9703985, ECO:0000269|PubMed:9808712}; Multi-pass membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000269|PubMed:15817714}; Multi-pass membrane protein {ECO:0000305}. Lateral cell membrane {ECO:0000250|UniProtKB:O15245}; Multi-pass membrane protein {ECO:0000305}. Basal cell membrane {ECO:0000250|UniProtKB:O15245}; Multi-pass membrane protein {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:10570053}; Multi-pass membrane protein {ECO:0000305}. Note=Localized to the sinusoidal/basolateral membrane of hepatocytes (PubMed:9703985). Mainly localized to the basolateral membrane of renal proximal tubular cells (PubMed:10997918, PubMed:11083459, PubMed:7990927, PubMed:9808712). Localized to the luminal/apical membrane of ciliated epithelial cells in the airway (PubMed:15817714). {ECO:0000250|UniProtKB:O15245, ECO:0000269|PubMed:10997918, ECO:0000269|PubMed:11083459, ECO:0000269|PubMed:15817714, ECO:0000269|PubMed:7990927, ECO:0000269|PubMed:9703985, ECO:0000269|PubMed:9808712}.
uniprot
proteins
transmembrane_region
TRANSMEM 22..42; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 151..171; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 178..198; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 212..231; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 239..259; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 264..284; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 349..369; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 378..398; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 404..424; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 430..452; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 466..486; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 494..514; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins